ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9VVW5 | MPETEHETCSKEWLQSQLRSLDSKDLILLDCRGSHEYSESHIRGAVNLCIPSIVLRRLAVGKIDLASTIKSPELKQRIQSGYKLCWFILYNGEGVPGQNQEIAGAGSLAVAMDSIISILHRRLKQDGCRVVALQDGFNNFRQAFPEWCEDDNQTHSKEIESSRNVQTDQLMGLRSLRISTTQSDSACSSSAESSDCESSSHHHHHHSHHNYNEAPVEIIPGLLFLGNATHSCDSEALKKYNIKYVLNVTPDLPNKFKESGDIKYLQIPITDHYSQDLAIHFPDAIQFIEEARSASSVVLVHCLAGVSRSVTVTLAYLMHT... | 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.... |
Q9VWF4 | MEQSQSQRQAWPSSSAGGGKAQDSGVLTREDFDGGPVSIDEVDTGLFLGNLTAATHMETLRSFKITHILTLDSVPLPQHILEASFLTTKYIQIADMPREDILQHLEGCVDFISSALAQQGNVLVHCYFGVSRSSSTVIAYMMKRHNLDFLPAYELVKAKRRFVQPNAGFVSQLKLFRRMGCKIDPNCQRYKIHRLRLAGEQMRKAKILPQSFHSVVRPDPDITRENPEPIVFRCRRCRRVLASKSHVLEHKPRDRPPQEVVPKEKEEVAAAKLPAQSHDQAENHHGARMLEQLSERIRQSSLGSPGHESTPNYCRSILFV... | 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... |
Q53UH4 | MGSQATTYHMAMYPWFGVGHLTGFFRLANKLAGKGHRISFLIPKNTQSKLESFNLHPHLISFVPIVVPSIPGLPPGAETTSDVPFPSTHLLMEAMDKTQNDIEIILKDLKVDVVFYDFTHWLPSLARKIGIKSVFYSTISPLMHGYALSPERRVVGKQLTEADMMKAPASFPDPSIKLHAHEARGFTARTVMKFGGDITFFDRIFTAVSESDGLAYSTCREIEGQFCDYIETQFQKPVLLAGPALPVPSKSTMEQKWSDWLGKFKEGSVIYCAFGSECTLRKDKFQELLWGLELTGMPFFAALKPPFEAESIEAAIPEEL... | 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 ... |
V6CIV8 | MTTHLPSTSQNGEEISAEQFNRIFHERNVIVLDCRSNGDSVKRANRFFCSLRLPALLQRRLMGGSMRLSTVPDLKDLNNSPDQCPEVLLIPGDSEQDEQLSAALARNLKSNHYRHFVLGEPVKTLLSQFPTLRDAADENWNTTFQMNSMPGQASGQQASSGPLLNLNQLRLEGEDQGGKQRAEFPVKLTNFLYLGNAETAKNRDVLKKYSISHVINVTSNLPNTFEEDPNMRYLRISADDNASHNLTKFFPEAISFIDDARRNDSACLVHCLAGISRSVTICLAYLMKTEMCTLDSAYEWVQKRNASIAPNFHFMGQLTD... | 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 kin... |
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 | MNDVSRIFPGFYIGSLPAVNRNTLDKYQITHVCSVLNEFQPKWTKIYKYLHIDIYDSPSVDIMKYFDKTFQFIEEGRKDGGVLVHCFAGISRSATICIAYIMRKLNISFEDAHGLVSDARPIIYPNESFIKQLKKYELILKKNRENPQIVEKESEEEDDDEDDDDDDYDSDEDDDDDSEDDDFEEEFDNVVKKKNNNNKKVNVKNTTKVFSNISISSEQTTTSTTTVPTPTLNPETKIEETTTTTTATATATLVEEVVESTSPKATLGEHRYSCRKCSKDLFLDFDILDHEQGQGQTSFKWNKRDNTTCNKSVGANGEQI... | 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 | MVLINRVNIQPEELPLLYHVNSMDVYNLLQDIGSSKIIIDLRTKEQYEKNHIRTSVNIPPPPSTTPLYENGEIKEFNLSKYIGSNVTAKHWNLIFQKLIVYSDKPFLYNIDELEKTISTTTITTTATTTTTTTTTSNSIGSDQDIIKSLKVSDWDKVVLRHFLLKKKKTKVIIYQGGFDQFQKDYSFMCNPSSSPSSSSGGGGGSQLYPSEIIKDFLYLGGAENAGNRQQLINLKITHLVNMAGELDDVYPHLYKYYRANLDDRPKANIYEHFEPVIQFINDCKKQGGRVLIHCAMGISRSTTVVLAYLMKEDHMTYSDA... | 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
Seq... |
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
Seq... |
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
Seq... |
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
Seq... |
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
Seq... |
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
Seq... |
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
Seq... |
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(... |
