wanglab/gogpt-training-data huggingface dataset:
Protein: Suppressor of cytokine signaling 2 (SOCS-2) (Cytokine-inducible SH2 protein 2) (CIS-2) (STAT-induced STAT inhibitor 2) (SSI-2) (O14508)
Organism: Homo sapiens (Human)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9727029}.
Interaction partners:
- Elongin-C
- Elongin-B
- Cullin-5
- Growth hormone receptor
- Tyrosine-protein kinase JAK2
- Suppressor of cytokine signaling 1
- Suppressor of cytokine signaling 3
- Insulin receptor substrate 1
- Erythropoietin receptor
- Insulin receptor substrate 2
Sequence:
MTLRCLEPSGNGGEGTRSQWGTAGSAEEPSPQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV
Protein: Kunitz type trypsin inhibitor 111 (G7LCV7)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Subcellular location: Secreted {ECO:0000250|UniProtKB:G7LCV1}. Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:G7LCV1}.
Interaction partners:
Sequence:
MSTISFTIFILANVWLLVVTTSIAQFVIDTSGEPVENDEDYFIRPAITGNGGSLTLVTRNSCPFNVGLDPDAPQGFAVLLSPFVSNREEDEVRLGRDLRVIFQAGTSCGQSTEWRLGERDATTGRRFIITGRDDSTVGSYGNFFRIVQTPSRGIFNIQWCPTEVCPSCKFECGTVGIVRENGKILLALDGSALPVAFQKE
Protein: Probable permease of ABC transporter (Q9HTI7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Probable glycine betaine-binding protein
- Probable ATP-binding component of ABC transporter
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- Quaternary amine transport ATP-binding protein
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- Probable binding protein component of ABC transporter
- ABC-type glycine betaine transport system substrate-binding domain-containing protein
- Probable permease of ABC transporter
- Quaternary amine transport ATP-binding protein
Sequence:
MFLTDHKLPLGEQIAGFVDWLTLHGASFFDKISDTLEFLIHGVTNGLLWFNPLVLIALLVGLVHFIQRSWGLTVFALASLLLILNLGYWQETMETLAQVIFATLVCIAVGVPLGIVAAHKPWFYTALRPLLDLMQTVPTFVYLIPTLTLFGLGVVPGLISTVIFAVAAPIRLTCLGIQDVPAELLDAGKAFGCSRWQLLTRIELPHAMPSIAAGITQCIMLSLSMVVIAALVGADGLGKPVVNALNTADISLGFEAGLAIVLLAILLDRVCKQRAVKGK
Protein: ATP synthase subunit b, chloroplastic (ATP synthase F(0) sector subunit b) (ATPase subunit I) (P0C2Z0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
Interaction partners:
- ATP synthase subunit a, chloroplastic
- ATP synthase epsilon chain, chloroplastic
- F-ATPase gamma subunit
- Os06g0714700 protein
- ATP synthase subunit alpha
- ATP synthase F1, delta subunit family protein, expressed
- Os06g0646500 protein
- ATP synthase subunit a
- ATP synthase subunit c, chloroplastic
- F-ATPase protein 6
Sequence:
MKNVTHSFVFLAHWPSAGSFGLNTDILATNLINLTVVVGVLIYFGKGVLKDLLDNRKQRILSTIRNSEELRRGTIEQLEKARIRLQKVELEADEYRMNGYSEIEREKANLINATSISLEQLEKSKNETLYFEKQRAMNQVRQRVFQQAVQGALGTLNSCLNTELHFRTIRANISILGAMEWKS
Protein: Venom prothrombin activator oscutarin-C non-catalytic subunit (vPA) (Venom coagulation factor Va-like protein) [Cleaved into: Oscutarin-C non-catalytic subunit heavy chain; Oscutarin-C non-catalytic subunit light chain] (Q58L91)
Organism: Oxyuranus scutellatus (Coastal taipan)
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis.
Subcellular location: Secreted {ECO:0000269|PubMed:15993914, ECO:0000269|PubMed:3531198, ECO:0000269|PubMed:6986908}.
