ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q9TXJ8 | MATFIFSRGNIFFYVNKITIPDLMSDVLLSKLSTELADLDGEIGQIDQQISQLRRKKSELTQKRQAIERKIELKTNEDSDVVTDRWDRDGFPWSDEATKILKEQFHLEKFRPLQRAAINAVMSKEDAVVILSTGGGKSLCYQLPALLANGLALVVSPLISLVEDQILQLRSLGIDSSSLNANTSKEEAKRVEDAITNKDSKFRLLYVTPEKLAKSKKMMNKLEKSLSVGFLKLIAIDEVHCCSQWGHDFRTDYSFLNVLKRQFKGVPILGLTATATSNVLDDVKDMLGIQAALTFRAGFNRSNLKYKVVQKPGSEDECTEEIAKTIKRDFAGQTGIIYCLSRNDCEKVAKALKSHGIKAKHYHAYMEPVDRSGAHQGWISGKIQVIVATVAFGMGIDKPNVRFVIHHSLPKSIENYYQESGRAGRDGQPATCILYYRLADIFKQSSMVQQERTGIQNLYNMVRYAADSSTCRRVKLAEHFEEAWEPSWCQKQCDTCENGNGFVGTSSKESTDVSEAAKTTVRIIEEHLNSAKDGSGRITGNKLVELLTKKLKGSRNREFCEKLIVNLLLEGYLQEDFHYTVYSVISYVVIGSKWRVYNGKDAIKMRHVEESKSRKRKASSSVEEEDVMVLD | Function: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 71096
Sequence Length: 631
Subcellular Location: Nucleus
EC: 3.6.4.12
|
P46063 | MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEELNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTLPREDLEKIIAHFLIQQYLKEDYSFTAYATISYLKIGPKANLLNNEAHAITMQVTKSTQNSFRAESSQTCHSEQGDKKMEEKNSGNFQKKAANMLQQSGSKNTGAKKRKIDDA | Function: DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 73457
Sequence Length: 649
Subcellular Location: Nucleus
EC: 3.6.4.12
|
Q5HP94 | MNYPNGKPYSKNKPLDGRKSSPFSSNIEYGGRGMTLEKDIEQSNTFYLKSGIAVIHKKPTPVQIVNVHYPKRSKAVINEAYFRTPSTTDYNGVYNGYYIDFEAKETKNKTSFPLNNIHAHQVEHMKNTYHQKGIVFLMIRFKSLDEVYLLPYSKFEKYWQRYINNIKKSITVEEIRKNGYHIPYQYQPRLNYLKAVDKLILDESEDRV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 24507
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 3.1.21.10
|
Q49XQ5 | MNYPNGKPFNRNKSQVGRTHKGQTSKIDYGGRGMSLEKDIELSNDYYLNRGIAVIHKKPTPIQIVNVHYPMRSKAVINEAYFRTPSTTDYNGIYHGRYLDFEAKETKNKTSFPLNNMHEHQVRHMEACYQQQGVVFLLIRFKSLDEVYLLPYANFKKFWERHIQEIKKSVTVEEIRKNGYYIPYQYQPRLNYLKTVDKLILDESEDRV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Sequence Mass (Da): 24678
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 3.1.21.10
|
Q9H6H4 | MVSWMICRLVVLVFGMLCPAYASYKAVKTKNIREYVRWMMYWIVFALFMAAEIVTDIFISWFPFYYEIKMAFVLWLLSPYTKGASLLYRKFVHPSLSRHEKEIDAYIVQAKERSYETVLSFGKRGLNIAASAAVQAATKSQGALAGRLRSFSMQDLRSISDAPAPAYHDPLYLEDQVSHRRPPIGYRAGGLQDSDTEDECWSDTEAVPRAPARPREKPLIRSQSLRVVKRKPPVREGTSRSLKVRTRKKTVPSDVDS | Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29395
Sequence Length: 257
Subcellular Location: Endoplasmic reticulum membrane
|
Q8K072 | MVSWMICRLVVLIFGMLYPAYASYKAVKSKNIREYVRWMMYWIVFAIFMAAETFTDIFISWFPFYYEFKMAFVLWLLSPYTKGASLLYRKFVHPSLSRHEKEIDACIVQAKERSYETMLSFGKRSLNIAASAAVQAATKSQGALAGRLRSFSMQDLRSIPDTPVPTYQDPLYLEDQVPRRRPPIGYRPGGLQGSDTEDECWSDNEIVPQPPVRPREKPLGRSQSLRVVKRKPLTREGTSRSLKVRTRKKAMPSDMDS | Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29691
Sequence Length: 257
Subcellular Location: Endoplasmic reticulum membrane
|
Q6AZM3 | MVSWIISRAVVLVFGLLYPAYASYKAVKTKNVRDYVRWMMYWIVFALFMTVETFTDIFIAWFPFYYEIKMAFVVWLLSPYTRGASLLYRKCIHPTLSLKEKEIDSYIIQAKERSYESFVNIGRKGLNIAASAAVQAATKGQGALVGRLRSFSMQDLRALPDDTPIHYTDALYPDEPQLHRRPMGFPTTSQADSDSMDERWSDSEIAETRTAARTRGGMPSKSLQRSQSLRVSKKKGLSREVSTKTTKPRAKKKPAQSEPEN | Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes (By similarity). May play a role in the maintenance of both the nervous system and the musculature.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29821
Sequence Length: 261
Subcellular Location: Endoplasmic reticulum membrane
|
Q6PBX9 | MAAALKQRFDNALHEKNMVTDLLAKIEAKTGVNRSYIAYAVIAFIAIYLVIGYGASLLCNLIGFVYPAYISIKAIESPAKDDDTKWLTYWVVYGVFSVVEFFADIFLSWFPFYFLAKCAFLVWCMAPTPSNGSIMLYTRIIRPFFLKNEAKIDNVMKDLTDKAAGAADKIKDEAKKATANIMFEEKKHY | Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21407
Sequence Length: 189
Domain: The short lumenal loops between transmembrane domains 1 and 2 and between transmembrane domains 3 and 4 may impart a wedge-like configuration, thus deforming membranes.
Subcellular Location: Endoplasmic reticulum membrane
|
Q00765 | MSAAMRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISIKAIESPNKEDDTQWLTYWVVYGVFSIAEFFSDIFLSWFPFYYMLKCGFLLWCMAPSPSNGAELLYKRIIRPFFLKHESQMDSVVKDLKDKAKETADAITKEAKKATVNLLGEEKKST | Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21493
Sequence Length: 189
Domain: The short lumenal loops between transmembrane domains 1 and 2 and between transmembrane domains 3 and 4 may impart a wedge-like configuration, thus deforming membranes.
Subcellular Location: Endoplasmic reticulum membrane
|
Q60870 | MRERFDRFLHEKNCMTDLLAKLEAKTGVNRSFIALGVIGLVALYLVFGYGASLLCNLIGFGYPAYISMKAIESPNKDDDTQWLTYWVVYGVFSIAEFFSDLFLSWLPFYYMLKCGFLLWCMAPSPANGAEMLYRRIIRPIFLRHESQVDSVVKDVKDKAKETADAISKEVKKATVNLLGDVKKST | Function: Plays an essential role in heart function and development by regulating the organization and function of the sarcoplasmic reticulum in cardiomyocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21051
Sequence Length: 185
Domain: The short lumenal loops between transmembrane domains 1 and 2 and between transmembrane domains 3 and 4 may impart a wedge-like configuration, thus deforming membranes.
Subcellular Location: Endoplasmic reticulum membrane
|
Q66IF1 | MFAIFTKIKDRVEAFLNEKNIVTDCLNKIEEKTGIKKRYLAYGAAGVTGAFLLLGYGASLICNLIGFVYPAYFSIKAIESPGKEDDTQWLTYWVIYGFFSVGEFFSDIFLHWFPFYYVCKCLFLLWCMAPVSWNGSQVLYRHVVRPFFLKHEAAVDGMVSNISVKAMSAAENVTREVLHTLVRNRTVGPAESEPRSLPSSAHTEPTVD | Function: Required correct function and survival of retinal photoreceptors . Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May play a role in clathrin-coated intracellular vesicle trafficking of proteins from the endoplasmic reticulum to the retinal rod plasma membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23536
Sequence Length: 208
Subcellular Location: Endoplasmic reticulum membrane
|
Q96HR9 | MDGLRQRVEHFLEQRNLVTEVLGALEAKTGVEKRYLAAGAVTLLSLYLLFGYGASLLCNLIGFVYPAYASIKAIESPSKDDDTVWLTYWVVYALFGLAEFFSDLLLSWFPFYYVGKCAFLLFCMAPRPWNGALMLYQRVVRPLFLRHHGAVDRIMNDLSGRALDAAAGITRNVLQVLARSRAGITPVAVAGPSTPLEADLKPSQTPQPKDK | Function: Required for correct function and survival of retinal photoreceptors . Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May play a role in clathrin-coated intracellular vesicle trafficking of proteins from the endoplasmic reticulum to the retinal rod plasma membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23418
Sequence Length: 211
Subcellular Location: Endoplasmic reticulum membrane
|
Q7XII4 | MLSEQTAASGSSSSSRGADDREIVISTGREIVVRSSGGEEREEEVVVEEELEEPEFRDIHALSPPPTPTPSQPSSSYHRRRRESWESAAGSRHTSIRSVGSDTAPSELFPTMSREFSAMVAAAANANAAAAAAANGGDSSRAGVDDALGRIGEDELEETNPLAIVPDSNPIPSPRRAHLALPAPGDVSSAGGGHGDEVSVGQVKKEEVESKIAAWQIAEVAKVNNRFKREEVVINGWEGDQVEKANAWLKKYERKLEEKRAKAMEKAQNEVAKARRKAEEKRASAEAKRGTKVARVLELANFMRAVGRAPSKRSFF | Function: Functions in abscisic acid (ABA) signaling downstream of BZIP23. Acts as antagonistic and negative regulator of brassinosteroid (BR) signaling. Binds to BAK1 and inhibits its interaction with the BR receptor BRI1. Inhibits the formation and subsequent activation of the BRI1-BAK1 receptor complex.
PTM: Phosphorylated by BRI1. Phosphorylation reduces the binding affinity to BAK1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34096
Sequence Length: 316
Subcellular Location: Cell membrane
|
P11334 | MACLRPLQVHNLKKGEKVNFKHYSNGDVARYDMNKNYIVNDSVPCRKCVGCRLDNSAEWGVRASLEIKSNPKHNWFVTLTYSDEHLVYNALGRPNCVPEHITKFIKSLRKYFERRGHIGIKYLASNEYGTKRMRPHYHICFFNLPLDDLEKTIDSQKGYQQWTSKTISRFWDKGFHTIGELTYHSANYTARYTTKKLGVKDYKALQLVPEKLRMSKGIGLKYFMENKERIYKEDSVLISTDKGIKRFKVPKYFDRRMEREWQDEFYLDYIKEKREKVAKRTLFQRQIVSSRSYTDYLGDEQKKLNNIVKRLTRPLKTGKK | Function: Plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates at the 3'-OH of the cleavage site. After one round of rolling circle synthesis, protein ORF2 is linked to the newly synthesized ssDNA and joins the ends of the displaced strand to generate a circular single-stranded molecule ready to be packed into a virion.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 38090
Sequence Length: 320
EC: 3.1.21.-
|
P03567 | MPSHPKRFQINAKNYFLTYPQCSLSKEESLSQLQALNTPINKKFIKICRELHEDGQPHLHVLIQFEGKYCCQNQRFFDLVSPTRSAHFHPNIQRAKSSSDVKTYIDKDGDTLVWGEFQVDGRSARGGCQTSNDAAAEALNASSKEEALQIIREKIPEKYLFQFHNLNSNLDRIFDKTPEPWLPPFHVSSFTNVPDEMRQWAENYFGKSSAARPERPISIIIEGDSRTGKTMWARSLGPHNYLSGHLDLNSRVYSNKVEYNVIDDVTPQYLKLKHWKELIGAQRDWQTNCKYGKPVQIKGGIPSIVLCNPGEGASYKVFLDKEENTPLKNWTFHNAKFVFLNSPLYQSSTQSS | Cofactor: Divalent metal cations, possibly Mg(2+) or Mn(2+).
Function: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities (By similarity).
Sequence Mass (Da): 40332
Sequence Length: 352
Domain: There are 3 rolling circle replication (RCR) motifs. RCR-2 is probably involved in metal coordination. RCR-3 is required for phosphodiester bond cleavage for initiation of RCR (By similarity).