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
Seq... |
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
Seq... |
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
Seq... |
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: Sin... |
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 coor... |
P51141 | MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNRDEAARTNGHPRGDRRRDLGLPPDSASTVLSSELESSSFIDSDEEDNTSRLSSSTEQSTSSRLVRKHKCRRRKQRLRQTDRASSFSSITDSTMSLNIITVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRV... | 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 f... |
Q5IS48 | MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNREEAARTNGHPRGDRRRDVGLPPDSASTALSSELESSSFVDSDEDGSTSRLSSSTEQSTSSRLIRKHKRRRRKQRLRQADRASSFSSITDSTMSLNIVTVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRV... | 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 f... |
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: Sin... |
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: Sin... |
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: Sin... |
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: Sin... |
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: Sin... |
Q60838 | MAGSSAGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDTPQPEVAPPAHESRTELVPPPPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRDRPRRRDSSEHGAGGHRPGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEDDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRMERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQV... | 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 ... |
P51142 | MAETKVIYHLDEEETPYLVKVPVPATDIRLRDFKAALGRGHAKYFFKAMDQDFGVVKEEISDDNAKLPCFNDRVVSWLASSEGSQPDSAPPAPATEVRPEPPPPVPPPIPPPPAERTSGIGDSRPPSFHPNVSGSTEQLDQDNESVISMRRDRVRRRESSEQAGVGRGVNGRTERHLSGYESSSTLLTSEIETSICDSEEDDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDINFENMSNDDA... | 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 p... |
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 coor... |
Q92997 | MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPDPAPFCADNPSELPPPMERTGGIGDSRPPSFHPHAGGGSQENLDNDTETDSLVSAQRERPRRRDGPEHATRLNGTAKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLR... | 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 | MKAITLVGSTGSIGTQTLDIVTQYPDQFRIVGLAAGNNVEMLAAQIRQFRPKIAAICSEDKLPALKEAIIDLDPQPILLAGEAGVIEVARYGDAQTVVTGIVGCAGLLPTIAAIEAGKDIALANKETLIAGAPVVLPLVEKHGVKLLPADSEHSAIFQCLQGVPKSGLRKILLTASGGAFRDWDVERLADVTVADALKHPNWSMGRKITVDSATLMNKGLEVIEAHFLFGLDYDNIEIVIHPQSIIHSLIELQDTSVLAQLGWPDMRLPLLYALSWPDRIYTDWERLDLVKAGNLTFREPDHQKYPCMQLAYAVGKAGGS... | 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
Pathw... |
Q313H2 | MNGYISPLPDAAWNSRFPRSLVLLGSTGSIGTSALRVVERQPELFRITALAGARNVRLLARQAAAYRPPHLAVINGNAADELASLLPAGYRPRIHTGQEGYEFLAALPEADCVLSAQVGAAGLRATVAAARAGKTIALANKESLVLAGGLIRRLCHETGASVLPVDSEHNAIFQALQGHDAAQMRRIILTASGGPFRGRDRTFLQSVTREQALNHPNWSMGAKISIDSATLMNKGLEVIEACHLYNAPLEKVEVVVHPQSIIHSLVEYNDGSQIAHMGTPDMRIAIAYCLGWPRVMHTGVEPLDLLSVGSLTFESPDISL... | 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
