wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase subunit d, mitochondrial (ATPase subunit d) (Q24251)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit g
- ATP synthase subunit b, mitochondrial
- ATP synthase F
- ATP synthase subunit O, mitochondrial
- ATP synthase F
- Putative ATP synthase subunit f
- Protein stunted
- ATP synthase-coupling factor 6, mitochondrial
- ATP synthase subunit alpha, mitochondrial
Sequence:
MAARRIAQSSINWSALAERVPANQKSSFGAFKTKSDIYVRAVLANPECPPQIDWANYKKLVPVAGLVDSFQKQYEALKVPYPQDKVSSQVDAEIKASQSEIDAYKKASEQRIQNYQKEIAHLKSLLPYDQMTMEDYRDAFPDSALDPLNKPTFWPHTPEEQVGYKSKEQLEAEAQGHH
Protein: Translation initiation factor eIF2B subunit delta (eIF2B GDP-GTP exchange factor subunit delta) (G5EG28)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MILGVKSENNQQVVPPTTAEEPAQGEDKNQYHKDVTAEDKKARKAAKAAEKKARAEKSVANKAAAAAGSTQNQGQKKEKPPKEHSAVPSESTTKLIEENAQLTKTTEQLAAKMETLVIEDVKINGSLKPAIKKSTGVEKNVRHVHNVIMPSVVTFDLPKNQTKTLPSASDSDEAVASEIESTAIAQLDDATSFVHIHPAFLTLMAKAELEKIPDVETVCIQFIAAFKEFLRDWTVEREKNNINASTFGHDLDLAIRPQLAHMTQNGHWPLPFALGNTVRLLKRTIKRLEESTNMKCEEELQVYLEDTLAINFCHAYKAISQLLVRKIQQFKKVVVFDWCPVVNHVLLEAKQQIPDMQLSVIDANSNGRGTRHVKSFVDQGYNVKYVTMKGASWASLASGVLILGCSAIFANGAVAARKGALAVVLCANHYNIPVIVVAEHFKFIDKGQVYQRVALLGRQNIECIQSDLVTAVVTDLRILGPTSAPAVLKAKALTDMA
Protein: Laccase-2 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase 2) (Diphenol oxidase 2) (Urishiol oxidase 2) (O81081)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lignin degradation and detoxification of lignin-derived products (By similarity). Required for root elongation in dehydration conditions.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Phenylalanine ammonia-lyase 1
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Phenylalanine ammonia-lyase 4
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 3
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Trans-cinnamate 4-monooxygenase
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Cytochrome P450 84A1
Sequence:
MVTWVLNYLLVAFLFAISYNIDAASAGITRHYQFDIQLKNITRLCKTKTIVTVNGKFPGPRVTAREGDNLQIKVVNHVSNNISIHWHGIRQLRSGWADGPSYVTQCPIRMGQSYVYNFTVTGQRGTLWWHAHIQWMRATVYGPLIILPKLHQPYPFPKPYKQVPILFGEWFNADPQAVVQQALQTGAGPNASDAHTFNGLPGPLYNCSTKDTYKLMVKPGKTYLLRLINAALNDELFFTIANHTLTVVEADACYVKPFQTNIVLLGPGQTTNVLLKTKPIYPNATFYMLARPYFTGQGTIDNTTVAGILQYQHHTKSSKNLSIIKPSLPPINSTSYAANFTKMFRSLASSTFPANVPKVVDKQYFFAIGLGTNPCPKNQTCQGPTNTTKFAASINNVSFILPNKTSLLQSYFVGKSKNVFMTDFPTAPIIPFNYTGTPPNNTMVSRGTKVVVLKYKTTVELVLQGTSILGIEAHPIHLHGFNFYVVGQGFGNFNPARDPKHYNLVDPVERNTINIPSGGWVAIRFLADNPGVWLMHCHIEIHLSWGLTMAWVVLDGDLPNQKLLPPPSDFPKC
Protein: Potassium channel subfamily K member 2 (Outward rectifying potassium channel protein TREK-1) (TREK-1 K(+) channel subunit) (Two pore potassium channel TPKC1) (K2P2.1) (P97438)
Organism: Mus musculus (Mouse)
Function: Ion channel that contributes to passive transmembrane potassium transport. Reversibly converts between a voltage-insensitive potassium leak channel and a voltage-dependent outward rectifying potassium channel in a phosphorylation-dependent manner. In astrocytes, forms mostly heterodimeric potassium channels with KCNK1, with only a minor proportion of functional channels containing homodimeric KCNK2. In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:10321245, ECO:0000269|PubMed:16636285, ECO:0000269|PubMed:22354168}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17110924, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:27035965, ECO:0000269|PubMed:9003761}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:17110924}. Postsynaptic density membrane {ECO:0000305|PubMed:17110924}; Multi-pass membrane protein {ECO:0000255}. Note=Location at the cell membrane requires interaction with KCNK1. Is not detected at the cell membrane when KCNK1 is absent. {ECO:0000269|PubMed:24496152}.; SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:Q920B6}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q920B6}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000250|UniProtKB:Q920B6}.