Subcellular Location: Host nucleus
EC: 2.7.7.-
|
Q67622 | MASSSAPRFRVYSKYLFLTYPECTLEPQYALDSLRTLLNKYEPLYIAAVRELHEDGSPHLHVLVQNKLRASITNPNALNLRMDTSPFSIFHPNIQAAKDCNQVRDYITKEVDSDVNTAEWGTFVAVSTPGRKDRDADMKQIIESSSSREEFLSMVCNRFPFEWSIRLKDFEYTARHLFPDPVATYTPEFPTESLICHETIESWKNEHLYSESPGRHKSIYICGPTRTGKTSWARSLGTHNYYNSLVDFTTYDVNAKYNIIDDIPFKFTPNWKCFVGAQRDFTVNPKYGKRKVIRGGIPCIILVNPDEDWLKDMTPEQSDYMYSNTVVHYMYEGETFINYSFASGEDVTASQ | Cofactor: Divalent metal cations, possibly Mg(2+) or Mn(2+).
Function: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities. Acts as an inhibitor of C-sense gene transcription (By similarity).
Sequence Mass (Da): 40511
Sequence Length: 351
Domain: There are 3 rolling circle replication (RCR) motifs. RCR-2 is probably involved in metal coordination. RCR-3 is required for phosphodiester bond cleavage for initiation of RCR.
Subcellular Location: Host nucleus
EC: 2.7.7.-
|
Q6NS82 | MASSGGGNTGAGGTSGLGLGLGLSLGMGEATGDAEEEAAAAEAVGRLATSLWLRLRGWEAVLAAAQRLLVWEKPLHSLVTAATLNGLFWLLSSSSLRPFFLLSISLLTYFLLDLWHPRFLPDVSAPPPEEPHSDSEGAGSGAQPHLLSVPELCRYLAESWLTFQIHLQELLQYKRQNPAQFCARGCAACAVLAVLGHYVPGVMISYIVLLSILLWPLVVYHELIQRMYTRLEPLLMQLDYSMKAEADALHHKHDKRKRQGKSAPPAGDEPLAETESESEAELAGFSPVVDVKKTALALAITDSELSDEEASILESGGFSVSRATTPQLTDVSEDLDQQSLPSEPEEALNRELGEGEETELASPEDLLSAPPALSKQALDTEEEGAADKEALLQLSSPLHFVNTHFNGAGSPQDGVKCPPGAPVKTLSPEAVSGDLMAPSSTLSPQLCLAESGPVTPLSPSVLPSLPQDSPQPLAAPEEEEALTTEDFELLDQGELEQLNAELGLGPEMPPKPPDVLPPPPLGADSHSLVQSDQEAHAEVEP | Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress . When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins . Required for collagen quality control in a LIR motif-independent manner .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57542
Sequence Length: 541
Domain: The LIR motif interacts with ATG8 family proteins.
Subcellular Location: Endoplasmic reticulum membrane
|
Q86VR2 | MAEAEGVPTTPGPASGSTFRGRRDVSGSWERDQQVEAAQRALVEVLGPYEPLLSRVQAALVWERPARSALWCLGLNAAFWFFALTSLRLVFLLAFGLMIIVCIDQWKNKIWPEIKVPRPDALDNESWGFVHPRLLSVPELCHHVAEVWVSGTIFIRNVLLFKKQNPGKFCLLSCGILTFLAVLGRYVPGLLLSYLMLVTVMMWPLAVYHRLWDRAYVRLKPALQRLDFSVRGYMMSKQRERQLRRRALHPERAMDNHSDSEEELAAFCPQLDDSTVARELAITDSEHSDAEVSCTDNGTFNLSRGQTPLTEGSEDLDGHSDPEESFARDLPDFPSINMDPAGLDDEDDTSIGMPSLMYRSPPGAEEPQAPPASRDEAALPELLLGALPVGSNLTSNLASLVSQGMIQLALSGASQPGPSGAPAQRATRGFLRSPSSDLDTDAEGDDFELLDQSELSQLDPASSRSH | Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress . When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins . Promotes ER membrane curvature and ER tubulation required for subsequent ER fragmentation and engulfment into autophagosomes . Required for collagen quality control in a LIR motif-dependent manner (By similarity). Mediates NRF1-enhanced neurite outgrowth .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51396
Sequence Length: 466
Domain: The LIR motif interacts with ATG8 family proteins.
Subcellular Location: Endoplasmic reticulum membrane
|
Q0P4Z1 | MAQRVGEEEQGASGLRRRRSGARCVEARERDEQVREVQEMLQRGLSSYEPVLSYVQAVLVWERPRHSALLHLALNAAFWFFALTSLRIIFLVAFGLMIIICADQWKNKLWPELGAARASELENESWGYVHPRLLSVPELCYHAADTWVSVYNFLRNLLLFKTENPGKFCLLACSFLTFLAVLGGYIPGVVLSYLLLLFLLLWPLAIYHQLGRRIYQKLEPALQRLDFSVRGYMMSKYKERQKHNRALPPTDASDSEEELAAFCPSLDDSAVAKELTISDSEHSDAEVSFTENGTFNLSRGQTPLTEGSEDLDRHSDPEESFARDLPDFPSINPDATGIEDDDETSIGIPSTALHPQFSSRQLYEEQESLDAELSLGGFPSTQNITENIAGFVTRGMIQLALAGASQQTHAYAESPRAKQYQRNSSSELDTDAEADDFELLDQSELSQMDPSSSHSHQ | Function: Endoplasmic reticulum (ER)-anchored autophagy regulator which exists in an inactive state under basal conditions but is activated following cellular stress. When activated, induces ER fragmentation and mediates ER delivery into lysosomes through sequestration into autophagosomes via interaction with ATG8 family proteins. Promotes ER membrane curvature and ER tubulation required for subsequent ER fragmentation and engulfment into autophagosomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51364
Sequence Length: 457
Domain: The LIR motif interacts with ATG8 family proteins.
Subcellular Location: Endoplasmic reticulum membrane
|
Q5BLE8 | MWFAVVAIFLALVAFLYRYVVGSGPNPFAIDTREPLKPMVFDRKLKNKVLKQGFLASRVPEDLDAVVVGSGIGGLAIAVLLAKVGKKVLVLEQHDRAGGCCHTFKEQGFEFDVGIHYIGELSNHKPLRCIIDQMTNGQLQWDPLENPFDNVVIGPPENRRIYQIYSGRKRYMDELKKCFPGEEKAIDEYVRLCKEVGQGVWVMVLLKFLPTPIANFLVRTGLANRLTSFSRYASRSLTDVVNELTQNKDLRAVLSYIFGTYGKIPKEASFSMHSLIVNHYMNGAWYPKGGATEIAYHMIPIIEKAGGAVLVRAPVNRILLNDAKEAIGVSVLKGQEEVHVRAPIVISDAGIFNTYEYLLPKDVQTMPAIQKQLSMLQHGDSGLSIFIGLDGTKEELGLKADNYFIYPENNIDELLEDYRSGNREESAKKNPLIFVASPSAKDSTWPERTPGKSTLTVVSFANYEWFEEWKDDKVKNRSTDYKQLKELFINYILEAVTEIYPKIKDRIEYVDAGTPITNQHYIAAPRGEIYGADHGIPRFSAELNATIRAQTPIKNLYLTGQDLMLCGFAGALTGALTCGSVILNRNLHLEAFSLAKRVQNGNNKKKT | Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol. In addition, saturates the 7-8 double bond of all-trans-retinol to produce all-trans-7,8-dihydroretinol. Can also use vitamin A2 (all-trans-3,4-didehydroretinol) as a substrate, to produce all-trans-13,14-dihydro-3,4-didehydroretinol or all-trans-7,8-dihydro-3,4-didehydroretinol. May play a role in vitamin A metabolism.
Catalytic Activity: A + all-trans-13,14-dihydroretinol = AH2 + all-trans-retinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67937
Sequence Length: 607
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.99.23
|
Q64FW2 | MWITALLLAVLLLVILHRVYVGLYAASSPNPFAEDVKRPPEPLVTDKEARKKVLKQAFSVSRVPEKLDAVVIGSGIGGLASAAVLAKAGKRVLVLEQHTKAGGCCHTFGENGLEFDTGIHYIGRMREGNIGRFILDQITEGQLDWAPMASPFDLMILEGPNGRKEFPMYSGRKEYIQGLKKKFPKEEAVIDKYMELVKVVARGVSHAVLLKFLPLPLTQLLSKFGLLTRFSPFCRASTQSLAEVLQQLGASRELQAVLSYIFPTYGVTPSHTAFSLHALLVDHYIQGAYYPRGGSSEIAFHTIPLIQRAGGAVLTRATVQSVLLDSAGRACGVSVKKGQELVNIYCPVVISNAGMFNTYQHLLPETVRHLPDVKKQLAMVRPGLSMLSIFICLKGTKEDLKLQSTNYYVYFDTDMDKAMERYVSMPKEKAPEHIPLLFIAFPSSKDPTWEERFPDRSTMTALVPMAFEWFEEWQEEPKGKRGVDYETLKNAFVEASMSVIMKLFPQLEGKVESVTGGSPLTNQYYLAAPRGATYGADHDLARLHPHAMASIRAQTPIPNLYLTGQDIFTCGLMGALQGALLCSSAILKRNLYSDLQALGSKVKAQKKKM | Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol . Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers . May play a role in the metabolism of vitamin A . Independently of retinol conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP . Required for adipocyte differentiation in a 3T3-L1 cell culture model . This effect seems not to mimic the in vivo situation in which animals show increased adiposity in the absence of RETSAT .
Catalytic Activity: A + all-trans-13,14-dihydroretinol = AH2 + all-trans-retinol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67334
Sequence Length: 609
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.99.23
|
Q9W0P2 | MTRDEDNGFSEWGGYFEAKKSKLEEQFAAASDPFRKSDLFQGISIFVNGRTDPSADELKRIMMVHGGTFHHYERSHTTYIIASVLPDVKVRNMNLSKFISAKWVVDCLEKKKIVDYKPYLLYTNQKTSQPMLIFGKPKDNGANESKSDVEPPKDKAEVEVDSTKDETQMELGGILKNLQQAVATSPEKEASASESKITNLSTTSNNSTTARTAADPNFLSEFYKNSRLHHIATLGAGFKQYVCRLRQKHGTQGFPKRETLKSLANSHHNCLERYVMHIDMDCFFVSVGLRTRPELRGLPIAVTHSKGGNAATDVPVHPQADRKAELELFAQRFEHHFHDGDKAEKVRSGFDKKMSLSEIASCSYEAREKGIRNGMFVGQALKLCPELKTIPYDFEGYKEVAFTLYDTVAQYTLNIEAVSCDEMFVELTDLAHELNVDVMAFVSHLRQEVYSKTGCPCSAGVAGNKLLARMATKEAKPNGQFLLDSSNDILAYMAPMSLDLLPGVGSSISHKLKQAGLNNCGDVQNTTLEKMEKVLGKKLGQNLFQNCRGIDDRPLAYEQIRKTVSAEMNFGIRFTNSVECEQFLCQLSEEVTKRLVEIRRKARSINLKIMVRAAEAPVETSKYMGHGVCDIINKSSLIKYATDDVNVITTVVLDLMKDADIPPDELRGLGIHLTRLEDANEVRKENNIKEMFGKMSEMRKDKPIPQGAVGDKSIGDDKVNKPLVFENKPKPREPRNVLSMLTAAAVSRKSVTEDRSQRGTSKPITRPLSLVPKLDEDVLAQLPEDIRLEVIANREEHLCIAEYDGYRSPQYPTLRSPPLLNPYVTTNVSPLKATDLKPSTSRAAVARLQKRKERKEQEHYIRSDQIVADYIDDLPDFVNPHILKLISHPVEMPELLMGDNYKDLLNDWVSREEVPKPNDVDLILKQVSRMIKNDQLDHVCDVMKYWCRIINMKRSSSCCWHVAYKHIEESIQNQMLTIEGYSLLFIEYIRCIKCS | Cofactor: Binds 2 magnesium ions.
Function: Deoxycytidyl transferase involved in DNA repair . Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents (By similarity). During homologous recombination (HR) repair of DNA double-strand breaks (DSBs) regulates the extent of repair synthesis . Possibly recruits the DNA polymerase zeta complex or another translesion polymerase to early DSB repair intermediates to initiate repair synthesis, while also blocking the access of more processive polymerases preventing them from acting during the initial stages of HR repair .