Pathw... |
Q6MEL5 | MKHIAILGSTGSIGKNTLQVARHLKERIKVVAIAARENIDLLEAQSKEFCPDIIAVFNNAKAYELQKRLPGKTVLAGMEGLLAAASYSEADLVISAMTGTMGLQPTIEAIKAGKDVGLANKEALVSGGAIIMKLVKEKNINLLPIDSEHSAIFQCLNGEALKSVQRIILTSSGGPFRTWTQEQLETVTVEQALNHPTWSMGPKVTIDSSTLMNKGLEVIEAFWLFDVSPEQIDVIVHPQSIIHSLVEFCDGSMLAQMSEPNMIVPIQYSLTYPDRAPGLFKPFDFMKNSKLEFFEPNKKTFRCLALAYEALKCGGTLPCY... | 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
Pathw... |
A5D2U3 | MKNIVLIGSTGSIGRQTLEVIGSLPDRFKVVGLGSGKNWRLMAEQIRVFRPSAVAMAGEREIMNLKELLAGSYCPELGWGRTGMESLASMPEADLVVVAVTGFAGIYPTIAAIQAGKDVALANKETLVAAGHLVMKMAERHRAAILPVDSEHSAVWQCLCGRNSGEVEKIILTASGGPFREMCLEKLEKVTVDMALKHPNWNMGSKITIDSATLMNKGLEVIEAKWLFGLNYSQIEVVIHPQSIVHSAVEFLDGSVIAQMGLPDMRLPIQYALTYPERLPGSFPKLKLASLQGLTFEEPDTRRFPCLSLAFEAGLAGGTM... | 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
Pathw... |
Q4FM64 | MKKIAIFGSTGSIGSSLLKIIKDDQKNFKIELLTVNKNYKKLIKQVKLFNVKNVIVTDYNSFLITTKLLKNAKVKVFNNFDSLNKIFNTNNKIDYSMCAISGFDGLKPTLDIIKFTKTIAIANKESIICGWNLIKKDLKKYKTYFVPVDSEHFSIWSLLDNNKKNNFEKIYITASGGPFRNLSLKKFRNISVKDALKHPNWSMGKKITIDSATMMNKVFEIIEAKKIFNLNYKQLEILIHPKSYLHAIVKFNNGLSKLLVHDTNMTIPIFNSIYFNTDKKLKSKNIDIKTLNNLNLKKIDNIRFPVIKILNNLSNEDSLF... | 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
Pathw... |
C0QTC4 | MKRLAVLGSTGSIGTQTLDIVRKYRDRLEVSLLAASRVSEKLLDQIDEFKPEYVYIAEGEKIKGVKTLIGEDGLYKLAQLDIDLFINGISGINGILPTYLLLENNKKLATANKEAIICLGEIYGDKYSDIFPIDSEHSAIFQCLLSGRKEEVEKIILTASGGPFLNLPKEEFRYITPDQALNHPRWKMGKKVSIDSATLMNKGFEIIEAHYLFNIPYSKIDVVIHPESIVHGLVQFIDGSVISHLSPPDMRIPICYAISYPERWEIDVRRLNLAQVKNLTFLEPDYDRFPLLNIAKECGEKGGACPTVLTTADEIAVNLF... | 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
Pathw... |
Q2IPZ2 | MGRLLDTIDSPADLKKVPVEQLPALCQEIRELIIQTCARNGGHLGSSLGAVEINVALHHVFASPQDKLVWDVGHQAYAHKLLTGRRDAFRTIRTEGGLAGFPERHESAHDAFGVGHASTAISAALGMIEAKRVTGEPGKVVAVVGDGAMTGGVAFEGLNQAGYLGRNLLVVLNDNEMSISPNVGALSEWFSKKFASRTYNRWRRQVKEFLESVPKGPEAIGIIRHGINATKALVTPGILFEGLGFHYVGPVDGHDVKGLVETFQKLAVFDGPVLLHAITTKGKGYHPAESDKATRGHGLSFFDVATGKPVKKSPGAKAYT... | 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
Sequ... |
O67036 | MLEKYEILKDYKGPFDIKNYDYETLQKLAQEVRDYIINVTSKNGGHVGPSLGVVELTIALLRVFNPPEDVIVWDIGHQGYPWKILTDRKEQFPTLRQYKGISGFLRREESIYDAFGAGHSSTSISAALGFRIGKDLKGEKEDYVIAVIGDGALTAGMAYEALNNAGHIRPDRFIVILNDNEMSISPNVGAISTYLNRIISGHFVQETRQKIKNFLQHFGETPLRIMKLTEEFLKGLISPGVIFEELGFNYIGPIDGHDIKALEDTLNNVKDIKGPVLLHVYTKKGKGYKPAEENPVKWHGVAPYKVESGEIIKKSSPPTW... | 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
Sequ... |
Q38854 | MASSAFAFPSYIITKGGLSTDSCKSTSLSSSRSLVTDLPSPCLKPNNNSHSNRRAKVCASLAEKGEYYSNRPPTPLLDTINYPIHMKNLSVKELKQLSDELRSDVIFNVSKTGGHLGSSLGVVELTVALHYIFNTPQDKILWDVGHQSYPHKILTGRRGKMPTMRQTNGLSGFTKRGESEHDCFGTGHSSTTISAGLGMAVGRDLKGKNNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPSPPVGALSSALSRLQSNPALRELREVAKGMTKQIGGPMHQLAAKVDEYARGMISGTGSSL... | 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.