Interaction partners:
- Potassium channel subfamily K member 1
- Potassium channel subfamily K member 10
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- A-kinase anchor protein 5
- Popeye domain-containing protein 2
- Popeye domain-containing protein 1
- Piezo-type mechanosensitive ion channel component 1
- Piezo-type mechanosensitive ion channel component 2
- Potassium channel subfamily K member 4
Sequence:
MLASASRERPGYTAGVAAPDLLDPKSAAQNSKPRLSFSSKPTVLASRVESDSAINVMKWKTVSTIFLVVVLYLIIGATVFKALEQPQEISQRTTIVIQKQTFIAQHACVNSTELDELIQQIVAAINAGIIPLGNSSNQVSHWDLGSSFFFAGTVITTIGFGNISPRTEGGKIFCIIYALLGIPLFGFLLAGVGDQLGTIFGKGIAKVEDTFIKWNVSQTKIRIISTIIFILFGCVLFVALPAVIFKHIEGWSALDAIYFVVITLTTIGFGDYVAGGSDIEYLDFYKPVVWFWILVGLAYFAAVLSMIGDWLRVISKKTKEEVGEFRAHAAEWTANVTAEFKETRRRLSVEIYDKFQRATSVKRKLSAELAGNHNQELTPCRRTLSVNHLTSEREVLPPLLKAESIYLNGLTPHCAGEDIAVIENMK
Protein: Concanavalin-A (Con A) (P81460)
Organism: Canavalia lineata (Beach bean) (Dolichos lineatus)
Function: Glucose/D-mannose specific lectin.
Interaction partners:
Sequence:
ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVDLDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFVFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGNSVGRALFYAPVHIWESSAVVASFDATFTFLIKSSDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
Protein: Prolactin-2C2 (Mitogen-regulated protein 1) (Proliferin-1) (P04095)
Organism: Mus musculus (Mouse)
Function: May have a role in embryonic development. It is likely to provide a growth stimulus to target cells in maternal and fetal tissues during the development of the embryo at mid-gestation. May play a role during wound healing and in the hair follicle cycle as a growth factor and/or an angiogenesis factor. May play a role in microvilli formation and cell proliferation of neuroblastoma cells.
Subcellular location: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:16876275}. Endoplasmic reticulum {ECO:0000269|PubMed:16876275}.
Interaction partners:
- Trophoblast-specific protein alpha
Sequence:
MLPSLIQPCSWILLLLLVNSSLLWKNVASFPMCAMRNGRCFMSFEDTFELAGSLSHNISIEVSELFTEFEKHYSNVSGLRDKSPMRCNTSFLPTPENKEQARLTHYSALLKSGAMILDAWESPLDDLVSELSTIKNVPDIIISKATDIKKKINAVRNGVNALMSTMLQNGDEEKKNPAWFLQSDNEDARIHSLYGMISCLDNDFKKVDIYLNVLKCYMLKIDNC
Protein: Basonuclin zinc finger protein 2 (F5H586)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLYGTQAVPVRLKILLDRLFSVLKQEEVLHILHGLGWTLRDYVRGYILQDAAGKVLDRWAIMSREEEIITLQQFLRFGETKSIVELMAIQEKEGQAVAVPSSKTDSDIRTFIESNNRTRSPSLLAHLENSNPSSIHHFENIPNSLAFLLPFQYINPVSAPLLGLPPNGLLLEQPGLRLREPSLSTQNEYNESSESEVSPTPYKNDQTPNRNALTSITNVEPKTEPACVSPIQNSAPVSDLTKTEHPKSSFRIHRMRRMGSASRKGRVFCNACGKTFYDKGTLKIHYNAVHLKIKHRCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMLRNNRDKDLIRATSGAATPVIASTKSNLALTSPGRPPMGFTTPPLDPVLQNPLPSQLVFSGLKTVQPVPPFYRSLLTPGEMVSPPTSLPTSPIIPTSGTIEQHPPPPSEPVVPAVMMATHEPSADLAPKKKPRKSSMPVKIEKEIIDTADEFDDEDDDPNDGGAVVNDMSHDNHCHSQEEMSPGMSVKDFSKHNRTRCISRTEIRRADSMTSEDQEPERDYENESESSEPKLGEESMEGDEHIHSEVSEKVLMNSERPDENHSEPSHQDVIKVKEEFTDPTYDMFYMSQYGLYNGGGASMAALHESFTSSLNYGSPQKFSPEGDLCSSPDPKICYVCKKSFKSSYSVKLHYRNVHLKEMHVCTVAGCNAAFPSRRSRDRNRNLRMERTIGPGHRDSLHLLPT
Protein: Protein GL2-INTERACTING REPRESSOR 2 (Q9SRN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of root hair development redundantly with GIR1. GIR1 and GIR2 may function as adapter proteins that associate with GL2 and participate in the control of root hair formation. GIR1 and GIR2 may function as adapter proteins that associate with TPL and participate in the repression of root gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:28526410, ECO:0000269|PubMed:28526412}.