Sequence Mass (Da): 112414
Sequence Length: 995
Subcellular Location: Nucleus
EC: 2.7.7.-
|
O94623 | MAFNQRKRRRPVGIADFDEANDEAYESVGFHDYADYFSRKQRKLQNQNAALYKSIDEDSKSDLFHGLAIAINGYTKPSYTELRQMIVSNGGTFIQYVDGKTSISYLVCSFLTPSKARQWKHQKVVKPEWIVDCIKQKKILPWINYRTFQASSAQATLSFVASKPSQPEGNLEDIQTSSQEEEHDNEKDKTKESKAKGFLDDLSGLSASSLHNYQLLKNPNVRNSTTQNQDFLENFFSSSRLHHLSTWKADFKNEIQAMTTASEPVRPIMKDKSKKSRFLLHVDFDCFFASVSTRFSHELRLKPVAVAHGIKNSEIASCNYEARKFGIKNGMYVGTAKNLCPSLRVVDYDFGAYESVSREFYTILVNTLHDYIKVISIDEALLDITSSVSSFQDCFEIAESIRSQVREKTNCEVSVGIGPNVLLARLALRKAKPHNVYSLSIENVFDVLSPLSVQDLPGVGSSQAQKLFNLYGVRTIGQLQRIEKFNLQETFGVNYGLHLYNISRGIDTDIINNETPRRSISVDVNWGVRFVFQEDGIDFLKRLLHELLSRMGKCQVLLHQIQLRILKRADGAPFSPPKYLGAGEVTSFTKSSTFTSATNSFDLIWKKVTSMYKTINVDPGDVRGIGLQALKIIKDNSKIRKDYRSIQSITSRNKVSLKGASVDISSKDKEIISQKKQLSPKLIPSTPYDLPSSSQISSSALAQLPPSMQSDIQQQLRLQKRSITEYPSQLDPLFMVELPTPIRNEVNDNHEIAMNKRLSLKSHADNKIDERGKKKIRQENAFDKLLQISKKSKTINKPNVDYLTLKELPKDLQKQILKESNLQKSDLISEVKLEKPHIVTFQHVQSLEDLRGLLTKWYSKASKGPNIHDVNYFANYVCRVIREEKNLGKAQMMLKWLYQLNRKECNKPWEKAIDKIIETVQGECLQRNIPPLMIF | Cofactor: Binds 2 magnesium ions.
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis (By similarity).
Sequence Mass (Da): 106526
Sequence Length: 935
Subcellular Location: Nucleus
EC: 2.7.7.-
|
A6Q162 | MLKEKLHPFIQRYNEINELLSSPEITQDIKKMTALSKEQSEIEPIVEKAKEYMNILEAIEENRSLIEDEELGELAKEELKELEPKKEQLEEEIKVLLISKDPNDEKDIYLEIRAGTGGEEAALFASDLFKAYARYAEKKGWRVEIVSSSESDSGGYKEIIAKIKGQGVYSRLKYEAGTHRVQRVPETESQGRIHTSAVTVAIMPEVDDVDVEINPNDLKIDVYRSSGHGGQSVNTTDSAVRITHIPTGIVVAMQDEKSQHKNKEKALKILKARIFEKRMREQQEALAKDRKEQVGSGDRSERIRTYNFPQNRVTDHRIGLTLYKLEEVMQGDLDQIIEPLIAHYQAQKIQEAGL | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40360
Sequence Length: 354
Subcellular Location: Cytoplasm
|
B2ITM5 | MAESYLLDKLKSVEQTFNELTRRLGDPDTASNPDEYQEIAKSRSSLEEVVNTYEIWKTAQEDLIGAREVYKESASDPELQEMASLEVKELEEKIEHLESRLKVLLLPRDPNDEKNIMLEIRAGTGGDEASIWAGDLMQMYTRYAQTQGWKVSLVSESRGEMGGWKEVILEIKGNDVYSQLKFEAGVHRVQRVPATESGGRVHTSTATVAIMPEVDDVEIHIDPKDIEMTTARSGGAGGQNVNKVETAVDLMHKPTGIRIFCTEERSQLQNKERAMQILRAKLYDIKLGEQQAAVTSMRRSQVGTGSRSEKIRTYNYKDNRATDHRLGQNYSLTPVLDGDLETLIQSCISLDQQERLAELATSAAN | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40969
Sequence Length: 365
Subcellular Location: Cytoplasm
|
Q9K4E4 | MFEAVEELVAEHADLEKKLADPSVHSDQANARKLNKRYAELTPIVATFRSWKQTGDDMETAREFAADDPDFAAEVKELDKQRDELTEKLRLLLVPRDPSDDKDVILEIKAGAGGDESALFAGDLLRMYLRYAERIGWKTEIIDSTESELGGYKDVQVAVKTKGGQGATEPGQGVWARLKYEGGVHRVQRVPATESQGRIHTSAAGVLVTPEAEEIDVEINPNDLRIDVYRSSGPGGQSVNTTDSAVRITHIPTGVVASCQNEKSQLQNKEQAMRILRSRLLAAAQEEAEKEAADARRSQVRTVDRSEKIRTYNFPENRISDHRVGFKAYNLDQVLDGDLDSVIQACVDADSAAKLAAA | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 39460
Sequence Length: 358
Subcellular Location: Cytoplasm
|
Q2GDG2 | MDFETQVVLHNLKKSVEVIRRQLDIEKKHSRLEEIQALVDSPTLWEDQSRAQLLLKEKSQIETSLKEFKELSIQLDDLIEMIELASKDHEEETMKDLERELLLLKEKIQKKEIECLFSGEADGNDCLLEIQSGAGGTESNDWAMMLLRMYTRWAEIYHKFQVQIVDKVEGEETGIKSCTLKVMGKNAYGWARTETGVHRLVRISPFDANAKRHTSFAKIFVSPCIEGEINISIDEKDLKIDTYRASGAGGQHVNKTESAIRITHLPSKIVVQSQSSRSQHQNKAEAMQMLKSRLYEIELRKKEEKLNAARNVEDSIGWGYQIRSYVLHPYQMIKDLRTGHEVGNITSVLDGDLDSFIIATISNNS | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 41764
Sequence Length: 365
Subcellular Location: Cytoplasm
|
Q04GC3 | MELAQARNSISDMQEQIDGFRSTLDLDALDASIAENEDKMSQPGFWDDQQSAQKIIDETNTLKNRRDSFLSLQKSVEDLTAMAELLSEEDDADMHAELDTDIEKTEKDLEKYNLNQLLTEKYDSNNAILEIHPGEGGTESTDWASNLYRMYTRWAQAHDFKVEVTDYQTGDVAGIDSATLRIIGHNAYGFLRSEKGVHRFVRISPFDSAGRRHTSFVSIDVMPELDDDEIEIEIKPQDVKMDVYRSGGAGGQNVNKVSTAVRLTHIPTGIVVASQVERTQYGNRDIAMKMLKAKLYEQEEQKREEEHAKLSGTKLDVAWGSQIRSYVFQPYRMVKDLRSGYETGDTDGVMDGNLDPFINAYLKWKLSQKNPE | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 42213
Sequence Length: 372
Subcellular Location: Cytoplasm
|
Q7U3W6 | MDLTDFKRDLSELTDRLGHAQDCLDVPALKARQQDLEQLAAQPDFWDDQQAAQKQMRRLDEVKAQLQQLADWGGAVDDAKATLELYELEPDEEMLTEAQEGLNQLRQGLDRWELERLLSGDYDKEGAVLTINAGAGGTDAQDWAQMLLRMYTRWAEDHGMKVTVDELSEGEEAGIKSCTIEVEGRYAYGYLRNEKGTHRLVRISPFNANDKRQTSFAGIEVMPKIDEEVDIDIPEKDLEVTTSRSGGAGGQNVNKVETAVRILHIPTGLAVRCTQERSQLQNKEKAMALLKAKLLVIAQEQRAAEIADIRGDIVEAAWGNQIRNYVFHPYQMVKDLRTSEETNDVQAVMDGALDPFIDASLRQGVDSPGADADS | Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Sequence Mass (Da): 41776
Sequence Length: 374
Subcellular Location: Cytoplasm
|
Q9ZQ19 | MFSSSQFEPNSGFSGGGFMSSQPSQAYESSSSTAKNRDFQGLVPVTVKQITECFQSSGEKSGLVINGISLTNVSLVGLVCDKDESKVTEVRFTLDDGTGRIDCKRWVSETFDAREMESVRDGTYVRLSGHLKTFQGKTQLLVFSVRPIMDFNEVTFHYIECIHFYSQNSESQRQQVGDVTQSVNTTFQGGSNTNQATLLNPVVSSQNNDGNGRKNLDDMILDYLKQPACTARQQGIHIDEIAQQLKIPKNKLEGVVQSLEGDGLIYSTIDEYHFKHVEL | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Required fo cell division in meristems. Involved in the maintenance of transcriptional epigenetic gene silencing (TGS) at specific loci (including some transposons) by regulating histone H3 acetylation, 'Lys-4' and 'Lys-9' methylation.
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In response to DNA damage, recruited to DNA-repair nuclear foci, as a hypophosphorylated form (By similarity).
Sequence Mass (Da): 30980
Sequence Length: 279
Subcellular Location: Nucleus
|
Q6K9U2 | MMSFSQPDAFSPSQFTSSQNAAADSTTPSKSRGASSTMPLTVKQISEAQQSGITGEKGAPFVVDGVETANVRLVGLVSGKTERNTDVSFTIDDGTGRLDFIRWVNDGADSAETAAVQNGMYVSVIGSLKGLQERKRATAFAIRPVTDYNEVTLHFIQCVRMHLENTKSQIGSPAKTYSAMGSSSSNGFSEMTTPTSVKSNPAPVLSVTNGSKTDLNTEVLNVFREPANVESEHGVHIDEIVKRFRLPEAKIKVAIDYLADIGHIYSTIDESHYKSAFNE | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In response to DNA damage, recruited to DNA-repair nuclear foci, as a hypophosphorylated form (By similarity).
Sequence Mass (Da): 30082
Sequence Length: 279
Subcellular Location: Nucleus
|
Q8LFJ8 | MYGGDFDGNAAFAGGGFMPSQATTQAHESSSSLKNRDVRTLLPLTLKQLSSASTTGESNFSIDGVDIKTVVIVGRISRMENRITQVDFVVDDGTGWVDCVRWCHARQETEEMEAVKLGMYVRLHGHLKIFQGKRSVNVFSVRPVTDFNEIVHHFTECMYVHMYNTKLRGGSITQDTATPRPQMPYSTMPTPAKPYQTGPSNQFPNQFNDSMHGVKQTVLNYLNQPMHIVSEAGVHCDIIARELRIPLLQVKEALEQLSNDGCIYSTLDETCFKSTANA | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Required fo cell division in meristems. Involved in the maintenance of transcriptional epigenetic gene silencing (TGS) at specific loci (including some transposons) by regulating histone H3 acetylation, 'Lys-4' and 'Lys-9' methylation (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In response to DNA damage, recruited to DNA-repair nuclear foci, as a hypophosphorylated form (By similarity).
Sequence Mass (Da): 30957
Sequence Length: 278
Subcellular Location: Nucleus
|
Q6H7J5 | MYGVGVGGGGGGNYDGGGGNASSLFGGGGFMPSQATNAAEGTSGGGGGFPKSRNAQALLPLTVKQIMDASQTNDDKSNFAVNGMEVSTVRLVGRMLNKLDRVTDVSFTLDDGTGRVPVNRWENDSTDTKEMADIQNGDYVIVNGGLKGFQGKRQVVAYSVRRITNFNDVTHHFLHCVHVHLELTRPKSQVNANTATGTPNQTMPRDSMAYNQSPLTNQASTFSAPQNTGTGTNMIDLVLNVFHDPAVMNDDHGVGVDYVSRRLNLPEETVGKIIIDQVDLGHLYATIDDHHYKSTMNG | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In response to DNA damage, recruited to DNA-repair nuclear foci, as a hypophosphorylated form (By similarity).
Sequence Mass (Da): 31821
Sequence Length: 298
Subcellular Location: Nucleus
|
Q5Z8L1 | MAAAASYFSGTALMPSQRSGAPAPEYSAAGTGAAAAPSPSKPRDPRFSGCVPATVLHISRSFAAALAADGGGDPVFSIDGVETTNVRVLGRVVSVVSRDTDVCFTLDDSTGKIPLVRWITDQSDTRDTSYIQEGVYVKVQVNLMGFQAKKQGLARSIRPINNFNEVVLHFIECMHVHLESVQSKMQRQLPPSVQTNEYTHVPSSGGVRDYQVHFTPQVNQGLPPAVQTNTSTYVPLLGGVRDHQAHFAQVNQGQFSPAVQANTSTHLPFSGGVGEHQIHFTPKVNQGQFPPSVQTNTSAHVPYSGGFREHQVHFTPPVNQGQFPPAVQTNLYNHAASSGGVREQVHLTQANQFSAYSSTGGLQHDPQRMVLEALQQPDILALEHGAHVDELVRRTGMPKANIMGVVKHLAAAGFVYWTIDDNHVKSMCNG | Function: Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions (By similarity).
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). In response to DNA damage, recruited to DNA-repair nuclear foci, as a hypophosphorylated form (By similarity).
Sequence Mass (Da): 46328
Sequence Length: 430
Subcellular Location: Nucleus
|
Q23697 | MLASQAGSNFSAAASSNGGQQQQQRRQHPIRPLTIKQMLEAQSVGGGVMVVDGREVTQATVVGRVVGYENANMASGGGAITAKHFGYRITDNTGMIVVRQWIDADRAQEPIPLNTHVRASGTVNVWQQSPIVTGTVVSMADSNEMNYHMLDAILTHLRLTQGNKRAAGNIGSGASVQNSAAAVGVQNMLPGGDNKVLLTDLLVSFIKQNGHGDAGMSMDELTMAAQRYSFTPGDVRTAMRTLAAEGKVYQTHDNRFNI | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage.
PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). Phosphorylated upon DNA damage, which promotes its translocation to nuclear foci (By similarity).
Sequence Mass (Da): 27509
Sequence Length: 258
Subcellular Location: Nucleus
|
P15927 | MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
PTM: Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence.
Sequence Mass (Da): 29247
Sequence Length: 270
Subcellular Location: Nucleus
|
Q62193 | MWNSGFESFTSSTYGGRGGYTQSPGGFGSPTPSQAEKKSRVRAQHIVPCTISQLLSATLTDEVFRIGDVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAPPMDVRQWVDTDDASGENAVVPPETYVKVAGHLRSFQNKKSLVAFKIIPLEDMNEFTAHILEVVNSHMMLSKPNSQASAGRPSMSNPGMSESFNFSGNNFMPANRLTVVQNQVLNLIKACPRPEGLNFQDLRSQLQHMPVPSIKQAVDFLCNEGHIYSTVDDDHFKSTDAE | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
PTM: Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence.
Sequence Mass (Da): 29718
Sequence Length: 270
Subcellular Location: Nucleus
|
Q92373 | MAYDAFGKPGYGPDFNSAFSPGMGGGAGFNEYDQSSQPSVDRQQGAGNKLRPVTIKQILNASQVHADAEFKIDGVEVGQVTFVGVLRNIHAQTTNTTYQIEDGTGMIEVRHWEHIDALSELATDTYVRVYGNIKIFSGKIYIASQYIRTIKDHNEVHFHFLEAIAVHLHFTQKANAVNGANAPGYGTSNALGYNNISSNGAANSLEQKLAEYSLTPAQMTVMQAIHSAPETNEGVHVRQLAQSVGPGIDLTAVTDFLQQEGIIYTTIDENHFKSVLQDQ | Function: Binds to single-stranded sequences.
PTM: Phosphorylated in a cell cycle-dependent manner. Hypophosphorylated in G1, becomes phosphorylated at the G1/S boundary, it is maintained in this state through the M phase.
Sequence Mass (Da): 30391
Sequence Length: 279
Subcellular Location: Nucleus
|
P26754 | MATYQPYNEYSSVTGGGFENSESRPGSGESETNTRVNTLTPVTIKQILESKQDIQDGPFVSHNQELHHVCFVGVVRNITDHTANIFLTIEDGTGQIEVRKWSEDANDLAAGNDDSSGKGYGSQVAQQFEIGGYVKVFGALKEFGGKKNIQYAVIKPIDSFNEVLTHHLEVIKCHSIASGMMKQPLESASNNNGQSLFVKDDNDTSSGSSPLQRILEFCKKQCEGKDANSFAVPIPLISQSLNLDETTVRNCCTTLTDQGFIYPTFDDNNFFAL | Function: Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
PTM: Phosphorylated in a cell cycle-dependent manner with phosphorylation increasing at the entry in S phase and dephosphorylation occurring at mitosis.
Sequence Mass (Da): 29936
Sequence Length: 273
Subcellular Location: Nucleus
|
P35244 | MVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLYNEAVKIIHDFPQFYPLGIVQHD | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage . In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response . It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair . Also plays a role in base excision repair (BER), probably through interaction with UNG . Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA . As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange .
PTM: Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination .
Sequence Mass (Da): 13569
Sequence Length: 121
Subcellular Location: Nucleus
|
Q9CQ71 | MEDIMQLPKARVNASMLPQYIDRPVCFVGKLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGKVTAKATVLCASYTLFKEDTNRFDLELYNEAVKIINELPQFFPVGLPQHE | Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER), probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA.
PTM: Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination.
Sequence Mass (Da): 13584
Sequence Length: 121
Subcellular Location: Nucleus
|
A4IIE8 | MERGSCSAPGDPGHLGLFLQRLRQVFDACDGDADGFIKVEHFVALGLQFAQGDEVKKLAKRLDPNAQGRIGFKDFCHGVLAMKGCDKFVKGILGVTGTAPQHYEAPYTPYYYQSPETIEGPFLDTESSYSDSEFFAYEDGLTLSHRDAQHESDLDSAMYSTPSSEASDEGRNEDKAGGLGSLYLPGEQNLLKPSAGSGFSTHSTASLISNEEQFEDYGEGEDIDYSPGSPCPDDESRTNALSDLGSSVPSSAGQTPRKARLMYNTDLLDIYCTQCSKKITLLNDLEARLKNLKANSPNRKISSTAFGRQLLHNSNLSSSNGSTEDLFRDSIDSCENDITEKVSFLEKKVTELENDNLTNGDVKNKLKHENIHLVHRVHELEEFLRDQETKSEQVLDEESKRHRETYSKLAREKGTEIVLLSARVQELQEENEDLLTSLTRLKSHTVRIDEERQRVWDKLEDTSLRLKDETDLYKRLMDKLRQNRLHFQKEREATQELIEDLRRELDHLQIYKLECERSGRGPPSGLTELNVKSREVELEQEIRRLKQDNQKLRDQNDDLNGQILSLSLYEAKSLFSTQTKAQSLAAEIDSASKDELMEALKEQEEINYRLRQYMDKIILAILDHNPSILEIKN | Function: Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71734
Sequence Length: 633
Domain: The RBD-FIP domain mediates the interaction with Rab11 (rab11a or rab11b).
Subcellular Location: Recycling endosome membrane
|
Q9BXF6 | MALVRGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWYKLHSKPGKKEKERGEIEVTIQFTRNNLSASMFDLSMKDKPRSPFSKIRDKMKGKKKYDLESASAILPSSAIEDPDLGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSASGSLAYQGPGAELLTRSPSRSSWLSTEGGRDSAQSPKLFTHKRTYSDEANQMRVAPPRALLDLQGHLDAASRSSLCVNGSHIYNEEPQGPVRHRSSISGSLPSSGSLQAVSSRFSEEGPRSTDDTWPRGSRSNSSSEAVLGQEELSAQAKVLAPGASHPGEEEGARLPEGKPVQVATPIVASSEAVAEKEGARKEERKPRMGLFHHHHQGLSRSELGRRSSLGEKGGPILGASPHHSSSGEEKAKSSWFGLREAKDPTQKPSPHPVKPLSAAPVEGSPDRKQSRSSLSIALSSGLEKLKTVTSGSIQPVTQAPQAGQMVDTKRLKDSAVLDQSAKYYHLTHDELISLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIPPGPPK | Function: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. Involved in insulin granule exocytosis. May regulate V-ATPase intracellular transport in response to extracellular acidosis.
PTM: Phosphorylated on serine and threonine residues. Phosphorylation at Ser-357 is PKA-dependent.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70415
Sequence Length: 653
Domain: Binds to vesicles enriched in neutral phospholipids via its C2 domain. The interaction is favored by Mg(2+) rather than Ca(2+).
Subcellular Location: Cytoplasm
|
Q9Y644 | MSRARGALCRACLALAAALAALLLLPLPLPRAPAPARTPAPAPRAPPSRPAAPSLRPDDVFIAVKTTRKNHGPRLRLLLRTWISRARQQTFIFTDGDDPELELQGGDRVINTNCSAVRTRQALCCKMSVEYDKFIESGRKWFCHVDDDNYVNARSLLHLLSSFSPSQDVYLGRPSLDHPIEATERVQGGRTVTTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAEQVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPPDTLLQQVTLSHGGPENPHNVVNVAGGFSLHQDPTRFKSIHCLLYPDTDWCPRQKQGAPTSR | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1. May be involved in limb formation and in neurogenesis.
Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36424
Sequence Length: 331
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.222
|
O09009 | MSRARRVLCRACLALAAVLAVLLLLPLPLPLPLPRAPAPDPDRVPTRSLTLEGDRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQMLAGGRMINTNCSAVRTRQALCCKMSVEYDKFLESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPSGAILQQVTLSYGGPENPHNVVNVAGSFNIQQDPTRFQSVHCLLYPDTHWCPMKNRVEGAFQ | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 . May be involved in limb formation and in neurogenesis (By similarity).
Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36926
Sequence Length: 332
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.222
|
Q9YHB3 | MNFSCLGLSKICFLVSVIFCTFLLLFIPKTKTPWRPRTYPQPRPPPLFNATCGKQFALPGIEHAQQKLPTHTTDITHFEDPGNVEDWRAYILGRENPDEKHEGPTDNPGEHKSVLASSINSSKDALEFEDLFIAVKTTRKYHKTRLDLLLQTWISRAKQQTFIFTDGEDQDLRQRAGIQVINTNCSAMHTRQALCCKMAVEYDKFIESERKWFCHVDDDNYVNLFSLRHLLASFSHSQDVYLGRPSLDHPIEAIERVKSDGSASVRFWFATGGAGFCISRGLALKMSPWASMGNFITTAELVRLPDDCTIGYIIEGLLGVKMHHTPLFHSHLENLQRLPLQSVLKQVTLSYGGPDNKRNVVSVGGIFSLENDPTRFRTVHCLLYPDTHWCPPRKTR | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (By similarity). Involved in forelimb development and in adult forelimb regeneration.
Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45048
Sequence Length: 396
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.222
|
A6X7E7 | MTDATAARRNIVILTIAQALGASSPPIVISLGGLVGQKLSSDPALVTLPVSLFNLGLALGTLPAAFFMRQFGRRNAYMLGALVGAAAGVIAAAGIFAASFLIFCLGTLTAGFYASYVQSYRFAATDAATGDMKARAISWVMVGGLVAAIVGPQLVIWTRDTIPDAMFAGSFLSQAVLGLLALPVLFMLRAPKVRKDPNAIHDTGRPLGEILRSPRFILSVAAGVCSYALMTFVMTAAPIAMVGHGHSVDHAALGIQWHVLAMFAPSFFTGKLITRFGKEKITALGLVLIAFSAIIALGGFDVGHFWGALIFLGIGWNFGFIGATAMVTDCHTPAERGKAQGANDFIMFGTVACASFFAGSLLHSSGWETINWLVFPIVALVLVPLILRLKPKGAAAEA | Function: Transports riboflavin into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41659
Sequence Length: 398
Subcellular Location: Cell membrane
|
Q08DC7 | MPTPPEAEKQQTGPEEADQPPSMSSHDAAPPAPPRRNPCCLCWCCCCSCSWNEERRRAWRASRESRLQPLPSCEVCATPTPTPTPTPEEVRSWAQSFDKLMHSPAGRSVFREFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPAYRALLLQGASQSSSEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity).
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 25353
Sequence Length: 223
Subcellular Location: Membrane
|
P49795 | MPTPHEAEKQITGPEEADRPPSMSSHDTASPAAPSRNPCCLCWCCCCSCSWNQERRRAWQASRESKLQPLPSCEVCATPSPEEVQSWAQSFDKLMHSPAGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPTYRALLLQGPSQSSSEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein.
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24636
Sequence Length: 217
Subcellular Location: Membrane
|
Q8H1F2 | MASGCALHGGCPSDYVAVAISVICFFVLLSRSVLPCLIHKAPRTNSSSFWIPVIQVISSFNLLFSIMMSVNLLRFRTKHWWRYCYLWAVWIEGPLGFGLLMSCRITQAFQLYFIFVKKRLPPVKSYIFLPLVLLPWIFGAAIIHATKPLNDKCHMGLQWTFPVAGLHALYVLALIAFTRAVRHVEFRFDELRDLWKGILVSATSIVIWVTAFVLNEIHEEISWLQVASRFVLLVTGGILVVVFFSISSNQPLLSQISLKKRQNFEFQRMGQALGIPDSGLLFRKEEFRPVDPNEPLDKLLLNKRFRHSFMEFADSCYAGETLHFFEEVYEHGKIPEDDSIRRIYMARHIMEKFIVAGAEMELNLSHKTRQEILTTQDLTHTDLFKNALNEVMQLIKMNLVRDYWSSIYFIKFKEEESCHEAMHKEGYSFSSPRLSSVQGSDDPFYQEHMSKSSRCSSPG | Function: Glucose-regulated GTPase-accelerating protein (GAP) for the GTP-bound self-activating heterotrimeric G alpha protein GPA1. Cooperates with G beta-gamma dimers to maintain an unactivated but fully functional pool of GPA1. Phosphorylation-dependent endocytosis of RGS1 physically uncouples the two proteins, resulting in signal activation. Free AGB1 is essential, but not sufficient, for RGS1 endocytosis. Modulates cell proliferation, abscisic acid (ABA) and drought stress signal transduction by acting in a hexokinase-independent glucose-signaling pathway . Involved in the shapes of leaves, the development of floral buds, the elongation of stems, siliques, and hypocotyls, the time of flowering and the regulation of guard-cell K(+) and anion channels. Important for the kinetics of voltage activation of inward K(+) current but not for the current amplitude.