Interaction partners:
Sequence:
MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYRLAAQLEDWDYNPQPEELSRLSESDLTFKKIVYREYELDFKQEKPRDELSGLLGPTLRGEVGDSLIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNADGAQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTANMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGNPDTLTRKLSFRERRRIMKWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDSNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAVYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPPLVCKRKALSIRGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSSVKKDDPKFYKSNVMYTLNGYASDRTEVWGFHQSEVVEWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFNPPEVVIKKEEVPVNFVPDPESDALAKELGLFDDEDNPKQSRSEQTEDDEEQLMIASMLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSAHNSDDIAGRYLRTINRRNKRRYYIAAEEVLWDYSPIGKSQVRSLPAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEVQFRNLASRPYSLHAHGLLYEKSSEGRSYDDNSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSRHTFPAINGIPYQLQGLMMYKDENVHWHLLNMGGPKDVHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVGYWEPKLARLNNTGMFNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLKHSYTVEYFVTYSKDGQNWITFKGRHSKTQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNTPTFRIELLGCEVEGCSVPLGMESGAIKDSEITASSYKKTWWSSWEPFLARLNLKGRTNAWQPKVNNKDQWLQIDLQHLTKITSIITQGATSMTTSMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFNPPILSRFIRIIPKTWNQYIALRIELFGCEVF
Protein: Beta-theraphotoxin-Cm2a (Beta-TRTX-Cm2a) (Ceratotoxin-3) (CcoTx3) (P84509)
Organism: Ceratogyrus marshalli (Straighthorned baboon tarantula) (Ceratogyrus cornuatus)
Function: Inhibits mammalian voltage-gated sodium channel subtypes Nav1.5/SCN5A and Nav1.8/SCN10A by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current. In vivo, this toxin causes erect, elevated tail, initial partial ataxia, followed by recovery over approximately 1 hour after injection and the progressive development of shaking. Although paralysis subsides, the body tremors never cease and persist until the end of the experiment.
Subcellular location: Secreted {ECO:0000269|PubMed:16267209}.
Interaction partners:
Sequence:
GVDKEGCRKLLGGCTIDDDCCPHLGCNKKYWHCGWDGTF
Protein: Interferon lambda-2 (IFN-lambda-2) (Interleukin-28A) (IL-28A) (Q4VK74)
Organism: Mus musculus (Mouse)
Function: Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8IZJ0}.
Interaction partners:
- Interferon lambda receptor 1
- Interleukin-10 receptor subunit beta
- Interferon lambda-3
- Interferon alpha/beta receptor 1
- Interferon gamma receptor 1
- Non-receptor tyrosine-protein kinase TYK2
- Interferon alpha/beta receptor 2
- Tyrosine-protein kinase JAK1
- Ifngr2 protein
- Interferon beta
Sequence:
MLLLLLPLLLAAVLTRTQADPVPRATRLPVEAKDCHIAQFKSLSPKELQAFKKAKDAIEKRLLEKDLRCSSHLFPRAWDLKQLQVQERPKALQAEVALTLKVWENMTDSALATILGQPLHTLSHIHSQLQTCTQLQATAEPRSPSRRLSRWLHRLQEAQSKETPGCLEASVTSNLFRLLTRDLKCVANGDQCV
Protein: GLI family zinc finger 1 (G3V6X8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Suppressor of fused homolog
- Kinesin family member 7
- Speckle-type POZ protein, isoform CRA_a.
- Protein smoothened
- Beta-transducin repeat containing E3 ubiquitin protein ligase
- GLI family zinc finger 2
- Kinesin-like protein
- Patched
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MFNPMTSPQVNSYGEPCCLRPLPSQGVPSMGTEGLSGLPFCHQANFMSGSQGYGSARETSSCTEGSLFPPPRSSVKLTKKRALSISPLSDASLDLQTVIRTSPSSLVAFINSRCTSPGGSYGHLSIGTMSPSLGFPPQMSHQKGTSPPYGVQPCVPHDSTQGSMMLHPQSRGPRATCQLKSELDIMVGKCPEEPLEGDMSSPNSTSTQDHLLGMLDGREDLEREEKPEPESVYETDCRWDGCSQEFDSQEQLVHHINSEHIHGERKEFVCHWGGCSRELRPFKAQYMLVVHMRRHTGEKPHKCTFEGCRKSYSRLENLKTHLRSHTGEKPYMCEQEGCSKAFSNASDRAKHQNRTHSNEKPYVCKLPGCTKRYTDPSSLRKHVKTVHGPDAHVTKRHRGDGPLPRAQPLSTVEPKREREGGSGREESRLTVPEGTMPQQSPGAQSSCSSDHSPAGSAANTDSGVEMAGNAGGSTEDLSSLDEGPCVAATGLSTLRRLENLRLDQLHQLRPIGSRGLKLPSLTHAGAPVSRRLGPPVSLDRRSSSSSSISSAYTVSRRSSLASPFPPGSPPENGASSLPGLTPAQHYMLRARYASARGSGTPPTAAHSLDRIGGLPAPPWRSRAEYPGYNPNAGVTRRASDPARAADHPAPARVQRFKSLGCVHTPPSVATGRNFDPHLPTSVYSPQPPSITENVAMDTRGLQGELEVGTSMMGNDLNPYMDFSSADTLGYGGPEGTAAESYGSKGPGSLPLGPGPPTNYGPGHCAQQVSYPDPTPETWGEFPSHAGVYPGTKALGTAYNQCPRLEHYGQVQVKPEQGCPVGSDSTGLAPCLNAHPSEGSPDPQPLFSHHSQLPPPQYLQSGPYPQPPHDCLSLESRPGLNFNPSSHSTGQLKAQLLCNYVQSQQELLWEGRSRGGIPNQELPYQSPKFLGGSQVSQSPTKVPAAAAAATFGSGFASPALANHKSVSYPAPSPCHETFTMGVNRPPHRPAAPPRLLPPLPPCYGPLKVGDANPSCGHPEVGRLGAGPALYPPPEGQVCNPLDSLDLDNTQLDFVAILDEAQGLSPPPSHEQGDSSKNTPPPSGPPNMAVGNMSVLLGSLPGETQFLNSSA
Protein: Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 (Csk-binding protein) (Transmembrane adapter protein PAG) (Transmembrane phosphoprotein Cbp) (Q9NWQ8)
Organism: Homo sapiens (Human)
Function: Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Promotes CSK activation and recruitment to lipid rafts, which results in LCK inhibition. Inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins. May be involved in cell adhesion signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}; Single-pass type III membrane protein {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}. Note=Present in lipid rafts.
Interaction partners:
- Tyrosine-protein kinase CSK
- Tyrosine-protein kinase Lyn
- Tyrosine-protein kinase Fyn
- Na
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein kinase Lck
- 7-dehydrocholesterol reductase
- Growth factor receptor-bound protein 2
- High affinity immunoglobulin epsilon receptor subunit alpha
Sequence:
MGPAGSLLGSGQMQITLWGSLAAVAIFFVITFLIFLCSSCDREKKPRQHSGDHENLMNVPSDKEMFSRSVTSLATDAPASSEQNGALTNGDILSEDSTLTCMQHYEEVQTSASDLLDSQDSTGKPKCHQSRELPRIPPESAVDTMLTARSVDGDQGLGMEGPYEVLKDSSSQENMVEDCLYETVKEIKEVAAAAHLEKGHSGKAKSTSASKELPGPQTEGKAEFAEYASVDRNKKCRQSVNVESILGNSCDPEEEAPPPVPVKLLDENENLQEKEGGEAEESATDTTSETNKRFSSLSYKSREEDPTLTEEEISAMYSSVNKPGQLVNKSGQSLTVPESTYTSIQGDPQRSPSSCNDLYATVKDFEKTPNSTLPPAGRPSEEPEPDYEAIQTLNREEEKATLGTNGHHGLVPKENDYESISDLQQGRDITRL
Protein: Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit) (P00158)
Organism: Mus musculus (Mouse)
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788, ECO:0000269|PubMed:6326133}; Multi-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 7
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome c oxidase subunit 2
- NADH-ubiquinone oxidoreductase chain 5
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 3
- NADH-ubiquinone oxidoreductase chain 1
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MTNMRKTHPLFKIINHSFIDLPAPSNISSWWNFGSLLGVCLMVQIITGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTFMETWNIGVLLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAIVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDILGILIMFLILMTLVLFFPDMLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILALMPFLHTSKQRSLMFRPITQILYWILVANLLILTWIGGQPVEHPFIIIGQLASISYFSIILILMPISGIIEDKMLKLYP
Protein: WD repeat domain-containing protein 83 (Mitogen-activated protein kinase organizer 1) (MAPK organizer 1) (Q9DAJ4)
Organism: Mus musculus (Mouse)
Function: Molecular scaffold protein for various multimeric protein complexes. Involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator (By similarity). Also acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation. May also be involved in pre-mRNA splicing.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BRX9}. Lysosome {ECO:0000250|UniProtKB:Q9BRX9}. Nucleus {ECO:0000250|UniProtKB:Q5BLX8}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000250}.
Interaction partners:
- Splicing factor 3B subunit 4
- Pre-mRNA-processing-splicing factor 8
- Ragulator complex protein LAMTOR3
- G patch domain-containing protein 1
- Prolyl hydroxylase EGLN3
- Ragulator complex protein LAMTOR2
- Dual specificity mitogen-activated protein kinase kinase 1
- Mitogen-activated protein kinase 3
Sequence:
MAFPEPKPRAPELPQKRMKTLDCSQGAVRAVRFNVDGNYCLTCGSDKTLKLWNPLRGTLLRTYSGHGYEVLDAAGSFDNSHLCSGGGDKTVVLWDVATGQVVRKFRGHAGKVNTVQFNEEATVILSGSIDSSVRCWDCRSRKPEPVQTLDEARDGISSVKVSDHEILAGSVDGRVRRYDLRMGQVSSDYVGSPITCTCFSRDGQCTLISSLDSTLRLLDKDTGELLGEYVGHKNQQYKLDCCLSERDTHVVSCSEDGKVFFWDLVEGALALALPVGSNVVQSLAYHPTEPCLLTAMGGSIQYWREETYEAEGGAG
Protein: Large ribosomal subunit protein eL29 (60S ribosomal protein L29) (L43) (Q92366)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL37B
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL38A
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL13
Sequence:
MAKSKNHTNHNQNKKAHRNGIKRPQKHRYDSLKYRDAKFRRNQKFANRGTVEAIRQAKASA
Protein: Cation efflux system protein CusF (P77214)
Organism: Escherichia coli (strain K12)
Function: Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.
Subcellular location: Periplasm.
Interaction partners:
- Cation efflux system protein CusC
- Cation efflux system protein CusB
- Cation efflux system protein CusA
- Sensor histidine kinase CusS
- Transcriptional regulatory protein CusR
- Multicopper oxidase CueO
- HTH-type transcriptional regulator CueR
- Copper-exporting P-type ATPase
Sequence:
MKKALQVAMFSLFTVIGFNAQANEHHHETMSEAQPQVISATGVVKGIDLESKKITIHHDPIAAVNWPEMTMRFTITPQTKMSEIKTGDKVAFNFVQQGNLSLLQDIKVSQ
Protein: V-type proton ATPase subunit a (K7EM24)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKF
Protein: Brorin (Brain-specific chordin-like protein) (CR (chordin-like cysteine-rich) domain-containing adhesive protein) (Cradin) (von Willebrand factor C domain-containing protein 2) (Q8C8N3)
Organism: Mus musculus (Mouse)
Function: BMP antagonist which may play a role in neural development. Promotes cell adhesion.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Synapse {ECO:0000305}.
