ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q9VVW5 | MPETEHETCSKEWLQSQLRSLDSKDLILLDCRGSHEYSESHIRGAVNLCIPSIVLRRLAVGKIDLASTIKSPELKQRIQSGYKLCWFILYNGEGVPGQNQEIAGAGSLAVAMDSIISILHRRLKQDGCRVVALQDGFNNFRQAFPEWCEDDNQTHSKEIESSRNVQTDQLMGLRSLRISTTQSDSACSSSAESSDCESSSHHHHHHSHHNYNEAPVEIIPGLLFLGNATHSCDSEALKKYNIKYVLNVTPDLPNKFKESGDIKYLQIPITDHYSQDLAIHFPDAIQFIEEARSASSVVLVHCLAGVSRSVTVTLAYLMHTRGLSLNDAFAMVRDRKPDVSPNFHFMQQLLSFESQLRLRPGSRFSCSCIAPDCNCMQTTGFMATHLANATGVSPDSGIEFDRWTPSDTGLK | Function: Negatively regulates the activity of members of the MAP kinase family in response to changes in the cellular environment. Has a specificity for the ERK family. Acts as negative regulator in a variety of developmental processes including cell differentiation and proliferation controlled by the Ras/ERK pathway. Suppresses the photoreceptor cell differentiation and wing vein formation. Required for proper oogenesis and early embryogenesis. Functions autonomously in a subset of photoreceptor progenitor cells in eye imaginal disks. Appears also to be required in surrounding non-neuronal cells for ommatidial patterning and photoreceptor differentiation. Plays a role in the maintenance of epithelial integrity during tracheal development.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 45792
Sequence Length: 411
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
Q9VWF4 | MEQSQSQRQAWPSSSAGGGKAQDSGVLTREDFDGGPVSIDEVDTGLFLGNLTAATHMETLRSFKITHILTLDSVPLPQHILEASFLTTKYIQIADMPREDILQHLEGCVDFISSALAQQGNVLVHCYFGVSRSSSTVIAYMMKRHNLDFLPAYELVKAKRRFVQPNAGFVSQLKLFRRMGCKIDPNCQRYKIHRLRLAGEQMRKAKILPQSFHSVVRPDPDITRENPEPIVFRCRRCRRVLASKSHVLEHKPRDRPPQEVVPKEKEEVAAAKLPAQSHDQAENHHGARMLEQLSERIRQSSLGSPGHESTPNYCRSILFVEPIAWMHRIMLNTQGRLYCPKCEQKLGNFSWINACKCPCGETMTPAFYLIPSKVELSKAVQNVQTTV | Function: Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues. May suppress bsk/JNK activation during the immune response.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 43742
Sequence Length: 387
Subcellular Location: Nucleus
EC: 3.1.3.16
|
Q53UH4 | MGSQATTYHMAMYPWFGVGHLTGFFRLANKLAGKGHRISFLIPKNTQSKLESFNLHPHLISFVPIVVPSIPGLPPGAETTSDVPFPSTHLLMEAMDKTQNDIEIILKDLKVDVVFYDFTHWLPSLARKIGIKSVFYSTISPLMHGYALSPERRVVGKQLTEADMMKAPASFPDPSIKLHAHEARGFTARTVMKFGGDITFFDRIFTAVSESDGLAYSTCREIEGQFCDYIETQFQKPVLLAGPALPVPSKSTMEQKWSDWLGKFKEGSVIYCAFGSECTLRKDKFQELLWGLELTGMPFFAALKPPFEAESIEAAIPEELKEKIQGRGIVHGEWVQQQLFLQHPSVGCFVSHCGWASLSEALVNDCQIVLLPQVGDQIINARIMSVSLKVGVEVEKGEEDGVFSRESVCKAVKAVMDEKSEIGREVRGNHDKLRGFLLNADLDSKYMDSFNQKLQDLLG | Function: Glycosyltransferase that mediates the glucosylation of anthocyanidin 3-O-glucosides to yield anthocyanidin 3-O-sophorosides. 3-O-sophoroside derivatives are required for the bright blue or red color of flowers.
Catalytic Activity: an anthocyanidin 3-O-beta-D-glucoside + UDP-alpha-D-glucose = an anthocyanidin 3-O-sophoroside + 2 H(+) + UDP
Sequence Mass (Da): 51170
Sequence Length: 459
Pathway: Pigment biosynthesis; anthocyanin biosynthesis.
EC: 2.4.1.297
|
V6CIV8 | MTTHLPSTSQNGEEISAEQFNRIFHERNVIVLDCRSNGDSVKRANRFFCSLRLPALLQRRLMGGSMRLSTVPDLKDLNNSPDQCPEVLLIPGDSEQDEQLSAALARNLKSNHYRHFVLGEPVKTLLSQFPTLRDAADENWNTTFQMNSMPGQASGQQASSGPLLNLNQLRLEGEDQGGKQRAEFPVKLTNFLYLGNAETAKNRDVLKKYSISHVINVTSNLPNTFEEDPNMRYLRISADDNASHNLTKFFPEAISFIDDARRNDSACLVHCLAGISRSVTICLAYLMKTEMCTLDSAYEWVQKRNASIAPNFHFMGQLTDYEKMLGLNSNRVGTYPSSAPRSPSCAIEAAAVSQVGGLLTPPPTSCSASPQSSNHSAKSFH | Function: Dephosphorylates MAP kinase mpk-1.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42174
Sequence Length: 381
Domain: The KIM (kinase interacting motif) region may be involved in the binding to MAP kinases.
Subcellular Location: Cell membrane
EC: 3.1.3.16
|
Q55E39 | MAKNKDDEESYCGGGGYWDMVEDLEEEICFDAQEVIPNLYIGSISAATCTTSLKEHKITHILSISTNPPKIKEFTTLCINIEDESQKDISSYFQQCHGFIENGRKLGGILVHCSAGVSRSASVVISYLMSVFFKPFWYCMQYLRNIRPCIQPNTGFINQLINYEATILKNQNVISTTTTTTTTTTITKKKLISNDCNNDDNSSGGSGGGMES | Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 23476
Sequence Length: 212
EC: 3.1.3.16
|
Q54R42 | MVNLEELSLKRNNMKRTETTFTDISGKRYQVANINEENSESNRIELNRTSGFVIDTKPDDLSHKIEIIIPQSILNNNNNNYESINLYIGSQDAAFNKLDLQLKNIKSILNVGIGINNLFTKENSDINDGFIINYCNVEIFDDVNFNIIEKFDKCFEFIDSNIGGVENNGILVHCNAGVSRSATILISYLMKKLKIPLSLSLEILKSSRPQCKPNQGFLKQLEIFEKELLF | Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 26189
Sequence Length: 230
EC: 3.1.3.16
|
Q55BI8 | MGISMILDNFLYLGAAKDTKDEKEMEKLKITHIFSCAGTVHSPEKYIIANEKFEDDETVDISEQIEKAYWFIERVRMKKGARVFIHCMAGKSRSASIVLSYLLKRDIHSLSDCLFYLHSKRLEIRPNDGFMNQLCDLELKLTNKQTLSKEIKEWRSLQSKALKTKIDVQTCHFIQPSLDSTKKANEQYLLHIQSISFTFFEIHLNQDKIIQLYQQQCQLLHSNNIDIKYFTSILQEELSNSTKKAFDFLLIHYYLDWQDIINNLLNYTNLKLNLN | Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 32332
Sequence Length: 275
EC: 3.1.3.16
|
Q54T76 | MNDVSRIFPGFYIGSLPAVNRNTLDKYQITHVCSVLNEFQPKWTKIYKYLHIDIYDSPSVDIMKYFDKTFQFIEEGRKDGGVLVHCFAGISRSATICIAYIMRKLNISFEDAHGLVSDARPIIYPNESFIKQLKKYELILKKNRENPQIVEKESEEEDDDEDDDDDDYDSDEDDDDDSEDDDFEEEFDNVVKKKNNNNKKVNVKNTTKVFSNISISSEQTTTSTTTVPTPTLNPETKIEETTTTTTATATATLVEEVVESTSPKATLGEHRYSCRKCSKDLFLDFDILDHEQGQGQTSFKWNKRDNTTCNKSVGANGEQIEDQNKVICTSYFISEIEFSLSQTYSGMEGKLFCPSCNEKLGSWSWSGEQCSCGAWIAPSFQIPKTRVDEKKVLK | Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 44884
Sequence Length: 394
EC: 3.1.3.16
|
Q556Y8 | MVLINRVNIQPEELPLLYHVNSMDVYNLLQDIGSSKIIIDLRTKEQYEKNHIRTSVNIPPPPSTTPLYENGEIKEFNLSKYIGSNVTAKHWNLIFQKLIVYSDKPFLYNIDELEKTISTTTITTTATTTTTTTTTSNSIGSDQDIIKSLKVSDWDKVVLRHFLLKKKKTKVIIYQGGFDQFQKDYSFMCNPSSSPSSSSGGGGGSQLYPSEIIKDFLYLGGAENAGNRQQLINLKITHLVNMAGELDDVYPHLYKYYRANLDDRPKANIYEHFEPVIQFINDCKKQGGRVLIHCAMGISRSTTVVLAYLMKEDHMTYSDAFTFCKQKRSCINPNFGFVKQLKDYQQHLTLEWEKQEKLKKQQQQTLNINNNNTGIPLSKKLQLDVSDPLSNSSPSSPLISSTLPIPETPPAIILKNEVASPCPIKTTTSSTTINNKGQQQDKAQEEKDSIFSYADKQEKMTHPTLHSPIELPQSSL | Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 53798
Sequence Length: 476
EC: 3.1.3.16
|
P61907 | MENDQEKPSMVAIQRLDPELPLPVRKHRGDAGADLFSAESVTIEPGHRILVGTGIAIALPIGTVGLIHPRSGRALKEGLSIVNTPGTIDADYRGEIKVCLINLDPTTPIRIERGERIAQLLVQKVELVDFCEVETLSETERGVNGYGSTGVN | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16404
Sequence Length: 152
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
Q4JVB1 | MTLKRNGNDAPLRIVRLDKELPLPRRAHPTDAGIDLYTAQDVTIAPGCRELVGTGIAIALPVGTVGLVHPRSGLALKKGLSIVNAPGTIDADYRGEIKVCLINLDPEEPIELARGERIAQLLVQEVSLCDVEEVNSVEELGVTVRGESGYGSTGV | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16458
Sequence Length: 155
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
B1WN93 | MQIKIIKLKEKAIIPKYEHDNDSGLDLVSTETVEIPSGESKLVKTGISIELPPNTEAQIRPRSGLALKHQITVLNTPGTIDEGYRGEIGVILINHGKRSFKVTEGMRIAQMVIAPVIRVKIQEVEQLSDTIRGQGGFGSTGV | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 15483
Sequence Length: 142
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
Q6A8W1 | MADVVVPTVAVPEAMPRYAMPGDAGADLTCRHDVDLAPGERAMVETGVRVALPDGYVGFVNPRSGLAARHGLSIVNAPGTIDSGYRGQINVLLVNTDPREPVHLDAGSRIAQLVVVPVVEAIFEPVEDLDDTERGQGGYGSTGVSAMPPVDG | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 15799
Sequence Length: 152
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
B8FQZ6 | MNSIKVKIAYVRKDKAPKLPQYATPGAAGVDLQASLDQELTIEPGQIVKIPTGLAIELPHAGVGAFVFARSGLASKYGLALANGVGVIDSDYRGEILVAVINQGSEPFVVKDGDRIAQMVFLPVFIGEFYLADQLDETGRGCGGFGSTGVS | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 15812
Sequence Length: 151
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
P14597 | MEFCHTETLQVVRLSQNATIPARGSPGAAGLDLCSAYDCVIPSHCSRVVFTDLLIKPPSGCYGRIAPRSGLAVKHFIDVGAGVIDEDYRGNVGVVLFNFGNSDFEVKKGDRIAQLICERISCPAVQEVNCLDNTDRGDSGFGSTGSGACGGRDTAWYIS | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16893
Sequence Length: 159
EC: 3.6.1.23
|
B3CSS7 | MKVKIKQIYQFEGTSSLPAYSTNGSAGMDLYAAIASPMIIKPHETALVPAGIAISLPYGYEAQIRSRSGLASKFGVIVLNSPGTIDSDYRGELKIIMINLGQKDFQLTPAMRIAQMVIAKYEVISWEIVDDLDETERGEKGFGSSGLK | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 16092
Sequence Length: 148
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