Catalyti... |
A0JVG9 | MGILDTIRNPQDLSKLTEEQLSQLAAEVRSFLIGNVSQTGGHLGPNLGVVELTMAVHRIFDSPRDSIVFDTGHQSYVHKLLTGRQDFSTLRQEGGMSGYPDRGESEHDIVESSHASSSLSWADGISRARQLTGDGDRYVIAVVGDGALTGGMAWEAINNIAADKRRRVVIVVNDNGRSYAPTVGGFADYLASLRPTIDSFRAAPAYEGTLDWWKRKLQNGGPVGQFTYRSLHAMKKGIKDWWAPQGMFEDLGMKYIGPVDGHNLQAMEHALSTAKNYAGPVIVHAMTEKGHGYAPARAHEADQFHAVGIIDPETGVPTEA... | 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
Sequ... |
B6YRV5 | MKKISDYSLLFKINSPEDLRKLAIEQVEQVCKELREYIIEVLSENPGHLGSNLGTVELTVALHYVFNTPYDRIVWDVGHQAYGHKILTERRESFHTLRKLGGISGFPNPQESEYDAFIAGHASNSISAALGMAIASWLKGENRKIVAIIGDGSITGGLAFEGLNNVSSNPNDLLIVLNDNNMAIDRSVGGLSQSLIKITTSYTYNTIRFKLYNFLKKYSIIKERERGFILRFTNSLKALLTKQHNIFEGLNIRYFGPIDGHNIKELVKVFEDIKSMKGPKLLHVCTVKGKGFGPAENKADVWHAPGKFNPETGERIKVWS... | 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
Sequ... |
Q7VIJ7 | MEVKTLDVANFLARIQKQESTFESLSKFSPTQLKELATCIRHRILEVVSSNGGHLSSTLGAVDLIIGMHLVFDANTNPFIFDVSHQAYAHKLLTGRWNDFSSLRQFGGLSGFCNPKESPSDYFIAGHSSTSISLAVGAAKALALKGSASMPVVMIGDGSMSAGLVYEALNELGDKKYPMVIILNDNKMSISKPIGAISNYLSQILTTSIYQKIRDTIKKVLTKMPDSATYLAKRFEESLKLITPGILFEELGLDYVGPIDGHNIELIIATLQRAKEMRKPVIIHAQTLKGKGYEIAEGRFEHWHGVGPFDVSTGSSLKSS... | 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
Sequ... |
B0TEJ5 | MTQILSRISNPGDLQRLSATELDQLAKEIREVIIQTTSKNGGHLAPNLGVVELTLALHLVFQSPKDKIIWDVGHQSYVHKLLTGRYNHFHTLRRYKGMAGFPKRSESEHDVFNTGHSSTSISAALGFAFARDLKKEDGAVIAVIGDGALTGGIALEALNHAGHAGNDMIVVLNDNEKSIADNVGAMSTYLSRIRTDPRYFRNKEEVEEIVRRIPSIGNHVLKVMEKMKDSFKHLVVPGILFEELGFSYLGPIDGHNLSQLREVMTNACRLKGPILVHVLTKKGKGYGPAETNPSVFHGVGPFDVETGKVKKHLGPPTYTQ... | 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
Sequ... |
O25121 | MILQNKTFDLNPNDIAGLELVCQTLRNRILEVVSANGGHLSSSLGAVELIVGMHALFDCQKNPFIFDTSHQAYAHKLLTGRFESFSTLRQFKGLSGFTKPSESAYDYFIAGHSSTSVSIGVGVAKAFCLKQALGMPIALLGDGSISAGIFYEALNELGDRKYPMIMILNDNEMSISTPIGALSKALSQLMKGPFYQSFRSKVKKILSTLPESVNYLASRFEESFKLITPGVFFEELGINYIGPINGHDLSAIIETLKLAKELKEPVLIHAQTLKGKGYKIAEGRYEKWHGVGPFDLDTGLSKKSKSAILSPTEAYSNTLL... | 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
Sequ... |
A9KMB8 | MPKILDEINQPNDIKKISAKKYTQLAAEIRRFLIANVSKTGGHLASNLGVVELTMALHLFLDFPEDKLVWDVGHQAYVHKLLTGRKNDFKTLRQYEGMSGFPKRKESDCDAFDTGHSSTSLSVAVGLVKARELSEEQRKVVAVIGDGALSGGMAFEALNNAGRLKENMIIVLNDNNMSISENVGGMSNYLGKARTNYRYMDFKGGLETALKKIPKVGDAIVTTLKQSKDSLKHLFIPGMLFEDMGMTYIGPIDGHNINQMLTALKSASRVNGAVLIHTVTKKGKGYEPAEKEPSKYHGVEPFDIKTGKKLKINSEVSYTE... | 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
Sequ... |
Q9RBN6 | MTILENIRQPRDLKALPEEQLHELSEEIRQFLVHAVTRTGGHLGPNLGVVELTIALHRVFESPVDRILWDTGHQSYVHKLLTGRQDFSKLRGKGGLSGYPSREESEHDVIENSHASTALGWADGLAKARRVQGEKGHVVAVIGGRALTGGMAWEALNNIAAAKDQPLIIVVNDNERSYAPTIGGLANHLATLRTTDGYEKVLAWGKDVLLRTPIVGHPLYEALHGAKKGFKDAFAPQGMFEDLGLKYVGPIDGHDIGAVESALRRAKRFHGPVLVHCLTVKGRGYEPALAHEEDHFHTVGVMDPLTCEPLSPTDGPSWTS... | 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
Sequ... |
Q67NB6 | MHLRDLTGPEQLKRLAPAELAQLAAEIRRVILETVATNGGHLAPNLGVVELTLALHIVFDSPRDKILWDVSHQSYVHKLLTGRLHQFHTLRQFGGIAGFTDPRESVHDHFHWGHASTSISAAVGMAKARDLAGDDYEVVAVIGDGALTGGMAYEALDHAGHDKTKVIVVLNDNSMSIAPNVGGISNYLARIRTGPSYQRVKHDVAEALRQIPLIGPQALELADRLKEGVKHLLVHNMFFEDLGFTYLGPVDGHNVSALVDVLRQARAYPGPTVVHVVTTKGKGVPYAEQLPDKFHGGGPFDVATGRTGPGSLTYSEVFGN... | 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
Sequ... |
Q27368 | MSKFFVNVAPINNSNSSSSHTTTSSNTQRHQQHQQHYGGSGTTGHTMVARRLNYDLHGGTTSINNNNNIVIKNESVDLDYDHVLSSSDSNSNGGVAAHLRDHVYISLDKGHNTGAVATAAAAATAGHTQQQLQQQHHHQNQQQRKATGKSNDITNYYKVKRRPHAVSDEIHPKKQAKQSAHHQTVYQKHTASSAPQQLRHSHHQLRHDADAELDEDVVERVAKPASHHPFSLSTPQQQLAASVASSSSSGDRNRADTSLGILTKKFVDLLQESPDGVVDLNEASNRLHVQKRRIYDITNVLEGINILEKKSKNNIQWRCG... | 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 t... |
Q01094 | MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEE... | 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 p... |
Q61501 | MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQLPAAPPTGPRDSDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTMVGIGKRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSETFQISLKSKQGPIDVFLCPEESADGISPGKTSCQETSSGEDRTAD... | 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 p... |
Q14209 | MLQGPRALASAAGQTPKVVPAMSPTELWPSGLSSPQLCPATATYYTPLYPQTAPPAAAPGTCLDATPHGPEGQVVRCLPAGRLPAKRKLDLEGIGRPVVPEFPTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKAKNNIQWVGRGMFEDPTRPGKQQQLGQELKELMNTEQALDQLIQSCSLSFKHLTEDKANKRLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRTEDNLQIYLKSTQGPIEVYLCPEEVQEPDSPSEEPLPS... | 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 pr... |
P56931 | MLRAPRTLAPATAQPTKSLPALNPTELWPSGLSSPQLCPATTATTYYTSLYTQTVPSSVALGTCLDATPHGPEGQIVRCAPAGRLPAKRKLDLEGIGRPTVPEFRTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKSKNNIQWVGRELFEDPTRPSRQQQLGQELKELMNAEQTLDQLIQSCSLSFKHLTEDNANKKLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRAEENLQIYLKSTQGPIEVYLCPEEGQEPDSPAKEAL... | 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 pr... |
Q16254 | MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSVSGPIEVLLVNKEAWSSPPVAVPVPPPEDLLQSPSAVSTPPPLPKPALAQSQEASRPNSPQLTPTAVPGSAEVQGMAGPAAEITVSGGPGTDSKDSGELSSLPLGPTTLDTRPLQSSALLDSSSSSSSSSSSSSN... | 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 pr... |
Q8R0K9 | MAEAGPQAPPPPGTPSRHEKSLGLLTTKFVSLLQEAKDGVLDLKLAADTLAVRQKRRIYDITNVLEGIGLIEKKSKNSIQWKGVGPGCNTREIADKLIELKAEIEELQQREQELDQHKVWVQQSIRNVTEDVQNSCLAYVTHEDICRCFAGDTLLAIRAPSGTSLEVPIPEGLNGQKKYQIHLKSMSGPIEVLLVNKEAWSSPPVAVPVPPPDDLLQSPPAVSTPPPLPKPALAQPQESSPPSSPQLTTPTPVLGSTQVSEVACQTSEIAVSGSPGTENKDSGEVSSLPLGLTALDTRPLQSSALLDSSSSSSSSSSSSS... | 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 pr... |
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... |
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... |
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... |