Interaction partners:
- Neuritin
- Noelin
- Glutamate receptor 2
- Glutamate receptor 1
- Noelin-3
- Voltage-dependent calcium channel gamma-2 subunit
- Protein shisa-6
- Phosphatidylinositol-3-phosphatase SAC1
- Glutamate receptor 4
- von Willebrand factor C domain-containing protein 2-like
Sequence:
MPSSSAMAVGALSSSLLVTCCLMVALCSPSIPLEKLAQAPEQPGQEKREHASRDSPGRVSELGRASRDEGSSARDWKSKGSRALSGREAWSKQKQAWAAQGGSAKAADWQVRPRGDTPQGEPPAAAQEAISLELVPTPELPEEYAYPDYRGKGCVDESGFVYAIGEKFAPGPSACPCLCTEEGPLCAQPECPRLHPRCIHVDNSQCCPQCKEKKNYCEFRGKTYQTLEEFVVSPCERCRCEANGEVLCTVSACPQTECVDPVYEPDQCCPICKNGPNCFAETAVIPAGREVKTDECTICHCTYEEGTWRIERQAMCTRHECRQM
Protein: Glycine--tRNA ligase (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase 1) (GlyRS) (Q9CZD3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P41250}. Mitochondrion {ECO:0000269|PubMed:18614015}. Cell projection, axon {ECO:0000250|UniProtKB:P41250}. Secreted {ECO:0000269|PubMed:26503042}. Secreted, extracellular exosome {ECO:0000305|PubMed:26503042}. Note=Associated with granules in cultured neuron cells (By similarity). Secreted by motor neuron and differentiated myotube cell lines, but not by undifferentiated myoblasts, possibly through the exosome pathway (PubMed:26503042). {ECO:0000250|UniProtKB:P41250, ECO:0000269|PubMed:26503042}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Gephyrin
- Serine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
Sequence:
MPCLLPSLLRATRAALPLLSPPRVVAASASQRLLSAPAQPAASRSSMDSAEELLAPLRLAVRQQGDFVRKLKEDKAPQVDVDRAVAELKARKRVLEAKELALQPKDDIVDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQAWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSAEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPTTGNDLSPPVPFNLMFQTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPTEKDHPKFQSVADLCLYLYSAKAQVTGQSARKMRLGDAVEQGVINNSVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPNKGAVGKAYKKDAKLVLEYLSACDECYISEMELLLSEKGEFTIETEGKTFQLTKDMVSVKRFQKTLHVEEVVPSVIEPSFGLGRIMYTILEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRNGVSHKVDDSSGSIGRRYARTDEIGVAFGITIDFDTVNKTPHTATLRDRDSMRQIRAEVSELPNVVRDLANGNITWADVEARYPLFEGQETGKKETVEE
Protein: Phospholipase D2 (PLD 2) (hPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2) (O14939)
Organism: Homo sapiens (Human)
Function: Function as phospholipase selective for phosphatidylcholine. May have a role in signal-induced cytoskeletal regulation and/or endocytosis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P97813}; Lipid-anchor {ECO:0000250|UniProtKB:P97813}.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor 6
- Ras-related protein Ral-A
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- 5'-3' exonuclease PLD3
- 5'-3' exonuclease PLD4
- Protein kinase C alpha type
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 2
- Cholinephosphotransferase 1
Sequence:
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFAPGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVVKDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRALMLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSESAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQCTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICDDFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQGHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Protein: Neurotrophin-4 (NT-4) (Neurotrophin-5) (NT-5) (Neutrophic factor 4) (Q80VU4)
Organism: Mus musculus (Mouse)
Function: Could serve as a target-derived trophic factor for sensory and sympathetic neurons.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P34130}.
Interaction partners:
- High affinity nerve growth factor receptor
- Tumor necrosis factor receptor superfamily member 16
- BDNF/NT-3 growth factors receptor
- NT-3 growth factor receptor
- Neurotrophic factor BDNF precursor form
- Beta-nerve growth factor
- Glial cell line-derived neurotrophic factor
- Sortilin
- Insulin-like growth factor 1 receptor
- Epidermal growth factor receptor
Sequence:
MLPRHSCSLLLFLFLLPSVPMEPHPPSSTLPPFLAPEWDLLSPRVALSRGAPAGPPLLFLLEAGAYGEPAGAPANRSRRGVSETAPASRRGELAVCDAVSGWVTDRRTAVDLRGREVEVLGEVPAAGGSPLRQYFFETRCKAESAGEGGPGVGGGGCRGVDRRHWLSECKAKQSYVRALTADSQGRVGWRWIRIDTACVCTLLSRTGRA
Protein: GCN5-related N-acetyltransferase (P96810)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MTPQARPARRADVRELSRTMARAFYDDPVMSWLLSNDNARTARLTRLFATIVRHQHLAGGGVEVARGAAGIGGAALWDPPDRWRESRRQQLAMTPGFLRVFGFRTAKARAALDVMMRVHPEEPHWYLAAIGSDPTVRGQGFGQVLMRSRLDRCDAEHCPAYLESTKPENVPYYQRFGFRVTREIALPDAGPPLWAMWREPR