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O19913 | MVSITLKTNRIFRSCLNLATNLKFSITLFIIICIVSAIGTIIPQDKPKEFYMNTYSLKVLGMPLWKIIQLLSLEKIFYSNFYLILLLCLSFSLFFCSLKSQFPYLRTSRIIKLNNNNPPTSPLHESKKIKYNNIASKNDSSCVQLVSQGYKIYTFDKNLDKAGPLLIHLSLILILLGSAIHAFNDFIAQEMIPIYEVSHIQNVISSGRISKIPQTISLKASAFTVEHENEKVVKQFITNLAMLNSKGEVLKQGLVSVNHPLVYKQVYIFQMDWKLFGIRVNYGKNKIYEFPVQKIEANNEQQWSCTIPAKNQSKLILIFKNMSDEFYVYDNNQNFLKIGKINTPQLIRNTYFTVISKISGTGLQIKKDSSINIVYTGFLLLIIGLVINHKGSKKRT | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45279
Sequence Length: 396
Subcellular Location: Plastid
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Q7VCA3 | MNLILMINLFLYINGLDPVLTLGSLAFVLILISLPFSFWNVGENSNSSIVRILIASANILLAIQLVFRWIQSGHFPISNLYESLCFLTWGLTFIQLLIERTFPYPLIQAALTPISLLSIAFASFVLPDELKASSSLVPALKSNWLVMHVSVIMCSYAALLIGSLLSLVVLLSSSRETLQIRSNSMGIGGFKNKSENLNIVKSIDELIPITFSKSEELDNLSYRTITFGFLLLTFGLISGAVWANEAWGSWWSWDPKETWAFISWLIYAAYLHTRLSRGWQGKRPAIIAIIGLFIILICYIGVNFLGIGLHSYGWFL | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35350
Sequence Length: 316
Subcellular Location: Cellular thylakoid membrane
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Q3ZBH3 | MGEFGEKSTTCGTVCLKYLLFTFNCCFWLAGLAVMAVGIWTLALKSDYISLLASGTYLATAYILVVAGIVVMVTGALGCCATFKERRNLLRLYFGLLLIIFLLEIIAGALAYIYYQQLNAELKENLKDTMTRRYHQPGHEGVTSAVDKLQQEFHCCGSNNSRDWQDSEWIHSGEAGGRVVPDSCCKTVVPGCGRRDHASNIYKVEGGCITKLETFIQEHLRIIGAVGLGIACVQVFGMLFTCCLYKSLKLEHY | Function: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney.
PTM: Palmitoylated. Palmitoylation by ZDHHC2 regulates CD151 expression, association with other tetraspanin family proteins and function in cell adhesion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27987
Sequence Length: 253
Subcellular Location: Membrane
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P48509 | MGEFNEKKTTCGTVCLKYLLFTYNCCFWLAGLAVMAVGIWTLALKSDYISLLASGTYLATAYILVVAGTVVMVTGVLGCCATFKERRNLLRLYFILLLIIFLLEIIAGILAYAYYQQLNTELKENLKDTMTKRYHQPGHEAVTSAVDQLQQEFHCCGSNNSQDWRDSEWIRSQEAGGRVVPDSCCKTVVALCGQRDHASNIYKVEGGCITKLETFIQEHLRVIGAVGIGIACVQVFGMIFTCCLYRSLKLEHY | Function: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney.
PTM: Palmitoylated. Palmitoylation by ZDHHC2 regulates CD151 expression, association with other tetraspanin family proteins and function in cell adhesion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28295
Sequence Length: 253
Subcellular Location: Membrane
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P42292 | MMEPPAAAARASCRRRPLLCLLLAALCMPPALGLYTVNAVYGDTITMPCRLEVPDGLMFGKWKYEMPNGSPVFIAFRSSTKKNVQYDDVPDYKDRLSLSENYTLSIKNARISDEKRFVCMLVTEDDVSEEPTVVKVFKQPSQPEILHQADFLETEKLKMLGECVVRDSYPEGNVTWYKNGRVLQPVEEVVVINLRKVENRSTGLFTMTSSLQYMPTKEDANAKFTCIVTYHGPSGQKTIQSEPVVFDVHYPTEKVTIRVLSQSSTIKEGDNVTLKCSGNGNPPPQEFLFYIPGETEGIRSSDTYVMTDVRRNATGEYKCSLIDKSMMDATTITVHYLDLQLTPSGEVTKQIGEALPVSCTISSSRNATVFWIKDNTRMKTSPSFSSLQYQDAGNYICETTLQEVEGLKKRKTLKLIVEGKPQIKMTKKTNTNKMSKTIVCHVEGFPKPAVQWTVTGSGSLINKTEETKYVNGKFSSKIIIAPEENVTLTCIAENELERTVTSLNVSAISIPEYDEPEDRNDDNSEKVNDQAKLIVGIVVGLLLVALVAGVVYWLYVKKSKTASKHVDKDLGNIEENKKLEENNHKSET | Function: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (By similarity). Mediates homotypic interactions with cells that express ALCAM . Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM . Mediates outgrowth and pathfinding for retinal ganglion cell axons .
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65726
Sequence Length: 588
Domain: The CD6 binding site is located in the N-terminal Ig-like domain.
Subcellular Location: Cell membrane
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Q13740 | MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA | Function: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts . Promotes T-cell activation and proliferation via its interactions with CD6 . Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 . Mediates homotypic interactions with cells that express ALCAM . Acts as a ligand for the LILRB4 receptor, enhancing LILRB4-mediated inhibition of T cell proliferation . Required for normal hematopoietic stem cell engraftment in the bone marrow . Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction . Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions . Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity).
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65102
Sequence Length: 583
Domain: The CD6 binding site is located in the N-terminal Ig-like domain.
Subcellular Location: Cell membrane
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Q8N6Q3 | MSAVLLLALLGFILPLPGVQALLCQFGTVQHVWKVSDLPRQWTPKNTSCDSGLGCQDTLMLIESGPQVSLVLSKGCTEAKDQEPRVTEHRMGPGLSLISYTFVCRQEDFCNNLVNSLPLWAPQPPADPGSLRCPVCLSMEGCLEGTTEEICPKGTTHCYDGLLRLRGGGIFSNLRVQGCMPQPGCNLLNGTQEIGPVGMTENCNRKDFLTCHRGTTIMTHGNLAQEPTDWTTSNTEMCEVGQVCQETLLLLDVGLTSTLVGTKGCSTVGAQNSQKTTIHSAPPGVLVASYTHFCSSDLCNSASSSSVLLNSLPPQAAPVPGDRQCPTCVQPLGTCSSGSPRMTCPRGATHCYDGYIHLSGGGLSTKMSIQGCVAQPSSFLLNHTRQIGIFSAREKRDVQPPASQHEGGGAEGLESLTWGVGLALAPALWWGVVCPSC | Function: In association with beta-2 integrin heterodimer ITGAM/CD11b and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils including degranulation and superoxide production . In addition, by preventing beta-2 integrin internalization and attenuating chemokine signaling favors adhesion over migration . Heterophilic interaction with PECAM1 on endothelial cells plays a role in neutrophil transendothelial migration in vitro . However, appears to be dispensable for neutrophil recruitment caused by bacterial infection in vivo . Acts as a receptor for the mature form of protease PRTN3 allowing its display at the cell surface of neutrophils . By displaying PRTN3 at the neutrophil cell surface, may play a role in enhancing endothelial cell junctional integrity and thus vascular integrity during neutrophil diapedesis .
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46363
Sequence Length: 437
Subcellular Location: Cell membrane
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Q8R2S8 | MNSIPVLTLLGVTALLPCVPALTCQKSSAQAVRNVAELPLRWWGAGEKTCEVSEGCQDLIMLLYNGPKVNLVIIKGCTEVEDQEPKVIWLRTGPGLSVVSYTRVCRHGDLCNDVNSTKILEELPTPTVPGSLRCPLCLSNDSCENAPEQVCPVGSTHCYDGVLRLRGDGIRTNLKVQGCMAQPDCNLLNGTQAIGTLYMSENCDLIGPQALDCNSGSLETVRNVSDLHLSWTTGWQTCEAGEGCYETVMLIQNGHEFHMVLTKGCTRDMNKKARLTRHRTGPGISIVSYVHVCRDRDFCNDLSTTDPLWTPPPDTELGTLRCRHCLSTGSCVSASELVCPAGSTHCYSGVLSLRGGGVISDLKVQGCISQSQPGCNLLNGTQTIGPVDVREDCGLQLDALKCQHGTLKTIQDISKLPLQWTAGQKICNVGEGCQDTLMLIENGEQVNLVLTKGCTTAKDQEAKVTEHRTGPGLSVTSYTRVCRKKDFCNDLSTTAPLWAPPPVTAPGTTRCPLCFSEQACENAPEQVCPAGSTHCYSGVLSLRGGGIISDLKVQGCMSQPGCNLLNGTQTIGPVDVSERCSPPSETTELSCYRGVMFELGNGFAEEPVKWTAPGSQVCAPDEICQETLLLIDVGQKSAFLGSKGCSSPGAQDNIGVSIFSRLPGMLVASYTKFCSSHLCNGADSSSVLLSILPRPDVPPPGDVQCPMCVELFGSCKSTDSVTCPRGATHCYKGDIALQGGGLTTRVSIQGCMAPPIKPLLGDSKTIGIFSAEESSNYRHEDDVTSAPSLAWTLRLSAWMLGLSALLSSLYAGICPLC | Function: In association with beta-2 integrin heterodimer ITGAM/CD11b and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils including degranulation and superoxide production (By similarity). In addition, by preventing beta-2 integrin internalization and attenuating chemokine signaling favors adhesion over migration (By similarity). Heterophilic interaction with PECAM1 on endothelial cells plays a role in neutrophil transendothelial migration in vitro (By similarity). However, appears to be dispensable for neutrophil recruitment caused by bacterial infection in vivo . Acts as a receptor for the mature form of protease PRTN3 allowing its display at the cell surface of neutrophils (By similarity). By displaying PRTN3 at the neutrophil cell surface, may play a role in enhancing endothelial cell junctional integrity and thus vascular integrity during neutrophil diapedesis (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 87091
Sequence Length: 817
Subcellular Location: Cell membrane
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Q99467 | MAFDVSCFFWVVLFSAGCKVITSWDQMCIEKEANKTYNCENLGLSEIPDTLPNTTEFLEFSFNFLPTIHNRTFSRLMNLTFLDLTRCQINWIHEDTFQSHHQLSTLVLTGNPLIFMAETSLNGPKSLKHLFLIQTGISNLEFIPVHNLENLESLYLGSNHISSIKFPKDFPARNLKVLDFQNNAIHYISREDMRSLEQAINLSLNFNGNNVKGIELGAFDSTIFQSLNFGGTPNLSVIFNGLQNSTTQSLWLGTFEDIDDEDISSAMLKGLCEMSVESLNLQEHRFSDISSTTFQCFTQLQELDLTATHLKGLPSGMKGLNLLKKLVLSVNHFDQLCQISAANFPSLTHLYIRGNVKKLHLGVGCLEKLGNLQTLDLSHNDIEASDCCSLQLKNLSHLQTLNLSHNEPLGLQSQAFKECPQLELLDLAFTRLHINAPQSPFQNLHFLQVLNLTYCFLDTSNQHLLAGLPVLRHLNLKGNHFQDGTITKTNLLQTVGSLEVLILSSCGLLSIDQQAFHSLGKMSHVDLSHNSLTCDSIDSLSHLKGIYLNLAANSINIISPRLLPILSQQSTINLSHNPLDCTCSNIHFLTWYKENLHKLEGSEETTCANPPSLRGVKLSDVKLSCGITAIGIFFLIVFLLLLAILLFFAVKYLLRWKYQHI | Function: May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 74179
Sequence Length: 661
Subcellular Location: Cell membrane
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Q08336 | VVLGKKGDTVELACNASQKKSTQFHWKNSKQIKILGNQGSFLTKGSSKLSDRADSRKSLWDQGCFSMIIKNLKIEDSETYICEVENKKEEVELLVFGLTANSDTHLLEGQSLTLTLESPPGSSPSVKCRSPRGKNIQGGRTLSVPQLERQDSGTWTCTVSQDQKTVEFKIDIVVLAFQKASSTVYKKEGEQVEFSFPLAFTLEELTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTEKLHQEVNLVVMRATQFQENLTCEVWGPTSPKLTLSLRLENKKATVSKQAKAVWVLNPEAGMWQCLLSDSGQALLESNIKVVPTWPTPVQPMALIVLGGVAGLLLFTGLGIFFCVRCRH | Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43927
Sequence Length: 397
Domain: The Ig-like V-type domain mediates the interaction with MHCII.
Subcellular Location: Cell membrane
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P01730 | MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI | Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51111
Sequence Length: 458
Domain: The Ig-like V-type domain mediates the interaction with MHCII.
Subcellular Location: Cell membrane
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P06332 | MCRAISLRRLLLLLLQLSQLLAVTQGKTLVLGKEGESAELPCESSQKKITVFTWKFSDQRKILGQHGKGVLIRGGSPSQFDRFDSKKGAWEKGSFPLIINKLKMEDSQTYICELENRKEEVELWVFKVTFSPGTSLLQGQSLTLTLDSNSKVSNPLTECKHKKGKVVSGSKVLSMSNLRVQDSDFWNCTVTLDQKKNWFGMTLSVLGFQSTAITAYKSEGESAEFSFPLNFAEENGWGELMWKAEKDSFFQPWISFSIKNKEVSVQKSTKDLKLQLKETLPLTLKIPQVSLQFAGSGNLTLTLDKGTLHQEVNLVVMKVAQLNNTLTCEVMGPTSPKMRLTLKQENQEARVSEEQKVVQVVAPETGLWQCLLSEGDKVKMDSRIQVLSRGVNQTVFLACVLGGSFGFLGFLGLCILCCVRCRHQQRQAARMSQIKRLLSEKKTCQCPHRMQKSHNLI | Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51297
Sequence Length: 457
Domain: The Ig-like V-type domain mediates the interaction with MHCII.
Subcellular Location: Cell membrane
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P46630 | MNRRIYFQCLLLVLPLALLPAATWGKTVVRGKAGAIVELPCQSSQKRNSVFNWKHANQVKILGNQGSSSSSFWLKGNSPLSNRVESKKNMWDQGSFPLVIKDLRMDDSGTYICEVGDKKMEVELLVFRLTANPNTRLLHGQSLTLTLEGPSVGSPSVQWKSPENKIIETGPTCSMPKLRLQDSGTWSCHLSFQDQNKLELDIKIIVLGFPKASATVYKKEGEQVEFSFPLNFEDESLSGELMWQVDGASSAQSWVSFSLEDRKVSVQKILPDLKIQMSKGLPLSLTLPQALHRYAGSGNLSLTLDKGKLHQQVSLVMLKVTQVKNKLTCEVLGPIDPKMKLSLKLEDQEAKVSTQKMVQVLDPKAGTWQCLLSSGDQVLLESKADVLATGLSHQQPTLLAGALGGTAGLVLFAGLCIYCCVKCRHRRHQAQRMSQIKKLLSEKKTCQCPHRLQKTYNLL | Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages.
PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 50886
Sequence Length: 459
Domain: The Ig-like V-type domain mediates the interaction with MHCII.
Subcellular Location: Cell membrane
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P05542 | KAVVLGKAGGTAELPCQASQ | Function: Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 1928
Sequence Length: 20
Subcellular Location: Membrane
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P31358 | MKRFLFLLLTISLLVMVQIQTGLSGQNDTSQTSSPSASSNISGGIFLFFVANAIIHLFCFS | Function: May play a role in carrying and orienting carbohydrate, as well as having a more specific role.
Location Topology: Lipid-anchor
Sequence Mass (Da): 6614
Sequence Length: 61
Subcellular Location: Cell membrane
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Q64389 | MKSFLLFLTIILLVVIQIQTGSLGQATTAASGTNKNSTSTKKTPLKSGASSIIDAGACSFLFFANTLMCLFYLS | Function: May play a role in carrying and orienting carbohydrate, as well as having a more specific role.
Location Topology: Lipid-anchor
Sequence Mass (Da): 7798
Sequence Length: 74
Subcellular Location: Cell membrane
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Q63064 | MNTFLLLLTISLLVVVQIQTGDLGQNSTAVTTPANKAATTAAATTKAAATTATKTTTAVRKTPGKPPKAGASSITDVGACTFLFFANTLMCLFYLS | Function: May play a role in carrying and orienting carbohydrate, as well as having a more specific role.
Location Topology: Lipid-anchor
Sequence Mass (Da): 9829
Sequence Length: 96
Subcellular Location: Cell membrane
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P81299 | MREDHSPRRNNTIENTLTELLPNRLYFGCFPNPDAIDKSDKSVKKTCFININNKFHYEPFYEDFGPWNLSVLYRLCVQVGKLLEVEEKRSRRVVLFCQDDGTGQYDKIRVNTAYVLGAYLIIYQGFSADDAYLKVSSGETVKFVGFRDASMGSPQYLLHLHDVLRGIEKALKFGWLDFSDFDYEEYEFYERVENGDFNWIIPGKILSFCGPHNESREENGYPYHAPDVYFDYFRENKVSTIVRLNAKNYDASKFTKAGFDHVDLFFIDGSTPSDEIMLKFIKVVDNTKGGVAVHCKAGLGRTGTLIACWMMKEYGLTAGECMGWLRVCRPGSVIGPQQPYLIEKQKFCWSLSQSNGVHLTQNKEEKRNVRRLVNQVDDINLGEERISPKSRENTRPNILRRRVQVQNGRSTAPVTIAPAGTSESRRSTKPSRVVDETALDDQGRSQGDRLLQLKAKHQHESETTSPNSSSSRRFVKSSTPQMTVPSQAYLNRNREPIIVTPSKNGTSSGTSSRQLKTTPNGNVAYRTRNSSGNTTSTLTRTGNESYRFHNSLFYEPASAVFPSMASRRSETTRYLSPTTPIKPMSPSYTDGTSPRYKARLRSENPIGSTTSTPFSLQPQITKCSLTAESKPPKRILSMPGTSKSTSSLKKIQVSRPRPYPSTGVRVELCANGKSYDIRPRKEAHVIPGAGLAANTEALLGVCKLVNTLS | Function: Protein phosphatase that negatively regulates the G1-to-S phase transition to inhibit the cell cycle and establish quiescence in cells of multiple lineages including vulval, hypodermal and intestinal . Promotes nuclear accumulation and activity of the cyclin-dependent kinase inhibitor cki-1 which leads to inhibition of G1 progression during vulval tissue development . Has been shown to not be required for cytokinesis . However, in the embryo, in a contrasting study, has been shown to act as a regulator of central spindle formation and cytokinesis, and may be required for localization of the spindle component zen-4, and its interacting partner air-2 at the spindle during late cell divisions .
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 79740
Sequence Length: 709
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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Q59NH8 | MHSSSVHVPLIEFLKNRIYLGAYDHHKRDTEDLAYFTVEDALPYNAFYMDFGPLNIGHLYRFAVLLHKKLNEDSTQGKGLVIYSSTSPKERANLACLLCCYMILLQNWAPHQVLQPIAQITPPLQAFRDAGYSSADYEITIQDVVYAMWRAKERGMIDLAKFDLDEYEQYERVDQGDFNVISKDFIAFASPQQSKRGGLNEPFQKVLEYFVENNVQLVVRLNSHLYDAKEFTKRNIKHIDMIFDDGTCPTLEYVQKFIGAAECIINKGGKIAVHCKAGLGRTGCLIGAHLIYTHGFTANECIAYMRMIRPGMVVGPQQHWLYLHHDDFRSWRHTMIVDNRPDPLIGNLFPLCSYEDYKQRLKEAKRKERLQLQQQLTSPLADSSVINTPIRRRKVSGALASKIQTVVPIESPGQPRKYFEDSEDIDEVEMVNNSDDENTMQDIIQSSPARYDSVTPKTKDNSDWRVLRSISTNNVSSQQSIHIIKTTTTKTVNETLSSPPGTSPTNVLRVSKARSKNRIASGNSQTSRAHSGGVRKLSGKKH | Function: Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases (By similarity). Plays a role in the expression of hydrolase genes such as CHT3 and ENG1 involved in septum degradation after cytokinesis. Also required for ACE2 localization to the daughter nucleus. Required for invasive and hyphal growth.
PTM: Mainly phosphorylated as the cells are passing through mitosis in yeast form cells. Phosphorylation is delayed in hyphal-induced cells, indicating that the timing of cell-cycle progression occurs with different kinetics in hyphae and in yeast cells.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 61582
Sequence Length: 542
Subcellular Location: Nucleus
EC: 3.1.3.48
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Q5B323 | MAGSTAGYGQIIEYIQDKLYLASYDHTPDAKTPFPYPAEQPKSPSKRRAQASPSKKRSPVYFTVDDTLLYNSFHADFGPLHIGHLYRFAVHFHDLLAANNDRAIVFYSRTDARSRANAACLVACYMVLIQSWPPHLALAPIAQADPPYMPFRDAGYSQADFILNIQDVVYGVWKAKEQGVCGLRDFSLEEYEKFERVDMGDFNWISPHFLAFASPQHQPVAPIPRDSPEYAALPSTVSEVRSSRLPLPFKNVLEHFATRGVGLVVRLNSELYSPSYFTALGISHIDMIFEDGTCPPLPLVKKFIRMAHEMINVKHKAIAVHCKAGLGRTGCLIGAYLIYRYGFTANEVIAFMRFMRPGMVVGPQQHWLHLNQGSFREWWFEDCMKEKLAQMQPNPVTPGRSPAKHRAAAVTTPPQNGHSKRSALGEIDNNEATPIYDDNLPAPTPGQPRKSHRKDSRHHPYSRTASGSLVVDKDTRKTRRSTDSSESEEETQLRMLAKQRSSKSPAASPGQRSISYSATVTASYTLNDDIHEDRENWGGAAQPPKTPVTSKTSGAVSVSKVRSSSRRVTGESKGVRKPSGRIGSTGSPVRVKAQA | Function: Protein phosphatase which antagonizes mitotic cyclin-dependent kinase nimX, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases (By similarity). Required for the transcription of the two major endoglucanase genes eglA and eglB and growth on synthetic cellulose as the sole carbon source.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 66129
Sequence Length: 595
Subcellular Location: Nucleus
EC: 3.1.3.48
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Q00684 | MRRSVYLDNTIEFLRGRVYLGAYDYTPEDTDELVFFTVEDAIFYNSFHLDFGPMNIGHLYRFAVIFHEILNDPENANKAVVFYSSASTRQRANAACMLCCYMILVQAWTPHQVLQPLAQVDPPFMPFRDAGYSNADFEITIQDVVYGVWRAKEKGLIDLHSFNLESYEKYEHVEFGDFNVLTPDFIAFASPQEDHPKGYLATKSSHLNQPFKSVLNFFANNNVQLVVRLNSHLYNKKHFEDIGIQHLDLIFEDGTCPDLSIVKNFVGAAETIIKRGGKIAVHCKAGLGRTGCLIGAHLIYTYGFTANECIGFLRFIRPGMVVGPQQHWLYLHQNDFREWKYTTRISLKPSEAIGGLYPLISLEEYRLQKKKLKDDKRVAQNNIEGELRDLTMTPPSNGHGALSARNSSQPSTANNGSNSFKSSAVPQTSPGQPRKGQNGSNTIEDINNNRNPTSHANRKVVIESNNSDDESMQDTNGTSNHYPKVSRKKNDISSASSSRMEDNEPSATNINNAADDTILRQLLPKNRRVTSGRRTTSAAGGIRKISGSIKK | Function: Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Inhibits transcription of ribosomal genes (rDNA) during anaphase and controls segregation of nucleolus by facilitating condensin targeting to rDNA chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, CDH1. Dephosphorylates the microtubule bundling factor ASE1 which is required to define a centered and focused mitotic spindle midzone that can drive continuous spindle elongation. Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3 complex formation which promotes cytokinesis through the dephosphorylation of CDC28-phosphosphorylated INN1. Reverts also the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that septum formation is contingent upon chromosome separation and exit from mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1, as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 61907
Sequence Length: 551
Subcellular Location: Nucleus
EC: 3.1.3.48
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Q09822 | MEVNGVSQSEAAPYVTKSSVKFRDNFWGSEDAGMDALMSRTKSSLSVLESIDEFYAKRASIEREYASKLQELAASSADIPEVGSTLNNILSMRTETGSMAKAHEEVSQQINTELRNKIREYIDQTEQQKVVAANAIEELYQKKTALEIDLSEKKDAYEYSCNKLNSYMRQTKKMTGRELDKYNLKIRQAALAVKKMDAEYRETNELLLTVTREWIDRWTEVCDAFQHIEEYRLEFLKTNMWAYANIISTACVKDDESCEKIRLTLENTNIDEDITQMIQNEGTGTTIPPLPEFNDYFKENGLNYDIDQLISKAPSYPYSSSRPSASASLASSPTRSAFRPKTSETVSSEVVSSPPTSPLHSPVKPVSNEQVEQVTEVELSIPVPSIQEAESQKPVLTGSSMRRPSVTSPTFEVAARPLTSMDVRSSHNAETEVQAIPAATDISPEVKEGKNSENAITKDNDDIILSSQLQPTATGSRSSRLSFSRHGHGSQTSLGSIKRKSIMERMGRPTSPFMGSSFSNMGSRSTSPTKEGFASNQHATGASVQSDELEDIDPRANVVLNVGPNMLSVGEAPVESTSKEEDKDVPDPIANAMAELSSSMRRRQSTSVDDEAPVSLSKTSSSTRLNGLGYHSRNTSIASDIDGVPKKSTLGAPPAAHTSAQMQRMSNSFASQTKQVFGEQRTENSARESLRHSRSNMSRSPSPMLSRRSSTLRPSFERSASSLSVRQSDVVSPAPSTRARGQSVSGQQRPSSSMSLYGEYNKSQPQLSMQRSVSPNPLGPNRRSSSVLQSQKSTSSNTSNRNNGGYSGSRPSSEMGHRYGSMSGRSMRQVSQRSTSRARSPEPTNRNSVQSKNVDPRATFTAEGEPILGYVIALYDYQAQIPEEISFQKGDTLMVLRTQEDGWWDGEIINVPNSKRGLFPSNFVQTV | Function: After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Appears to mediate cytoskeletal rearrangements required for cytokinesis. Essential for viability.
Sequence Mass (Da): 102119
Sequence Length: 927
Domain: The N-terminal region is in a coiled coil structure.
Subcellular Location: Cytoplasm
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P27636 | MNSMADTDRVNLTPIQRASEKSVQYHLKQVIGRGSYGVVYKAINKHTDQVVAIKEVVYENDEELNDIMAEISLLKNLNHNNIVKYHGFIRKSYELYILLEYCANGSLRRLISRSSTGLSENESKTYVTQTLLGLKYLHGEGVIHRDIKAANILLSADNTVKLADFGVSTIVNSSALTLAGTLNWMAPEILGNRGASTLSDIWSLGATVVEMLTKNPPYHNLTDANIYYAVENDTYYPPSSFSEPLKDFLSKCFVKNMYKRPTADQLLKHVWINSTENVKVDKLNKFKEDFTDADYHWDADFQEEKLNISPSKFSLAAAPAAWAENNQELDLMPPTESQLLSQLKSSSKPLTDLHVLFSVCSLENIADTIIECLSRTTVDKRLITAFGSIFVYDTQHNHSRLRLKFIAMGGIPLIIKFEHLAKEFVIDYPQTLIECGIMYPPNFASLKTPKYILELVYRFYDLTSTAFWCRWCFKHLDISLLLNNIHERRAQSILLKLSSYAPWSFEKILPSLIDSKLKKKILISPQITYVVFKSINYMITTNDDKIHKSAIPSSSSLPLSSSPTRNSPVNSVQSPSRSPVHSLMATRPSSPMRHKSISNFPHLTISSKSRLLIELPEGFFTWLTSFFVDMAQIKDLSVLKYFTKLCYLTVHINSTFLNDLLDNDAFFAFIRNIDTIIPFIDDAKTAAFIWKQITAICVEMSLDMDQMSASLFSTAMNFIRKKNNTSISGLEIILNCLHFTLRNVNDDVAPTVGSSESHSVFLIKVNNDAAIELPIDQLVDLFYALNDDDVNLSKLISIFTKICSLPGFENLTINIIFHPNFYEKIVSFFDTYFNSLLIQIDLLKFIKLIFSKSLLKLYDYTGQPDPIKQTEPNRRNKATVFKLRAILVQITEFLNNNWNKDVPKRNSNQVGGDSVLICQLCEDIRSLSKKGSLQKVSSVTAAIGSSPTKDERSNLRSSKDKSDGFSVPITTFQT | Function: Protein kinase of the mitotic exit network (MEN) essential for late nuclear division in the mitotic cycle. Promotes mitotic exit by phosphorylating DBF2 and directly switching on DBF2 kinase activity. Involved in the localization of DBF2 and DBF20 to the neck which is necessary to undergo cytokinesis. Plays a role in segregation of chromosomes during recovery from spindle checkpoint activation. Required for spindle pole localization of CDK1 and inactivation of CDC2 kinase activity at the end of mitosis. Required for spindle disassembly after meiosis II and plays a role in spore morphogenesis.