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... |
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 ... |
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 T... |
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 comple... |
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... |
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... |
A1CSU3 | MRLLLSVLLVLVASVGVGLVSAVPAGSSITPPPPIEPIHLLSAPSPSQDSRRPWTRLRDWVIESIWGISKSCSHPHSSSHSSSRDRPPSQALARYGSDVVLRFYPGSAQDAEALAEASEILFLDVWASTPEFVDIRLAEEVISSLLGLLPDSLRTAYTPLIDDLAEMIHASYPTRRSAGVGDQSGFMPTVRQSAQLGDLFFRDYQPLSVIVPWMRLMASMFSSHVEKISVGVSYEGREIPALRLGVREADPEPARPRKTILIVGGSHAREWISTSTVTYVAYQLIARYGKSPEVTRLLEDYDWVLVPTLNPDGYAYTWES... | 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 | MRQPTFAALSLLLVAPSLVAAVPHDSTSTSTSTSTRSPSYDPDSTAAHDTTTPHTPPSPWRRLSEAIIRRIGSLPHENHLQKSMLALATGPSSRAPGKQWVAHYGGDVVLRFKMQTADEARALSQAAATLFLDVWEFNEDWADIRLAKDVLPSLLGLLPRSLHASYEPLMQDAALVQAIFDTYPSSSASPSHNTNRFSPNLRPSPHHANGHPFFQDYQPLSVIDPWMSLMSSMFTTHVRKINIGISYEGRDIPALRVGVHPTNKDEPTKPRKTVLITAGLHAREWISTSTVNYLAWSVINAYGKDREITHLLEKFDFVFV... | 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 | MRLFSHLAVLAILACAVPITAIPSFLSNSYPAHPAEGISLFPQTQPQAPLGLWTRLRNTVIERLWRVPPQLCKNRPGHKGKFPLFSAPASLRARYGDDVVLRFTIRNAEEVKALAEASNILFLDVWASTDEWVDIRLSKDVVPSLLGLLPKSLQTSHIPLIHDLPQTIYESYPSSSQRSSYDVQGFSPSTKHSSDKTNIFFQDYQPFSVIVPWMRLLTSMFSSHVQMINIGSTFEGRDIPALQIGVWPANNPKPRKTVVVSGGSHAREWISVSTVNYVAYSLITNYAKSKHVAELLQQFDFIFIPTLNPDGYIYTWEVDR... | 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... |
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-ace... |
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... |
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... |
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... |
P32940 | MATVILFVAWMACLMVGVCYQEFQTQQNFPDISNPSQELNQEPAHRIVQLDSIQNNGALNMSTGNVLNMSPPPPSPCLSRAKIRHAFKYVTTILSCVIFLVGIVGNSTLLRIIYKNKCMRNGPNVLIASLALGDLFYILIAIPIISISFWLSTGHSEYIYQLVHLYRARVYSLSLCALSIDRYRAVASWNRIRSIGIPVRKAIELTLIWAVAIIVAVPEAIAFNLVELDFRGQTILVCMLPMEQTSDFMRFYQEVKVWWLFGFYFCLPLACTGVFYTLMSCEMLSIKNGMRIALNDHMKQRREVAKTVFCLVVIFALCWL... | 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 | METFWLRLSFWVALVGGVISDNPESYSTNLSIHVDSVATFHGTELSFVVTTHQPTNLALPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFEQNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYKGAQHRTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWF... | 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
... |
Q61614 | MSIFCLAAYFWLTMVGGVMADNPERYSANLSSHMEDFTPFPGTEINFLGTTHRPPNLALPSNGSMHGYCPQQTKITTAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLITAIEIVSIWILSFILAIPEAIGFVMVPFEYKGELHRTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWF... | 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
Seque... |