PTM: Phosphorylated by WNK8 and WNK10, and in vitro by WNK1. Also phosphorylated at Ser-435 or Ser-436.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52947
Sequence Length: 459
Domain: The C-terminal domain (249-459) is able to bind to and to accelerate the GTPase activity of GPA1.
Subcellular Location: Cell membrane
|
Q6RG78 | MPGMFFSANPKDLKGTDQSLLDDKTQKRRPKTFGMDVKAYLRSMIPHLESGMKSSKSKDILSADEVMQWSQSLEKLLANQTGQDVFGNFLKSEFSEENIEFWLACEDYKKTESDLLRCKAEKIYKAFVHSDAAKQINIDFHTRESTAKKIKAPTLTCFDEAQKVIYTLMEKDSYPRFLKSNIYLNLLNDLQANSLK | Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors. Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22544
Sequence Length: 196
Subcellular Location: Cell membrane
|
Q08116 | MRAAAISTPKLDKMPGMFFSANPKELKGTTHSLLDDKMQKRRPKTFGMDMKAYLRSMIPHLESGMKSSKSKDVLSAAEVMQWSQSLEKLLANQTGQNVFGSFLKSEFSEENIEFWLACEDYKKTESDLLPCKAEEIYKAFVHSDAAKQINIDFRTRESTAKKIKAPTPTCFDEAQKVIYTLMEKDSYPRFLKSDIYLNLLNDLQANSLK | Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors . Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23858
Sequence Length: 209
Subcellular Location: Cell membrane
|
Q09777 | MPALHNPSSPPPSYEAVTSYRNGNSIDSGDKRQQCSRLMKITSNGRPYSKDFLELFSTMVISTNFSRNRYRFSYVENSCTLLQLLSTLENLQLSQVNRIKSRCGSKVLKSTTKFTIPKTAAKCLCNTFLNARLLQIVNNPSARKFSNEKCLLQLTRKGYSVVSEFLQHNGHNSQAELYASKWNHSAPVIVSISRFSSTDQILKDSSFCEMLLVRMLGSVHEIGKSKNPLLVPVYSVSSPSPKDSLSKVTKYQMFGIDIAEWLMCNTMLLDWSEMETVASDLLIHSYIAYENNSETPLKFSYAKGVSYFLTGKGIATLGWTKNVSNNKLINKINEVEKGSTNKEILETILRKPNLQTYFFEFLKKNFCDENQRFYSEVCEFNDYFSHANETNDHEAIRESFAHACGIYNCFLSSNAPNAVNLPSDLYEKITNHMALAMEVEPLNEWLQLIHILLLEAQTAVLDLMAGDSLLKFLELNGGLGI | Function: Negatively regulates pheromone signaling during mating. Acts in a negative feedback loop that is essential for the mating process. This loop acts to down-regulate cellular sensitivity to pheromone. Activated by ste11.
Sequence Mass (Da): 54362
Sequence Length: 481
Domain: The fungal-differentiation regulator (Fungal-DR) domain is only found in fungal regulator of G-protein signaling (RGS) proteins that regulate differentiation pathways. It is required for function.
Subcellular Location: Nucleus
|
A1A643 | MPGIFFSHPNALKEVTNKPDEVMAQKKKNFAVPWKNYLKSMLPHLETIKSSSSSSSSDTEKNKLTPNEIIQWTMSLEKLLVSEEGQAVFRAFLKSEFSEENIEFWLACEDYKATNDSEELRCKANVIYQEFIQPNANKQINIDFSTRNSVTKDLLEPTKATFNGAQKMIFILMERDSYPRFLKSEIFFRLAERHHGNNMRG | Function: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors. Inhibits B cell chemotaxis (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23299
Sequence Length: 201
Subcellular Location: Cell membrane
|
P79348 | MPRLSQDNQQGHQKHFSRPSRRIQFLPPPWTEAYNVNVHQTVENEGCATAMHNVKLLGSPAAPTLLSLLSGTLSGFARFFALLLRRPPPEAPLRRRDFSALIPALPAAVLSPGHEERPGRLSLLLRAALALPGRPPGGRLPREVDASAGQSSSIPPMGSEWMEMRKRPVCAAQEPTACAPGQPGVENQGSNACCFCWCCCCSCSCLTVRNQEEQRLRRTSYEARTEDLPTCEESPGPTLEEASAWAQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKATIEEKARIIYEDYISILSPKEVSLDSRVRETINRSMAEPSRNIFDDAQLQIYTLMHRDSYPRFMNSALYKDLLRSLSEKAVEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity).
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 41917
Sequence Length: 374
Subcellular Location: Membrane
|
Q9PWA1 | MGSERTEMRKRQMAATQETPGTAQAQHSVGNRGPNACCFCWCCCCSCSCLTVRNQEEERARRTSHELQAEGIPNCEESPAPTLEEVNAWAQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKQESNKSVIEEKARLIYEDYISILSPKEVSLDSRVREVINRNMLEPSQHTFDDAQLQIYTLMHRDSYPRFMNSAIYKDLLRSLSEKSIEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity).
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 25141
Sequence Length: 218
Subcellular Location: Membrane
|
O76081 | MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVEPSQHIFDDAQLQIYTLMHRDSYPRFMNSAVYKDLLQSLSEKSIEA | Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity).
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 43692
Sequence Length: 388
Subcellular Location: Membrane
|
Q93ZG7 | MADTVEKVPTVVESSSSSTVEASNSAEKTEPTTEKKKWGDVEDDDDEEEAVSELNSLSIKEEEKPDSILEEPEDSNIKAVTSGDTPYTSASRFEDLNLSPELMKGLYVEMKFEKPSKIQAISLPMIMTPPHKHLIAQAHNGSGKTTCFVLGMLSRVDPTLREPQALCICPTRELANQNMEVLQKMGKFTGITAELAVPDSTRGAPAATRGAPVSAHVVIGTPGTLKKWMAFKRLGLNHLKILVFDEADHMLATDGFRDDSLKIMKDIGRVNPNFQVLLFSATFNETVKDFVARTVKDPNQLFVKREDLALDSVKQYKVVCPKEQNKIEVIKDQIMELGDIGQTIIFVKTKASAQKVHKALAEMGYDVTSVHGNLTESDRDKIVKEFKECLTQVLIATDVIARGFDQQRVNLVVNYNLPTKYETGEPDYEVYLHRVGRAGRFGRKGAVFNLLLDDGWDKEVMEKIEKYFEANVKEIKSWNSEEEYKSALKEAGLLDE | Function: ATP-dependent RNA helicase essential for mRNA export from the nucleus. Plays an important role in the positive regulation of CBF/DREB transcription factors.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55384
Sequence Length: 496
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
Q10RI7 | MADGGKPPTPEKKSWADVEEEEEAKAKAAAAAEAASSSSSNEPAVDAQAKQIEALSLSVPEEHGGSGGGGDDQGPPLLDDSDESQIQAVTSGGTVYESAAAFEDLKLTPELLKGLHDEMGFSRPSKIQAVTLPMILTPPYKDLIAQAHNGSGKTTCFVLGMLSRVDPNRKVTQAICICPTRELAQQNKSVLMRMGKFTGITCACAIPPAQKDYVPIAKMPKITDQVVIGTSGTLMKWINHKKILTNDIKILVFDEADHMLAEDGFRSDSERIMRDIQRSAGGCQVLLFSATFNERVKDFVTRVIKDGNQIFVKKEELTLEKVKQYKVQVPDERAKIAVIKDKIFEFGQKVGQVIIFVRTKQSTKDVHNALTLEDYVCSSIQGSLDQSEREKIIQEFKNGYTKVLISTDVLARGFDQAQVNLVINYDMPIKFGTRDEPDYEVYLHRIGRAGRFGRKGAVFNLLCGETDNTVMRKIETYFQHNVPEVRNWQSEEDFERALKDAGLVE | Function: ATP-dependent RNA helicase essential for mRNA export from the nucleus. Plays an important role in the positive regulation of CBF/DREB transcription factors (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55855
Sequence Length: 505
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
Q56X76 | MVGASRTILSLSLSSSLFTFSKIPHVFPFLRLHKPRFHHAFRPLYSAAATTSSPTTETNVTDPDQLKHTILLERLRLRHLKESAKPPQQRPSSVVGVEEESSIRKKSKKLVENFQELGLSEEVMGALQELNIEVPTEIQCIGIPAVMERKSVVLGSHTGSGKTLAYLLPIVQLMREDEANLGKKTKPRRPRTVVLCPTRELSEQVYRVAKSISHHARFRSILVSGGSRIRPQEDSLNNAIDMVVGTPGRILQHIEEGNMVYGDIAYLVLDEADTMFDRGFGPEIRKFLAPLNQRALKTNDQGFQTVLVTATMTMAVQKLVDEEFQGIEHLRTSTLHKKIANARHDFIKLSGGEDKLEALLQVLEPSLAKGSKVMVFCNTLNSSRAVDHYLSENQISTVNYHGEVPAEQRVENLKKFKDEEGDCPTLVCTDLAARGLDLDVDHVVMFDFPKNSIDYLHRTGRTARMGAKGKVTSLVSRKDQMLAARIEEAMRNNESLESLTTDNVRRDAARTHITQEKGRSVKQIREVSKQRNSRDKPSSSSPPARSTGGKTPVRKSSSSSFSKPRKASSPPEKSSKPKRKILKTVGSRSIAARGKTGSDRRPGKKLSVVGFRGKSSSARAS | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 68924
Sequence Length: 621
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
A0A1D6LAB7 | MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTSKRTVLSDLITVYAKGGKTIVFTRTKKDADEVSLALTNSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTSSQKRTVKSLERDVGCNFEFISPPSIEEVLESSAEHVIATLRGVHPESTKYFLGAAEKLTEELGPHALASALAHLSGFSQPPSSRSLISHEQGWVTLQLTREQGFGRGFFSPRSVTGFLSDVCSAAADEVGKIYLTADENVQGAVFDLPEEIAKDLLTMELPPGNTLTKISKLPALQDDGPATDSYGRFSNDRGSRNNRRSRGGGASRGRGGWDTDGEDRFRRGGRSLRSDNDSWSDDDWSGGGRKSNRSSSFGSRSSSYSSRGSPSFGGRSSSFGGRESNRSFSGACFNCGESGHRATDCPNK | Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 80171
Sequence Length: 743
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Plastid
EC: 3.6.4.13
|
Q8L7S8 | MASTVGVPSLYQVPHLEISKPNSKKRSNCLSLSLDKPFFTPLSLVRRTRRIHSSSLLVPSAVATPNSVLSEEAFKSLGLSDHDEYDLDGDNNNVEADDGEELAISKLSLPQRLEESLEKRGITHLFPIQRAVLVPALQGRDIIARAKTGTGKTLAFGIPIIKRLTEEAGDYTAFRRSGRLPKFLVLAPTRELAKQVEKEIKESAPYLSTVCVYGGVSYTIQQSALTRGVDVVVGTPGRIIDLIEGRSLKLGEVEYLVLDEADQMLAVGFEEAVESILENLPTKRQSMLFSATMPTWVKKLARKYLDNPLNIDLVGDQDEKLAEGIKLYAIATTSTSKRTILSDLITVYAKGGKTIVFTQTKRDADEVSLALSNSIATEALHGDISQHQRERTLNAFRQGKFTVLVATDVASRGLDIPNVDLVIHYELPNDPETFVHRSGRTGRAGKEGSAILMHTSSQKRTVRSLERDVGCHFEFISPPTVGDLLESSADQVVATLNGVHPDSIKFFSATAQKLYEEKGTDALAAALAHLSGFSQPPSSRSLLSHEKGWVTLQLIRDPTNARGFLSARSVTGFLSDLYRTAADEVGKIFLIADDRIQGAVFDLPEEIAKELLEKDVPEGNSLSMITKLPPLQDDGPSSDNYGRFSSRDRMPRGGGGSRGSRGGRGGSSRGRDSWGGDDDRGSRRSSGGGSSWSRGGSSSRGSSDDWLIGGRSSSSSRAPSRERSFGGSCFICGKSGHRATDCPDKRGF | Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts . Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit . Required for normal development of chloroplasts . Required for the expression of transcripts encoding plastid-localized enzymes involved in abscisic acid (ABA) biosynthesis. Required for maintenance of ABA levels and response to salt stress . Possesses RNA chaperone activity for proper splicing of introns in chloroplasts. Essential for chloroplast function and abiotic stress responses .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81156