Interaction partners:
Sequence:
MSRRNKNGPKLELRLNLSPPPSQASQMSLVRSPNRSNTTSPSSCVSSETNQEENETITSMVLVGCPRCLMYVMLSDDDPKCPKCKSTVLLDFLQENAFAATTATAANTRRKKKTWWN
Protein: U2 small nuclear ribonucleoprotein A' (U2 snRNP A') (Q9USX8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-mRNA splicing. This protein is associated with sn-RNP U2. It helps the A' protein to bind stem loop IV of U2 snRNA (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Pre-mRNA-splicing factor sap61
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- Pre-mRNA-splicing factor prp12
- Small nuclear ribonucleoprotein-associated protein B
- Pre-mRNA-splicing factor sap145
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor brr2
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43
Sequence:
MRLNAEFLSQVPSFISPLKETELDLRWYQIPIIENLGVLRDVHDAIDFTDNDIRYLGNFPRMKRLQTLLCGNNRITAIAPDIGKVLPNLKTLSLAQNHLQEIADLDPLASCPQLTNLSCIDNPVAQKQYYRLYLIWRIPSLHILDFERVRRNERLRAEEVFGQIQNPTEIASSIMGVKSRVFDLAALVQSHPEANSPITTGYTLTPEEREKIKEAIKNASSIAEINRLEAMLLEGKIPK
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q6FVK5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Nucleoporin NSP1
- FK506-binding protein 1
- FK506-binding protein 2
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- GTP-binding nuclear protein GSP1/Ran
- Candida glabrata strain CBS138 chromosome G complete sequence
- Large ribosomal subunit protein uL13m
Sequence:
MSKVYFDIEADGQPLGRVVFQLYDDVVPKTAANFRALCTGEKGFGYAGSPFHRVIPDFMLQGGDFTAGNGTGGKSIYGGKFPDENFVKRHERPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGEVSEGYDVVKKVESMGSSSGATRARIIVSKSGEL
Protein: Metalloreductase STEAP3 (EC 1.16.1.-) (Dudulin-2) (Six-transmembrane epithelial antigen of prostate 3) (Tumor suppressor-activated pathway protein 6) (hTSAP6) (pHyde) (hpHyde) (Q658P3)
Organism: Homo sapiens (Human)
Function: Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can also reduce of Cu(2+) to Cu(1+), suggesting that it participates in copper homeostasis. Uses NADP(+) as acceptor. May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q8CI59}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to vesicular-like structures at the plasma membrane and around the nucleus. {ECO:0000269|PubMed:15319436}.