PTM: Phosphorylation by CDK1 reduces the binding to the mother spindle pole body. The extent of phosphorylation gradually increases during cell-cycle progression until some point during late anaphase/telophase when it is rapidly dephosphorylated by CDC14. Phosphorylation inhibits kinase activity and dephosphorylation by CDC14 activates CDC15.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 110242
Sequence Length: 974
Domain: The region between residues 360 and 702 is essential for function and is required for self-association and for binding to spindle pole bodies.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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B3DNN5 | MREEEIEKIRGVVRDCVSKHLYSSAIFFADKVAALTNDPSDIYMQAQALFLGRHYRRAFHLLNASKIVLRDLRFRYLAAKCLEELKEWDQCLLMLGDAKVDDDGIVYDAKDGNVIDFDKDGEDREINISSAICFLRGKAYGALQNRSQARQWYKAAIKADPLCYEALECLIESHMLTSEEESSLLSSLQFSPEDGWLSSFYSCLIKKYDKESTVELKFKKLENETSGSVSGSSMITLANNTDLLACKAEYYHQCCEYQKCFELTAALLEKDPFHLKCTLVHLAAAMELGNSNELYLMACNLVKDYPSKALSWFAVGCYYYCIKKYAEARRYFSKATGIDGSFSPARIGYGNSFAAQEEGDQAMSAYRTAARLFPGCHLPTLYIGMEYMRTHSYKLADQFFMQAKAICPSDPLVYNELGVVAYHMKEYGKAVRWFEKTLAHIPSALTESWEPTVVNLAHAYRKLRKDREAISYYERALTLSTKSLSTYSGLAYTYHLQGNFSAAISYYHKALWLKPDDQFCTEMLNVALMDECQNGVDSKVELC | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication.
Sequence Mass (Da): 61762
Sequence Length: 543
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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G5EG38 | MSAISPDTKSFAIPTLADEGSSSKPASSLDLPKHESIRFKPIKTLASRIDGSEYYDEASMEKVMEMLEIGRTDEAVAYADTLYSNIIDDEQQDIVTIAEYVKILVVLRQWRRISHIIARGNYHQIHIVFAYYAATALFQRKLYEDVAELSVGHLLPSNGQIGPLPVRTLSQVTGRYVEEERMKYSFANMAELDNSSKKLRMVPALMITIAESFLKLMNRDAAMICINYALSLDNTTLHVERLMAKYNLVEPAMWEKYRKVRNEQLKLHEGNHDPRILMERAQRAYEMGRFRETKKITDELFDLFGPHPECIILRIHCLTMLKDSRSLLELGHQLVSDDPHIPLPWYCVAMYYYSIGANSRARNFISKCTMMDSTFAEGWVAFGHILHYEVEHEQSMSCYYRASKLVDKSSEPFLYTSLQYSTHSQKLSKKFMGEAVARAPNDPLIRHEEACVAYTAKSYAEADILFRTVLYMVTETDEIIPIEEVLKKKIDDFWHPMLNNIGHIARRQGRLNEAIMFYQKAIRMEPKFVDAIASTALCYAVLGNIDKATEFFNKALAIDPFNETIRQCLSKMIQASKESYSVDQQTLPPAYNSETYFGAQEILPYCAIRKPRNDGFVVPSIVSSSQPFMSMLRDRLRRQDQLYAQEPDNDAGNQV | Function: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (By similarity). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (By similarity). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells . Required for embryonic anterior-posterior axis formation . Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion . Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons .
Sequence Mass (Da): 75153
Sequence Length: 655
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cell junction
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Q1ZXE6 | MADNLYDSSIIEKQLKEKIENALSIHSYPTAIFFSDKLLNLVTIHSKEYVKILYILCDALYLDRQFQRSSYLIQKYLNAIEEIDKKGEDYQYIDDIHSHHHNQQQNIFYKRIKKEKEDEQYTNTILKLKYLAAKCKIETNEFDQCLQILNKDNDSSENMDDENNNINNNNNKIKKENEINNDNCDDDDDDDDDDDDDDDDEKDSNQLLKFYTNSKSNKSKDISENNSNNENTTKESINKNNTDSSSIDNKNNNKNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNFNKETLIIRSSISCLKGKCYESMDNLKKAKFWYIKALLTDYNCFEAFESLTKNHLLTYQEEISLLEKLKFSSDDSWIKEIYSLSLKKYDSPKFTFNYKYLELYDSLNHQNSNNNTFGANNNNNNNNNNNNNNNNNNNNNSNNDISTEDLISVKTLSSSSSSPSKKQENNNLITINEIRKKLIECNDIQTWISEYYFYRHQFQESYSITKRILKQDKYYSNQICLMVNISSMFELQLTNELYFTCHQLVDSFTSSLNNGSHGGSHGGGGGGSHGGSSGNGGAISWYGVACYYHLIQNSDQTQRFFTKSTTLDSRMGASWLGFGHFFASKGEHDQAMAAYRTSSRLLTGCHLPLLCIGMELIRVHNLNLASQYILQAKDICPYDPMIFNELGIIEYKNSQYNEAIKLFETALEICKIKSKASSSSSSSSNYHNLNLSNISFSGVGSSGIGNNNNNNNNRRTTTTTTTTSNNQKKNSSNNKTMIAYLESWEPTIYNLAHCYRKLRKFELALHYYTMSLSLLPNNPSTYSALGFTHHLQGNFDEAIDYYHQSLSIRDDTFTNVLLHKALSLSILQYD | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence Mass (Da): 99379
Sequence Length: 865
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q13042 | MNLERLRKRVRQYLDQQQYQSALFWADKVASLSREEPQDIYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDVLDMEEPINKRLFEKYLKDESGFKDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLESLPLSKLCNEEQELLRFLFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHASCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFSQALSIAPEDPFVMHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFREFEVEKQTAEETGLTPLETSRKTPDSRPSLEETFEIEMNESDMMLETSMSDHST | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis.
Sequence Mass (Da): 71656
Sequence Length: 620
Domain: TPR repeats 1-7 mediate homodimerization, while the C-terminal TPR repeats bind to CDC26, burying its hydrophobic N-terminus.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q8R349 | MNLEPLRKRVRQYLDQQQYQSALFWADKVASLSHEEPQDVYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDILDMEEPINRRLFEKYLKDDNGSRDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLDSLPLNKLCAEEQELLRFVFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSTVMEKDPFHANCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFGQALSIAPEDPFVIHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFRDFEVEKQNTEEAGLAPLQNSTKAPESRPNLEETFEIEMNESDMMLETSMSDHST | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
PTM: Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis (By similarity).
Sequence Mass (Da): 71460
Sequence Length: 620
Domain: TPR repeats 1-7 mediate homodimerization, while the C-terminal TPR repeats bind to CDC26, burying its hydrophobic N-terminus.
Pathway: Protein modification; protein ubiquitination.
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P09798 | MKFCLYCCHCYIVICGKATHYYKSSKATSNLKSSNRVLMRNPMSPSEQHSQHNSTLAASPFVSNVSAARTQQSLPTDAQNDRLQQPWNRTNTATSPYQSLANSPLIQKLQANIMTPHQPSANSNSNSNSITGNVVNDNNLLASMSKNSMFGSTIPSTLRKVSLQREYKDSVDGVVRDEDNDEDVHNNGDAAANANNDRESKLGHNGPLTTTTLTTTTTATQLDVSELSAIERLRLWRFDALMQHMYRTAEYIADKVYNISNDPDDAFWLGQVYYNNNQYVRAVELITRNNLDGVNILCRYLLGLSFVKLQRFDDALDVIGEYNPFSEDPSTTAANTMSNNGNNSNTSQPVTDGGIKMESSLCFLRGKIYFAQNNFNKARDAFREAILVDIKNFEAFEMLLSKNLLTPQEEWDLFDSLDFKEFGEDKEIMKNLYKINLSKYINTEDITKSNEILAKDYKLADNVDVVRSKVDICYTQCKFNECLELCETVLENDEFNTNILPAYIGCLYELSNKNKLFLLSHRLAETFPKSAITWFSVATYYMSLDRISEAQKYYSKSSILDPSFAAAWLGFAHTYALEGEQDQALTAYSTASRFFPGMHLPKLFLGMQFMAMNSLNLAESYFVLAYDICPNDPLVLNEMGVMYFKKNEFVKAKKYLKKALEVVKDLDPSSRTTISIQLNLGHTYRKLNENEIAIKCFRCVLEKNDKNSEIHCSLGYLYLKTKKLQKAIDHLHKSLYLKPNNSSATALLKNALELNVTLSLDASHPLIDKSNLMSQASKDKASLNKKRSSLTYDPVNMAKRLRTQKEIFDQNNKALRKGGHDSKTGSNNADDDFDADMELE | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
PTM: Phosphorylated by CDC28, which is required for the early mitotic activity of the APC/C in its CDC20-bound form.
Sequence Mass (Da): 94992
Sequence Length: 840
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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P40986 | MVYRNRSKSVLSTHSKKSDDKAHYKSRSKKKSKSRSKKRLRIYWRYISIVWILWLGLISYYESVVVKRAMKKCQWSTWEDWPEGAESHRVGLFADPQIMDEYSYPGRPQIVNYFTRVIVDHYHRRNWKYVQYYLDPDSNFFLGDLFDGGRNWDDKQWIKEYTRFNQIFPKKPLRRTVMSLPGNHDIGFGDTVVESSLQRFSSYFGETSSSLDAGNHTFVLLDTISLSDKTNPNVSRVPRQFLDNFAMGSHPLPRILLTHVPLWRDPEQQTCGQLRESKEPFPIQKGHQYQTVIENDISQEILTKIQPEILFSGDDHDHCQISHSYPFQGKTKNAQEITVKSCAMNMGISRPAIQLLSLYNPSDLTMVNAGGEYASKTYQTELCYMPDPYKAIRMYLWGLLFSAAFIAYMHFFPKSFNNRVATIMNRVFTRPDGNTSDLPLPTSISKSKSKKSLTHSKYAVNDTRSIKQFLVNAIVLFVSVMPIFIYFYTVV | Cofactor: Binds 2 divalent metal cations.
Function: Probable metallophosphoesterase which may participate in recombinational repair of double -strand breaks.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57147
Sequence Length: 491
Subcellular Location: Membrane
EC: 3.1.-.-
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Q54MZ3 | MNSNYETAELEQLLSLNAPLENVEARWQRKARQNNSNTNNNNGNNGGDRFIPNKMNIDIGHFNLTKENSNPNPNAINNNSSTSTSTTATSSTTNNIESTLYKDTLANQLFESNSGDLESKILSFKSKAPVGNVSSSTNSLRVLYSQNQVGSTPTDQSLKKQFRQIPQQPERILDAPDIVDDYYLNLLDWSSQNVIAIPLGQTVYLWNATTSEIQRLFQVEQQDDYITSLQWTKDGNYLAVGTNSCTIQLWDVAHTKKVRELRGHAGRVGALAWNDYILSSGSSDTNIFNHDVRVQNHHVSTLSGHSQEVCGLKWSHDGGQLASGGNDNIINIWDINSENFETPAHTFEQHTAAVRALAWCPFQPNLLATGGGAADRTIRFWNTITGVCLNTVDTMSQVCSIQWSTTYRELVSSHGYSQNQLCVWKYPSMVKCAELTGHTSRALHTAISPDGETVVSASADETLRFWRVFEKENKLPTANRKSKEVSDGSMMRNINSLIR | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence Mass (Da): 55544
Sequence Length: 499
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q12834 | MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR | Function: Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation.
PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation enhances the interaction of CDC20 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C).
Sequence Mass (Da): 54723
Sequence Length: 499
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q9JJ66 | MAQFVFESDLHSLLQLDAPIPNAPVARWQRKAKEATGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRFIPQRSASQMEVASFLLSKENQPEDRGTPTKKEHQKAWSLNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWNAGSGDILQLLQMEQPGDYISSVAWIKEGNYLAVGTSNAEVQLWDVQQQKRLRNMTSHSARVSSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNIVNVWPSGPGESGWAPLQTFTQHQGAVKAVAWCPWQSNILATGGGTSDRHIRIWNVCSGACLSAVDVHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTARVLGLTMSPDGATVASAAADETLRLWRCFEMDPALRREREKASVAKSSLIHQGIR | Function: Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation.
PTM: Acetylated. Deacetylated at Lys-66 by SIRT2; deacetylation enhances the interaction of CDC20 with CDC27, leading to activation of anaphase promoting complex/cyclosome (APC/C).
Sequence Mass (Da): 54816
Sequence Length: 499
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q9LSE1 | MVSCLCFRPSRKTKLKDKSHKRSIRNQTSSSSAQPAGTAKEVDSSSSQTVVQDSSRYRCQIFSYRELAIATNSFRNESLIGRGGFGTVYKGRLSTGQNIAVKMLDQSGIQGDKEFLVEVLMLSLLHHRNLVHLFGYCAEGDQRLVVYEYMPLGSVEDHLYDLSEGQEALDWKTRMKIALGAAKGLAFLHNEAQPPVIYRDLKTSNILLDHDYKPKLSDFGLAKFGPSDDMSHVSTRVMGTHGYCAPEYANTGKLTLKSDIYSFGVVLLELISGRKALMPSSECVGNQSRYLVHWARPLFLNGRIRQIVDPRLARKGGFSNILLYRGIEVAFLCLAEEANARPSISQVVECLKYIIDHTIRKERRTRRRLLGGNKDGAGTSRSPDETMMRMLEEEEEYVTSEEAIERRRVIVDDARTWAGMNRRGATPPTPTP | Function: Serine/threonine-protein kinase involved in the positive regulation of brassinosteroid (BR) signaling and plant growth. Mediates BR signal transduction from BRI1 receptor kinase to BSU1 phosphatase. After activation by phosphorylation at Ser-234 by BRI1, CDG1 phosphorylates BSU1 at 'Ser-764' in the phosphatase domain, increasing the ability of BSU1 to inactivate the negative regulator of BR signaling ASK7/BIN2 by dephosphorylation at 'Tyr-200'. The full kinase activity of CDG1 is required for its biological function.
PTM: Phosphorylated at Ser-44, Ser-47 and Ser-234 by BRI1.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48507
Sequence Length: 432
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P76236 | MIQSTRISMGLFFKYFLSLTKIDPGQNYISLPSIKSSTHIALLFMVSMGTQKLKAQSFFIFSLLLTLILFCITTLYNENTNVKLIPQMNYLMVVVALFFLNAVIFLFMLMKYFTNKQILPTLILSLAFLSGLIYLVETIVIIHKPINGSTLIQTKSNDVSIFYIFRQLSFICLTSLALFCYGKDNILDNNKKKTGILLLALIPFLVFPLLAHNLSSYNADYSLYVVDYCPDNHTATWGINYTKILVCLWAFLLFFIIMRTRLASELWPLIALLCLASLCCNLLLLTLDEYNYTIWYISRGIEVSSKLFVVSFLIYNIFQELQLSSKLAVHDVLTNIYNRRYFFNSVESLLSRPVVKDFCVMLVDINQFKRINAQWGHRVGDKVLVSIVDIIQQSIRPDDILARLEGEVFGLLFTELNSAQAKIIAERMRKNVELLTGFSNRYDVPEQMTISIGTVFSTGDTRNISLVMTEADKALREAKSEGGNKVIIHHI | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56101
Sequence Length: 491
Pathway: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.7.65
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Q9KVK6 | MVRCLWAAECCWLPPKRKQPFEDTMYTTYVARQPILNAKRHTLGYELLFRDGEKNAFPEYMDADRATYRLIVENFLSLGTNPRIARSRCFINFPHKSLIRRLPLTLPREQIVVEILETCQPTDDLFEAVQELSQRGYLLALDDFVYSPAWERFLPYVQIVKIDIMAMGLDKACEFVRGRLAQGSRRRFLAERVETEDEFHQARHAGFTFFQGYFFSKPEIIKQRYVSPEHVIAMQLFREVCQPEVDYVRVERLVAQDIALSYKLLRFVNTMSDRISVSISSFRQALVYLGQDKLRIFVSLAVASYISSKKPKELYNLSLQRAQFCQLMATHTHFKAHREQAFLIGMFSVLDALLDTSIEQLVEQLPLADDVKLALREREGPLGTLLDLEECFEKADWQGVEQHCLELGFDLEDVRQELIEAQRWSQDINRLI | Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP). Positively regulates motility and negatively regulates biofilm formation.
Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
Sequence Mass (Da): 50458
Sequence Length: 432
EC: 3.1.4.52
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P43379 | MKKFLKSTAALALGLSLTFGLFSPAQAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADLNHNNSTVDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYKPVFTFGEWFLGVNEVSPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTLTSRGVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKCNPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTSLPQGSYNDVLGGLLNGNTLSVGSGGAASNFTLAAGGTAVWQYTAATATPTIGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGADITSWEDTQIKVKIPAVAGGNYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTALGQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP | Cofactor: Binds 3 Ca(2+) ions per subunit.
Catalytic Activity: Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.
Sequence Mass (Da): 77309
Sequence Length: 713
Domain: May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.
Subcellular Location: Secreted
EC: 2.4.1.19
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P31835 | MKKQVKWLTSVSMSVGIALGAALPVWASPDTSVNNKLNFSTDTVYQIVTDRFVDGNSANNPTGAAFSSDHSNLKLYFGGDWQGITNKINDGYLTGMGITALWISQPVENITAVINYSGVNNTAYHGYWPRDFKKTNAAFGSFTDFSNLIAAAHSHNIKVVMDFAPNHTNPASSTDPSFAENGALYNNGTLLGKYSNDTAGLFHHNGGTDFSTTESGIYKNLYDLADINQNNNTIDSYLKESIQLWLNLGVDGIRFDAVKHMPQGWQKSYVSSIYSSANPVFTFGEWFLGPDEMTQDNINFANQSGMHLLDFAFAQEIREVFRDKSETMTDLNSVISSTGSSYNYINNMVTFIDNHDMDRFQQAGASTRPTEQALAVTLTSRGVPAIYYGTEQYMTGNGDPNNRGMMTGFDTNKTAYKVIKALAPLRKSNPALAYGSTTQRWVNSDVYVYERKFGSNVALVAVNRSSTTAYPISGALTALPNGTYTDVLGGLLNGNSITVNGGTVSNFTLAAGGTAVWQYTTTESSPIIGNVGPTMGKPGNTITIDGRGFGTTKNKVTFGTTAVTGANIVSWEDTEIKVKVPNVAAGNTAVTVTNAAGTTSAAFNNFNVLTADQVTVRFKVNNATTALGQNVYLTGNVAELGNWTAANAIGPMYNQVEASYPTWYFDVSVPANTALQFKFIKVNGSTVTWEGGNNHTFTSPSSGVATVTVDWQN | Cofactor: Binds 2 calcium ions per subunit.
Catalytic Activity: Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.
Sequence Mass (Da): 76857
Sequence Length: 713
Domain: May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.
Subcellular Location: Secreted
EC: 2.4.1.19
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Q00526 | MDMFQKVEKIGEGTYGVVYKAKNRETGQLVALKKIRLDLEMEGVPSTAIREISLLKELKHPNIVRLLDVVHNERKLYLVFEFLSQDLKKYMDSTPGSELPLHLIKSYLFQLLQGVSFCHSHRVIHRDLKPQNLLINELGAIKLADFGLARAFGVPLRTYTHEVVTLWYRAPEILLGSKFYTTAVDIWSIGCIFAEMVTRKALFPGDSEIDQLFRIFRMLGTPSEDTWPGVTQLPDYKGSFPKWTRKGLEEIVPNLEPEGRDLLMQLLQYDPSQRITAKTALAHPYFSSPEPSPAARQYVLQRFRH | Function: Serine/threonine-protein kinase that plays a critical role in the control of the eukaryotic cell cycle; involved in G0-G1 and G1-S cell cycle transitions. Interacts with CCNC/cyclin-C during interphase. Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation triggers ATF1 transactivation and transcriptional activities, and promotes cell proliferation and transformation. CDK3/cyclin-C mediated RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S transition probably by contributing to the activation of E2F1, E2F2 and E2F3 in a RB1-independent manner.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35046
Sequence Length: 305
EC: 2.7.11.22
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Q9XTR1 | MTIRHILAIRKKSLELPSDLKTFLRVLANCQHLKKNKKCRRTIFSVDFQNNQRQKPSNFHFWTVIKKFSKKILKSFIIKFGNNGTIAVVFSIFPTGATPSLTFLFQALGKGAYGNVYRVRSLHDGKDYALKQIMISSKNEGIPQSVLREITVMKHLARKAHPNIISLKSVFHQLDPVRAILKINMIMERCDWDLHTFLRNIPRGVPEQQAKHVTAQIVRALDFLHTHSIIHRDLKPQNILLNRDQTVKLADFGLSKEYSNTTAFTTLVVTLWYRSPEVLLQSYYNSTVDMWALGCIVSEIYCRQPLFVGQNEAEQLTDIFKKMGTPVGKDWPSESVIARDSFPQYRPTNLKDLSPQMSKQAIEFVQQCLRYDHSKRLSARGALSHPFLKPAVATKSRVLKQINFNK | Function: Serine/threonine-protein kinase which, in association with cyclin D-like protein cyd-1, is required for the progression through the G1 phase of the cell cycle during postembryonic development by phosphorylating and inhibiting lin-35 and fzr-1 . In complex with cyd-1, involved in sex determination during gonadogenesis by regulating the asymmetric division of the somatic gonadal precursor cell (SGP) .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46694
Sequence Length: 406
EC: 2.7.11.22
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P11802 | MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE | Function: Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex.
PTM: Phosphorylation at Thr-172 is required for enzymatic activity. Phosphorylated, in vitro, at this site by CCNH-CDK7, but, in vivo, appears to be phosphorylated by a proline-directed kinase. In the cyclin D-CDK4-CDKN1B complex, this phosphorylation and consequent CDK4 enzyme activity, is dependent on the tyrosine phosphorylation state of CDKN1B. Thus, in proliferating cells, CDK4 within the complex is phosphorylated on Thr-172 in the T-loop. In resting cells, phosphorylation on Thr-172 is prevented by the non-tyrosine-phosphorylated form of CDKN1B.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33730
Sequence Length: 303
Subcellular Location: Cytoplasm
EC: 2.7.11.22
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G5ECH7 | MLNYDKMEKIGEGTYGTVFKARNKNSGEIVALKRVRLDDDDEGVPSSALREICILRELKHRNVVRLYDVVHSENKLTLVFEYCDQDLKKFFDSLNGYMDAQTARSLMLQLLRGLSFCHAHHVLHRDLKPQNLLINTNGTLKLADFGLARAFGVPVRCFSAEVVTLWYRPPDVLFGAKLYNTSIDMWSAGCIFAEISNAGRPLFPGADVDDQLKRIFKQLGSPSEDNWPSITQLPDYKPYPIYHPTLTWSQIVPNLNSRGRDLLQKLLVCNPAGRIDADAALRHAYFADTSDV | Cofactor: Binds 2 Mg(2+) ions.
Function: Proline-directed serine/threonine-protein kinase which, in several motor neurons, promotes the polarized trafficking of synaptic vesicles and dense-core vesicles (DCV). In the ventral nerve cord, phosphorylates lin-10 and thereby prevents lin-10-mediated anterograde trafficking of the glutamate receptor glr-1 . Involved in the inhibition of glr-1 trafficking in hypoxic conditions . In DA motor neurons but not in DB motor neurons, regulates axonal transport of synaptic vesicle precursors by inhibiting dynein-mediated retrograde transport . Regulates the trafficking of dense-core vesicles in DA and DB motor neurons by promoting anterograde trafficking to the axon and preventing dynein-dependent trafficking to the dendrite . May regulate these processes in association with cdka-1/p35 . Activity may be regulated by cyy-1 . Involved in synapse formation during DD motor neuron remodeling by regulating transport of disassembled synaptic material to the new synaptic sites probably by activating the motor protein unc-104/kinesin-3 . Regulates microtubule polarity in the dendrite of DB motor neurons . May also play a role in GABAergic synaptic vesicle localization in the ventral nerve cord .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33063
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P48609 | MQKYDKMEKIGEGTYGTVFKGRNRDTMEIVALKRVRLDEDDEGVPSSALREICLLKELKHKNIVRLIDVLHSDKKLTLVFEHCDQDLKKYFDSLNGEIDMAVCRSFMLQLLRGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVKCYSAEVVTLWYRPPDVLFGAKLYTTSIDMWSAGCILAELADAGRPLFPGSDVLDQLMKIFRVLGTPNEDSWPGVSHLSDYVALPSFPAITSWSQLVPRLNSKGRDLLQKLLICRPNQRISAEAAMQHPYFTDSSSSGH | Function: Probably involved in the control of the cell cycle. Interacts with D1 and D3-type G1 cyclins. Possible regulator of neuronal differentiation and/or development (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33180
Sequence Length: 294
EC: 2.7.11.22
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P49615 | MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPAMTKLPDYKPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP | Function: Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Negatively regulates the CACNA1B/CAV2.2 -mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in postmitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution.
PTM: Phosphorylation on Tyr-15 by ABL1 and FYN, and on Ser-159 by casein kinase 1 promotes kinase activity. By contrast, phosphorylation at Thr-14 inhibits activity (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33288
Sequence Length: 292
Subcellular Location: Nucleus
EC: 2.7.11.1
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Q03114 | MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSLLFQLLKGLGFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPAMTKLPDYKPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP | Function: Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Negatively regulates the CACNA1B/CAV2.2 -mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals . Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in postmitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution (By similarity).
PTM: Phosphorylation on Tyr-15 by ABL1 and FYN, and on Ser-159 by casein kinase 1 promotes kinase activity. By contrast, phosphorylation at Thr-14 inhibits activity (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33254
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P51166 | MQKYEKLEKIGEGTYGTVFKAKNRDTHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFMYQLLKGLAFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPAMTKLPDYKPYPMYPATMSLVNVVPKLNATGRDLLQNLLKCNPVQRICADEALQHPYFADFCPP | Function: Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. The complex p35/CDK5 may participate in the regulation of the circadian clock.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33339
Sequence Length: 292
Subcellular Location: Nucleus
EC: 2.7.11.1
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P62344 | MGCSQSSNVKDFKTRRSKFTNGNNYGKSGNNKNSEDLAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCREKHGHGEKAIKVIKKSQFDKMKYSITNKIECDDKIHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKHSLLNIKIVDFGLSSFFSKDNKLRDRLGTAYYIAPEVLRKKYNEKCDVWSCGVILYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISEEAKELIKLMLTYDYNKRITAKEALNSKWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNILRSFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRDAFNLFDTDKSGKITKEELANLFGLTSISEQMWNEVLGEADKNKDNMIDFDEFVNMMHKICDNKSS | Function: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase . By phosphorylating various proteins, required for microneme secretion and thus merozoite egress from and invasion of host erythrocytes . During gametogenesis, essential for the development of both male and female gametes (By similarity). Phosphorylates SERA5 p50 which enhances SERA5 p50 protease activity; however, SERA5 p50 protease activity has been shown in other studies to be controversial . Probably by phosphorylating SERA5 p50, plays a role in merozoite egress from host erythrocytes . Probably prior or during merozoite invasion of host erythrocytes, phosphorylates rhoptry protein RhopH3 which is required for RhopH3 localization to rhoptries and for its secretion . Probably in late schizonts, phosphorylates myosin A tail domain-interacting protein MTIP and glideosome-associated protein 45 GAP45, both of which are components of the motor complex that generates the force required by the parasite to invade host cells . In late schizonts, phosphorylates inner membrane complex protein IMC1g . In late schizonts, phosphorylates PKA regulatory subunit PKAr in a calcium-dependent manner, which may contribute to the dissociation of regulatory PKAr and catalytic PKAc subunits and promote the activation of PKAc . May phosphorylate raf kinase inhibitory protein RKIP which in turn may regulate CDPK1 catalytic activity . May phosphorylate proteins of the host erythrocyte membranes (By similarity).
PTM: Myristoylated . Myristoylation, palmitoylation and the basic cluster motif are required for the localization to the parasitophorous vacuole membrane .
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 60800
Sequence Length: 524
Domain: The junction domain (J domain) is composed of 2 motifs that maintain the kinase inactive . The N-terminal autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic domain while the C-terminal motif binds the EF-hand domains .
Subcellular Location: Membrane
EC: 2.7.11.1
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Q38870 | MGNACVGPNISGNGFLQTVTAAMWRPRIGAEQASSSSHGNGQVSKEAASEPATDQVQNKPPEPITMPSSKTNPETKLKPDLEIQPEEKKEKVLAEETKQKVVPEESKQEVPPEESKREVVVQPESAKPETKSESKPETTKPETTSETKPETKAEPQKPKHMRRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCLEKGTGNEYACKSISKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMELCSGGELFDRIIQRGHYTERKAAELARTIVGVLEACHSLGVMHRDLKPENFLFVSREEDSLLKTIDFGLSMFFKPDEVFTDVVGSPYYVAPEVLRKRYGPESDVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKRRLTAHQVLCHPWVQIDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKQMFKMIDADNSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFSYFDKDESGFITPDELQQACEEFGVEDARIEEMMRDVDQDKDGRIDYNEFVAMMQKGSIMGGPVKMGLENSISISLKH | Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 72254
Sequence Length: 646
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (450-480) inactivates kinase activity under calcium-free conditions (By similarity).
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.11.1
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Q5VQQ5 | MGNCCPGSGDAEPASSDASTGNGSSSFKAGASPSSAPAQNKPPAPIGPVLGRPMEDVRSIYTIGKELGRGQFGVTSLCTHKATGQKFACKTIAKRKLSTKEDVEDVRREVQIMYHLAGQPNVVELKGAYEDKQSVHLVMELCAGGELFDRIIAKGHYTERAAASLLRTIVEIIHTCHSLGVIHRDLKPENFLLLSKDEDAPLKATDFGLSVFFKQGEVFKDIVGSAYYIAPEVLKRSYGPEADIWSVGVILYILLCGVPPFWAESEHGIFNSILRGQVDFTSDPWPRISASAKDLVRKMLNSDPKKRISAYEVLNHPWIKEDGEAPDTPLDNAVMNRLKQFRAMNQFKKAALRVIAGCLSEEEIRGLKEMFKSMDSDNSGTITVDELRKGLSKQGTKLTEAEVQQLMEAADADGNGTIDYDEFITATMHMNRMDREEHLYTAFQYFDKDNSGCISKEELEQALREKGLLDGRDIKDIISEVDADNDGRIDYSEFAAMMRKGNPEANPKKRRDVVI | Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 56951
Sequence Length: 515
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (325-355) inactivates kinase activity under calcium-free conditions.
Subcellular Location: Membrane
EC: 2.7.11.1
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Q8ICR0 | MGNHLSVNKLKRKKKKKSFLNIYGKNTNENTSKQSNDYKYDINTSCISREGTTTLERKNLILCHSGKLEDKYIIDEKLGQGTYGCVYKGIDKVTNQLYAIKEEKKDRLKNINRFFQEIEIMKKLDHPNIVKLYETYENDNYIYLIMELCSGRELFDSIIENGSFTEKNAATIMKQIFSAIFYLHSLNIVHRDLKPENFLFQSENKDSLLKIIDFGLSKNLGTGEFTTTKAGTPYYVAPQVLDGKYDKKCDIWSSGVIMYTLLCGYPPFYGDTDNEVLKKVKKGEFCFYENDWGSISSDAKNLITKLLTYNPNERCTIEEALNHPWITQMTKSHEHVELSSTLLKNLKNFKKENELKKIALTIIAKHLCDVEINNLRNIFIALDVDNSGTLSSQEILDGLKKIGYQKIPPDIHQVLRDIDSNASGQIHYTDFLAATIDKQTYLKKEVCLIPFKFFDIDGNGKISVEELKRIFGRDDIENPLIDKAIDSLLQEVDLNGDGEIDFHEFMLMMSKKK | Function: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase . During male gametogenesis in the mosquito gut, required for male exflagellation, possibly by regulating male gamete exit from the host erythrocytes . Not required for asexual blood stage proliferation .
PTM: Myristoylated; myristoylation may target it to different subcellular compartments.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59048
Sequence Length: 513
Domain: The EF-hand domain 2 appears to lack a functional calcium binding site.
EC: 2.7.11.1
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Q42479 | MGHRHSKSKSSDPPPSSSSSSSGNVVHHVKPAGERRGSSGSGTVGSSGSGTGGSRSTTSTQQNGRILGRPMEEVRRTYEFGRELGRGQFGVTYLVTHKETKQQVACKSIPTRRLVHKDDIEDVRREVQIMHHLSGHRNIVDLKGAYEDRHSVNLIMELCEGGELFDRIISKGLYSERAAADLCRQMVMVVHSCHSMGVMHRDLKPENFLFLSKDENSPLKATDFGLSVFFKPGDKFKDLVGSAYYVAPEVLKRNYGPEADIWSAGVILYILLSGVPPFWGENETGIFDAILQGQLDFSADPWPALSDGAKDLVRKMLKYDPKDRLTAAEVLNHPWIREDGEASDKPLDNAVLSRMKQFRAMNKLKKMALKVIAENLSEEEIIGLKEMFKSLDTDNNGIVTLEELRTGLPKLGSKISEAEIRQLMEAADMDGDGSIDYLEFISATMHMNRIEREDHLYTAFQFFDNDNSGYITMEELELAMKKYNMGDDKSIKEIIAEVDTDRDGKINYEEFVAMMKKGNPELVPNRRRM | Function: May play a role in signal transduction pathways that involve calcium as a second messenger. Functions in abscisic acid (ABA) regulation of guard cell S-type anion- and Ca(2+)-permeable channels and stomatal closure.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59336
Sequence Length: 529
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (342-372) inactivates kinase activity under calcium-free conditions (By similarity).
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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A0A509AFG4 | MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVKKGKYNFKGKEWNNISEEAKDLIKRCLTIDSGKRINASEALKHPWFKKKKGSFNLDVKMDIHVLENFKNYALLLKLQKLAMTIIAQQSNDYDLQQLKTVFLYLDEDGKGNITKNQLKKGLENSGLKLPQNFDVLLDQIDSDGSGRIDYTEFLAAALDRKHLSKKLIYCAFRVFDVDNDGEITTAELAHILYNGNKKGSITQKDVNQVKKMIQEVDKNNDGKIDFYEFCEMMKLKY | Function: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). In the mosquito midgut, regulates the gliding motility of the ookinete which is essential for the ookinete to invade the midgut epithelium . However, another study showed that while required for ookinete invasion of the midgut epithelium, is not required for ookinete gliding motility .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64328
Sequence Length: 554
Domain: The EF-hand domain 1 cannot bind calcium due to the presence of a Lys instead of an Asp at position 427 and a Gln instead of a Glu at position 434 preventing calcium binding (By similarity). The EF-hand domains 3 and 4 probably bind calcium constitutively when calcium levels are low, while the EF-hand domain 2 binds calcium following an increase in calcium levels (By similarity).
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P62345 | MGQEMSTQSDMQNENQKGNKRNLKGSQGKNGLKERSTSISKEIVKNSFNNSKLRPGMFIQNSNVVFNEQYKGIKILGKGSFGEVILSKDKHTGHEYAIKVISKKHVKRKTDKQSLLREVELLKMLDHINIMKLYEFFEDNNYYYLVSDVYSGGELFDEIISRKRFYEVDAARIIKQVLSGITYMHKNNVVHRDLKPENILLETKNKEDMIIKIIDFGLSTHFEYSKKMKDKIGTAYYIAPDVLHGTYDEKCDIWSCGVILYILLSGCPPFNGSNEYDILKKVETGKYTFDLPQFKKISDKAKDLIKKMLMYTSAVRISARDALEHEWIRLMTSKDNVNIDIPSLELSITNIKQFQSTQKLAQAALLYMGSKLTTIDETKELTKIFKKMDKNGDGQLDRNELIIGYKELLKLKGDDTTDLDNAAIEVEVDQILSSIDLDQNGYIEYSEFLTVAIDRKLLLSTERLEKAFKLFDKDGSGKISANELAQLFGLGDVSSDCWKTVLKEVDQNNDGEIDFKEFRDMLIKLCNY | Function: Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase . Plays a central role in the host erythrocytes and hepatocytes infection cycles, sexual reproduction and mosquito transmission of the parasite . During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK5 . Involved in merosome egress from host hepatocytes, probably together with CDPK5 . During the asexual blood stage, involved in merozoite invasion of host erythrocytes and motility by stabilizing the inner membrane complex, a structure below the plasma membrane which acts as an anchor for the glidosome, an acto-myosin motor . Required for cell cycle progression in the male gametocyte . During male gametogenesis in the mosquito gut, required to initiate the first round of DNA replication, probably by facilitating the assembly of the pre-replicative MCM complex, to assemble the first mitotic spindle and, at the end of gametogenesis, to initiate axoneme motility, cytokinesis and subsequent exflagellation . For each of these steps, may phosphorylate SOC1, SOC2 and SOC3, respectively . Together with CDPK1, regulates ookinete gliding in the mosquito host midgut .
PTM: Myristoylated; myristoylation may target it to different subcellular compartments . During male gametogenesis, myristoylation is required to initiate DNA replication but not for mitotic spindle assembly or axoneme activation .
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 60590
Sequence Length: 528
Domain: The junction domain (J domain) is composed of 2 motifs that maintain the kinase inactive. The N-terminal autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic domain while the C-terminal motif binds the EF-hand domains.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q02637 | MLNMESPQMYADAVQTLAQLDLKKEPPLQQATIGQITLTAMSTAQQQQQQQQQQQQQQQQQQQQQQQQPQQQTTDANNNTSQDAALLVKQHAMHQMQQVAALGSNNNLLQKQMLQQYSTQTDLDELTTQEITLDLQHLIDDQFRDTETLGIFSDMVTSPGGLSATLPPSGMVSAAAKVLQQQTLRNQHGYGGRGGGGGAGGALAYMPQPVHATYNNSSDENSSVGSDSSTIKEEPIDPEYRRHLQEAASQQAAFMGNGAGLYNGYGSGANGLTGGGNPLNGGNTTPSSNGSNGSTGSSNGSQFTNLTTANVLAHHNLPHLAAAAGAHNLLKQHSKLHAQQQHQQHQQQQQHRKHSNKHVDKGTDEYRRRRERNNIAVRKSREKAKVRSREVEERVKSLLKEKDALIRQLGEMTNELQLHKQIYMQLMNHANPEVSRVCRSFLNTNEHSL | Function: Required for the expression of gene products mediating border cell migration . Among the DNA sequences that this protein binds with high affinity is a conserved site within the promoter of its gene .
PTM: Ubiquitination/deubiquitination regulates border cell migration. Ubiquitination is stimulated by trbl, which leads to proteasomal degradation and inhibits border cell migration. Deubiquitination by Usp47, leads to its stabilization and promotes border cell migration.
Sequence Mass (Da): 49420
Sequence Length: 449
Subcellular Location: Nucleus
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Q19972 | MAKKTVEGEHGTPKTNFTKKETSKNHDDFKKIIGHKVVEEHYVEYEVELTSGKTITATEFDFKGDDSLLSTYKKKVTKQSDDSSGEYAVERVLAHRKVKGSPLYLVQWKGYPHPVWNSEMWEEDLDNCKDLLAAYKKHQEDLKIAQTPKKTPSKTPKKTPKSLKRRALTPSDDEEEAGPIAPEPKKTPKQSTKKLKRTTSPETNLVEKSKKKAIPDLENHTLDQEKNDVIERVEEIQEDEDDDDEQREEVVTTAPVETKSRWGFGSWKWF | Function: Chromatin anchor protein which binds to methylated lysine residues on histone H3, thereby recruiting heterochromatin to the nuclear periphery, especially in embryonic cells, with a lesser role in differentiated cells . May be required for the correct positioning of chromatin and nucleoli in embryos .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31072
Sequence Length: 270
Subcellular Location: Nucleus inner membrane
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Q4JB69 | MLNPFQLLFYSQLLASLTYFIGAAIYALPVPVYGVKKWAPRLITDSIYVVVWNSIYLGVLLFLGELLSLLGVTWDGYFSWLNNILYIEQSLYLMVKTILTASNAVPEVSALIQVVPFGALLTVITSALTFTSTLIAVSKIVYQYVAVFIATGVLFLSIPFRIGRSVGGAFIGSGIVFYVGLPYLPQFLAAFQMLPTQELNTPPQNASAIIDYYVHVVPSIITSLVIGPVIYIFILVGFSMGVASLVSGYGSRLPLIIDVF | Function: Part of the Ced system, which is involved in DNA import.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28418
Sequence Length: 260
Subcellular Location: Cell membrane
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Q4JAQ5 | MNKAFIVVAVVLLILGIISFNLVFIILAIISLFFVDPQIMRKFYKFFLKSNISKIFVKNYKTNHSIVIEDGYLKIEDNVKAFLIVDDIPFDYRDLSDESLRVKISSFHKVLDIAGQIDIVFRKSSIDKNKFLSDLFQKAQNIRVIIDADPSNERAKNELMMIQHMIKKISEGEMPFKYLIFFIINSDSKEKALATADVVKKGLESIGVKSRLAYKHEIEDLLNDKLSLKKIVFPSQIPFLSVFSLQKQPDYEIITDGIYLGQEINDRRAVFWNVNRVINPHALIIGPTGSGKTEFLLSLGVKTNILYGIPIVFFDVKKDISLRLKKYGYKYKYINPLLNSINLLKFSNVNKDIYLIQLENIIRNSFKLDRFVSALLYRILLESISDNYYEVSWDYIIDKIEKYDINEDVKAYLLRIVSAIKSLDAGVEDIDLISAISEGINVVDLSSIKSEELRRLVMYGIIIKFINKYNIADDRLKLVLVIDEAWTLLRSEDRDYQIVADLIKRGRGFGIGIFMATQNFDDLGELSDIFLENIGLLGFMNNGDKKFWNEVMRFADLNIEETLRSLIFLGKGEMLIRFINDPRPIMIKTDVLVRNSF | Function: Part of the Ced system, which is involved in DNA import.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68901
Sequence Length: 597
Subcellular Location: Cell membrane
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G5EBI4 | MLFESIYIQCLNKFSKYKKFVCHTTCNCPNYKIIGYLLYFLCLCRPINCSLPLSRHDLAFGSFSYYLTMFLYRILVRLLQFYYFVKFSAILFLGFAVKGRSLFEKKQREKPNVLEGWDSRYIKLKKVRLHYVQTGSDDKPLMLFIHGYPEFWYSWRFQLKEFADKYRCVAIDQRGYNLSDKPKHVDNYSIDELTGDIRDVIEGLGYDKAIVVAHDWGGLVAWQFAEQYPEMVDKLICCNIPRPGSFRKRIYTSWSQFRKSWYMFFYQNEKIPEMLCSADDMKMLELCFRAKEIGIQNNKNFTDEDLEAWKYSFSMNGASFKYPINYYRNIFNAKKQQADLVLEMPTLIIWGTADGALDIEAAVDSLNTLKQGTMKKIEGASHWVQQDEPEMVNEHIKKFLNKYQ | Function: Catalyzes the hydrolysis of epoxide-containing fatty acids. Active against epoxyeicosatrienoic acids (EETs) including 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate (8,9-EET), 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate (11,12-EET) and 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate (14,15-EET) and the linoleic acid metabolites 12,13-epoxy-(9Z)-octadecenoate (12,13-EpOME) and 9,10-epoxy-(12Z)-octadecenoate (9,10-EpOME). These epoxides function as lipid signaling molecules, the enzyme can deplete the supply of the epoxide signal by transforming them into diol species that are more readily eliminated through excretion.
Catalytic Activity: an epoxide + H2O = an ethanediol
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 47865
Sequence Length: 404
Pathway: Lipid metabolism.
Subcellular Location: Membrane
EC: 3.3.2.10
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G5EDL5 | MGFFADLFKVVYSTWRQYIYTTGALLTLTWKWFTEGNEYFVEHVYPEPECLKNWNHKFVQLKNIRMHYVEEGPADGDVLLMVHGFPEFWYSWRFQLEHFKHTHRCIAIDMRGYNTTDRPSGISDYNLTHLVEDIRQFIEILELKRVTLAAHDWGAIVCWRVAMLHSNLIDRLVICNVPHPFAFFEVYNMSKEQRNKSWYIYLFQSQYIPEIAMRSNKMKMLEAMFRGSKAGIRNSENFTDEDMLAWKHVFSQPGGTTGPLNYYRDLFNAPAIPRKLQIVQPKVLILWGDEDAFLDKKGAELSVQFCRDCRVQMIRGASHWVQQDQPQLVNVYMEQFMNEDSYRPIGEIKTFKSHL | Function: Catalyzes the hydrolysis of epoxide-containing fatty acids. Active in vitro against trans-1,3-diphenylpropene oxide (t-DPPO), epoxyeicosatrienoic acids (EETs) including 8,9-EET, 11,12-EET and 14,15-EET and the linoleic acid metabolites 12,13-epoxy-9-octadecenoate (12,13-EpOME) and 9,10-epoxy-12-octadecenoate (9,10-EpOME).
Catalytic Activity: an epoxide + H2O = an ethanediol
Sequence Mass (Da): 42116
Sequence Length: 355
Pathway: Lipid metabolism.
EC: 3.3.2.10
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Q5LH66 | MDEILKQEMQKELTTRILPYWMERMVDQENGGFYGRITGQEELMPRADKGAILNARILWTYSAAYRLLGREEYKEMANRAKRYLIDHFYDSEFGGVYWSLNYRGEPLDTKKQIYAIGFAIYGLSEFHRATGDPEALMYAVRLFNDIESHSFDGLKNGYCEALTREWNEIADMRLSEKDANERKTMNTHLHILEPYTNLYRVWKDARLERQLYNLIGLFTEKILDKDTSHLQLFFDNDWQSKYPVVSYGHDIEASWLLHEAARVLGDAGLIAEIEPVVKKIAAAASEGLTSDGGMIYEKNLTTGHIDGDYHWWVQAETVVGYYNLFRYFGDRGALQHSIDCWEFIKRHLTDDVHGEWFWSLRADGSLNRDDDKAGFWKCPYHNGRMCIELLGE | Function: Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize cellotriose to Glc-Glc-Man, cellotetraose to Glc-Glc-Glc-Man, lactose to epilactose, and mannobiose to 4-O-beta-D-mannopyranosyl-D-glucopyranose (Man-Glc). May function as a mannobiose 2-epimerase in vivo and be involved in a mannan catabolic pathway which feeds into glycolysis.
Catalytic Activity: D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose
Sequence Mass (Da): 45778
Sequence Length: 392
EC: 5.1.3.11
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B8DZK4 | MDLKVLKSEIFEHLNNKIIPFWEELKDENNGGYISYVGFDLKPDPYAPKGLVLTSRILWFFSRLYNQLRKEEFINFADHSYKFLIKSFLDKENKGFYWMVDYKGEPIDKRKHLYGQAFVLYGLSEYYKATQKKESLDLALEIYKIIEEVCKNDVGYKEEFDEKWNPKENIIVSEYGIICERSMNTLLHILEAYTNLFTATYDQSIKKKIEDLIILFKEKIYDSKTNHLYVFFDKKMNPIIDAISYGHDIEATWLIDEALRYIDNNKLIKEMSEINLKIAEKVLEEAFESGSLLNERVRGIVDKNRIWWVQAEALVGFLNAYQKSKLDKFLKAVFELWEFIKDFLVDKRAQGEWFWKLDENYIPSPMPEVDLWKCPYHNGRMCLEVIKRI | Function: Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). Catalyzes epimerization but also isomerization for beta-1,4- and alpha-1,4-gluco-oligosaccharides. Can use cellobiose, lactose, cellotriose, maltose and maltotriose.
Catalytic Activity: D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose
Sequence Mass (Da): 46393
Sequence Length: 389
EC: 5.1.3.11
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B3XZI5 | MKNEVVYKQLTEKILPFWNAMRDDENGGFYGYMSEDLHIDDHADKGCILNSRILWFYSTAYMYLQDEKLLDNAKHAFEFLKTYCFDPMCGGIFWSVRYNGKPADTTKHTYNQAFAIYALSAYYEATGSIEAIAIAEIIYEKIEDTMRDTKGYLEAFTRDFRPADNDKLSENGVMAERTMNTLLHIIEAYSALVHALRKKVADPAKGDVRDELFMNVVENKLAAALELMRDKFYNSDRHRLDVFFDKEYESLIDLTSYGHDIEASWLLEWAAGILDDEEITESLHPISSDLVEKVYKEAFDGHSIVNECEDGDVNTDRIWWVEAESVLGFLKAFEREGKEEYRKAAHEILAFILDKQVDKREGSEWFEMLKEDGTPCHKPMVREWKCPYHNGRMCLEILKSGIEIG | Function: Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize lactose to epilactose.
Catalytic Activity: D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose
Sequence Mass (Da): 46964
Sequence Length: 405
EC: 5.1.3.11
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P30122 | LGASRLGPSPGCLAVASAAKLGSVYTEGGFVEGVNKKLSLFGDSIDIFKGIPFAAAPKALEKPERHPGWQGTLKAKSFKKRCLQATLTQDSTYGNEDCLYLNIWVPQGRKEVSHDLPVMIWIYGGAFLMGASQGANFLSNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDSNLPGNYGLWDQHMAIAWVKRNIEAFGGDPDNITLFGESAGGASVSLQTLSPYNKGLIKRAISQSGVGLCPWAIQQDPLFWAKRIAEKVGCPVDDTSKMAGCLKITDPRALTLAYKLPLGSTEYPKLHYLSFVPVIDGDFIPDDPVNLYANAADVDYIAGTNDMDGHLFVGMDVPAINSNKQDVTEEDFYKLVSGLTVTKGLRGANATYEVYTEPWAQDSSQETRKKTMVDLETDILFLIPTKIAVAQHKSHAKSANTYTYLFSQPSRMPIYPKWMGADHADDLQYVFGKPFATPLGYRAQDRTVSKAMIAYWTNFARTGDPNTGHSTVPANWDPYTLEDDNYLEINKQMDSNSMKLHLRTNYLQFWTQTYQALPTVTSAGASLLPPEDNSQASPVPPADNSGAPTEPSAGDSEVAQMPVVIGF | Function: Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFA) . Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity). Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (By similarity).
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 65162
Sequence Length: 597
Subcellular Location: Secreted
EC: 3.1.1.13
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P19835 | MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF | Function: Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFAs) . Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity). Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins .
PTM: N- and O-glycosylated.
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 79322
Sequence Length: 753
Subcellular Location: Secreted
EC: 3.1.1.13
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P07882 | MGRLEVLFLGLTCCLAAACAAKLGAVYTEGGFVEGVNKKLSLLGGDSVDIFKGIPFATAKTLENPQRHPGWQGTLKATDFKKRCLQATITQDDTYGQEDCLYLNIWVPQGRKQVSHDLPVMVWIYGGAFLMGSGQGANFLKNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNFGLRDQHMAIAWVKRNIAAFGGDPDNITIFGESAGAASVSLQTLSPYNKGLIRRAISQSGVALSPWAIQENPLFWAKTIAKKVGCPTEDTAKMAGCLKITDPRALTLAYRLPLKSQEYPIVHYLAFIPVVDGDFIPDDPINLYDNAADIDYLAGINDMDGHLFATVDVPAIDKAKQDVTEEDFYRLVSGHTVAKGLKGTQATFDIYTESWAQDPSQENMKKTVVAFETDILFLIPTEMALAQHRAHAKSAKTYSYLFSHPSRMPIYPKWMGADHADDLQYVFGKPFATPLGYRAQDRTVSKAMIAYWTNFAKSGDPNMGNSPVPTHWYPYTTENGNYLDINKKITSTSMKEHLREKFLKFWAVTFEMLPTVVGDHTPPEDDSEAAPVPPTDDSQGGPVPPTDDSQTTPVPPTDNSQAGDSVEAQMPGPIGF | Function: Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFA) . Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity). Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (By similarity).
Catalytic Activity: a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+)
Sequence Mass (Da): 67040
Sequence Length: 612
Subcellular Location: Secreted
EC: 3.1.1.13
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P39525 | MSRRVVITGLGCVTPLGRSLSESWGNLLSSKNGLTPITSLPNYNEDYKLREKSIPSTITVGKIPENFQNENSAINKLLFTSQDERRTSSFIKLALRTTYEALHNAGLLNPNDITINTSLCNLDHFGCLIGSGIGSIQDIYQTSLQFHNDNKRINPYFVPKILTNMAAGNVSIKFNLRGLSHSVSTACATGNNSIGDAFNFIRLGMQDICVAGASETSLHPLSLAGFIRAKSITTNGISRPFDTQRSGFVLGEGCGMIVMESLEHAQKRNANIISELVGYGLSSDACHITSPPADGNGAKRAIEMALKMARLEPTDVDYVNAHATSTLLGDKAECLAVASALLPGRSKSKPLYISSNKGAIGHLLGAAGAVESIFTICSLKDDKMPHTLNLDNVLTLENNEADKLHFIRDKPIVGANPKYALCNSFGFGGVNTSLLFKKWEGS | Function: Possibly involved in the synthesis of a specialized molecule, probably related to a fatty acid, which is essential for mitochondrial respiration. Is essential for oxygen uptake and the presence of cytochromes A and B.
Catalytic Activity: a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]
Sequence Mass (Da): 47555
Sequence Length: 442
Subcellular Location: Mitochondrion
EC: 2.3.1.41
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Q85FL0 | MAAGNSSWARAAFTFKATVFKKSRYVIYYSLLEHRFSLSLWGILKYSGIYFCTEILRSFPKKRCKSHPYRVDGYPAGSCLDPPLHEPLDTSTPKKISLVSCSNSYMRNKTDNGKVGSRNVSEYKLEGDFASTSKSIYYKLNNLEKMNRKLAWIEAVSSEFSFWEKLRSKQIFPFQNEKDLIAEPFNYELAVSHRRPVIYESISLVPRSVTRTLSRFKAELTNQSNLNLSVHNKFDLAKNQASVSLQYVGFLLFLFPIQIAIENWFLEPRIRGWWNIRQIQLFSNVFQEENALKQLREAEALFWLDDVIGNLADTQLQNFDTDARNETTRLAMMYDELNIQLLLRLATNAISIATLFPLLIFGRKRLAVLNSWIQELFYSLNDTMKAFSILLLTDLCVGFHSPHGWEILVQSLFEYFGLTPNKYVTPCFVSTFPVILDTLFKYWIFRHLNRTSPSIVATYHTMSE | Function: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53857
Sequence Length: 464
Subcellular Location: Plastid
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Q53EZ4 | MSSRSTKDLIKSKWGSKPSNSKSETTLEKLKGEIAHLKTSVDEITSGKGKLTDKERHRLLEKIRVLEAEKEKNAYQLTEKDKEIQRLRDQLKARYSTTTLLEQLEETTREGERREQVLKALSEEKDVLKQQLSAATSRIAELESKTNTLRLSQTVAPNCFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAHSLPQQTKKPESEGYLQEEKQKCYNDLLASAKKDLEVERQTITQLSFELSEFRRKYEETQKEVHNLNQLLYSQRRADVQHLEDDRHKTEKIQKLREENDIARGKLEEEKKRSEELLSQVQFLYTSLLKQQEEQTRVALLEQQMQACTLDFENEKLDRQHVQHQLHVILKELRKARNQITQLESLKQLHEFAITEPLVTFQGETENREKVAASPKSPTAALNESLVECPKCNIQYPATEHRDLLVHVEYCSK | Function: Plays a role in mitotic exit and cytokinesis . Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis . Not required for microtubule nucleation . Plays a role in the development of the brain and kidney .
PTM: There is a hierachy of phosphorylation, where both Ser-425 and Ser-428 are phosphorylated at the onset of mitosis, prior to Ser-436. Phosphorylation at Ser-425 and Ser-428 is required for dissociation from the centrosome at the G2/M boundary. Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is required for protein function at the final stages of cell division to complete cytokinesis successfully.
Sequence Mass (Da): 54178
Sequence Length: 464
Subcellular Location: Cytoplasm
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Q865V0 | MAAASVSETSASQFSNILAEPSKSNGSMVRHSSSPYVVYPPDKPFLNSDLRRSPNKPTFAYPESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSKETIEYKKVLDEQIPERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQNQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLRQEEQERKRMQAKAAQLQTGLEVNRLIYEDKATSCVPNTKRIKKKKSKPPEKKGSRNYFAVQPHYRLCLGDMPFVAGKSTSPSHAVVANVQHVLHLMKQHSKVLCNDRVVSSIPLAKQVSSRTGKSKKSATPPSSSSVNEELSEVLQTLQDEFGQMSFDHQQLAKLIQESPTVELKDNLECELEALVGRMEAKANQITKVRKYQAQLEKQKLEKQKKELKATRKTLDEEGNSSSRSTTTGTTNKKDFAKPRPGEKSRKNLQLLKDMQSIQNSLQSNSLCWDY | Function: Centrosomal protein which may be required for microtubule attachment to centrosomes. May act by forming ring-like structures around microtubules. Mediates nuclear translocation and mitogenic activity of the internalized growth factor FGF2 (By similarity).
Sequence Mass (Da): 56986
Sequence Length: 499
Domain: The C-terminal region mediates the interaction with microtubules and is able to nucleate and bundles microtubules in vitro.
Subcellular Location: Nucleus
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Q86XR8 | MAAASVSAASGSHLSNSFAEPSRSNGSMVRHSSSPYVVYPSDKPFLNSDLRRSPSKPTLAYPESNSRAIFSALKNLQDKIRRLELERIQAEESVKTLSRETIEYKKVLDEQIQERENSKNEESKHNQELTSQLLAAENKCNLLEKQLEYMRNMIKHAEMERTSVLEKQVSLERERQHDQTHVQSQLEKLDLLEQEYNKLTTMQALAEKKMQELEAKLHEEEQERKRMQAKAAELQTGLETNRLIFEDKATPCVPNARRIKKKKSKPPEKKSSRNYFGAQPHYRLCLGDMPFVAGKSTSPSHAVVANVQLVLHLMKQHSKALCNDRVINSIPLAKQVSSRGGKSKKLSVTPPSSNGINEELSEVLQTLQDEFGQMSFDHQQLAKLIQESPTVELKDKLECELEALVGRMEAKANQITKVRKYQAQLEKQKLEKQKKELKATKKTLDEERNSSSRSGITGTTNKKDFMKLRPGEKRRKNLQLLKDMQSIQNSLQSSSLCWDY | Function: Centrosomal protein which may be required for microtubule attachment to centrosomes. May act by forming ring-like structures around microtubules. Mediates nuclear translocation and mitogenic activity of the internalized growth factor FGF2, but that of FGF1.
Sequence Mass (Da): 57089
Sequence Length: 500
Domain: The C-terminal region mediates the interaction with microtubules and is able to nucleate and bundles microtubules in vitro.
Subcellular Location: Nucleus
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Q96MT8 | MEALLEGIQNRGHGGGFLTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQELKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKKQMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGTSMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKATNTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESVSATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHLTQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMVMKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQNDRIFKPTHSRTTEFKNTEFKPTHGQHRHDGIKTEHYKTDLHSPRGQASDSINPMSRVLSPLSPQISPCSSTRSLTSYSLCKTHSLPSALDTNEANFSDTMSESMNDQEEFISSCSLPVSPLGSIATRFLEEEELRSHHILERLDAHIEELKRESEKTVRQFTALK | Function: Required for normal spindle assembly . Plays a key role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication . Reported to be required for centrosomal recruitment of CEP152; however, this function has been questioned . Also recruits CDK1 to centrosomes . Plays a role in DNA damage response . Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression . Promotes stabilization of FXR1 protein by inhibiting FXR1 ubiquitination .
PTM: Polyubiquitinated via 'Lys-48'-linked ubiquitin, leading to its degradation . Deubiquitinated by USP36, promoting its stabilization .
Sequence Mass (Da): 81344
Sequence Length: 703
Subcellular Location: Cytoplasm
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Q4KLY0 | MEALLEGIQTRGHSGGFLTSCEAELQELMKQIDIMVAHKKSEWEGQTHALETCLDMRDRELKALRSQLDMKHKEVGILHQQIEEQEKTKQEMALEYKEELMKLQEELSRLKRSYEKLQKKQLREFRGNTKSLREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQSEIIQAQLANRKQKLESVELSSQSEIQHLSSKLERAKDTICANELEIERLNIRVKDLMGTNVTILQEQRQKEEKLRESEKLLEALQEEQKELKASLQAQESFILDAKMQEKLQTKLKAVDTKHSVERSLEDCQVERKYSSSGQGVLDNVLSQLDISHSSEELLQAEVTRLEGSLESVSTTCKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKTEISQLTRELHQRDITIASAKCSSSDMERQLKAEMQKAEEKAVEHKEILSQLESLRLENRRLSETVMKLELGLHECSMPVSPLGLIATRFLEEEELRSHHILERLDAHIEELKRESEKTVRQFTALV | Function: Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication. Reported to be required for centrosomal recruitment of CEP152; however, this function has been questioned. Also recruits CDK1 to centrosomes. Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression. Promotes stabilization of FXR1 protein by inhibiting FXR1 ubiquitination.
PTM: Polyubiquitinated via 'Lys-48'-linked ubiquitin, leading to its degradation. Deubiquitinated by USP36, promoting its stabilization.
Sequence Mass (Da): 62680
Sequence Length: 538
Subcellular Location: Cytoplasm
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Q76N32 | MALGEEKAEAEASEDTKAQSYGRGSCRERELDIPGPMSGEQPPRLEAEGGLISPVWGAEGIPAPTCWIGTDPGGPSRAHQPQASDANREPVAERSEPALSGLPPATMGSGDLLLSGESQVEKTKLSSSEEFPQTLSLPRTTTICSGHDADTEDDPSLADLPQALDLSQQPHSSGLSCLSQWKSVLSPGSAAQPSSCSISASSTGSSLQGHQERAEPRGGSLAKVSSSLEPVVPQEPSSVVGLGPRPQWSPQPVFSGGDASGLGRRRLSFQAEYWACVLPDSLPPSPDRHSPLWNPNKEYEDLLDYTYPLRPGPQLPKHLDSRVPADPVLQDSGVDLDSFSVSPASTLKSPTNVSPNCPPAEATALPFSGPREPSLKQWPSRVPQKQGGMGLASWSQLASTPRAPGSRDARWERREPALRGAKDRLTIGKHLDMGSPQLRTRDRGWPSPRPEREKRTSQSARRPTCTESRWKSEEEVESDDEYLALPARLTQVSSLVSYLGSISTLVTLPTGDIKGQSPLEVSDSDGPASFPSSSSQSQLPPGAALQGSGDPEGQNPCFLRSFVRAHDSAGEGSLGSSQALGVSSGLLKTRPSLPARLDRWPFSDPDVEGQLPRKGGEQGKESLVQCVKTFCCQLEELICWLYNVADVTDHGTAARSNLTSLKSSLQLYRQFKKDIDEHQSLTESVLQKGEILLQCLLENTPVLEDVLGRIAKQSGELESHADRLYDSILASLDMLAGCTLIPDKKPMAAMEHPCEGV | Function: Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting . Required for localization of CDK5RAP2 to the centrosome during interphase . Contributes to CROCC/rootletin filament formation .
PTM: Phosphorylation by PLK1 is required for binding to BTRC in prometaphase . Phosphorylated directly or indirectly by NEK2 . NEK2-mediated phosphorylation promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis .
Sequence Mass (Da): 81102
Sequence Length: 757
Subcellular Location: Cytoplasm
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Q8NHQ1 | MFPVAPKPQDSSQPSDRLMTEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDLIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLSRACHQQNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETRPTQHELRLYKQQVKKLEKALKKNVKLQELINHKKAEDTEKKDEPSKYNQQQALIDQRYFQVLCSINSIIHNPRAPVIIYKQTKGGVQNFNKDLVQDCGFEHLVPVIEMWADQLTSLKDLYKSLKTLSAELVPWLNLKKQDENEGIKVEDLLFIVDTMLEEVENKEKDSNMPHFQTLQAIVSHFQKLFDVPSLNGVYPRMNEVYTRLGEMNNAVRNLQELLELDSSSSLCVLVSTVGKLCRLINEDVNEQVMQVLGPEDLQSIIYKLEEHEEFFPAFQAFTNDLLEILEIDDLDAIVPAVKKLKVLSY | Function: Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle.
Sequence Mass (Da): 69752
Sequence Length: 597
Domain: The coiled-coil domains may be important for tubulin-gamma-binding and hence for centrosomal localization.
Subcellular Location: Cytoplasm
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Q9UEE9 | MEEFDSEDFSTSEEDEDYVPSGGEYSEDDVNELVKEDEVDGEEQTQKTQGKKRKAQSIPARKRRQGGLSLEEEEEEDANSESEGSSSEEEDDAAEQEKGIGSEDARKKKEDELWASFLNDVGPKSKVPPSTQVKKGEETEETSSSKLLVKAEELEKPKETEKVKITKVFDFAGEEVRVTKEVDATSKEAKSFFKQNEKEKPQANVPSALPSLPAGSGLKRSSGMSSLLGKIGAKKQKMSTLEKSKLDWESFKEEEGIGEELAIHNRGKEGYIERKAFLDRVDHRQFEIERDLRLSKMKP | Function: May play a role during embryogenesis.
PTM: Phosphorylated by CK2 (casein kinase II) in vitro.
Sequence Mass (Da): 33593
Sequence Length: 299
Subcellular Location: Chromosome
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Q27082 | MLVLLCCVVLHVGVARICCSHEPKWQLVWSDEFTNGISSDWEFEMGNGLNGWGNNELQYYRRENAQVEGGKLVITAKREDYDGFKYTSARLKTQFDKSWKYGKIEAKMAIPSFRGVWVMFWMSGDNTNYVRWPSSGEIDFIEHRNTNNEKVRGTIHWSTPDGAHAHHNRESNTNGIDYHIYSVEWNSSIVKWFVNGNQYFEVKIQGGVNGKSAFRNKVFVILNMAIGGNWPGFDVADEAFPAKMYIDYVRVYQDASTSSPVGDTSLDGYYFVQNRHSELYLDVTDASNEDGAFLQQWSYSGNENQQFDFEHLENNVYKITNKKSGKSLDVYNFGTENGVRIQQWSYGGARNQQFTVQSVGDGYYKIIPRGSGKLVEVADFSKDAGGKIQQWSDNNQLSGQWKLIKSKSYSKLIQAESYFDSSKVQLEDTSDVGGGKNVKCDNEGAWMAYKDIDFPSSGNYRIEYRVASERAGGKLSLDLNAGSIVLGMLDVPSTGGWQKWTTISHTVNVDSGTYNLGIYVQRASWNINWIKITKIPEQSNLNQGRRNSKLIQAESYFSYSEVQLEDTLDVGGGKNVKCDKEGAWMAYKDIDFPSSGSYRVEYRVASERAGGKLSLDLNAGSIVLGMLDIPSTGGLQKWTTISHIVNVDLGTYNLGIYVQKASWNINWIRITKV | Function: Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme .
PTM: In presence of (1->3)-beta-glucan, proteolytically cleaved into a 55kDa and a 17kDa forms.
Sequence Mass (Da): 75952
Sequence Length: 673
EC: 3.2.1.-
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Q27083 | MDISFLVFITLSMALFSSNVTGTSVTSRVRRGINEKHCGFRPVITRIIGGGIATPHSWPWMVGIFKVNPHRFLCGGSIINKVSVVTAAHCLVTQFGNRQNYSIFVRVGAHDIDNSGTNYQVDKVIVHQGYKHHSHYYDIGLILLSKPVEYNDKIQPVCIPEFNKPHVNLNNIKVVITGWGVTGKATEKRNVLRELELPVVTNEQCNKSYQTLPFSKLNRGITNDMICAGFPEGGKDACQGDSGGPLMYQNPTTGRVKIVGVVSFGFECARPNFPGVYTRLSSYVNWLQEITFGQSLASLFEVVPIFIPE | Function: Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme .
Catalytic Activity: Selective cleavage of 98-Arg-|-Ile-99 bond in Limulus proclotting enzyme to form active clotting enzyme.
Sequence Mass (Da): 34265
Sequence Length: 309
EC: 3.4.21.85
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P41088 | MSSSNACASPSPFPAVTKLHVDSVTFVPSVKSPASSNPLFLGGAGVRGLDIQGKFVIFTVIGVYLEGNAVPSLSVKWKGKTTEELTESIPFFREIVTGAFEKFIKVTMKLPLTGQQYSEKVTENCVAIWKQLGLYTDCEAKAVEKFLEIFKEETFPPGSSILFALSPTGSLTVAFSKDDSIPETGIAVIENKLLAEAVLESIIGKNGVSPGTRLSVAERLSQLMMKNKDEKEVSDHSVEEKLAKEN | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 26596
Sequence Length: 246
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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P28012 | MAASITAITVENLEYPAVVTSPVTGKSYFLGGAGERGLTIEGNFIKFTAIGVYLEDIAVASLAAKWKGKSSEELLETLDFYRDIISGPFEKLIRGSKIRELSGPEYSRKVMENCVAHLKSVGTYGDAEAEAMQKFAEAFKPVNFPPGASVFYRQSPDGILGLSFSPDTSIPEKEAALIENKAVSSAVLETMIGEHAVSPDLKRCLAARLPALLNEGAFKIGN | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 23826
Sequence Length: 222
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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P11650 | MSPPVSVTKMQVENYAFAPTVNPAGSTNTLFLAGAGHRGLEIEGKFVKFTAIGVYLEESAIPFLAEKWKGKTPQELTDSVEFFRDVVTGPFEKFTRVTMILPLTGKQYSEKVAENCVAHWKGIGTYTDDEGRAIEKFLDVFRSETFPPGASIMFTQSPLGLLTISFAKDDSVTGTANAVIENKQLSEAVLESIIGKHGVSPAAKCSVAERVAELLKKSYAEEASVFGKPETEKSTIPVIGV | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 26089
Sequence Length: 241
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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O81980 | YTGIGVYLEDKAVPSLAAKWKGKTSEELVHTLHFYRDIISGPFEKLIRGSKILPLAGAEYSKKVMENCVAHMKSVGTYGDAEAAAIEKFAEAFKNVNFAPGPLFLYRQSPDGILGLSFSEDVTIPEKEAAVIENKAVSAAVLETMIGEHAVSPDLKRILASRLLRIEHGIIV | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin (By similarity).
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 18744
Sequence Length: 172
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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O82279 | MAILSYISATSTTPPIPQDQSPNSRLPTKIILPNKKPEKWSTGVAPGEYGGPPTTTKLRKYWGGEKEDPITSTDLIWNRDFMDQMKKLFDDPNDSSLDPSPSKEKSSGFLSFSRVMSLDSMDVDLSKELASSSKSVVKNRLDTSKSEAKKQMSKAIVSPKWKLAPTRREQEKWDRATKAATGGSDVMFRELRRPRGDPEVQAAKDREQYFKLKNKIQVLTLGIGGVGLVSAYISYTPEIALSFGAGLLGSLAYMRMLGNSVDAMADGARGVAKGAANQPRLLVPVVLVMIFNRWNAILVPEYGFMHLELIPMLVGFFTYKIATFFQAIEEAISITTQKPESISPDTQASD | Function: Facilitates the assembly of the membrane proton channel of the chloroplastic F-type ATPase. Specifically required for the efficient assembly and integration of the CF(0) subunit c into the chloroplastic ATPase complex in the thylakoid membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38610
Sequence Length: 350
Subcellular Location: Plastid
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Q9M2Y6 | MARRQVGSTRRVGDGGSFPFAGALHSKSRSSPLLSICLVLVGACLLIGYAYSGPGIFKSIKEVSKVTGDYSCTAEVQRAIPVLKKAYGDGMRKVLHVGPDTCSVVSSLLKEEETEAWGVEPYDIEDADSHCKSFVSKGLVRVADIKFPLPYRAKSFSLVIVSDALDYLSPKYLNKTVPELARVASDGVVLFAGLPGQQRAKVAELSKFGRPAKMRSASWWNRFFVQTNLEENDAPSKKFEQAVSKGLYKPACQVFHLKPLH | Function: Together with CGR3, required for homogalacturonan pectins (HG) methylesterification in the Golgi apparatus prior to integration into cell walls, essential for general growth and development . Promotes rosette growth . Impacts carbon (C) partitioning, photosynthesis and respiration efficiency by influencing leaf mesophyll cell walls morphology and physiology; pectin methylesterification modulates both expansion and positioning of cells in leaves, probably by changing cell walls plasticity .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28532
Sequence Length: 261
Subcellular Location: Golgi apparatus membrane
EC: 2.1.1.-
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C8WLM1 | MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAELCMQQAVCMNDSIYVGGISDWGMSEILGKDVNIHDSSNIDAILVDKTGRRFCQDDAEWGYVMHECAQAAWKQGFTPDDPTTGYIFYVYDATGAPFFEMKGHTPDTCDTTFSADSVDGLAEFIGCDPTALASEVERWNSFCEAGLDADFGRRANMAPIATPPFYCDVVRPGPMGTFAGAKSNVEAEIIGLDGNPIPRLYGAGCIIGGNVSGAFYFGCGWSITNTVVWGREAGRNVAALEPWE | Function: Involved in the inactivation of the cardiac medication and plant natural product digoxin, thus decreasing drug efficacy and toxicity. Catalyzes the reduction of the alpha,beta-unsaturated butyrolactone ring of digoxin to the inactive metabolite dihydrodigoxin. Likely uses the cytochrome Cgr1 as the physiological electron donor, encoded by the adjacent gene in the locus. Only reduces digoxin and other cardenolide toxins, such as digitoxin, digoxigenin, ouabain and ouabagenin. Therefore is a specialized enzyme present in some gut bacteria E.lenta that protects their human host against ingested plant toxins.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Peripheral membrane protein
Catalytic Activity: digoxin + 2 Fe(II)-[cytochrome c] + 3 H(+) = dihydrodigoxin + 2 Fe(III)-[cytochrome c]
Sequence Mass (Da): 59161
Sequence Length: 560
Subcellular Location: Cell membrane
EC: 1.3.2.-
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Q99674 | MLPLTMTVLILLLLPTGQAAPKDGVTRPDSEVQHQLLPNPFQPGQEQLGLLQSYLKGLGRTEVQLEHLSREQVLLYLFALHDYDQSGQLDGLELLSMLTAALAPGAANSPTTNPVILIVDKVLETQDLNGDGLMTPAELINFPGVALRHVEPGEPLAPSPQEPQAVGRQSLLAKSPLRQETQEAPGPREEAKGQVEARRESLDPVQEPGGQAEADGDVPGPRGEAEGQAEAKGDAPGPRGEAGGQAEAEGDAPGPRGEAGGQAEAEGDAPGPRGEAGGQAEARENGEEAKELPGETLESKNTQNDFEVHIVQVENDEI | Function: Mediates cell-cell adhesion in a calcium-dependent manner (By similarity). Able to inhibit growth in several cell lines.
PTM: Probably digested extracellularly by an unknown serine protease generating extremely hydrophobic bioactive peptides.
Sequence Mass (Da): 33456
Sequence Length: 318
Domain: Both EF-hands are required for function.
Subcellular Location: Secreted
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P97586 | MSRWLMQMLMLPLLLLPLGQAAPKDGVARLDPEAQQQLTTNPFQPGPEQLRRLRDYLKGLEKMEEDPEQMNREQVLLYLFALHDFDQNGQLDGLELLSMLTAALAPGAAHFPINPVILVVDMVLETQDLDGDGLMTPAELINFPGEAPKRAESLPPALQEPQPAGSQPLLANSPLQSETQQSLGTKEEITSQVEAKRALEPEQEAGHHIETKVDALSPEGEARGQAESEGDAPGPREDAERQVESKDNEGEAKDLPAETLETQNTPNVVEAHSIQLENDEI | Function: Mediates cell-cell adhesion in a calcium-dependent manner. Able to inhibit growth in several cell lines.
PTM: Probably digested extracellularly by an unknown serine protease generating extremely hydrophobic bioactive peptides.
Sequence Mass (Da): 30835
Sequence Length: 281
Domain: Both EF-hands are required for function.
Subcellular Location: Secreted
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P55217 | MAVSSFQCPTIFSSSSISGFQCRSDPDLVGSPVGGSSRRRVHASAGISSSFTGDAGLSSRILRFPPNFVRQLSIKARRNCSNIGVAQIVAAKWSNNPSSALPSAAAAAATSSASAVSSAASAAAASSAAAAPVAAAPPVVLKSVDEEVVVAEEGIREKIGSVQLTDSKHSFLSSDGSLTVHAGERLGRGIVTDAITTPVVNTSAYFFKKTAELIDFKEKRSVSFEYGRYGNPTTVVLEDKISALEGAESTLVMASGMCASTVMLLALVPAGGHIVTTTDCYRKTRIFMENFLPKLGITVTVIDPADIAGLEAAVNEFKVSLFFTESPTNPFLRCVDIELVSKICHKRGTLVCIDGTFATPLNQKALALGADLVVHSATKYIGGHNDVLAGCICGSLKLVSEIRNLHHVLGGTLNPNAAYLIIRGMKTLHLRVQQQNSTAFRMAEILEAHPKVSHVYYPGLPSHPEHELAKRQMTGFGGVVSFEIDGDIETTIKFVDSLKIPYIAPSFGGCESIVDQPAIMSYWDLPQEERLKYGIKDNLVRFSFGVEDFEDVKADILQALEAI | Cofactor: Binds 1 pyridoxal 5'-phosphate per subunit.
Function: Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction. Substrate preference for cystathionine synthesis is O-phospho-L-homoserine (OPH) > O(4)-succinyl-L-homoserine (OSH) >> O-acetyl-L-homoserine (OAH). Is able, at extremely low rate, to catalyze a gamma-elimination of OPH in the absence of cysteine to produce inorganic phosphate (Pi), 2-oxobutanoate and ammonia.
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate
Sequence Mass (Da): 59919
Sequence Length: 563
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
Subcellular Location: Plastid
EC: 2.5.1.48
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Q9C876 | MQILKENASNQRFVTRESEVNRICCGFNGFQLGERLRRDMKTSSITTLVVNTTTYFFKDTTELIDFKEKRIDLYEYARYGNPTTMALEEKISVLEGAESTLVMASGMYASNVMLLALVPTNGHIVATKDCYKETRIFMENFLTKLGITVTFIDSDDIAGLQTLVNNHEVSLFFTESPTNPFLRCVDIKLVSKICHRRGTLVCIDATIATPINQKTLALGADLVHHSATKYIGGHNDFLAGSISGSMELVSKIRNLHKLLGGTLNPNAAYLLIRGMKTMHLRVRQQNSTGMKMAQVLEAHPKVSRVYYLGLPSHPEHLIAKRQMTGIGGLISFEIDGDLKTTIKFIDALKIPYLAASFGGCESLVDQLATGIWDIPREERLKDGFQDNLVRFSFGIEDFEDIKADVLQALETI | Cofactor: Binds 1 pyridoxal 5'-phosphate per subunit.
Function: Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate
Sequence Mass (Da): 46004
Sequence Length: 412
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
EC: 2.5.1.48
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A0A077K8G3 | MLQMHSNSSFSPKCYYPLQHAGCVKTLQLPLTKVHGGLNRSESKNYAIKCTQSDSFYSTNKIRNNENSSSRNCKPFNKYRVAVTLQQQDCASNNEDDINSTSFRDVLLKKLHALYVFTRPFAMIGTIVGITSIAILPLQSFADLTPKYFMEFLKALLSAVLMNNYVGTVNQVADVEIDKVNKPGLPLASGDLSVGTGLAITLILSLTSLAIALSLQSPPLIFGLIVWFLLGTAYSVDLPFLRWKTNPFLAGMCMVIVFGLVYQFSFFIHFQKYVLGRPVVITRPLIFAAAIISTISAVMSLLKDIPDEDGDKQFGYQSISSKLGKENVLRLCVYALFFAYGVAVIVGASSSFQLGKLVSIIGHSTLAFLLWLRAQTVDLSNNASTFSFYLFVWKLFYGEYLLIHFLR | Function: Prenyltransferase specific for geranyl diphosphate as prenyl donor and coumarin as prenyl acceptor. Can use umbelliferone and esculetin as substrates, and with a lower activity, 5,7-dihydroxy-coumarin and 5-methoxy-7-hydroxycoumarin. No activity with 5-hydroxy-7-methoxycoumarin, bergaptol, xanthotoxol, p-coumaric acid, caffeic acid, 2,4-dihydroxycinnamic acid, kaempferol, genistein or homogentisate. No activity with dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl diphosphate as prenyl donors.
Catalytic Activity: (2E)-geranyl diphosphate + umbelliferone = 8-geranylumbelliferone + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45250
Sequence Length: 407
Subcellular Location: Plastid
EC: 2.5.1.138
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Q05972 | MAKSIIYNDEARRALERGMDILAEAVAVTLGPKGRNVVLEKKFGSPQIINDGITIAKEIELEDHVENTGVSLIRQAASKTNDVAGDGTTTATVLAHAIVKEGLRNVAAGANPISLKRGIDKATDFLVARIKEHAQPVGDSKAIAQVGAISAGNDEEVGQMIANAMDKVGQEGVISLEEGKSMTTELEITEGMRFDKGYISPYFVTDAERMEAVLEDPRILITDKKINLVQDLVPILEQVARQGKPLLIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKQMLEDIATLTGGQVISEDAGLKLESATVDSLGSARRINITKDNTTIVAEGNEAAVKSRCEQIRRQIEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDRKLRLEDAINATKAAVEEGIVPGGGTTLAHLAPQLEDWATGNLKDEELTGALIVARALPAPLKRIAENAGQNGAVISERVKEKEFNVGYNAASLEYVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEKEKAPAGAPGGDFDY | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 57653
Sequence Length: 541
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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Q9KNR7 | MAAKDVRFGNDARVKMLEGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFQNMGAQMVKEVASQANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVIAAVEELKALSVPCADTKAIAQVGTISANSDSSVGNIIAEAMEKVGRDGVITVEEGQALQDELDVVEGMQFDRGYLSPYFINNQESGSVELDNPFILLVDKKISNIRELLPVLEGVAKASRPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAILTGGVVISEEIGLELEKATLEDLGQAKRVSITKENSTIIDGAGDQAAIQGRVAQIRQQIEEATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGVVAGGGVALIRAASKLSSLVGDNEEQNVGIRVALRAMEAPLRQIVKNAGDEESVVANNVRAGEGNYGYNAATGVYGDMIEMGILDPTKVTRSALQFAASVAGLMITTEAMITELPKKDAPAMPDMGMGGMGGMM | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 57153
Sequence Length: 544
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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P81874 | SAKDVKFGDSARSMMIAGVNVIAD | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 2483
Sequence Length: 24
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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Q9KKF0 | MAKEIKFSEETRRALEAGVNKLADTVKVTLGPKGRNVILDKKFGSPLITNDGVTIAKEIELEDRFENMGAQLVKEVATKTNDVAGDGTTTATVLAQAIIREGLKNVTAGANPILLRKGIQKAVTVAVEELKNQSRIVETQEAISQVASISAGDEEVGKLIAEAMEIVGKDGVITVEESQTMNTELDAVEGMQFDRGFVSAYMVTDVDKMEAVLNDPYILITDKKISNIQELLPVLEQIVQQGKKLLIIAEDVEGEALSTLVVNKLRGTFDVVAVKAPGFGDRRKEMLQDIAILTGAQVISEELGYDLKEADLSMLGRASSVKVTKESTTIVDGSGDKKAIEDRVTQIKHQVEQTTSDFDREKLMERLAKLAGGVAVVKVGAATEVELKERKLRIEDALNATRAAVEEGIVAGGGTAFVSVIPAIGTLIESLEGEVKLGAQIVKKALEEPLRQIAINAGLEGAVIVQNVVNSEAETGFDALNEKYVNMIEAGIVDPTKVSRSALQNAASIASTFLTTEAAVADLPEKEDAGMPGTGMDGMY | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 57677
Sequence Length: 540
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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P81339 | AKSILLGEEGRHSMQAGVDKLANTVKVTLG | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 3124
Sequence Length: 30
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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P86206 | ALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKLVQDVANNTNEEAGDGTTTATVLARGANPVEIRRGVMLAVDAVIAELKKTLNDELEIIEGMKFDRGYISPYFINTSKCEFQDAYVLLSEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLNLNLEDVQAHDLGKIQEITEQLDITTSEYEKEKVTDALNATRAAVEEGIVLGGGCALLRIGIEIIKR | Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 29037
Sequence Length: 271
Subcellular Location: Mitochondrion matrix
EC: 5.6.1.7
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P46224 | MRRFSETYGQKKQITFFCSNLSITAVVIEGLLKHKEEYGALERGMDILAEAVSVTLGPKGRNVVLESGKYGPPQIVNDGVTIAKEIELEDHIENTGVALIRQAASKTNDVAGDGTTTATVLAHAMVKQGMKNVRCRSKSIAIKRGIEKATQFVISQIAEYSRPVEDTKSITQVAAISAGNDMEVGQMIADAIEKVGREGVISLEEGKSTVTELELTEGNGWFLKKGFISPYFVTDTDRMETTQENPYILLTDKKISLVQELVPIHLELISKTSRPLLIIAEDVEKEALATLVVNKLRGIVNVVAVRAPGFGDRRKTMLEDIAILTGGQVISEDAGFSLETVQLDMLGQARRITVVKEGTTIIAEGHEREVKARCEQIRRQIEASESSYEREKLQERLAKLAGGVAVIKVGAATETEKDKKLRLEDAINATKAAVEEGIVPGGATLIHFIEDLNDWAEDNLLDDELIGALIVEKALSAPMKRIIENTGISSSIIIEKIKDKDFSIGYNAAQGEIEDMYEIGVIDPAKVTRSAMQNAASIASMILTTECIVVDKKKTCSLETSIYWLVLTNKYFCLDLLRLYFFLKD | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 64243
Sequence Length: 585
Subcellular Location: Plastid
EC: 5.6.1.7
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P34939 | MASKEIKFGRTGREKMLRGVDILADAVKVTLGPKGRNVIIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVREGNKAVAAGMNPMDLKRGIDLAVADVVKDLQAKAKKISTSEEVAQVGTISANGDKQVGLDIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMIADLEDVFILLHEKKLSNLQSMLPVLEAVVQTGKPLLIVAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKRMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAKKVSISKENTTIVDGSGAKTDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRIDDALNATRAAVQEGIVPGGGIALARSSTKITVKGANDDQEAGINIVRRALQSLVRQIAENAGDEASIVVGKVLDKNEDNFGYNAQTSEYGDMIAMGIVDPLKVVRTALQNAASVASLLITTEAMIAELPKKDAPAGMPGGMGGMGGMDMM | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 57884
Sequence Length: 546
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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Q1IQS9 | MRTTPIRVLVVDDSALMRKMITQMLQKDPAIEVIGTAMDGAFGLKKIEELRPDVVTLDLEMPNMDGMEMLRHITKRGQTPVIVVSAHTTQGARETFKALQLGAFDFVAKPQEGSSLTLENVADEIIAKIKVAGAARKPRPQIATVDEALLRSARKPARPPVASRTTPSKIIAIGISTGGPNALLFMLSQLPADFAGTILIVQHMPEGFTQMFSNRLAESCAIEVKEAASGDLLLAGRALICPGNRHMRVRRMPMGDVVVLSDEPPVNGHRPSADVLFRSVAQEFGPKVVALIMTGMGEDGADAIGAVKAAGGLAVAQDEGSSVVFGMPKVAIERGNVNRVVALDALPNLLMVQSAAQRVSSFD | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 38701
Sequence Length: 363
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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P62642 | MNYEAIVIGVSAGGINAMKTILPTLPTQFGIPIVIVQHIGARSDGEWFRILEKLCNIKIKEAEEKEEIKSGMVYVAPPNYHLLIEKDKTFSFSIGERVNFSRPSIDVLFETASEVYEDKLIGVILTGANSDGAQGLKKIKENGGLAVVQDPLTAEIALMPRSAIEATSVDYVLSLEKIAELFIRLDQNNLEQR | Function: May be involved in chemotaxis.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 21292
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q2W5V5 | MRKKIKVLIVEDSLVVRELLKHIIGSDERFEVMAAVTSAEDCLEMLETQQPDVISLDIRLPGMNGLDATLKIMSRRPTPIVVVAAQVDDNELNIAMNALRAGALSVVEKPVGVTNAGYDTMAAKICTQLAIMSQVQVVRQGINRGLNFGSDDTPARVSQGRPGTYSMVGIVASTGGPQALVQLLGGLGADFPLPILLVQHITSSFLEGFVTWLSGTTPFEARIAQDGEKPVAGKVYVAPVDHHLGLVNDQLVILDLPAVCNQKPSGTVLFGSMARDIGKHGIGVVLTGMGADGSEGLRQMADKGAYTIVEDASTCVVNGMPAAAAKLGAARETLPLPAIAARLRDLALGGEK | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 37022
Sequence Length: 352
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Subsets and Splits