Sequence Length: 748
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Plastid
EC: 3.6.4.13
|
Q0DM51 | MASLLTLPSLSLSNPSASAAAAGAGAAPSLRLRAAFRCWALRRAGGGRWAAAGAIASPNSVLSEHAFKRLQLSDEEEEEEEGAYGSDEEGVEAVGGGEGDEDELAIARLGLPEQLVSTLEKRGITHLFPIQRAVLIPALDGRDLIARAKTGTGKTLAFGIPMIKQLMEEDDGRSVRRGRIPRVLVLAPTRELAKQVEKEIKESAPKLSTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVKYLVLDEADQMLAVGFEEDVETILQQLPAERQSMLFSATMPGWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTSTSKRTVLSDLITVYAKGGKTIVFTKTKRDADEVSLALTNSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTNSQRRTVRSLERDVGCRFDFISPPAIEDVLESSAEHVIATLRGVHTESIQYFIPAAERLQEELGPNALASALAHLSGFSQPPSSRSLISHEQGWVTLQLTRDPGYGRGFFSPRSVTGFLSDVSSAAADEVGKIFLTADEKVQGAVFDLPEEIARDLLSMELPPGNTITKVTKLPALQDDGPATDSYGRFSNSDRGFRNRRSRGGGSRGGRGGWDSDGEDRFRRGGRSFRSDNDSWSDDDFGGGRRSNRSSSFGGRGSSYGSRSSSSFGGRSSSFGSRDSSRSFSGACFNCGESGHRASDCPNK | Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Required for normal development of chloroplasts.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81615
Sequence Length: 758
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Plastid
EC: 3.6.4.13
|
Q5JKF2 | MSAGTAPAAPRYAPDDPSLPKPWRGLVDGTTGYLYYWNPETNITQYEKPLPPEDQLPPPPPLPPPPPRSGRGDRDRDRRDRSRSRTPPRRDHRDRDRDRDRRHDDHRSAPSHHHPLPAAAAIAADDPSTEAYRHRHEITVVGDNVPAPITSFETGGFPPEILKEIQRAGFSSPTPIQAQSWPIALQCQDVVAIAKTGSGKTLGYLLPGFMHIKRLQNNPRSGPTVLVLAPTRELATQILEEAVKFGRSSRISSTCLYGGAPKGPQLRDLDRGVDVVVATPGRLNDILEMRRISLKQVSYLVLDEADRMLDMGFEPQIRKIVKEIPPRRQTLMYTATWPKEVRRIAEDLLVHPVQVTIGSVDELVANSAITQNVELITPSEKLRRLEQILRSQDSGSKVLIFCTTKRMCDQLARTLTRQFGASAIHGDKSQSEREKVLSHFRSGRSPILVATDVAARGLDIKDIRVVINYDFPTGIEDYVHRIGRTGRAGATGVAYTFFCDQDSKYAADLIKILEGANQRVPRDLADMASRGGRGGRKRNRWATRSDRGGSHSELDSRYGGRDGLSGSSGRLDSSRSSRRHDYGDDGRSRRSGRGRSRSRSRSDSDRYSRSPKRSRRHSRSRTRSRSRSRSRSYTRNRRASRSRSRSPGASRRHERSATGSGSALPDSGHGERKRTPEADPSRNHTNHSDPKDDRHPEDGKVGKVDLDRSPTPQDKSGPYSPAYNGKTSRSVSPGNQVEGNNKAAEVSKNPDPSSPPHHGKTREDEEEGMIDEDGEIADDPRANATVQNGGDN | Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 87980
Sequence Length: 792
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
|
Q3EBD3 | MNEEGCVPHNSDVVKQKSIDQRAPLSGEPKCVICSRYGEYICDETNDDVCSLECKQALLRRVDSARVFPATDECFYVRDPGSSSHDAQLLRRKLDIHVQGQGSAVPPPVLTFTSCGLPPKLLLNLETAGYDFPTPIQMQAIPAALTGKSLLASADTGSGKTASFLVPIISRCTTYHSEHPSDQRRNPLAMVLAPTRELCVQVEDQAKMLGKGLPFKTALVVGGDPMSGQLYRIQQGVELIIGTPGRVVDLLSKHTIELDNIMTFVLDEVDCMLQRGFRDQVMQIFQALSQPQVLLFSATISREVEKVGGSLAKEIILVSIGNPNKPNKAVNQLAIWVDAKQKKQKLFDILRSQNHFKPPAVVYVSSRVGADLLANAITVVTGVKALSIHGEKPMKERRDVMGSFLGGEVPVLVSTGVLGRGVDLLVVRQVIVFDMPSTIKEYIHVIGRASRMGEKGTAIVFVNEDDRNLFPDLVAALKSSGAAIPKELINLTSREMHNKKRRVGY | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55218
Sequence Length: 505
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q0E2Z7 | MEQEENHSADHLSAQPGNGNELEESSVKERCFEQREALVGEPRCVICGRYGEYICDQTDDDICSVECKTILLSKLSAETRPVVKAAKRVNLPVGDESFCIRDENFPKIPSMHDGQIASLRSKLDICVKGEDVPDPIMCFSSSGLPEKLVLNLEAAGYVMPTPVQMQVIPSSICNRSLLVSADTGSGKTASFLVPIIAHCSHVRSERCTDKQGPLAIVLAPTRELCLQVEEQAKVLGKGLPFKTALVVGGDPLAQQIYRIENGIELIVGTPGRLIDLLMKHNVDLNKVDVFVLDEVDCLLERGFRDQVMQIFQALSHPQVMMFSATVNSEVEKMSNSLAKNAIHISCGNPSRPNKSVKQVVIWVESKQKKQKIFEIMTSKQHFKPPAVVFVSSRIGADLLSEAITVATGLKVVSIHGDKTMNERRESLRRFLTGEVSVVVCTGVLGRGMDLLKVRQVILFDMPNSIDEYVHQVGRASRMGVEGMAIVFVNEEDRNLFRELVQILKTAGAPIPRELANSKYTTGIPLGGGKKRKLKSR | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 59046
Sequence Length: 536
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q9SZB4 | MEVDDGYVEYVPVEERLAQMKRKVVEEPGKGMMEHLSDKKKLMSVGELARGITYTEPLSTWWKPPLHVRKMSTKQMDLIRKQWHITVNGEDIPPPIKNFMDMKFPSPLLRMLKDKGIMHPTPIQVQGLPVVLSGRDMIGIAFTGSGKTLVFVLPMIILALQEEIMMPIAAGEGPIALVICPSRELAKQTYDVVEQFVASLVEDGYPRLRSLLCIGGVDMRSQLDVVKKGVHIVVATPGRLKDILAKKKMSLDACRLLTLDEADRLVDLGFEDDIRHVFDHFKSQRQTLLFSATMPAKIQIFATSALVKPVTVNVGRAGAANLDVIQEVEYVKQEAKIVYLLECLQKTTPPVLIFCENKADVDDIHEYLLLKGVEAVAIHGGKDQEDRDYAISLFKAGKKDVLVATDVASKGLDFPDIQHVINYDMPGEIENYVHRIGRTGRCGKTGIATTFINKNQSEITLLDLKHLLQEAKQRIPPVLAELNGPMEETETIANASGVKGCAYCGGLGHRILQCPKFEHQKSVAISSSRKDHFGSDGYRGEV | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 60258
Sequence Length: 542
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q9SF41 | MLEKSKSRKENDRKDRDRSKKENGRRDTTEMRSRVKRCDSEEEERIRIRRDRKSSDFEEEEYERDSKRRGEDKGRGRRERDRDRGKYLKRDRERREREKEKGRKKQKKERSREDCNEESDDVKCGLKRKRTERSRHGDDDVEKKTRDEQVEDEQKQLAEEVEKRRRRVQEWQELKRQNEEAQIESKGPETGKAWTLDGESDDEVKSDSEMDVDRDTKLENGGDAKMVASENETAVTVSENGGDRAADEDEIDPLDAFMNTMVLPEVEKLSNIVIDGILDFKMNGKETGDQAKKGFNKAALGRIIQGEDSDSDYSEPKSDDDPSLDEDDEEFMKRVKKTKAEKLSLVDHSKIEYEPFRKNFYIEVKDISRMTQDAVNAYRKELELKVHGKDVPRPIQFWHQTGLTSKILDTLKKLNYEKPMPIQAQALPIIMSGRDCIGVAKTGSGKTLGFVLPMLRHIKDQPPVEAGDGPIGLVMAPTRELVQQIYSDIRKFSKALGIICVPVYGGSGVAQQISELKRGTEIVVCTPGRMIDILCTSSGKITNLRRVTYLVMDEADRMFDMGFEPQITRIVQNIRPDRQTVLFSATFPRQVETLARKVLNKPVEIQVGGRSVVNKDITQLVEIRPESERFSRLLELLGEWYEKGKVLVFVRSQEKSISDFKSDVCNLLIATSVAARGLDVKELELVVNFDAPNHYEDYVHRVGRTGRAGRKGCAVTFISEDDAKYAPDLVKALELSEQPVPDDVKAVAEGFMAKVKQGIEQAHGTGYGGSGFKFNEEEDEVRKAAKKAQAKEYGFEEEKSDSEDENDVVRKAGGDISQQQITLAQIAAIASAASKAPVTANQLLPNGGGLATEPGIPPTDGAGRVAAMIAAANVQQYLAKIQADAIPEHYEAELEINDFPQNARWKVTHKETLGPISEWSGASITTRGKFYEAGRIPGPEERKLYLFVEGPTEISVKTAKAELKRVLEDITNQTFSLPGGAQSGRYSVL | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 111625
Sequence Length: 989
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q0J7Y8 | MEEEEVVVVVDEEESERRRQKMIEEEKKRLDEEMELRRRRVKEWQEQKRLEEEEAKRREQEAAAGAGTPAAAAGADGDSNAGKKWTLDGEESDEEGYKEDSQNAEDDGGITADLPSEVNDANVAAPMEEDEIDPLDAFMSSMVLPEVAKLETAVASMESMPASNMGDKNGKSAKDAVSNGDKKGQKKAMGRIMQGDDSDSDYDDDDDDEGGSKDEDDEEFMKRVKKTKVEKLAIVDHSKIEYQPFRKNLYIEVKDITMMTGEEVATYRKNLELKVHGKDVPKPIKTWVQSGLTSKLLDTIKKLGFEKPMPIQAQALPIIMSGRDCIGIAKTGSGKTLAFVLPMLRHVKDQPPVVPGDGPIGLIMAPTRELVVQIHSDIKKFAKSLGINCVAIYGGSGVAQQISELKRGAEIVVCTPGRMIDILCTSSGKITNLRRVTFLVMDEADRMFDMGFEPQITRIVQNTRPDRQTVLFSAIFPRQVEILARKVLTKPVEIQVGGRSVVNKDITQLVEVRPENERFLRLLELLGEWFDRGKILVFVHSQDKCDSLLKDLFQRGYPCLSLHGGKDQTDRESTLADFKSNLELVVNYDVPNHYEDYVHRVGRTGHAGRKGFAVTFISDEEERYAPDLAKALELSEQAVPQDLKGLADRFMAKVKQGTEQAHGTGYGGSGFKFNEEEDEARRSAKKAQAREYGYEEDKSDSDSDEEGGVRKAGGDLAAQAIAAAQAAATLAAAKAASNANQQVQSTNAGSLLSIPVVANAPNNEATARALQAALNIQQNLARIQAHVVPEHYEVELDINDFPQNARWKITHKETLGPIQDWTEAAITTRGTFIPQGKIVGANERKLYLFIEGPTELSVKKAKSELKRVLEDCANHALNLPGSAQTGKTANSEMQGFLVKVFLGRWTAILVFLDDGVICNIRAEKLDKWQVRVFYVKVADPLGYSITE | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 104832
Sequence Length: 947
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
O05263 | MKRKASIMFVHQDKYEEYKQRHDDIWPEMAEALKAHGAHHYSIFLDEETGRLFAYLEIEDEEKWRKMADTEVCQRWWKSMAPLMKTNSDFSPVAIDLKEVFYLD | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12575
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
Q8A044 | MKREAFKMYLKPGYEAEYEKRHAAIWPELKALLSKNGVSDYSIYWDKETNILFAFQKTEGEGGSQDLGNTEIVQKWWDYMADIMEVNPDNSPVSIPLPEVFHMD | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12123
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
Q0BA68 | METIAFRMRLHPGKRDEYRRRHDAIWPELADALRAAGISDYWIFLDEDTHHLFAVLKRPIGHRIAQLAETDVMRRWWAYMADLMATGPDGRPVEKSLEPMFHLE | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12314
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
A6LQL0 | MIQKAFKMKLFEGKEEEYKKRHNEIWPDLVKELKSHGTSKYLIFYDKDTNILFSYIEMENEELWDEIAETDACKKWWAFMKDIMETNPDNSPISVELSNVFNLK | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12547
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
A7ML65 | MIRKAFVMQVNPDAHEEYQRRHSPIWPELEAVLKQHGAHHYAIWLDAQRHLLFATVEIESEARWNAVAQTEVCQRWWKHMREIMPSNPDNSPVSQELKNVFYLE | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12446
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
A8LS71 | MEKIAFKMMLNPGCREEYIKRHDAIWPELVDLLRKAGVSDYSIHLDPETDTLFAVLWRKEGHGMDDLPSHPVMQKWWAHMADIMQTQPDNAPVVTPLDTVFHMP | Function: Involved in the anomeric conversion of L-rhamnose.
Catalytic Activity: alpha-L-rhamnose = beta-L-rhamnose
Sequence Mass (Da): 12083
Sequence Length: 104
Pathway: Carbohydrate metabolism; L-rhamnose metabolism.
Subcellular Location: Cytoplasm
EC: 5.1.3.32
|
Q53QZ3 | MQKSTNSDTSVETLNSTRQGTGAVQMRIKNANSHHDRLSQSKSMILTDVGKVTEPISRHRRNHSQHILKDVIPPLEQLMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSSRRIEFYKESKQQALSNMKTGHKPESVDLCGAHIEWAKEKSSRKNVFQITTVSGNEFLLQSDIDFIILDWFHAIKNAIDRLPKDSSCPSRNLELFKIQRSSSTELLSHYDSDIKEQKPEHRKSLMFRLHHSASDTSDKNRVKSRLKKFITRRPSLKTLQEKGLIKDQIFGSHLHKVCERENSTVPWFVKQCIEAVEKRGLDVDGIYRVSGNLATIQKLRFIVNQEEKLNLDDSQWEDIHVVTGALKMFFRELPEPLFPYSFFEQFVEAIKKQDNNTRIEAVKSLVQKLPPPNRDTMKVLFGHLTKIVAKASKNLMSTQSLGIVFGPTLLRAENETGNMAIHMVYQNQIAELMLSEYSKIFGSEED | Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54544
Sequence Length: 475
Domain: The PH domain is required for localization to the membrane.
Subcellular Location: Cytoplasm
|
Q811M1 | MEKRTSCSVQTSTNCDNSLEILNSAHQATGAVQMRIKNANSHQDRQSQTKSMILTDAGKVTEPISRHRRNHSQHVLKDVIPPLEHPMVEKEGYLQKAKIADGGKKLRKNWSTSWIVLSGRKIEFYKDSKQQALPNMKTRHNVESVDLCGAHIEWAKEKSSRKSVFQITTVSGNEFLLQSDIDFLILDWFQAIKNAIDRLPKNPSCGSLELFNLQRSSSSELPSHCHIDRKEQKPEHRKSFMFRLHHSASDTSDKNRVKSRLKKFISRRPSLKTLQEKGLIKDQIFGSHLHTVCEREHSTVPWFVKQCIEAVEKRGLDVDGIYRVSGNLATIQKLRFIVNQEEKLNLDDSQWEDIHVVTGALKMFFRELSEPLFPYSFFERFVEAIKKQDSNEKIETMRSLVKRLPPPNHDTMKILFRHLTKIVAKASQNLMSTQSLGIVFGPTLLRAENESGNVAVHMVYQNQIAEFMLTEYDKIFSSEED | Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has activity toward RAC1. Overexpression results in an increase in actin stress fibers and cell contraction (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55339
Sequence Length: 481
Domain: The PH domain is required for localization to the membrane.
Subcellular Location: Cytoplasm
|
Q68EM7 | MKKQFNRMKQLANQTVGRAEKTEVLSEDLLQIERRLDTVRSICHHSHKRLVACFQGQHGTDAERRHKKLPLTALAQNMQEASTQLEDSLLGKMLETCGDAENQLALELSQHEVFVEKEIVDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKTLPEMRAHQDKWAEKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFNLYEEWTQVASVQDQDKKLQDLWRTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWARNEGTLAEMAAATSVHVVAVIEPIIQHADWFFPEEVEFNVSEAFVPLTTPSSNHSFHTGNDSDSGTLERKRPASMAVMEGDLVKKESFGVKLMDFQAHRRGGTLNRKHISPAFQPPLPPTDGSTVVPAGPEPPPQSSRAESSSGGGTVPSSAGILEQGPSPGDGSPPKPKDPVSAAVPAPGRNNSQIASGQNQPQAAAGSHQLSMGQPHNAAGPSPHTLRRAVKKPAPAPPKPGNPPPGHPGGQSSSGTSQHPPSLSPKPPTRSPSPPTQHTGQPPGQPSAPSQLSAPRRYSSSLSPIQAPNHPPPQPPTQATPLMHTKPNSQGPPNPMALPSEHGLEQPSHTPPQTPTPPSTPPLGKQNPSLPAPQTLAGGNPETAQPHAGTLPRPRPVPKPRNRPSVPPPPQPPGVHSAGDSSLTNTAPTASKIVTDSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL | Function: Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95437
Sequence Length: 881
Domain: The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions.
Subcellular Location: Membrane
|
Q9FMM4 | MQGERASLGYLSEALNFEHGSSSSNGVIDHWENIHSLGDNDLQDYMIANSESNTSLANSVYHEQQGLRRFSLGEASSSGTKDEASSHNEQRMETRCFDGRGNEIIDLDPVFAQPSGTNQPVQNVNLNAEYIEIHEDINPYRGRSGFIEANGPGTRVSQPGRSFEENGVGTGSSVEGRRASCKRKALEGSISQSSSGGYHDFQRGESSSWTPGSTVFRPGNGLNISGSLDNGPRGMVSGTVPNFPVSAPNFPVSAIAESSSRNICVRSNPSDHQETVNPSTFAAGTVVRRPVPPSQLNLSRHLPADQHSLDLRPGQSFVVSRNPNSTPVSIPPGSRTMLPPFRWTGSSLVGGTSNSTAPVERNLHLDETRSRSIPGNTLEIPMFAAPEVGNFARSQSSRNVTNGNLNSASSVSRTGSTTSVPPPPPPSSNLAWTSYQNSPHYQRRRTERSELARRSLLSSLAADATNQRSGDHPTLRSLAPPASSDGLVLQPGGDNSQMHNRAYSRAGPLFDRQGDSVVGIPHPLRALAAASRGRSRLMVSQMQNVLDVMRRDANNNNLRLEDVMLLNHSVLFDGATGHDRYRDMRLDVDNMSYEELLALEERIGDVCTGVNEETISNRLKQRKYKSNTKSPQDAEPCCVCQEEYTEGEDMGTLECGHEFHSQCIKEWLKQKNLCPICKTTGLNTAKKRRIA | Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 75284
Sequence Length: 691
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
|
P25888 | MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLTKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASDQVTQHVHFVDKKRKRELLSHMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQNGRQQRGGGGRGQGGGRGQQQPRRGEGGAKSASAKPAEKPSRRLGDAKPAGEQQRRRRPRKPAAAQ | Function: DEAD-box RNA helicase involved in ribosome assembly. Has RNA-dependent ATPase activity and unwinds double-stranded RNA. May play a role in the interconversion of ribosomal RNA-folding intermediates that are further processed by DeaD or SrmB during ribosome maturation.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49989
Sequence Length: 454
Subcellular Location: Cytoplasm
EC: 3.6.4.13
|
Q9RPT1 | MHPYFSLAGRIALVTGGSRGIGQMIAQGLLEAGARVFICARDAEACADTATRLSAYGDCQAIPADLSSEAGARRLAQALGELSARLDILVNNAGTSWGAALESYPVSGWEKVMQLNVTSVFSCIQQLLPLLRRSASAENPARVINIGSVAGISAMGEQAYAYGPSKAALHQLSRMLAKELVGEHINVNVIAPGRFPSRMTRHIANDPQALEADSASIPMGRWGRPEEMAALAISLAGTAGAYMTGNVIPIDGGFHL | Function: Required for the synthesis of the beta-hydroxy acid moiety of rhamnolipids.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Mass (Da): 26831
Sequence Length: 256
Pathway: Lipid metabolism; rhamnolipid biosynthesis.
EC: 1.1.1.100
|
P54291 | MIELLSESLEGLSAAMIAELGRYRHQVFIEKLGWDVVSTSRVRDQEFDQFDHPQTRYIVAMSRQGICGCARLLPTTDAYLLKDVFAYLCSETPPSDPSVWELSRYAASAADDPQLAMKIFWSSLQCAWYLGASSVVAVTTTAMERYFVRNGVILQRLGPPQKVKGETLVAISFPAYQERGLEMLLRYHPEWLQGVPLSMAV | Function: Required for the synthesis of BHL (N-butanoyl-L-homoserine lactone), and HHL (N-hexanoyl-L-homoserine lactone) autoinducer molecules which bind to RhlR and thus acts in elastase biosynthesis regulation.
Catalytic Activity: a fatty acyl-[ACP] + S-adenosyl-L-methionine = an N-acyl-L-homoserine lactone + H(+) + holo-[ACP] + S-methyl-5'-thioadenosine
Sequence Mass (Da): 22630
Sequence Length: 201
EC: 2.3.1.184
|
Q9LPG6 | MDDTTYKPKNILITGAAGFIASHVANRLIRNYPDYKIVVLDKLDYCSDLKNLDPSFSSPNFKFVKGDIASDDLVNYLLITENIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDAAVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKMIPKFILLAMSGKPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEIGHVYNVGTKRERRVIDVARDICKLFGKDPESSIQFVENRPFNDQRYFLDDQKLKKLGWQERTNWEDGLKKTMDWYTQNPEWWGDVSGALLPHPRMLMMPGGRLSDGSSEKKDVSSNTVQTFTVVTPKNGDSGDKASLKFLIYGKTGWLGGLLGKLCEKQGITYEYGKGRLEDRASLVADIRSIKPTHVFNAAGLTGRPNVDWCESHKPETIRVNVAGTLTLADVCRENDLLMMNFATGCIFEYDATHPEGSGIGFKEEDKPNFFGSFYSKTKAMVEELLREFDNVCTLRVRMPISSDLNNPRNFITKISRYNKVVDIPNSMTVLDELLPISIEMAKRNLRGIWNFTNPGVVSHNEILEMYKNYIEPGFKWSNFTVEEQAKVIVAARSNNEMDGSKLSKEFPEMLSIKESLLKYVFEPNKRT | Function: Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II). Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose . Required for the normal seed coat epidermal development .
Catalytic Activity: UDP-alpha-D-glucose = H2O + UDP-4-dehydro-6-deoxy-alpha-D-glucose
Sequence Mass (Da): 75226
Sequence Length: 667
Domain: The dehydratase activity is contained in the N-terminal region while the epimerase and reductase activities are in the C-terminal region.
Pathway: Carbohydrate biosynthesis.
|
Q9LH76 | MATYKPKNILITGAAGFIASHVANRLVRSYPDYKIVVLDKLDYCSNLKNLNPSKSSPNFKFVKGDIASADLVNYLLITEEIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDASVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMNGKPLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEVNHVYNIGTTRERRVIDVANDISKLFGIDPDSTIQYVENRPFNDQRYFLDDQKLKKLGWCERTNWEEGLRKTMEWYTENPEWWGDVSGALLPHPRMLMMPGDRHSDGSDEHKNADGNQTFTVVTPTKAGCSGDKRSLKFLIYGKTGWLGGLLGKLCEKQGIPYEYGKGRLEDRASLIADIRSIKPSHVFNAAGLTGRPNVDWCESHKTETIRVNVAGTLTLADVCRENDLLMMNFATGCIFEYDAAHPEGSGIGFKEEDKPNFTGSFYSKTKAMVEELLREFDNVCTLRVRMPISSDLNNPRNFITKISRYNKVVNIPNSMTILDELLPISIEMAKRNLRGIWNFTNPGVVSHNEILEMYKSYIEPDFKWSNFNLEEQAKVIVAPRSNNEMDGAKLSKEFPEMLSIKDSLIKYVFEPNKRT | Function: Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II) . Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose (By similarity).
Catalytic Activity: UDP-alpha-D-glucose = H2O + UDP-4-dehydro-6-deoxy-alpha-D-glucose
Sequence Mass (Da): 74914
Sequence Length: 664
Domain: The dehydratase activity is contained in the N-terminal region while the epimerase and reductase activities are in the C-terminal region.