Interaction partners:
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
- Translationally-controlled tumor protein
- Cellular tumor antigen p53
- Transferrin receptor protein 1
- Natural resistance-associated macrophage protein 2
- Plasma membrane ascorbate-dependent reductase CYBRD1
Sequence:
MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRNPKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQEHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSEMALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYVQESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFCAALHALYSFCLPLRRAHRYDLVNLAVKQVLANKSHLWVEEEVWRMEIYLSLGVLALGTLSLLAVTSLPSIANSLNWREFSFVQSSLGFVALVLSTLHTLTYGWTRAFEESRYKFYLPPTFTLTLLVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPTDHALAEKTSHV
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (W8C8I9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
VKMKTLLNKAIHCYESLIVKAEGKVESDFFCQLGHFNLLLEDYSKALSSYQRYYSLQTDYWKNAAFLYGLGLVYFYYNAFQWAIRAFQEVLYVDPNFCRAKEIHLRLGFMFKVNTDYESSLKHFQLALRDSNVCTLSSVEIQFHIAHLFEIQRKYHSAKAAYEQLLQIESLPSQVKATVLQQLGWMHHNMDLVGDNTTKERYAIQYLQKSLEEDPNSGQSWYFLGRCYSCIGKVQDAFVSYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGILYESCNQTQDAIKCYLNATRSKSCSNTSVLISRIKFLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELASRQGAMNTAQQNVSDSWNSVHTASHHPVQQQVYTQCFTTQKLQGLGKDQQRPFQTGSTRYIHAACVDNQNQNGNHTLPQNSKGDTQNHSSLHIPTSEEQKIFNFTKESKDSRSKSLSPKTSRQDRDTSNIYVNAKEHSKNIHEITSVPISSLNNEDSVSPNLIIVDNPQLSVLVGEAMDSVDHDSRTCDKVNNVHPTLHKKPDNLTASSPSSASSTETLSLKVTEQMHTHIVTSFISPNSGLDTINGGPENSESSISVSVGLRPRPQIIPSMSVSIYSSSTEVLKACRNLGKNGLSNGHILLDICPPPRPPTSPYPPLPKEKLNPPTPSIYLENKRDAFFPPLHQFCINPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHIVEVRTQFLQPADENWDPSGTKKIWRYENKSSHTTIAKYAQYQACSFQESLREENERKTQVKDYSDNESTCSDISRRRQKVPFKTIKCGINIDLSDNKKWKLQLHELTKLPAFVRVVSAGNLLSHVGYTILGMNSVQLCMKVPGSRIPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNNLNFLMSSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNITWNVGPLTAFQYKLAVERYEWNKLQSIKSVVPMVHLSWNMARNIKVSDPKLFEMIKYCLLKILKQCQTLREALVAAGKEVLWHGRINDEPAPYCSICEVEVFNLLFVTNESNSQKTYIVHCQNCARKTSGNLENFVVLEQYKMEDLIQVYDQFTLAPSLSSSS
Protein: Enolase 2 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (Q74J64)
Organism: Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
Interaction partners:
Sequence:
MTVYVEKVRALEIFDSRGNPTVEVHAYLSDGTVAKAEVPSGASTGEKEAVELRDGGNRLQGKGVTQAVTNVNGPINDALKGLSPYNQAEIDRTMIKLDGTLNKAKLGANAILGTSMAIARAAARSKDEPLYRYLGGCELEMPQTFHNVINGGKHADNGIDIQEFMITPVAKNSFRDGFEKIVNTYHALKAVIEEAGFETGLGDEGGFAPNLNSSEEALKMLRKAIIKAGYKPRKDIAIAFDAAASSFYNTEDGKYHFEGHIWNGEEMLQYYDKLLKEFPEIISCEDPFDENDWENFEKFTAKFGSTHQVVADDNVCTNPKLVRKAIKDKLCNSILIKLNQIGTITETLETIRLARKNNMTTMVSHRSGETGDTFIADFTVATNAGQLKSGAPARSERVEKYNRLLEIENQIGVENERLNHFPNNVDFD
Protein: Photosystem I reaction center subunit III, chloroplastic (Light-harvesting complex I 17 kDa protein) (PSI-F) (Q9SHE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18431481}; Single-pass membrane protein; Lumenal side.
Interaction partners:
- Photosystem I chlorophyll a/b-binding protein 2, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem I reaction center subunit IV A, chloroplastic
- Photosystem I reaction center subunit IV B, chloroplastic
- Photosystem I reaction center subunit psaK, chloroplastic
- Chlorophyll a-b binding protein 4, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit II-1, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I subunit O
Sequence:
MSLTIPANLVLNPRSNKSLTQSVPKSSARFVCSDDKSSSSTPQSMKAFSAAVALSSILLSAPMPAVADISGLTPCKDSKQFAKREKQQIKKLESSLKLYAPESAPALALNAQIEKTKRRFDNYGKYGLLCGSDGLPHLIVNGDQRHWGEFITPGILFLYIAGWIGWVGRSYLIAISGEKKPAMKEIIIDVPLASRIIFRGFIWPVAAYREFLNGDLIAKDV
Protein: Interference hedgehog (Q9VM64)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates response to the active Hedgehog (Hh) protein signal in embryos, functioning upstream or at the level of patched (ptc).