Q95L55 | METFWLRVSFWVALVGGVISDNPESYSTNLSIHVDSVTTFRGTELSFVVTTHQPTNLALPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFEQNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYKGAQHRTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWF... | 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
Seque... |
Q90328 | EIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPISVYKLLAEDWPFGVEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVISVVLAVPEAIAFDMITMEYRGKDLRICLLHPTQKTSFMMFYKQAKDWWLFSFYFCLPLAITALFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTIYDQKDPNRCELLSFFLVMDYIGINMASLNSCINPIALYLVSKRFQNCFKSCLCCWCQSKDLLSLE... | 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 me... |
P24530 | MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRRE... | 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.
Locati... |
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 | MQSPASRCGRALVALLLACGFLGVWGEKRGFPPAQATLSLLGTKEVMTPPTKTSWTRGSNSSLMRSSAPAEVTKGGRGAGVPPRSFPPPCQRNIEISKTFKYINTIVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPINTYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDMITSDYKGKPLRVCMLNPFQKTAFMQFYKTAKDWWLFSFYFCLPLAITAVFYTLMTCEMLRKKSGMQIALNDHLKQRRE... | 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
S... |
P35463 | MQPLRSLCGRALVALIFACGVAGVQSEERGFPPAGATPPALRTGEIVAPPTKTFWPRGSNASLPRSSSPPQMPKGGRMAGPPARTLTPPPCEGPIEIKDTFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPINVYKLLAEDWPFGVEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEALGFDMITTDYKGNRLRICLLHPTQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRR... | 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 | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAGGVGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSTEPPYSQARFEEITKEVSAYIKKIGYNPASVAFVPISGWHGDNMLEASSNMGWFKGWKIERKEGNASGTTLLDALDAILPPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPANVTTEVKSVEMHHESLTEATPGDNVGFNVKNVSVKDI... | 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 ... |
Q8SS29 | MATKVEDDSKPRLNACFIGHVDSGKSTTVGMLSYQLGAVDKREMEKYEKEAALNNKETFYLAYLTDKTDAERKRGITITTTLVNLPTEKFNINILDCPGHKDFVKNMVTGASQADVAVVIVPASGFESCVGVGGMLKTHIMISGILGCEKLIVCVNKMDEIPENKRMEKFNEVSAEMLRIVKRSHKDKNPIIIPISAFKGINLTKKGEKFEWFKGWKEKEGSSVIYTLEEALNYQDVPERHNDKPLRMPITKVCSIAGVGKIFTGRVEYGTITPNLKITIQPAGVVGETRSVEIHNKPRSMIPCGENCGVALKGGVIGEI... | 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 ribos... |
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 concentr... |
Q7CI09 | MRDKTGPKFGPYQPDDEAVSPSRRRLILGMGMVSGALVLGGAKTAQAADCRSPDVAGTQDERWQKQPFYGQHQAGVLTPQQAAMMLVAFDVLATDKTSLIRLFKLLTERLAFLTTGGRAPSVNAKLPPLDSGIMGPEIYPDNLTVTVSVGNALFDERFGLQGQKPLRLQRMTRFPNDSLDAGLCHGDVMLQICANTNETVIHALRDIIKHTPDLLSVRWKREGFISAHAARSKGQDTPINLLGFKDGTANPKISNKPLINNVVWVSNNAGEPAWAVGGSYQVVRIIRFKVEFWDRTPLQEQQTIFGRDKNSGAPLGMQHE... | 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... |
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.
... |
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 (... |
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.
... |
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.
... |
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 (... |
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.
... |
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.
... |
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 (... |
Q20402 | MRTSDSHLPLSNLARSDSIEFKDAVINEKWVHSANRRKGHLTPKAPEKKSGWFGGQKSEEELLMERVEQHELEELQTFIAQKLFRVDGIICDEETRILLVEKLMNAKEYPTINHDELAHRYGSSMAGWLRDRLVPSMSDCSSVLQRAAAEFYQNKMSDPLCNWGQLNPEHVSMVAARIAKFSEEMSSKVKWSLLVEPGKFSCHLTEFVQEFNRLDRMFVSNELSDEESLQTAFNANYLTKARSKMVPCAEFSRVKLNDGLGRLDDRNELRNGMFSDEHEFLQEEGYTAKSTYGTTDFIHANYVKGGPLLNTFICAQAPLK... | 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 ps... |
P90920 | MRWLTLIAVAHLIAFLSSAEITCPRIPEKCDCKISKSMIILSCNGEDVKTIAQTVGTSQIDELHILNGTDVKIESLPFNGLRTIAILNSTLQSFSPTAWRHVEATIEHITINGNELKTVPVFGNLSTLMSMNLNSNQISSIPDKAFNGLSALTQLRLENNAICDFPPKSLDAVKASLVLLDVSGNCLDAIPAQILRNAANLMYLDLGSNNISEINNFELMNLPFLRELRVQNNTLRRIHPMAFMNVPQLQYLYLQDNIISTLDGNRLQGFKNLEVLDVSNNALYALPSLKDLPNLKQVRVDGNLITKIETLAFSNNPNLQ... | 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 | MPAKIHISADGQFCDKDGNEIQLRGVNLDPSVKIPAKPFLSTHAPIENDTFFEDADKVSFINHPLVLDDIEQHIIRLKSLGYNTIRLPFTWESLEHAGPGQYDFDYMDYIVEVLTRINSVQQGMYIYLDPHQDVWSRFSGGSGAPLWTLYCAGFQPANFLATDAAILHNYYIDPKTGREVGKDEESYPKMVWPTNYFKLACQTMFTLFFGGKQYAPKCTINGENIQDYLQGRFNDAIMTLCARIKEKAPELFESNCIIGLESMNEPNCGYIGETNLDVIPKERNLKLGKTPTAFQSFMLGEGIECTIDQYKRTFFGFSKG... | 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... |
O01346 | MNSTTKHLLHCTLLITVIVTFEVFSGGIKIDENSFTLVDPWTEYGQLATVLLYLLRFLTLLTLPQVLFNFCGLVFYNAFPEKVVLKGSPLLAPFICIRVVTRGDFPDLVKTNVLRNMNTCLDTGLENFLIEVVTDKAVNLSQHRRIREIVVPKEYKTRTGALFKSRALQYCLEDNVNVLNDSDWIVHLDEETLLTENSVRGIINFVLDGKHPFGQGLITYANENVVNWLTTLADSFRVSDDMGKLRLQFKLFHKPLFSWKGSYVVTQVSAERSVSFDNGIDGSVAEDCFFAMRAFSQGYTFNFIEGEMYEKSPFTLLDFL... | 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
Subcellu... |
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
Subcellul... |
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