Pathway: Carbohydrate biosynthesis.
|
B7MG11 | MNALLTNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASHPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTADQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDTMLYSDALDQRLAMFKSGKNGPRVKGSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
Catalytic Activity: 2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate
Sequence Mass (Da): 28911
Sequence Length: 267
EC: 4.1.2.53
|
Q8XE09 | MNALLTNPFKERLRKGEVQIGLWLSSTTAYMAEIAATSGYDWLLIDGEHAPNTIQDLYHQLQAVAPYASQPVIRPVEGSKPLIKQVLDIGAQTLLIPMVDTADQARQVVSATRYPPYGERGVGASVARAARWGRIENYMAQVNDSLCLLVQVESKTALDNLDEILDVEGIDGVFIGPADLSASLGYPDNAGHPEVQRIIETSIRRIRAAGKAAGFLAVAPDMAQQCLAWGANFVAVGVDTMLYSDALDQRLAMFKSGKNGPRIKGSY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
Catalytic Activity: 2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate
Sequence Mass (Da): 28916
Sequence Length: 267
EC: 4.1.2.53
|
Q9Z3Q5 | MGNNENGGISFCVFVVVIGFGTGAVAQEPANQSEAVTSLEEIVVTGGRSAQQISEIARTIYVVDSDQIQAEARSGKTLQQILGETIPSFDPASDGARTSFGQNLRGRPPLILVDGVSMNSARSLSRQFDAIDPFNIERVEVLSGATAIYGGNATGGIINIITKKGKDAEPGLHAEVTGGMGSGFAGSQDFDRNAAGAVTYNSENWDARLSIAGNRTGAFYDGSGTLLIPDITQTSTAFNERIDLMGSIGYQIDDDRRVEFSGQYFDSKQDSDYGLYYGPFFAALADPSLFETRSGYESDFNPQTRRSMLNVTYTDNDVFGQQLLLQGSYRTERIKFHPFPASGNSETGPYFYGSSQDTDYYGIRAALVAEPTDALKITYGIDADMDSFTARQNIFDMVAAGQSGGLDFNTIGKTGLYPSIDVSTVAGFAEASYEATDRLTLNGGVRYQFVNTEVSDFIGAAQQVAILQGRATSADTIPGGEVNYDAALFSAGATYQLTNTQQVYANFSQGFELPDPAKYYGIGNYSFSGGHYTLVNSVNVGDSALEAIKTNSFEIGYRLDDGTFNLETAAYYSLSDRSINLNRSSLAVEIIDRERRVYGIEGKAGVKLDHGFDVGVLGHWVRTEVKGADGWEKDSVGSASVSKLGGYVGWTNDALSLRFSGQHIFELTDAQNFTIDDYTLFDLTGGYRFENTDTTLNFGIHNVFDTDYTTVWGSRAKALYGGLADESVFDYKGRGRTFAVSLTKVF | Function: Receptor for the siderophore rhizobactin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80634
Sequence Length: 746
Subcellular Location: Cell outer membrane
|
E1W9W8 | MPGSTRKLPVWLPILVLLIAMSSIQSGASLAKSLFPLVGAPGVTALRLALGTLILIAFFKPWRLRFAKEQRLPLLFYGLSLGGMNYLFYLSIQTVPLGIAVALEFTGPLAVALFSSRRPVDFIWVVLAVLGLWFLLPLGQDMSHVDLTGAALALGAGACWAVYILTGQRAGAEHGPATVAVGSLIAAIIFVPIGAVQAGDALWHWSILPLGLAVAVLSTALPYSLEMIALTRLPTRTFGTLMSMEPALAAVSGMIFLGETLTGIQILALCAIIAASMGSTLTIRREPQIKQVDVK | Function: Involved in the efflux of threonine and homoserine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31228
Sequence Length: 295
Subcellular Location: Cell inner membrane
|
P0AG36 | MTLEWWFAYLLTSIILSLSPGSGAINTMTTSLNHGYRGAVASIAGLQTGLAIHIVLVGVGLGTLFSRSVIAFEVLKWAGAAYLIWLGIQQWRAAGAIDLKSLASTQSRRHLFQRAVFVNLTNPKSIVFLAALFPQFIMPQQPQLMQYIVLGVTTIVVDIIVMIGYATLAQRIALWIKGPKQMKALNKIFGSLFMLVGALLASARHA | Function: Conducts the efflux of homoserine and homoserine lactone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22427
Sequence Length: 206
Subcellular Location: Cell membrane
|
Q9L6N6 | MTFEWWFAYLLTSTLLSLSPGSGAINTMTTSINHGYRGAVASIAGLQTGLGIHIVLVGVGLGTLFSRSLLAFEILKWAGAAYLIWLGIQQWRAAGAIDLHTLAQTQSRGRLFKRAIFVNLTNPKSIVFLAALFPQFIMPQQPQLAQYLILGVTTIVVDMVVMTGYATLAQRIAAWIKGPKQMKALNKAFGSLFMLVGALLASARHA | Function: Conducts the efflux of homoserine and homoserine lactone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22322
Sequence Length: 206
Subcellular Location: Cell membrane
|
P0AG39 | MLMLFLTVAMVHIVALMSPGPDFFFVSQTAVSRSRKEAMMGVLGITCGVMVWAGIALLGLHLIIEKMAWLHTLIMVGGGLYLCWMGYQMLRGALKKEAVSAPAPQVELAKSGRSFLKGLLTNLANPKAIIYFGSVFSLFVGDNVGTTARWGIFALIIVETLAWFTVVASLFALPQMRRGYQRLAKWIDGFAGALFAGFGIHLIISR | Function: Conducts the efflux of threonine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22474
Sequence Length: 206
Subcellular Location: Cell inner membrane
|
H2DF87 | MDTSTSAYAPLPGEDPLFSGHPPASLRRSWKGFAVIFASVLFLLSLVGLIIHQGPQQPPDVMPDKQDEHHHPQSTTPASETTASWEPRGKALGVSAKSNPPVSDELSYNWTNAMFSWQRTAFHFQPERNWMNDPNGPLFYKGWYHLFYQYNPDSAIWGNITWGHAVSTDLIHWLYLPIAMVADQWYDANGVWSGSATLLPDGQIVMLYTGDTVDAVQVVCLAHPANLSDPLLLDWVKYSGNPVLTPPPGILTTDFRDPTTAWTGPDGKWRITIGSKVNTTGISFVYHTEDFKTYNMSKGVLHAVPGTGMWECIDFYPVAINGSKGVETSVNNPSVKHVLKASLDNTKVDHYALGTYFEENETWVPDNPGLDVGIGLRYDYGRYYASKTFYDQNKERRILRGWINETDTESDDLAKGWASVQTIPRTVLFDNKTGTNLIQWPVEEIEELRLNNTDFSDVLVEAGTVVELDIGTATQLDILVEFELEPLESSETVNSSVGCGGGAVDRGTFGPFGILVIADETLTELTPIYFNLANSTEGDVITYFCADERRSSKAPDVFKQVYGSEVPVLDGEKHFARVLRALRKEVGR | Function: Acidic vacuolar invertase involved in light-induced bud burst .
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Sequence Mass (Da): 65375
Sequence Length: 588
Subcellular Location: Membrane
EC: 3.2.1.26
|
H2DF88 | MDTNTTSYTPLPGDPFLSGPPETPRRPLKGFAVIFASVIFLMSLVALIIHQGPQQPPDVMPDKQDEHHHPQSTTNTMLSWQRTAFHFQPEKNWMNDPNGPMYYKGWYHFFYQYNPRGAVWGNIVWGHAVSRDLIHWLHLPLAMVADQWYDINGVWTGSATILPNDQIVMLYTGSTNESVQVQCLAYPADHKDPLLTKWVKYSGNPVLVPPPGIGVKDFRDPTTAWYITEGKWRITIGSKVNKTGISLVYDTKDFIKYEQLDGVLHAVPGTGMWECIDFYPVSKTSDKGLDTSQNGADVKHVMKASLDDDRNDYYALGSYNEKTGKWVPDNQKIDVGIGIRYDYGKFYASKTFYDQNKQRRVLWGWIGESDSENADVKKGWASLQGIPRTVLFDQKTGSNLLQWPVEEIEKLRLNKKNFDKVQVKAGSVVPLDVGTATQLDIVAEFQLDQKVVESAAETNEEFSCQTSGGAAKRGALGPFGLLVLADDSLSERTPVYFYVVKGSGGTVNTYFCADQTRSSVATDVVKQVSGSYVPVLKGETLSLRILVDHSIIESFAQGGRTTITTRVYPTQAIYGAARLFLFNNATDTSFTASLQIWQMNSAFIRPFSPDAASHSSFTPVTVFIKFIVPFGIFLTLYFVR | Function: Vacuolar invertase.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71647
Sequence Length: 640
Subcellular Location: Membrane
EC: 3.2.1.26
|
Q8NHV9 | MARSLVHDTVFYCLSVYQVKISPTPQLGAASSAEGHVGQGAPGLMGNMNPEGGVNHENGMNRDGGMIPEGGGGNQEPRQQPQPPPEEPAQAAMEGPQPENMQPRTRRTKFTLLQVEELESVFRHTQYPDVPTRRELAENLGVTEDKVRVWFKNKRARCRRHQRELMLANELRADPDDCVYIVVD | Function: Transcription factor maybe involved in reproductive processes. Modulates expression of target genes encoding proteins involved in processes relevant to spermatogenesis.
Sequence Mass (Da): 20542
Sequence Length: 184
Domain: Mutagenesis of amino acids 147 to 164 and 155 to 164 lead to a major cytoplasmic localization, with only minor localization in the nucleus.
Subcellular Location: Nucleus
|
Q852U6 | MTSASELFSTRRSRPGRSDPALESDTSSYRHHSHHHHRRHGVHHHNQRHDSDGCDPLRRPTPRLRRFFHHPIQERSRPIRDVQGTSQYLNTDSTDTETQSSSFVNLNGSERLPGAVLLARDRLFERLRGVSLSSNSRSNRVSLDDQRESSFHSIDGDPIFQLAGLQVTYECNKKPQGLTQDAINCLHRQTFSSAEVKSEMRDCSICLESFTKGDMLISLPCTHSFHSSCLNPWLRACGDCPCCRRAIAKE | Function: Probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 28447
Sequence Length: 250
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
|
Q9XVW1 | MSSSPHTHTLIIMERLSEVRLYSSPMTSVLNSNLSSCLTNAFIPDTVRMASSPLLAWMTLVVIGTLAPVSVFSCLSLKRSVKELLTERSSKLDVLDIFRFVAILWVMLNHTGSEGRIDILDRLPSADAFKSAMHDHPIFGALMGNSALGVEIFLVLSGLLAARSWLRKADEPFFQHWKSFIARRLLRLAPSMFIFVYIAAGPIMNALLPRYSSSMVSACGFWGILSHVTFTSNWQSTPTCMGYLWYLGLDMQLYMVAPIFLNLLHKFPKRGMALTITTIIASMVIRAGYCTAYGTCNQSDVDIPFISYPGQDAETLKSIYAGLWDMYSRPYTKCGPFLIGLLLGYITVSSKYIMVSTTSKTLFRSSLIVAIATIYAILPEYWNPNAGNTLYNTVYTAVFRSVFAMAISGMIAALYFRQEYRPTNPIFAMLAKLTYNAYLLHMPVVYIFNWLPFLQAATSPIHLLLVLPFVAILSFIAALIFYLFIEAPIGHLTSQYATRLGL | Function: Involved in the response to variation in environmental oxygen levels by inhibiting hif-1-mediated gene transcription in a vhl-1-independent manner . Plays a role in susceptibility to killing mediated by P.aeruginosa and by pore-forming toxins produced by B.thuringiensis . Probably by preventing hif-1 transcriptional activity, regulates behavioral responses, such as locomotion speed following acute reoxygenation . Plays a role in normal egg-laying probably by regulating spermatogenesis and in body morphogenesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56103
Sequence Length: 502
Subcellular Location: Endoplasmic reticulum membrane
|
O88011 | MTEKIGVLGKKTTQRTDVERIVVTPLPTVYGKFRAFGYFDHERGDEQVALVHGDLGAEDVLTRLHSECLTGDAFGSQHCECGAQLASALRQVADAGSGIVVYLRGHEGRGIGLLAKLRAMALQAEGLDTVEANLALGLPVDARDYGVAARILDDLGVRSVRLMSNNPRKREALVRHGIRVAEQVPLLIPPCESNITYLRTKRERLDHHLPHLDAAMAHVSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 24087
Sequence Length: 221
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
|
O68248 | HSECLTGDALGSLKCDCGEQLEFALQNISLLGGMIIYLRQEGRNIGLFNKVNAYALQDQGFDTIEANHQLGFKSDERSYEVVETILEHFKIDKIRLLTNNPKKMSCLKNIMIIERWPIIIPSNNHNVDYLKTKKEMMGHLL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 16138
Sequence Length: 141
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
|
Q97B83 | MIELYSNAKLPTEFGLFRIYTFVNDENKDHAVIVRGDPRGKENVPLRIHSECLTGDVLGSLRCDCRDQLIQSLRYLGRQEYGMLIYLRQEGRGIGLLNKIKAYSLQDMGADTVEANLKLGLPVDSRNYSFAAEVLRYFEIKSIYIMTNNPEKIKSLIESGINVKGRIPIFSDPTPYDKFYLETKKTKLGHEIENI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 22328
Sequence Length: 195
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
|
Q9KSJ3 | MAEVRARVDFKVGAKSNIDAEILSFHGLQSDKEHVAVIFKSADTTQEAPLVRMHSECLTGDVFHSSRCDCGEQLEETITRMGQSGGIILYLRQEGRGIGLYNKIDAYRLQSQGMNTYEANNHLGFGDDLRDFTEAAQMLQALGVKKIRLVTNNPKKIRELQEHGIEIVEVVHTSAHIKDGNENYLKAKVSHGKHQLKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Catalytic Activity: GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 3 H(+) + 2 phosphate
Sequence Mass (Da): 22158
Sequence Length: 198
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
EC: 3.5.4.25
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.