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255, ECO:0000269|PubMed:16630821}.
Interaction partners:
- Protein patched
- Protein hedgehog
- Brother of ihog, isoform G
- Dally-like, isoform A
- Protein smoothened
- Protein dispatched
- Protein shifted
- Neural/ectodermal development factor IMP-L2
- Kinesin-like protein costa
- Transcriptional activator cubitus interruptus
Sequence:
MTLLTSSLLLFSLLTSRLEAIPVLEKSPAHPAHSAHPAHPAHPAHPAHPSPGVRILRAPESLVAPLGDEVVLECETSLQPERFEWSHRSSRSPGAGFKYLKTGTAKANVSQEAAISRLRVLVRPDTLGEYRCVGWFGPLVVTSTIARLELASTSLVDAQESESPLQWRVSAGNSVLWSCGQQVQSNPSASWSYYRNGVEIKPEFIGTNGNLFLSNVSSESSGSYSCQATNPASGERIQLPGSLQLQVTPEQRSESKSPHLLRGQPSSQEITIREGSSLLLLCPGVGSPPPTVVWSSPDVVGAVKNKRSKVFGHALEISNTRVNDAGTYICFQDNGVRPALEHYIKVHVEQPPQIVRPPWADLTNEGDRLKLECKATGVPTPEIYWLLNGHSSIDDSEAELSNNFLILHSVLKRHAGYVQCFARNRLGEHSAGTLLQVNPKQIQEPRESGGTHRPKPNQGSRQKQMYPPTPPNVTRLSDESVMLRWMVPRNDGLPIVIFKVQYRMVGKRKNWQTTNDNIPYGKPKWNSELGKSFTASVTDLKPQHTYRFRILAVYSNNDNKESNTSAKFYLQPGAALDPMPVPELLEIEEYSETAVVLHWSLASDADEHLITGYYAYYRPSSSAGEYFKATIEGAHARSFKIAPLETATMYEFKLQSFSAASASEFSALKQGRTQRPKTSTTEEPTLQMGDRDTTTPSHNETFNMSPMLTGTIGGGAVLILLLISTCFCVCRRRNSRSRGNNPNKPRMAELRDDFVPLGNCSPTKQRQRTRHIHITLNPLAQQQQQALEEKNDTDQDAPYYQRPSSYDYDPTLRRMSSSSLRRSQRTLERAGGSNGSNNGNNNNLNQSAEAGSIENPGKPGRVLMKRPRLSSRSENLSSGSLNSVGV
Protein: Transcription factor JunD (Transcription factor AP-1 subunit JunD) (P52909)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor binding AP-1 sites (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Protein c-Fos
- Fos-related antigen 1
- Protein FosB
- Transcription factor Jun
- Menin
- Fos-related antigen 2.
- Transcription factor JunB
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 8
Sequence:
METPFYGEEALSGLAAGASSVAGAAGAPGGGGFAPPGRAFPGAPPTSSMLKKDALTLSLAEQGAAGLKPGSATAPSALRPDGAPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSTQFLYPKVAASEEQEFAEGFVKALEDLHKQSQLGAATAATSGAPAPPAPADLAATPGATETPVYANLSSFAGGAGPPGGAATVAFAAEPVPFPPPPGALGPPPPPHPPRLAALKDEPQTVPDVPSFGDSPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQKVLSHVNSGCQLLPQHQVPAY
Protein: Serine hydroxymethyltransferase 4 (AtSHMT4) (EC 2.1.2.1) (Glycine hydroxymethyltransferase 4) (Serine methylase 4) (O23254)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion of serine and glycine with the conversion of tetrahydrofolate (THF) into 5,10-methylene-THF.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Formate--tetrahydrofolate ligase
- Glycine dehydrogenase
- Glycine dehydrogenase
- Phosphoserine phosphatase, chloroplastic
- Aminomethyltransferase, mitochondrial
- Serine--glyoxylate aminotransferase
- AICARFT/IMPCHase bienzyme family protein
- Formyltetrahydrofolate deformylase 1, mitochondrial
- Formyltetrahydrofolate deformylase 2, mitochondrial
- Methylenetetrahydrofolate reductase 1
Sequence:
MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGGKKISATSIYFESLPYKVNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMIFYRKGPKPPKKGQPEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNNKDLDQLKADVEKFSASYEMPGFLMSEMKYKD
Protein: ATP phosphoribosyltransferase (ATP-PRT) (ATP-PRTase) (EC 2.4.2.17) (P9WMN1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00079}.