Q10FF9 | MATATNGNASAAAAAADSAVQEPPHKIAKVAPLLKVKKLSENAVLPSRGSALAAGYDLSSAAEVVVPARGKAMVPTDLSIAIPEGTYARVAPRSGLALKHSIDVGAGVIDADYRGPVGVILFNHSDTDFAVKPGDRIAQMIIEVIVTPEVAEVEDLDATVRGEGGFGSTGV | Cofactor: Binds 1 Mg(2+) per trimer.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP, preventing uracil incorporation into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 17340
Sequence Length: 171
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
O41033 | MSSLLVKKLVESATTPMRGSEGAAGYDISSVEDVVVPAMGRIAVSTGISIRVPNGTYGRIAPRSGLAYKYGIDVLAGVIDSDYRGELKAILYNTTERDYIIKKGDRIAQLILEQIVTPDVAVVLELEDTARGGGGFGSTGI | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 14879
Sequence Length: 141
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
A6L083 | MKIQVINKSKHALPEYATGQSAGMDIRANLDEPIVLKPLQRCLVPTGLYIALPEGFEAQIRPRSGLAIKKGIGVLNSPGTIDADYRGEICIILVNLSSEDFMIEDGERIAQMVVARHEHAEWQEVEVLDETERGAGGFGHTGKK | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 15779
Sequence Length: 144
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
B2RJH1 | MKIKIINRSHHPLPAYATSASAGMDLRASIEEPITLLPLERRLIPTGLFIELPVGYEAQIRPRSGLALRHGITLVNSPGTIDADYRGEIGIIMINLSNTPFTIADGERICQLVIARHEQAEWVLTDELADTERGAGGFGHTGKE | Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Catalytic Activity: dUTP + H2O = diphosphate + dUMP + H(+)
Sequence Mass (Da): 15736
Sequence Length: 144
Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
EC: 3.6.1.23
|
Q6IM82 | MAGLKRKFNKGHAFTSKCVSLVKEQRARLYILRRCATMLCCWYIHGDE | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5634
Sequence Length: 48
Subcellular Location: Cell membrane
|
Q6X5V0 | MEMKRVMMSSAERSKEKKRSISRRLGKYMKEQKGRIYIIRRCMVMLLCSHD | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, including leaves shape, pedicule elongation, inflorescence organization and fruit maturation, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6211
Sequence Length: 51
Subcellular Location: Cell membrane
|
P51141 | MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNRDEAARTNGHPRGDRRRDLGLPPDSASTVLSSELESSSFIDSDEEDNTSRLSSSTEQSTSSRLVRKHKCRRRKQRLRQTDRASSFSSITDSTMSLNIITVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTIPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAITRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAIVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSMLKHGFLRHTVNKITFSEQCYYVFGDLCSNLASLNLNSGSSGASDQDTLAPLPHPSVPWPLGQGYPYQYPGPPPCFPPAYQDPGFSCGSGSAGSQQSEGSKSSGSTRSSHRTPGREERRATGAGGSGSESDHTVPSGSGSTGWWERPVSQLSRGSSPRSQASAVAPGLPPLHPLTKAYAVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM | Function: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ).
PTM: Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination (By similarity). Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75359
Sequence Length: 695
Domain: The DIX domain promotes homooligomerization.
Subcellular Location: Cell membrane
|
Q5IS48 | MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNREEAARTNGHPRGDRRRDVGLPPDSASTALSSELESSSFVDSDEDGSTSRLSSSTEQSTSSRLIRKHKRRRRKQRLRQADRASSFSSITDSTMSLNIVTVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTVPRADPVRPIDPAAWLSHTAALTGALPRYELEEAPLTVKSDMSAVVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSLLKHGFLRHTVNKITFSEQCYYVFGDLCSNLATLNLNSGSSGASDQDTLAPLPHPAAPWPLGQGYPYQYPGPPPCFPPAYQDPGFSYGSGSTGSQQSEGSKSSGSTRSSRRAPGREKERRAAGAGGSGSESDHTAPSGVGSSWRERPAGQLSRGSSPRSQASATAPGLPPPHPTTKAYTVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM | Function: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) (By similarity).
PTM: Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, leading to its subsequent degradation by the ubiquitin-proteasome pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS is required for ubiquitination. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72851
Sequence Length: 670
Domain: The DIX domain promotes homooligomerization.
Subcellular Location: Cell membrane
|
Q8LBB5 | MGEENSTSGTCKPSKTFKAKCSHMVRKQRAKFYILGRCLAMLVCGRGRDRERDRILI | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6535
Sequence Length: 57
Subcellular Location: Cell membrane
|
Q6IM80 | MLVSNISGKLMSQLMEKMKERLEKMKRTVRQQRAKLHIIRICITMLLSSDDYS | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6284
Sequence Length: 53
Subcellular Location: Cell membrane
|
F4HTB2 | MAEFKSKLNKGHAFTSKCASLVKEQRARLYILRRCATMLCCWYIQGDE | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5600
Sequence Length: 48
Subcellular Location: Cell membrane
|
A8MRE9 | MKMSERRVGSYRKSTLRCWDWCKEQRTRAYIIWRCLIFLLRWDDY | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5820
Sequence Length: 45
Subcellular Location: Cell membrane
|
A8MS09 | MCIILHSCTARLPQAQNLQIELKQDQVQASFKSNEKKNSIFIKLVSEKPMLINRRVESSNLLHSNMGGFLAKKTNSNSKIRNSFTSKCTSLMKQQHARLCIIRLCATMLLRSYTDHDDY | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13646
Sequence Length: 119
Subcellular Location: Cell membrane
|
Q60838 | MAGSSAGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDTPQPEVAPPAHESRTELVPPPPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRDRPRRRDSSEHGAGGHRPGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEDDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRMERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQAYFTLPRNEPIQPIDPAAWVSHSAALTGAFPAYPGSSSMSTITSGSSLPDGCEGRGLSVHMDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLPGATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESELSSRGGSLRRGGEPGGTGDGGPPPSRGSTGAPPNLRALPGLHPYGAPSGMALPYNPMMVVMMPPPPPPVSTAVQPPGAPPVRDLGSVPPELTASRQSFHMAMGNPSEFFVDVM | Function: Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling.
PTM: Phosphorylated by CSNK1D (By similarity). WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78861
Sequence Length: 736
Domain: The DIX domain mediates homooligomerization.
Subcellular Location: Cell membrane
|
P51142 | MAETKVIYHLDEEETPYLVKVPVPATDIRLRDFKAALGRGHAKYFFKAMDQDFGVVKEEISDDNAKLPCFNDRVVSWLASSEGSQPDSAPPAPATEVRPEPPPPVPPPIPPPPAERTSGIGDSRPPSFHPNVSGSTEQLDQDNESVISMRRDRVRRRESSEQAGVGRGVNGRTERHLSGYESSSTLLTSEIETSICDSEEDDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDINFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQGYFTLPRNEPIHPIDPAAWVSHSAALSGSFPVYPGSASMSSMTSSTSVTETELSHALPPVSLFSLSVHTDLASVVKVMASPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFQDRREARKFASNLLKAGFIRHTVNKITFSEQCYYIFGDLTGCENYMTNLSLNDNDGSSGASDQDTLAPLPLPGASPWPLLPTFSYQYQAPHPYSTQPPAYHELSSYSYGMGSAGSQHSEGSRSSGSNRSDGGRGMQKDDRSGVAGVGGGDSKSGSGSESEYSTRSSIRRVGGGEAGPPSERSTSSRLPPHHPPSVHSYAAPGVPLSYNPMMLMMMPPPPLPPPGVCPPNSSVPPGAPPLVRDLASVPPELTATRQSFHMAMGNPSEFFVDVM | Function: Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia.
PTM: Phosphorylated. Phosphorylation is controlled by frizzled proteins, correlates with the onset of embryo dorsalizing events and is higher in the dorsal half of early cleavage embryos. Phosphorylated on tyrosine residues in response to association with efnb1/ephrin-B1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 79787
Sequence Length: 736
Domain: The C-terminal region containing the DEP domain is required for membrane accumulation and phosphorylation. Wnt signaling and axis induction requires the DIX domain. The C-terminus contributes to the localization at the cilia base.
Subcellular Location: Cytoplasm
|
Q6X5U0 | MKGTKKKTPCNKKLGGYLKEQKGRLYIIRRCVVMLICWHD | Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, including leaves shape, pedicule elongation, inflorescence organization and fruit maturation, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4738
Sequence Length: 40
Subcellular Location: Cell membrane
|
Q92997 | MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPDPAPFCADNPSELPPPMERTGGIGDSRPPSFHPHAGGGSQENLDNDTETDSLVSAQRERPRRRDGPEHATRLNGTAKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPRGCFTLPRSEPIRPIDPAAWVSHTAAMTGTFPAYGMSPSLSTITSTSSSITSSIPDTERLDDFHLSIHSDMAAIVKAMASPESGLEVRDRMWLKITIPNAFIGSDVVDWLYHNVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLCGNMANLSLHDHDGSSGASDQDTLAPLPHPGAAPWPMAFPYQYPPPPHPYNPHPGFPELGYSYGGGSASSQHSEGSRSSGSNRSGSDRRKEKDPKAGDSKSGGSGSESDHTTRSSLRGPRERAPSERSGPAASEHSHRSHHSLASSLRSHHTHPSYGPPGVPPLYGPPMLMMPPPPAAMGPPGAPPGRDLASVPPELTASRQSFRMAMGNPSEFFVDVM | Function: Involved in the signal transduction pathway mediated by multiple Wnt genes.
PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-63'-linked ubiquitin chains.
Sequence Mass (Da): 78055
Sequence Length: 716
Subcellular Location: Cytoplasm
|
B2ITX3 | MKAITLVGSTGSIGTQTLDIVTQYPDQFRIVGLAAGNNVEMLAAQIRQFRPKIAAICSEDKLPALKEAIIDLDPQPILLAGEAGVIEVARYGDAQTVVTGIVGCAGLLPTIAAIEAGKDIALANKETLIAGAPVVLPLVEKHGVKLLPADSEHSAIFQCLQGVPKSGLRKILLTASGGAFRDWDVERLADVTVADALKHPNWSMGRKITVDSATLMNKGLEVIEAHFLFGLDYDNIEIVIHPQSIIHSLIELQDTSVLAQLGWPDMRLPLLYALSWPDRIYTDWERLDLVKAGNLTFREPDHQKYPCMQLAYAVGKAGGSMPAVLNAANEQAVALFLDEKIRFLDIPRCIEWVCDRHQNDNRANPSLDDILAADKWARQEVLTATEKLETPSRIISLR | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 43472
Sequence Length: 398
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
|
Q313H2 | MNGYISPLPDAAWNSRFPRSLVLLGSTGSIGTSALRVVERQPELFRITALAGARNVRLLARQAAAYRPPHLAVINGNAADELASLLPAGYRPRIHTGQEGYEFLAALPEADCVLSAQVGAAGLRATVAAARAGKTIALANKESLVLAGGLIRRLCHETGASVLPVDSEHNAIFQALQGHDAAQMRRIILTASGGPFRGRDRTFLQSVTREQALNHPNWSMGAKISIDSATLMNKGLEVIEACHLYNAPLEKVEVVVHPQSIIHSLVEYNDGSQIAHMGTPDMRIAIAYCLGWPRVMHTGVEPLDLLSVGSLTFESPDISLFPCLELARKAYAGGNGLPVVLNAANEVAVDLFLQGAIAFLDIPRLIEAAMQAHDAAPHQNMYDEVESILTLDKTTRRVTADLAGARG | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 43573
Sequence Length: 407
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
|
Q6MEL5 | MKHIAILGSTGSIGKNTLQVARHLKERIKVVAIAARENIDLLEAQSKEFCPDIIAVFNNAKAYELQKRLPGKTVLAGMEGLLAAASYSEADLVISAMTGTMGLQPTIEAIKAGKDVGLANKEALVSGGAIIMKLVKEKNINLLPIDSEHSAIFQCLNGEALKSVQRIILTSSGGPFRTWTQEQLETVTVEQALNHPTWSMGPKVTIDSSTLMNKGLEVIEAFWLFDVSPEQIDVIVHPQSIIHSLVEFCDGSMLAQMSEPNMIVPIQYSLTYPDRAPGLFKPFDFMKNSKLEFFEPNKKTFRCLALAYEALKCGGTLPCYMNAANEVLVERFLKGELSWKNIGIQLEKLMDQHASISVDSLETILAVDALAREEAARSKLISTK | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 42135
Sequence Length: 384
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
|
A5D2U3 | MKNIVLIGSTGSIGRQTLEVIGSLPDRFKVVGLGSGKNWRLMAEQIRVFRPSAVAMAGEREIMNLKELLAGSYCPELGWGRTGMESLASMPEADLVVVAVTGFAGIYPTIAAIQAGKDVALANKETLVAAGHLVMKMAERHRAAILPVDSEHSAVWQCLCGRNSGEVEKIILTASGGPFREMCLEKLEKVTVDMALKHPNWNMGSKITIDSATLMNKGLEVIEAKWLFGLNYSQIEVVIHPQSIVHSAVEFLDGSVIAQMGLPDMRLPIQYALTYPERLPGSFPKLKLASLQGLTFEEPDTRRFPCLSLAFEAGLAGGTMPAVLNAANEVAVEFFLKGLLPFLGIPSVVRSVMEKHEMASDPGLEEIIEADRWARNMGVKVIRDLFN | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 42114
Sequence Length: 387
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
|
Q4FM64 | MKKIAIFGSTGSIGSSLLKIIKDDQKNFKIELLTVNKNYKKLIKQVKLFNVKNVIVTDYNSFLITTKLLKNAKVKVFNNFDSLNKIFNTNNKIDYSMCAISGFDGLKPTLDIIKFTKTIAIANKESIICGWNLIKKDLKKYKTYFVPVDSEHFSIWSLLDNNKKNNFEKIYITASGGPFRNLSLKKFRNISVKDALKHPNWSMGKKITIDSATMMNKVFEIIEAKKIFNLNYKQLEILIHPKSYLHAIVKFNNGLSKLLVHDTNMTIPIFNSIYFNTDKKLKSKNIDIKTLNNLNLKKIDNIRFPVIKILNNLSNEDSLFETIIVSANDKLVKLFLNNKIKFNDISNTLIKICNTPEFNKFKSMKPRNIDEIQNLNDYVSLKISSMSV | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 44678
Sequence Length: 388
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
|
C0QTC4 | MKRLAVLGSTGSIGTQTLDIVRKYRDRLEVSLLAASRVSEKLLDQIDEFKPEYVYIAEGEKIKGVKTLIGEDGLYKLAQLDIDLFINGISGINGILPTYLLLENNKKLATANKEAIICLGEIYGDKYSDIFPIDSEHSAIFQCLLSGRKEEVEKIILTASGGPFLNLPKEEFRYITPDQALNHPRWKMGKKVSIDSATLMNKGFEIIEAHYLFNIPYSKIDVVIHPESIVHGLVQFIDGSVISHLSPPDMRIPICYAISYPERWEIDVRRLNLAQVKNLTFLEPDYDRFPLLNIAKECGEKGGACPTVLTTADEIAVNLFLEGKITFDMIPVYIQQVLDQADFSKPETFEDIIFIIKETEKIFWNILKLQNVN | Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Mass (Da): 42175
Sequence Length: 373
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
|
Q2IPZ2 | MGRLLDTIDSPADLKKVPVEQLPALCQEIRELIIQTCARNGGHLGSSLGAVEINVALHHVFASPQDKLVWDVGHQAYAHKLLTGRRDAFRTIRTEGGLAGFPERHESAHDAFGVGHASTAISAALGMIEAKRVTGEPGKVVAVVGDGAMTGGVAFEGLNQAGYLGRNLLVVLNDNEMSISPNVGALSEWFSKKFASRTYNRWRRQVKEFLESVPKGPEAIGIIRHGINATKALVTPGILFEGLGFHYVGPVDGHDVKGLVETFQKLAVFDGPVLLHAITTKGKGYHPAESDKATRGHGLSFFDVATGKPVKKSPGAKAYTDLFAEALCEEMEHDPRVVAITAAMLEGTGLIKAKQRFPDRTYDVGIAEQHAVTFAAGLACEGIRPVVAIYSTFLQRAYDQIIHDVALQKLPVTFALDRGGLVGADGKTHQGAFDLAYLRCVPGLVLMAPSDENELRHMLHTSLQHDGPAALRYPRGAGEGVPLEPARVLEIGKGRLVRNVPGKPDVCVVAAGTTLKAALAAAEALAAEGVAVTVVDPRFVKPLDEALICAEAARAKRVVTVEEGCLAGGFGTACLEAFERHGLLEAGLGVRRLGIPDEFITHAEQAKQRAWVGIDAEAIAAACRALVGDRKARGVA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 67628
Sequence Length: 636
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
O67036 | MLEKYEILKDYKGPFDIKNYDYETLQKLAQEVRDYIINVTSKNGGHVGPSLGVVELTIALLRVFNPPEDVIVWDIGHQGYPWKILTDRKEQFPTLRQYKGISGFLRREESIYDAFGAGHSSTSISAALGFRIGKDLKGEKEDYVIAVIGDGALTAGMAYEALNNAGHIRPDRFIVILNDNEMSISPNVGAISTYLNRIISGHFVQETRQKIKNFLQHFGETPLRIMKLTEEFLKGLISPGVIFEELGFNYIGPIDGHDIKALEDTLNNVKDIKGPVLLHVYTKKGKGYKPAEENPVKWHGVAPYKVESGEIIKKSSPPTWTSVFGKALVELAERDEKIVAITPAMREGSGLVEFAKRFPDRFFDVGIAEQHACTFAAGLAAEGLRPVAAYYSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGDDGPTHHGVFDLSYLRCVPNMVVCAPKDEQELRDLLYTGIYSGKPFALRYPRGAAYGVPTEGFKKIEIGTWEELLEGEDCVILAVGYPVYQALRAAEKLYKEGIRVGVVNARFVKPMDEKMLRDLANRYDTFITVEDNTVVGGFGSGVLEFFAREGIMKRVINLGVPDRFIEHGKQDILRNLVGIDAEGIEKAVRDALKGGRLI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 69926
Sequence Length: 628
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
Q38854 | MASSAFAFPSYIITKGGLSTDSCKSTSLSSSRSLVTDLPSPCLKPNNNSHSNRRAKVCASLAEKGEYYSNRPPTPLLDTINYPIHMKNLSVKELKQLSDELRSDVIFNVSKTGGHLGSSLGVVELTVALHYIFNTPQDKILWDVGHQSYPHKILTGRRGKMPTMRQTNGLSGFTKRGESEHDCFGTGHSSTTISAGLGMAVGRDLKGKNNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPSPPVGALSSALSRLQSNPALRELREVAKGMTKQIGGPMHQLAAKVDEYARGMISGTGSSLFEELGLYYIGPVDGHNIDDLVAILKEVKSTRTTGPVLIHVVTEKGRGYPYAERADDKYHGVVKFDPATGRQFKTTNKTQSYTTYFAEALVAEAEVDKDVVAIHAAMGGGTGLNLFQRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMIVMAPSDEADLFNMVATAVAIDDRPSCFRYPRGNGIGVALPPGNKGVPIEIGKGRILKEGERVALLGYGSAVQSCLGAAVMLEERGLNVTVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKWRPMVLPDRYIDHGAPADQLAEAGLMPSHIAATALNLIGAPREALF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). Is a limiting enzyme for plastidic isoprenoid biosynthesis and essential for chloroplast development.
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 76833
Sequence Length: 717
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
Subcellular Location: Plastid
EC: 2.2.1.7
|
A0JVG9 | MGILDTIRNPQDLSKLTEEQLSQLAAEVRSFLIGNVSQTGGHLGPNLGVVELTMAVHRIFDSPRDSIVFDTGHQSYVHKLLTGRQDFSTLRQEGGMSGYPDRGESEHDIVESSHASSSLSWADGISRARQLTGDGDRYVIAVVGDGALTGGMAWEAINNIAADKRRRVVIVVNDNGRSYAPTVGGFADYLASLRPTIDSFRAAPAYEGTLDWWKRKLQNGGPVGQFTYRSLHAMKKGIKDWWAPQGMFEDLGMKYIGPVDGHNLQAMEHALSTAKNYAGPVIVHAMTEKGHGYAPARAHEADQFHAVGIIDPETGVPTEAGGAQSWTSVFADEIAAIADERKDIVGITGAMLIPVGLHKFAARHPERVFDVGIAEQHALTSAAGMAFGGLHPVVAVYATFLNRAFDQLLMDVALHKAGVTIVLDRAGVTGPDGASHHGMWDMAMVQIVPGLHLAAPRDATRLREELREAVAIEDAPTVVRYSKGNVGAEVEALERLSDGVDVLARRPAGSSENDVLIVSVGAMSELALDVSNRLGAQGISSTVVDPRWLLPVRKSIIALAARHRLVICIEDGVRAGGVGSRIRQEMRAAGVDTALNEVGLPVEFLDHGTRAQVLERVGLTARQITHDVVAQVLGTKVPFARPLPGQEHPTTGSLPKL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 70491
Sequence Length: 657
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
B6YRV5 | MKKISDYSLLFKINSPEDLRKLAIEQVEQVCKELREYIIEVLSENPGHLGSNLGTVELTVALHYVFNTPYDRIVWDVGHQAYGHKILTERRESFHTLRKLGGISGFPNPQESEYDAFIAGHASNSISAALGMAIASWLKGENRKIVAIIGDGSITGGLAFEGLNNVSSNPNDLLIVLNDNNMAIDRSVGGLSQSLIKITTSYTYNTIRFKLYNFLKKYSIIKERERGFILRFTNSLKALLTKQHNIFEGLNIRYFGPIDGHNIKELVKVFEDIKSMKGPKLLHVCTVKGKGFGPAENKADVWHAPGKFNPETGERIKVWSENLPSLYQDVFGHTLVELARMNNNIVGVTPAMSSGCSMTFLMKEMPHRTFDVGIAEGHAITFAAGLAKEGMIPFCNVYSSFMQRAYDNIIHDAVLQNLNMILCLDRAGLVGEDGVTHHGVLDLAYLRCIPNITITAPLNEKDLRNLMFTAIQPNAKGVFVIRYPKGYGELKNWEYSFEALPVGKGRKLKEGKEIAVVSIGTIGNLARKAIRLVEKLGISVAHYDMIYLKPIDEELLHEIGKNYRCVVVIEDGTIKGGLGTAVIEFMVQNGYDPKIKQIGVPDEFIPHGTIAELYKLCGMDIKSIVKCLIEEK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 70381
Sequence Length: 632
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
Q7VIJ7 | MEVKTLDVANFLARIQKQESTFESLSKFSPTQLKELATCIRHRILEVVSSNGGHLSSTLGAVDLIIGMHLVFDANTNPFIFDVSHQAYAHKLLTGRWNDFSSLRQFGGLSGFCNPKESPSDYFIAGHSSTSISLAVGAAKALALKGSASMPVVMIGDGSMSAGLVYEALNELGDKKYPMVIILNDNKMSISKPIGAISNYLSQILTTSIYQKIRDTIKKVLTKMPDSATYLAKRFEESLKLITPGILFEELGLDYVGPIDGHNIELIIATLQRAKEMRKPVIIHAQTLKGKGYEIAEGRFEHWHGVGPFDVSTGSSLKSSAPQSPTAVFSESLESYLTDEKVVGVTAAMPSGTGLDKLIEKYPQRFWDVAICEAHAVTSMAAIAKEGFKPFVAIYSTFLQRAYDQIIHDVGILGLPVRFCIDRAGIVGEDGETHQGLFDIAYLRSIPHMVLFAPRDNASLQQAVAFAYRYNDSPCAFRYPRGSFTLEEGVFVSNEFVLGQAEMLKRGKKILLVGYGNGVGRAYKVYQALITEGYEPSLLDLRFVKPLDKHMLNEVFKTHTHICVFSDSYYMGGVASALLEFMAEENIKDVQLKSFEIKDRFVPHGNTALIEQSLGLDTPHLVSKIKEWI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 69412
Sequence Length: 629
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
B0TEJ5 | MTQILSRISNPGDLQRLSATELDQLAKEIREVIIQTTSKNGGHLAPNLGVVELTLALHLVFQSPKDKIIWDVGHQSYVHKLLTGRYNHFHTLRRYKGMAGFPKRSESEHDVFNTGHSSTSISAALGFAFARDLKKEDGAVIAVIGDGALTGGIALEALNHAGHAGNDMIVVLNDNEKSIADNVGAMSTYLSRIRTDPRYFRNKEEVEEIVRRIPSIGNHVLKVMEKMKDSFKHLVVPGILFEELGFSYLGPIDGHNLSQLREVMTNACRLKGPILVHVLTKKGKGYGPAETNPSVFHGVGPFDVETGKVKKHLGPPTYTQVFSDTLLRLAREDERIVGVTAAMPDGTGMTPFARAFPSRFFDVGIAEQHAVNMSAALALQGLKPVVAIYSTFLQRAYDQVFHDVCLQRAPVVFAIDRGGIVGDDGETHHGLFDIAFLRHIPELVMMAPKDENELQHMLRTALEYEGPIAVRYPRGTGVGVTLDEELTTVPIGRGELLRQGSDVTIVAIGAMVGIAEEAADLLEAEGIRAAVVNARFVKPLDKELIIKQARETGRIVTVEEHVLAGGFGSAILELLEMEGVHCAVRRIGIPDEYVQHGSVSVLREDYGLTASNVARVARELADADRSRASIRMAPPAPIKIAFRGESR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 70697
Sequence Length: 647
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
O25121 | MILQNKTFDLNPNDIAGLELVCQTLRNRILEVVSANGGHLSSSLGAVELIVGMHALFDCQKNPFIFDTSHQAYAHKLLTGRFESFSTLRQFKGLSGFTKPSESAYDYFIAGHSSTSVSIGVGVAKAFCLKQALGMPIALLGDGSISAGIFYEALNELGDRKYPMIMILNDNEMSISTPIGALSKALSQLMKGPFYQSFRSKVKKILSTLPESVNYLASRFEESFKLITPGVFFEELGINYIGPINGHDLSAIIETLKLAKELKEPVLIHAQTLKGKGYKIAEGRYEKWHGVGPFDLDTGLSKKSKSAILSPTEAYSNTLLELAKKDEKIVGVTAAMPSGTGLDKLIDAYPLRFFDVAIAEQHALTSSSAMAKEGFKPFVSIYSTFLQRAYDSIVHDACISSLPIKLAIDRAGIVGEDGETHQGLLDVSYLRSIPNMVIFAPRDNETLKNAVRFANEHDSSPCAFRYPRGSFALKEGVFEPSGFVLGQSELLKKEGEILLIGYGNGVGRAHLVQLALKEKNIECALLDLRFLKPLDPNLSAIVAPYQKLYVFSDNYKLGGVASAILEFLSEQNILKPVKSFEIIDEFIMHGNTALVEKSLGLDTESLTDAILKDLGQER | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 67634
Sequence Length: 618
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
A9KMB8 | MPKILDEINQPNDIKKISAKKYTQLAAEIRRFLIANVSKTGGHLASNLGVVELTMALHLFLDFPEDKLVWDVGHQAYVHKLLTGRKNDFKTLRQYEGMSGFPKRKESDCDAFDTGHSSTSLSVAVGLVKARELSEEQRKVVAVIGDGALSGGMAFEALNNAGRLKENMIIVLNDNNMSISENVGGMSNYLGKARTNYRYMDFKGGLETALKKIPKVGDAIVTTLKQSKDSLKHLFIPGMLFEDMGMTYIGPIDGHNINQMLTALKSASRVNGAVLIHTVTKKGKGYEPAEKEPSKYHGVEPFDIKTGKKLKINSEVSYTEVFGKKLIELAKVRNDVVAITAAMPDGTGLTAFGDVFPNRFFDVGIAEEHAVTFAAGLAAAGFKPVVAVYSTFLQRAYDQILHDVCVGKLPVVFALDRAGIVGNDGETHQGMFDLSYLSHMPGLTVIAPKNSWEFERMLEYCIDFDGPIAIRYPKNTAYLGLEDHKKEIIYGKGELIASEEEIALIAIGSMVETAVLVREHLHKLGLKATLVNARFISPLDEEMLHQLTKSHTLFVTMEENVKRGGFGEEVSVFLCEHDYQGIKHLNISIPNMFVEHGDRTLLKEKLGLDAESIVDKICRQRGMQK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 69069
Sequence Length: 625
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
Q9RBN6 | MTILENIRQPRDLKALPEEQLHELSEEIRQFLVHAVTRTGGHLGPNLGVVELTIALHRVFESPVDRILWDTGHQSYVHKLLTGRQDFSKLRGKGGLSGYPSREESEHDVIENSHASTALGWADGLAKARRVQGEKGHVVAVIGGRALTGGMAWEALNNIAAAKDQPLIIVVNDNERSYAPTIGGLANHLATLRTTDGYEKVLAWGKDVLLRTPIVGHPLYEALHGAKKGFKDAFAPQGMFEDLGLKYVGPIDGHDIGAVESALRRAKRFHGPVLVHCLTVKGRGYEPALAHEEDHFHTVGVMDPLTCEPLSPTDGPSWTSVFGDEIVRIGAEREDIVAITAAMLHPVGLARFADRFPDRVWDVGIAEQHAAVSAAGLATGGLHPVVAVYATFLNRAFDQLLMDVALHRCGVTFVLDRAGVTGVDGASHNGMWDMSVLQVVPGLRIAAPRDADHVRAQLREAVAVDDAPTLIRFPKESVGPRIPALDRVGGLDVLHRDERPEVLLVAVGVMAQVCLQTAELLRARGIGCTVVDPRWVKPVDPVLPPLAAEHRLVAVVEDNSRAAGVGSAVALALGDADVDVPVRRFGIPEQFLAHARRGEVLADIGLTPVEIAGRIGASLPVREEPAEEQPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 67962
Sequence Length: 631
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
Q67NB6 | MHLRDLTGPEQLKRLAPAELAQLAAEIRRVILETVATNGGHLAPNLGVVELTLALHIVFDSPRDKILWDVSHQSYVHKLLTGRLHQFHTLRQFGGIAGFTDPRESVHDHFHWGHASTSISAAVGMAKARDLAGDDYEVVAVIGDGALTGGMAYEALDHAGHDKTKVIVVLNDNSMSIAPNVGGISNYLARIRTGPSYQRVKHDVAEALRQIPLIGPQALELADRLKEGVKHLLVHNMFFEDLGFTYLGPVDGHNVSALVDVLRQARAYPGPTVVHVVTTKGKGVPYAEQLPDKFHGGGPFDVATGRTGPGSLTYSEVFGNVMCKLAAEDPRVCAITAAMPSGTGLSRFARQFPDRYFDVGIAEQHAVTFAAGLAKGGMRPVFAVYSTFLQRAYDQVIHDVALQNLPVTLAIDRGGLVEDGATHQGVFDVAYLRAIPNMVVMAPKDENELQHMLYTALCHDGPAALRYPRGKAQGVPLDETLQPLPIGRGEVMQEGADVALIGLGTMARVCQEAARLLAEKSISAMVINPRFVKPLDAELLLRAGREVGAVVTVEEACLAGGFGSAVLELYAAHGVNARVERMGIPDEFVDHGQPARYLERYGLTPEGVAQRAEALLLRMRSDLAAQPARRSRSVRRLSGAKAAGNGET | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Catalytic Activity: D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-xylulose 5-phosphate + CO2
Sequence Mass (Da): 69789
Sequence Length: 648
Pathway: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.
EC: 2.2.1.7
|
Q27368 | MSKFFVNVAPINNSNSSSSHTTTSSNTQRHQQHQQHYGGSGTTGHTMVARRLNYDLHGGTTSINNNNNIVIKNESVDLDYDHVLSSSDSNSNGGVAAHLRDHVYISLDKGHNTGAVATAAAAATAGHTQQQLQQQHHHQNQQQRKATGKSNDITNYYKVKRRPHAVSDEIHPKKQAKQSAHHQTVYQKHTASSAPQQLRHSHHQLRHDADAELDEDVVERVAKPASHHPFSLSTPQQQLAASVASSSSSGDRNRADTSLGILTKKFVDLLQESPDGVVDLNEASNRLHVQKRRIYDITNVLEGINILEKKSKNNIQWRCGQSMVSQERSRHIEADSLRLEQQENELNKAIDLMRENLAEISQEVENSGGMAYVTQNDLLNVDLFKDQIVIVIKAPPEAKLVLPNTKLPREIYVKAENSGEINVFLCHDTSPENSPIAPGAGYVGAPGAGCVRTATSTRLHPLTNQRLNDPLFNNIDAMSTKGLFQTPYRSARNLSKSIEEAAKQSQPEYNNICDIAMGQHHNLNQQQQQQQQQLLQQPEEDDVDVELNQLVPTLTNPVVRTHQFQQHQQPSIQELFSSLTESSPPTPTKRRREAAAAAIAAGSSTTATTTLNSHNNRNHSNHSNHSNHSSSNNSKSQPPTIGYGSSQRRSDVPMYNCAMEGATTTSATADTTAATSRSAAASSLQMQFAAVAESNNGSSSGGGGGGGGYGSIAGAGANADPHQPYSHDRNSLPPGVADCDANSNSSSVTLQGLDALFNDIGSDYFSNDIAFVSINPPDDNDYPYALNANEGIDRLFDFGSDAYGP | Function: Transcriptional activator that binds to E2f sites. Required for wild-type growth in mitotic and polytene tissues, Contributes to the expression of replication genes at the G1-S transition and Cyclin E. Activates cell proliferation in wing imaginal disk, which requires expression of vg.
PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2) complex, leading to its degradation during S phase. Ubiquitination by the DCX(DTL) complex is essential for cell cycle control and is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to its degradation.
Sequence Mass (Da): 87460
Sequence Length: 805
Domain: The PIP-box K+4 motif mediates both the interaction with PCNA and the recruitment of the DCX(DTL) complex: while the PIP-box interacts with PCNA, the presence of the K+4 submotif, recruits the DCX(DTL) complex, leading to its ubiquitination.
Subcellular Location: Nucleus
|
Q01094 | MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication . The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase . E2F1 binds preferentially RB1 in a cell-cycle dependent manner . It can mediate both cell proliferation and TP53/p53-dependent apoptosis . Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters . Directly activates transcription of PEG10 . Positively regulates transcription of RRP1B .
PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase . Phosphorylation at Ser-364 by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis . Phosphorylation at Ser-403 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization .
Sequence Mass (Da): 46920
Sequence Length: 437
Subcellular Location: Nucleus
|
Q61501 | MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQLPAAPPTGPRDSDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTMVGIGKRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSETFQISLKSKQGPIDVFLCPEESADGISPGKTSCQETSSGEDRTADSGPAGPPPSPPSTSPALDPSQSLLGLEQEAVLPRMGHLRVPMEEDQLSPLVAADSLLEHVKEDFSGLLPGEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication . The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (By similarity). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (By similarity). It can mediate both cell proliferation and TP53/p53-dependent apoptosis . Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters . Directly activates transcription of PEG10 (By similarity). Positively regulates transcription of RRP1B (By similarity).
PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis. Phosphorylation at Ser-396 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization.
Sequence Mass (Da): 46323
Sequence Length: 430
Subcellular Location: Nucleus
|
Q14209 | MLQGPRALASAAGQTPKVVPAMSPTELWPSGLSSPQLCPATATYYTPLYPQTAPPAAAPGTCLDATPHGPEGQVVRCLPAGRLPAKRKLDLEGIGRPVVPEFPTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKAKNNIQWVGRGMFEDPTRPGKQQQLGQELKELMNTEQALDQLIQSCSLSFKHLTEDKANKRLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRTEDNLQIYLKSTQGPIEVYLCPEEVQEPDSPSEEPLPSTSTLCPSPDSAQPSSSTDPSIMEPTASSVPAPAPTPQQAPPPPSLVPLEATDSLLELPHPLLQQTEDQFLSPTLACSSPLISFSPSLDQDDYLWGLEAGEGISDLFDSYDLGDLLIN | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.
PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
Sequence Mass (Da): 47506
Sequence Length: 437
Subcellular Location: Nucleus
|
P56931 | MLRAPRTLAPATAQPTKSLPALNPTELWPSGLSSPQLCPATTATTYYTSLYTQTVPSSVALGTCLDATPHGPEGQIVRCAPAGRLPAKRKLDLEGIGRPTVPEFRTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKSKNNIQWVGRELFEDPTRPSRQQQLGQELKELMNAEQTLDQLIQSCSLSFKHLTEDNANKKLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRAEENLQIYLKSTQGPIEVYLCPEEGQEPDSPAKEALPSTSALSPIPDCAQPGCSTDSGIAETIEPSVLIPQPIPPPPPPPLPPAPSLVPLEATDNMLELSHPLLQQTEDQFLSPILAANSPLISFSPPLDQDEYLWGMDEGEGISDLFDSYDLGDLLIN | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.
PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
Sequence Mass (Da): 48499
Sequence Length: 443
Subcellular Location: Nucleus
|
Q16254 | MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSVSGPIEVLLVNKEAWSSPPVAVPVPPPEDLLQSPSAVSTPPPLPKPALAQSQEASRPNSPQLTPTAVPGSAEVQGMAGPAAEITVSGGPGTDSKDSGELSSLPLGPTTLDTRPLQSSALLDSSSSSSSSSSSSSNSNSSSSSGPNPSTSFEPIKADPTGVLELPKELSEIFDPTRECMSSELLEELMSSEVFAPLLRLSPPPGDHDYIYNLDESEGVCDLFDVPVLNL | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis.
PTM: Differentially phosphorylated in vivo.
Sequence Mass (Da): 43960
Sequence Length: 413
Subcellular Location: Nucleus
|
Q8R0K9 | MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSMSGPIEVLLVNKEAWSSPPVAVPVPPPDDLLQSPPAVSTPPPLPKPALAQPQESSPPSSPQLTTPTPVLGSTQVSEVACQTSEIAVSGSPGTENKDSGEVSSLPLGLTALDTRPLQSSALLDSSSSSSSSSSSSSSSSSGPNPSTSFEPIKADPTGVLDLPKELSEIFDPTRECMSSELLEELMSSEVFAPLLRLSPPPGDHDYIYNLDESEGVCDLFDVPVLKL | Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1. Specifically required for multiciliate cell differentiation: together with MCIDAS and E2F5, binds and activate genes required for centriole biogenesis.
PTM: Differentially phosphorylated in vivo.
Sequence Mass (Da): 43833
Sequence Length: 410
Subcellular Location: Nucleus
|
A3DJK3 | MKDIIVKANDVEYAYKKNSDETPKVLVLKELNTEICEGEFVAVIGRNGSGKSTFARLLNAILIPTRGVLYIGGKETYTEANLWEIRRTVGMVFQNPDNQIIATSVEEDVAFGPENIGIPSDEIVKRVEEALRSVGLEEYKKALPHHLSGGQKQRVAIAGILAMKPKCIVLDEATSMLDPSGRKEVLKVLRDLNEKENITIIHITHYMEEAILAKRILVMDEGKIVMDGNPRQIFSKVEEIKALGLDVPQVAELFHELKKDGYNVPDNILTVEEAVQCLAEMIAKA | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31708
Sequence Length: 285
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
P40735 | MNQNQLISVEDIVFRYRKDAERRALDGVSLQVYEGEWLAIVGHNGSGKSTLARALNGLILPESGDIEVAGIQLTEESVWEVRKKIGMVFQNPDNQFVGTTVRDDVAFGLENNGVPREEMIERVDWAVKQVNMQDFLDQEPHHLSGGQKQRVAIAGVIAARPDIIILDEATSMLDPIGREEVLETVRHLKEQGMATVISITHDLNEAAKADRIIVMNGGKKYAEGPPEEIFKLNKELVRIGLDLPFSFQLSQLLRENGLALEENHLTQEGLVKELWTLQSKM | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31459
Sequence Length: 281
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q8R7Y4 | MAFIIRAQNVSFCYSEGESKSPPVLKDINLQFEKGQFIGIIGHNGSGKSTLAKHFNALLLPTKGNVYVKDMDTKDAKHLWDIRQTAGLVFQNPDNQIVAAIVEEDVAFGPENLGIPPEEIRKRVEYALKAVGMWEYKDFPPHMLSGGQKQRVAIAGIIAMKPECIVLDEPTAMLDPIGRREVISTIKKLNKEEGITVILITHFMEEVVDADRVIVMDDGKVVLDGTPKEVFKEVEVLKKIGLDVPQVTELAHQLRKEGIDIPSDILTIEEMVEFICR | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30917
Sequence Length: 277
Subcellular Location: Cell membrane
EC: 7.-.-.-
|
Q74L61 | MSIEFKNVDYVYAPGTPFQTQGLIDISFKIEKGSFVAIAGHTGSGKSTLMQHFDGLLLPSKGEITVAGEQINANTSSKALKAIRKKVGLVFQFPENQLFEETVLKDVMFGPLNFGFSEQKAKEQAVEWIKKVGLSEDMMDKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGQKQMFEIFKEYQRAGHTVILISHNMDDISEYADDMLVLDHGHLIKHASPQEIFSDQEWVKKHYLDEPATSRLTRELQKGGFQFSEMPLTIESLVSKVANELKKKGDMDE | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32312
Sequence Length: 289
Subcellular Location: Cell membrane
EC: 3.6.3.-
|
A2RI02 | MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKATHFADQLQKTGAVAFEKLPITRAELVTLLTSLSVNSGGEN | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. In this organism these probably include biotin, thiamine precursor, niacin, pantothenic acid, queuosine precursor, riboflavin and thiamine. Uptake of niacin or riboflavin into proteosomes containing EcfA1A2T and Niax or RibU has been demonstrated. Uptake requires hydrolyzable Mg-ATP and is substrate-specific; NiaX-containing proteosomes did not transport riboflavin.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31624
Sequence Length: 288
Subcellular Location: Cell membrane
EC: 3.6.3.-
|
Q035B3 | MDITFDHVSFTYQAGTPFAGDGIKDVSGVIRDGSYTAIIGHTGSGKSTILQHLNALLKPTSGTVTIGDKVITNETNNKNLKPLRQKVGMVFQFAENQLFEQTVAKDIAFGPQNFGVSEKDALALADKMVKMVGLPHDVLEKSPFDLSGGQMRRVAIAGVLAMQPEVLVLDEPTAGLDPSGRHEMMQMFEQLHREQGQTIVLVTHQMDDVADYADTVWVMAEGKLIKTGTPREIFADPAWLKANQLGLPKTAQLAQQLAAKGFHFDPQPLTESELADQLVPQIGGGQRG | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates including 5-formyltetrahydrofolate and thiamine. Expression of the complex plus FolT or ThiT in Lactococcus lactis subsp. cremoris (strain NZ9000) allows 5-formyltetrahydrofolate or thiamine uptake respectively; 5-formyltetrahydrofolate or thiamine are not taken up in the absence of FolT/ThiT or the EcfA1A2T complex. Deenergized L.lactis subsp. cremoris (treated with 2-deoxyglucose) do not take up substrate.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31235
Sequence Length: 288
Subcellular Location: Cell membrane
EC: 3.6.3.-
|
Q03ZL5 | MAINFEQVNFSYGAGTTLAQPILHDINVTIPDGQVTAIIGQTGSGKSTFIQHLNGLLKPTTGRVVIDDFVLTSDLKEKNLTSLRARVGMVFQFPENQLFANTVLEDVMYAPINFGYAKADAEFAAKTALKQVNVSEELWDKSPFELSGGQMRRVAMAGTLASNPDIIVLDEPAAGLDPKGQKELLAIVRGLKEAGKLVVFISHQMDHVIAVADHVIVMHDGGVVAEGTPVEIFNKDLVWFKTVALDLPKAGQFAEQLRQKGHILRHRPLLLTELATMLNEEKRHE | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates including 5-formyltetrahydrofolate, pantothenate and riboflavin. Expression of the complex plus FolT in E.coli allows 5-formyltetrahydrofolate uptake; 5-formyltetrahydrofolate is not taken up in the absence of FolT or the EcfA1A2T complex.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31232
Sequence Length: 285
Subcellular Location: Cell membrane
EC: 3.6.3.-
|
Q71WH8 | MEIKLEQLGYCYQKNSPFEKRALLDVNVSFDSGSYSAIIGHTGSGKSTLLQHLNALLMPTEGKITVGDREIVAGVKQKKLRDLRKKVGIVFQFPEAQLFEETVEKDICFGPMNFGVSEEDAKLRAKKVIYEVGLTEEILSRSPFELSGGQMRRVAIAGVLAMDPEVLVLDEPTAGLDPHGREEIMEMFYNLHKEKGLTTVLVTHSMEDAARYAEKIVLMKAGTVLQIGTPREVFAKPDELVDLGLSVPDVVRFQGLFERKFDVKLTKTCLTIDELTTEMAPYLAKGGA | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31957
Sequence Length: 288
Subcellular Location: Cell membrane
EC: 3.6.3.-
|
Q6F1W4 | MQINKKEIKQNLKKWNEEKKSIKSFSFTGDIILDNVSYTYSKKTPFEFRALDNADLTISDKKITCVIGTTGSGKSTMIQLTNGLLISETGQTIVGDYKIPAGLKKIKEVKDLRREVGLVFQFPEYQLFQDTIEKDIAFGPIHLGADKEEVYKKIPELLDLVSLPREYAKRSPFELSGGQKRRTAIAGIIAMDGKTLVLDEPTGGLDPKGEEDFMNLFLRLNKNQGKRIIMVTHNMDQVLKVADEVIVMHEGKVISKGSPFEIFSNQELLSKIQIEPPKLYKLMYKLKEKGTDLLNKNIRTIDEFAKAFKEVRKGK | Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35738
Sequence Length: 315
Subcellular Location: Cell membrane
EC: 3.6.3.-
|
A1CSU3 | MRLLLSVLLVLVASVGVGLVSAVPAGSSITPPPPIEPIHLLSAPSPSQDSRRPWTRLRDWVIESIWGISKSCSHPHSSSHSSSRDRPPSQALARYGSDVVLRFYPGSAQDAEALAEASEILFLDVWASTPEFVDIRLAEEVISSLLGLLPDSLRTAYTPLIDDLAEMIHASYPTRRSAGVGDQSGFMPTVRQSAQLGDLFFRDYQPLSVIVPWMRLMASMFSSHVEKISVGVSYEGREIPALRLGVREADPEPARPRKTILIVGGSHAREWISTSTVTYVAYQLIARYGKSPEVTRLLEDYDWVLVPTLNPDGYAYTWESDRLWRKNRQPTSLRFCPGIDLDRAWAFEWDGERTRTNPCSETYAGDAPFDGTEAQQLAQWALAQTQSANATIVGFLDLHAYSQQILYPYSYSCSAVPPTLESLEELAMGLAKVIRLTTHEVYDVTSACEGITVSKSTPHVQTNPGSSGGSALDWFYHQLHTNYAYQIKLRDRGSYGFLLPAEYIVPTGREIYNVVLTFGKFLLGDAAAHLDHLDWEAAMATEPEGVVEAQQTLHQPEGGEVAAAADQTEDENENEDEDEEWDEHGWEFRR | Cofactor: Binds 1 zinc ion per subunit.
Function: Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Sequence Mass (Da): 65533
Sequence Length: 590
Subcellular Location: Vacuole
|
E5A0U8 | MRQPTFAALSLLLVAPSLVAAVPHDSTSTSTSTSTRSPSYDPDSTAAHDTTTPHTPPSPWRRLSEAIIRRIGSLPHENHLQKSMLALATGPSSRAPGKQWVAHYGGDVVLRFKMQTADEARALSQAAATLFLDVWEFNEDWADIRLAKDVLPSLLGLLPRSLHASYEPLMQDAALVQAIFDTYPSSSASPSHNTNRFSPNLRPSPHHANGHPFFQDYQPLSVIDPWMSLMSSMFTTHVRKINIGISYEGRDIPALRVGVHPTNKDEPTKPRKTVLITAGLHAREWISTSTVNYLAWSVINAYGKDREITHLLEKFDFVFVPTLNPDGYVYTWETDRLWRKNRQPTSLRFCHGIDLDRSFPYQWNGDQMGSNPCSESFAGDAPFEGVESQRFADWARNETESNNVEFVGLLDLHSYSQQILYPYSYSCHDEPPSLEDLEELGLGLAKAIRISRKGHTYKVTSACEGNVAFANKEKTVLPRIESSGGSALDFFYHELRVKYSYQIKLRDTGNYGFLLPKEEIIPTGEEMLDAVLYLGRFMLGEVGWARRRSRSRWSAPDRGTGDFDEAEQVAIEL | Cofactor: Binds 1 zinc ion per subunit.
Function: Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Sequence Mass (Da): 64366
Sequence Length: 573
Subcellular Location: Vacuole
|
C1GDH9 | MRLFSHLAVLAILACAVPITAIPSFLSNSYPAHPAEGISLFPQTQPQAPLGLWTRLRNTVIERLWRVPPQLCKNRPGHKGKFPLFSAPASLRARYGDDVVLRFTIRNAEEVKALAEASNILFLDVWASTDEWVDIRLSKDVVPSLLGLLPKSLQTSHIPLIHDLPQTIYESYPSSSQRSSYDVQGFSPSTKHSSDKTNIFFQDYQPFSVIVPWMRLLTSMFSSHVQMINIGSTFEGRDIPALQIGVWPANNPKPRKTVVVSGGSHAREWISVSTVNYVAYSLITNYAKSKHVAELLQQFDFIFIPTLNPDGYIYTWEVDRIWRKNRQDTSLPFCPGVDLDRTWGFKWDGNITADNPCSESYPGEDPFAGIEAKQFSQWAKNQTAQNNTEFVAFIDLHSYSQQIRYPYSYSCQPDPPNLENLEELAIGIAKAIRLTNRETYEVSSACEGLMASQAKVKSDDPFPRIERTGGSALDWFYHDLNVKYSYQIKLRDRGSYGFLLPRENIVPTGQEMFNAVMVLGRFLSGHDGFGPLDWEDESQRPKADEDDIPSENELDENDDSWIPYDYRNHDDQNEGEGYDNDEWGFRRRRKR | Cofactor: Binds 1 zinc ion per subunit.
Function: Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Sequence Mass (Da): 67374
Sequence Length: 591
Subcellular Location: Vacuole
|
Q2SLV8 | MIVRTLEQARQSDRRVKADNWESVRMLLKDDNMGFSFHITTLYANKETPIHYQNHLESVYCISGEGEVETVADGEVHAIKPGTLYVLDKHDKHLLRAFSEMTVACVFNPPLNGKETHDENGVYPLEAETIME | Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
Catalytic Activity: (2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine
Sequence Mass (Da): 15077
Sequence Length: 132
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
EC: 4.2.1.108
|
O52251 | MIVRNLEEARQTDRLVTAENGNWDSTRLSLAEDGGNCSFHITRIFEGTETHIHYKHHFEAVYCIEGEGEVETLADGKIWPIKPGDIYILDQHDEHLLRASKTMHLACVFTPGLTGNEVHREDGSYAPADEADDQKPL | Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant. Does not act on N-acetylated amino acids like N-alpha-acetyl-L-asparagine,N-alpha-acetyl-L-ornithine, N-alpha-acetyl-L-lysine and N-epsilon-acetyl-L-lysine.
Catalytic Activity: (2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine
Sequence Mass (Da): 15458
Sequence Length: 137
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
EC: 4.2.1.108
|
O06061 | MKVIKLEDLLGTEREVDDGNWVSRRFIMKDDNMGYSVNDTIIRAGTETHIWYQNHLETVYCIEGDGEIETLSDNKVYQLEPGVLYALDKNDEHMLRGGSKDMRMVCVFNPPLSGREVHDENGVYPADLD | Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
Catalytic Activity: (2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine
Sequence Mass (Da): 14797
Sequence Length: 129
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
EC: 4.2.1.108
|
Q5YW76 | MIVRTTDEITGTERDVAGPGWRSKRIVLGGDGVGFSFHETTIDAGTTHEFHYVHHIEAVWLVEGEGTLTDLDNDQVYDLRPGTMYLLNGHEKHRVQARTTMRMMCVFNPPVTGQEVHDENGVYPLVAVPAS | Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
Catalytic Activity: (2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine
Sequence Mass (Da): 14604
Sequence Length: 131
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
EC: 4.2.1.108
|
Q0SH55 | MIVRTTAEITDTDRDITSEDGNWRSKRIILGGDKVGFSFHETTIKAGSVNEFHYANHVEAVWLVEGTGKLIDLDNDKVYELGPGSMYLLNGHERHRVEPETEMRMLCVFNPPVTGREVHDENGVYPLVEVPA | Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
Catalytic Activity: (2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine
Sequence Mass (Da): 14883
Sequence Length: 132
Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
EC: 4.2.1.108
|
P32940 | MATVILFVAWMACLMVGVCYQEFQTQQNFPDISNPSQELNQEPAHRIVQLDSIQNNGALNMSTGNVLNMSPPPPSPCLSRAKIRHAFKYVTTILSCVIFLVGIVGNSTLLRIIYKNKCMRNGPNVLIASLALGDLFYILIAIPIISISFWLSTGHSEYIYQLVHLYRARVYSLSLCALSIDRYRAVASWNRIRSIGIPVRKAIELTLIWAVAIIVAVPEAIAFNLVELDFRGQTILVCMLPMEQTSDFMRFYQEVKVWWLFGFYFCLPLACTGVFYTLMSCEMLSIKNGMRIALNDHMKQRREVAKTVFCLVVIFALCWLPLHVSSIFVRLSATVKRACILKNKRSCIMAEIQTGVNYQLLMVMNYTGINMASLNSCIGPVALYFVSRKFKNCFQSCLCCWCHRPTLTITPMDEKGSGGKWKANGHDLDLDRSSSRLSNKYSSS | Function: Receptor for endothelin-3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50172
Sequence Length: 444
Subcellular Location: Cell membrane
|
P21450 | METFWLRLSFWVALVGGVISDNPESYSTNLSIHVDSVATFHGTELSFVVTTHQPTNLALPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFEQNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYKGAQHRTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYDEMDTNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQWKNHEQNNHNTERSSHKDSIN | Function: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48515
Sequence Length: 427
Subcellular Location: Cell membrane
|
Q61614 | MSIFCLAAYFWLTMVGGVMADNPERYSANLSSHMEDFTPFPGTEINFLGTTHRPPNLALPSNGSMHGYCPQQTKITTAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLITAIEIVSIWILSFILAIPEAIGFVMVPFEYKGELHRTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYDEMDKNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCHQSKSLMTSVPMNGTSIQWKNQEQNNHNTERSSHKDSMN | Function: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48578
Sequence Length: 427
Subcellular Location: Cell membrane
|
Q95L55 | METFWLRVSFWVALVGGVISDNPESYSTNLSIHVDSVTTFRGTELSFVVTTHQPTNLALPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFEQNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYKGAQHRTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYDEMDTNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQWKNPEQNNHNTERSSHKDSIN | Function: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3 (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48510
Sequence Length: 427
Subcellular Location: Cell membrane
|
Q90328 | EIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPISVYKLLAEDWPFGVEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVISVVLAVPEAIAFDMITMEYRGKDLRICLLHPTQKTSFMMFYKQAKDWWLFSFYFCLPLAITALFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTIYDQKDPNRCELLSFFLVMDYIGINMASLNSCINPIALYLVSKRFQNCFKSCLCCWCQSKDLLSLEERQSCLKFKANDHGYDNFRSSNKYSSS | Function: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39826
Sequence Length: 347
Subcellular Location: Cell membrane
|
P24530 | MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS | Function: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
PTM: Palmitoylation of Cys-402 was confirmed by the palmitoylation of Cys-402 in a deletion mutant lacking both Cys-403 and Cys-405.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49644
Sequence Length: 442
Subcellular Location: Cell membrane
|
Q28468 | PFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGIPKWTAVEIVLIWVVSVVLAVPEAIGFDMITMDYKGSYLRICLLHPVQKTAFM | Function: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10943
Sequence Length: 99
Subcellular Location: Cell membrane
|
P48302 | MQSPASRCGRALVALLLACGFLGVWGEKRGFPPAQATLSLLGTKEVMTPPTKTSWTRGSNSSLMRSSAPAEVTKGGRGAGVPPRSFPPPCQRNIEISKTFKYINTIVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPINTYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDMITSDYKGKPLRVCMLNPFQKTAFMQFYKTAKDWWLFSFYFCLPLAITAVFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYDQSNPHRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQTFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS | Function: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Essential component in the normal development of two neuronal crest-derived cell lineages.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49561
Sequence Length: 442
Subcellular Location: Cell membrane
|
P35463 | MQPLRSLCGRALVALIFACGVAGVQSEERGFPPAGATPPALRTGEIVAPPTKTFWPRGSNASLPRSSSPPQMPKGGRMAGPPARTLTPPPCEGPIEIKDTFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPINVYKLLAEDWPFGVEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEALGFDMITTDYKGNRLRICLLHPTQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYDQNDSNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS | Function: Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49595
Sequence Length: 443
Subcellular Location: Cell membrane
|
Q92005 | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAGGVGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSQARFEEITKEVSAYIKKIGYNPASVAFVPISGWHGDNMLEASSNMGWFKGWKIERKEGNASGTTLLDALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPANVTTEVKSVEMHHESLTEATPGDNVGFNVKNVSVKDIRRGNVAGDSKNDPPMEAANFNAQVIILNHPGQISQGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDNPKALKSGDAAIVEMVPGKPMCVESFSTYPPLGRFAVRDMRQTVAVGVIKSVEKKIGGAGKVTKSAQKAAKTK | Function: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome. The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 50048
Sequence Length: 462
Subcellular Location: Cytoplasm
EC: 3.6.5.-
|
Q8SS29 | MATKVEDDSKPRLNACFIGHVDSGKSTTVGMLSYQLGAVDKREMEKYEKEAALNNKETFYLAYLTDKTDAERKRGITITTTLVNLPTEKFNINILDCPGHKDFVKNMVTGASQADVAVVIVPASGFESCVGVGGMLKTHIMISGILGCEKLIVCVNKMDEIPENKRMEKFNEVSAEMLRIVKRSHKDKNPIIIPISAFKGINLTKKGEKFEWFKGWKEKEGSSVIYTLEEALNYQDVPERHNDKPLRMPITKVCSIAGVGKIFTGRVEYGTITPNLKITIQPAGVVGETRSVEIHNKPRSMIPCGENCGVALKGGVIGEIDKVDAGHVISANDENKAVAYPGAKIRTIVVGRPKGLSPGYTPQINFGNCHSPGRIAKILSKVVGKEVHENPENVANGENFTGIVVFQKPLVIDKMERFQNLAKFALMDSNGVVGIGNVMEPLTRDQLLKDYGIDLNEDPKAAKKAASKKKA | Function: GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome (By similarity).
Sequence Mass (Da): 51587
Sequence Length: 471
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
P32471 | MASTDFSKIETLKQLNASLADKSYIEGTAVSQADVTVFKAFQSAYPEFSRWFNHIASKADEFDSFPAASAAAAEEEEDDDVDLFGSDDEEADAEAEKLKAERIAAYNAKKAAKPAKPAAKSIVTLDVKPWDDETNLEEMVANVKAIEMEGLTWGAHQFIPIGFGIKKLQINCVVEDDKVSLDDLQQSIEEDEDHVQSTDIAAMQKL | Function: Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex.
PTM: S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.
Sequence Mass (Da): 22627
Sequence Length: 206
Domain: The C-terminus (pos. 119-205) exhibits guanine nucleotide exchange activity.
Pathway: Protein biosynthesis; polypeptide chain elongation.
|
Q7CI09 | MRDKTGPKFGPYQPDDEAVSPSRRRLILGMGMVSGALVLGGAKTAQAADCRSPDVAGTQDERWQKQPFYGQHQAGVLTPQQAAMMLVAFDVLATDKTSLIRLFKLLTERLAFLTTGGRAPSVNAKLPPLDSGIMGPEIYPDNLTVTVSVGNALFDERFGLQGQKPLRLQRMTRFPNDSLDAGLCHGDVMLQICANTNETVIHALRDIIKHTPDLLSVRWKREGFISAHAARSKGQDTPINLLGFKDGTANPKISNKPLINNVVWVSNNAGEPAWAVGGSYQVVRIIRFKVEFWDRTPLQEQQTIFGRDKNSGAPLGMQHEHDEPNYAKDPEGKVIPMDAHIRLANPRTIETQRNLMLRRGYSYSLGVSNSGQLDMGLLFVCYQSDLAQAFLTVQERLNGEALEEYVKPIGGGYFFTLPGVADANHYLAQSLLEA | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.
Function: Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 47801
Sequence Length: 434
Subcellular Location: Periplasm
EC: 4.98.1.1
|
B7GHE5 | MISVNDFRTGLTIEVDGDIWRVIEFQHVKPGKGAAFVRSKLRNLRTGAIQEKTFRAGEKVSKAQIDNRKMQYLYANGDQHVFMDMESYEQIELPAKQIEHELKFLKENMEVFIMMYQGETIGVELPNTVELKVVETEPGIKGDTASGGSKPATLETGLVVQVPFFVNEGDVLIINTTDGTYVSRA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 20760
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
O67376 | MATEIDINRIQKDIFIEHKGEPYRVLDYEHVKPGKGQAFVRVKAKNMLTGNVTELTFKASDRIPLADFEQVYATYSYNDGENYYFMNTQTYDMIAVPKEKIEEEAKFLKEGMEVIVFLYKGQPIGIELPKHVELQVVETEPAFKGDTQAGGTKPAKLETGAVIQVPFFVKEGDIVKVDTRTGSYVERVKEAK | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Sequence Mass (Da): 21807
Sequence Length: 192
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q2NJ31 | MINTNDFKTGKTIKFNNQIYQILEFLHVKPGKGSAFVRTKLRNLRTGSVIDYTFNAGIKVQPALITKIKMQLIYVLEDNYIFMNTQNYEQLEINKYQLKDFLKYLYEGLLVDIIFYENDEIVGISLPEKISIKVAYTEPGAKGDTKTNSLKDATLETGLVIKVPLFINIGEKIIINTETGLYLSRDNNK | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 21657
Sequence Length: 189
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q9RY32 | MISVTELRNGTKVQMDGGLWECLDYSHLKMGRGGAKVVTKFRNMESGSIVDRTFNSTEKLQDIYVEGKKMQYLYPDGDDYVFMDMETFDQVHLGKNIVSDAAKFMKENTEVEVAMYGDKALSISLPNQVILKITQTDPGVRGDTVSGGTKPATLETGAVVQVPLFVEQGTDVKVDTRTGQYLSRA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 20475
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q44247 | MISSNDFRPGVSIVLDGSVWRVIDFLHVKPGKGSAFVRTTLKNVQSGKVLEKTFRAGETVPQATLEKITMQHTYKEGDEFVFMDMESYEEGRLSAAQIGDRVKYLKEGMEVNVIRWGEQVLEVELANSVVLEVIQTDPGVKGDTATGGTKPAIVETGATVMVPLFISQGERIKIDTRDDKYLGRE | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Sequence Mass (Da): 20496
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q2G6X5 | MKISGVDIRPGNILEYEKGIWKVAKTQHTQPGKGGAFMQVEMKNLIDGRKTNVRFRSADTVERVRLDTKDFQFLYAEGDDLVFMDVETYDQITLPSDLLGDAAAFLQDGMTVLLEMYDERPISVQLPEQVEATIVEADAVVKGQTASSSYKPAILDNGVRVMVPPHIESGTRIVVDVYERSYVGKAN | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 20831
Sequence Length: 187
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q0AZH4 | MISVNDFKTGVTIELEGQAFQVVEFMHVKPGKGSAFVRAKLKNVKTGGTVEKTFRGGEKVPRAHLDKREMQYLYNDGEGYVCMDTENYEQISISKESIGEGAKWLMENMILGVLFFQGNIIGVDLPNFVEMLVVDTEPGVKGDTATGAVKNATLESGAVVQVPLFVNTGDRLRIDIRTGEYMERV | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Sequence Mass (Da): 20443
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q9X284 | MIEVGDLKKGMFIIYDGEIYRVLEASKHFMGRGSGLIRTKLKNVKTGFVREVNFPSGEKVQEAELSFRKAQYLYRDGDHYYFMTLDDYEQYALSEEEIGDAKYYLVENMEVDLVFHEGTPIGIELPTTVELTVVETEPSFKGDTVSGGGKPAVLETGLKITVPYFIEVGDKIKVDTRTGEYVGRA | Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Sequence Mass (Da): 20875
Sequence Length: 185
Pathway: Protein biosynthesis; polypeptide chain elongation.
Subcellular Location: Cytoplasm
|
Q20402 | MRTSDSHLPLSNLARSDSIEFKDAVINEKWVHSANRRKGHLTPKAPEKKSGWFGGQKSEEELLMERVEQHELEELQTFIAQKLFRVDGIICDEETRILLVEKLMNAKEYPTINHDELAHRYGSSMAGWLRDRLVPSMSDCSSVLQRAAAEFYQNKMSDPLCNWGQLNPEHVSMVAARIAKFSEEMSSKVKWSLLVEPGKFSCHLTEFVQEFNRLDRMFVSNELSDEESLQTAFNANYLTKARSKMVPCAEFSRVKLNDGLGRLDDRNELRNGMFSDEHEFLQEEGYTAKSTYGTTDFIHANYVKGGPLLNTFICAQAPLKNTQEDFWRMVFQEKCQFIVMLNSAVDSSTLGPLDSANRNHCPYYWPRAENESLRFGSFHITCMKVDSKADPLFTITKLKVQKVGGNLLDAEFDEELFLEHWQWDWQYLGDVHWPFRVLRKARQLSTPTIVQCIDGCSKSGTLVSIETALMHFIRGSPITKSLILQSCVFVRLQRRLSVSSVLLYLFIYRVILRWIEPYVNKWYHRAALGLRFKSIGFIQKYNAMIQEFSRITPAY | Function: Probable pseudophosphatase required for the oocyte-to-zygote transition during which it regulates the polarized dispersal of the cortical actin cytoskeleton, the synthesis of the eggshell chitin layer and the formation of the polar bodies after meiosis I and II . Acts as scaffold to tether kinase mbk-2 and pseudophosphatases egg-4 and egg-5 to the oocyte cortex and thus restricts mbk-2 activity to the cortex during meiosis I . Regulates mbk-2 localization to cytoplasmic foci during meiosis II . Also required for chitin synthase chs-1 localization to the cell cortex of unfertilized oocytes and to cytoplasmic foci in the fertilized embryo .
Sequence Mass (Da): 64151
Sequence Length: 555
Domain: The N-terminal destruction box (D-box) motifs 1 and 2 act as a recognition signal for degradation via the ubiquitin-proteasome pathway.
Subcellular Location: Cytoplasm
|
P90920 | MRWLTLIAVAHLIAFLSSAEITCPRIPEKCDCKISKSMIILSCNGEDVKTIAQTVGTSQIDELHILNGTDVKIESLPFNGLRTIAILNSTLQSFSPTAWRHVEATIEHITINGNELKTVPVFGNLSTLMSMNLNSNQISSIPDKAFNGLSALTQLRLENNAICDFPPKSLDAVKASLVLLDVSGNCLDAIPAQILRNAANLMYLDLGSNNISEINNFELMNLPFLRELRVQNNTLRRIHPMAFMNVPQLQYLYLQDNIISTLDGNRLQGFKNLEVLDVSNNALYALPSLKDLPNLKQVRVDGNLITKIETLAFSNNPNLQLISVQNNNIVQISRNSFESLDKLVVLLVGNNSLAKIERGMFDGMKNLQQLSIRNNTLTALDASSFAQLAHLTTLDLGHNKIHDIEEGTFDKLSKLFWLDLSNNKISGFKTSVFKKKISNILLDGNQLICDESFNEFLTYLIANKVRTFLPFQQEIMCHGPEKYAGVRLKDLMMKKANETLSEGSRLLGVPQGSNQHSLLSSFLPSLGPLGTLNGAGGAAIPLVNTLTNTIPALRSIPGFGGNIPVGTGASSVPNKNLNDAIEGFTGPLVRFATGGQPVASDIEQLIRSIPNMVVNVPGFGDIDLSKMDPTMIQYVLNGGQIPGIDKATLDKIVKQTMNKMHTAAAANLAGNPVEGQEKVLPPLDKLPSGLVTQVMSGEPLPGLNENQTKIIMEYYTHQMPGMDGIPARPVESQGNTTANNMFNPAMFDLLKMLPPGYNLSKIPMEVIAAVTRGEVPDMRLLPEDLLEHFKQHTTSLTSMFAGATAKNISIEEILEKLPVFVRPELSTFVPYDINELTSEMVLEQEQNERHRNIRIITAIALAFVGAVTVVVIIFFVNYTKKQRRLRKSLVYRSSPSSSGSSGQNAANESGRSSAAPSPIRPPLMNIPKTPNNRTMESTFGQPQLCSTLLENPQAVSHRSRH | Function: Required for apical extracellular matrix organization and epithelial junction maintenance.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 105365
Sequence Length: 961
Subcellular Location: Apical cell membrane
|
P40566 | MPAKIHISADGQFCDKDGNEIQLRGVNLDPSVKIPAKPFLSTHAPIENDTFFEDADKVSFINHPLVLDDIEQHIIRLKSLGYNTIRLPFTWESLEHAGPGQYDFDYMDYIVEVLTRINSVQQGMYIYLDPHQDVWSRFSGGSGAPLWTLYCAGFQPANFLATDAAILHNYYIDPKTGREVGKDEESYPKMVWPTNYFKLACQTMFTLFFGGKQYAPKCTINGENIQDYLQGRFNDAIMTLCARIKEKAPELFESNCIIGLESMNEPNCGYIGETNLDVIPKERNLKLGKTPTAFQSFMLGEGIECTIDQYKRTFFGFSKGKPCTINPKGKKAWLSAEERDAIDAKYNWERNPEWKPDTCIWKLHGVWEIQNGKRPVLLKPNYFSQPDATVFINNHFVDYYTGIYNKFREFDQELFIIIQPPVMKPPPNLQNSKILDNRTICACHFYDGMTLMYKTWNKRIGIDTYGLVNKKYSNPAFAVVLGENNIRKCIRKQLSEMQKDAKSMLGKKVPVFFTEIGIPFDMDDKKAYITNDYSSQTAALDALGFALEGSNLSYTLWCYCSINSHIWGDNWNNEDFSIWSPDDKPLYHDTRAKTPTPEPSPASTVASVSTSTSKSGSSQPPSFIKPDNHLDLDSPSCTLKSDLSGFRALDAIMRPFPIQIHGRFEFAEFNLCNKSYLLKLVGKTTPEQITVPTYIFIPRHHFTPSRLSIRSSSGHYTYNTDYQVLEWFHEPGHQFIEICAKSKSRPNTPGSDTSNDLPAECVIS | Function: Ergosteryl beta-glucosidase involved in the ergosteryl beta-glucoside (EG) catabolic pathway and vacuole formation via hydrolysis of EG to generate glucose . Is also able to hydrolyze cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate C6-NBD-ceramide (Cer) .
Catalytic Activity: ergosteryl 3-beta-D-glucoside + H2O = D-glucose + ergosterol
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86979
Sequence Length: 764
Subcellular Location: Cytoplasm
EC: 3.2.1.-
|
O01346 | MNSTTKHLLHCTLLITVIVTFEVFSGGIKIDENSFTLVDPWTEYGQLATVLLYLLRFLTLLTLPQVLFNFCGLVFYNAFPEKVVLKGSPLLAPFICIRVVTRGDFPDLVKTNVLRNMNTCLDTGLENFLIEVVTDKAVNLSQHRRIREIVVPKEYKTRTGALFKSRALQYCLEDNVNVLNDSDWIVHLDEETLLTENSVRGIINFVLDGKHPFGQGLITYANENVVNWLTTLADSFRVSDDMGKLRLQFKLFHKPLFSWKGSYVVTQVSAERSVSFDNGIDGSVAEDCFFAMRAFSQGYTFNFIEGEMYEKSPFTLLDFLQQRKRWLQGILLVVHSKMIPFKHKLLLGISVYSWVTMPLSTSNIIFAALYPIPCPNLVDFVCAFIAAINIYMYVFGVIKSFSLYRFGLFRFLACVLGAVCTIPVNVVIENVAVIWGLVGKKHKFYVVQKDVRVLETV | Function: Glycosyltransferase with a proposed role in glycosphingolipid biosynthesis. Neurogenic protein implicated in epithelial development. Critical component of a differential oocyte-follicle cell adhesive system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51984
Sequence Length: 457
Subcellular Location: Membrane
EC: 2.4.1.-
|
P91082 | MLTCIQPSSSSIGGFGKADDNVRILLMASVRNEFGDTSIFSRLGVTALGQHYVLVTKKKMFGGYTTHMITANMRNRPFISIPFKVSSGAQSIEESRDLISRLTTVLGRPGMFSFDDPPIGSQFPVGKELIQLDEVPVGVHDRQDKYLEKGDEVFCEVNVSGVKFYHSGIYAGDGMCYHFVCDAQESESFADALAVFSGASAHVVYDTWFEFVYALVEVSDVPPKIFRASHPLICRSGEQVVKYAEHLQRELENYDIRRCNCQHFSSECSTGVPFSYDMTSNFKYLACTVLKPTSTVVNAMTRPNRDRSSFASSSTSS | Function: Putative acyltransferase (Probable). Plays a role in the morphogenesis of a vulval toroid cell, vulF, which is located where the vulva and the uterus connect . Not required for specifying vulval cell fate .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35164
Sequence Length: 317
Subcellular Location: Apical cell membrane
|
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.