Interaction partners:
- Phosphoribosyl-ATP pyrophosphatase
- Histidinol dehydrogenase
- Phosphoribosyl isomerase A
- Imidazoleglycerol-phosphate dehydratase
- Imidazole glycerol phosphate synthase subunit HisF
- Imidazole glycerol phosphate synthase subunit HisH
- Phosphoribosyl-AMP cyclohydrolase
- Histidinol-phosphate aminotransferase
- Histidine--tRNA ligase
- Ribose-phosphate pyrophosphokinase
Sequence:
MLRVAVPNKGALSEPATEILAEAGYRRRTDSKDLTVIDPVNNVEFFFLRPKDIAIYVGSGELDFGITGRDLVCDSGAQVRERLALGFGSSSFRYAAPAGRNWTTADLAGMRIATAYPNLVRKDLATKGIEATVIRLDGAVEISVQLGVADAIADVVGSGRTLSQHDLVAFGEPLCDSEAVLIERAGTDGQDQTEARDQLVARVQGVVFGQQYLMLDYDCPRSALKKATAITPGLESPTIAPLADPDWVAIRALVPRRDVNGIMDELAAIGAKAILASDIRFCRF
Protein: Uncharacterized tRNA/rRNA methyltransferase YfiF (EC 2.1.1.-) (P0AGJ5)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized tRNA/rRNA methyltransferase LasT
- Probable phospholipid transport protein YdbH
- Probable GTP-binding protein EngB
Sequence:
MNDEMKGKSGKVKVMYVRSDDDSDKRTHNPRTGKGGGRPGKSRADGGRRPARDDKQSQPRDRKWEDSPWRTVSRAPGDETPEKADHGGISGKSFIDPEVLRRQRAEETRVYGENACQALFQSRPEAIVRAWFIQSVTPRFKEALRWMAANRKAYHVVDEAELTKASGTEHHGGVCFLIKKRNGTTVQQWVSQAGAQDCVLALENESNPHNLGGMMRSCAHFGVKGVVVQDAALLESGAAIRTAEGGAEHVQPITGDNIVNVLDDFRQAGYTVVTTSSEQGKPLFKTSLPAKMVLVLGQEYEGLPDAARDPNDLRVKIDGTGNVAGLNISVATGVLLGEWWRQNKA
Protein: Dual specificity protein phosphatase 15 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase T-DSP10) (Q8R4V2)
Organism: Mus musculus (Mouse)
Function: May dephosphorylate MAPK13, ATF2, ERBB3, PDGFRB and SNX6 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9H1R2}; Lipid-anchor; Cytoplasmic side.
Interaction partners:
Sequence:
MGNGMTKVLPGLYLGNFIDAKDPDQLGRNKITHIISIHESPQPLLQDITYLRISVSDTPEVPIKKHFKECVHFIHSCRLNGGNCLVHCFAGISRSTTIVIAYVMTVTGLGWQEVLEAIKASRPIANPNPGFRQQLEEFGWANSQKLRRQLEERFGEIPFRDEEDLRALLPLCRRCRQGSATSAASATTASSAAEGTLQRLVPRSPRDSHQPLPLLARVKQTFFCLPRCLSRKGGK
Protein: Follitropin subunit beta (Follicle-stimulating hormone beta subunit) (FSH-B) (FSH-beta) (Follitropin beta chain) (Q6EV79)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and spermatogenesis in reproductive organs (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10612425}. Note=Efficient secretion requires dimerization with CGA. {ECO:0000250|UniProtKB:P01225}.
Interaction partners:
- Follicle-stimulating hormone receptor
- Lutropin-choriogonadotropic hormone receptor
- Thyrotropin receptor
- Glycoprotein hormones alpha chain
- Adenosine receptor A2
- Glucagon-like peptide 1 receptor
- D
- D
- Gastric inhibitory polypeptide receptor
- Vasoactive intestinal peptide receptor 2
Sequence:
MKTVQFCFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPNIQKTCTFKEVVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFSEMKE