wanglab/gogpt-training-data huggingface dataset:
Protein: Cytokine receptor common subunit beta (CDw131) (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131) (P32927)
Organism: Homo sapiens (Human)
Function: Cell surface receptor that plays a role in immune response and controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Acts by forming an heterodimeric receptor through interaction with different partners such as IL3RA, IL5RA or CSF2RA. In turn, participates in various signaling pathways including interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor/CSF2 pathways. In unstimulated conditions, interacts constitutively with JAK1 and ligand binding leads to JAK1 stimulation and subsequent activation of the JAK-STAT pathway.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-3 receptor subunit alpha
- Granulocyte-macrophage colony-stimulating factor receptor subunit alpha
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-3
- Interleukin-5
- Interleukin-5 receptor subunit alpha
- Tyrosine-protein kinase JAK2
- Erythropoietin receptor
- GTPase KRas
- GTPase HRas
Sequence:
MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC
Protein: Nodal-related protein 1 (Q8QGA0)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
ETAVPQELADSVLLLVFSKDKAPGQHSLLRAVESSKHVMRDGGPRDVGTRRHRRTRKERQRLRVSDAPAASPVDEARSLCRRVDMMVDFEQTGWGSWIVYPKKYNAYRCEGLCPSPVDESFKPTNHAYMQSLLQLYKPSQVPCPACSPIRMSPLSMLYYEKG
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (A0A1W2PQP4)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Protein: Trace amine-associated receptor 4 (TaR-4) (Trace amine receptor 4) (2-phenylethylamine receptor) (Trace amine receptor 2) (TaR-2) (Q923Y7)
Organism: Rattus norvegicus (Rat)
Function: Olfactory receptor specific for 2-phenylethylamine, a trace amine present at high concentration in the urine of carnivore species, playing a key role in fear and avoidance responses. 2-phenylethylamine acts as a kairomone in the chemical detection of carnivore odor and triggers fear in mice. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Signal transducer and activator of transcription 5A
- Flavin-containing monooxygenase 3
Sequence:
MNSPDLWYSPETQFCFAAANNSCPRKARPALVVCAMYLVMIGAIVMTMLGNMVVIISIAHFKQLHSPTNFLILSMATTDFLLSCVVMPFSMVRSIESCWYFGDLFCKVHSCCDIMLCTTSIFHLCFISVDRHYAVCDPLHYVTQITVGVVGVFLLISWSVPILFAFGLVFSELNLIGAEDFVAAIDCTGLCVLIFNKLWGVLASFIAFFLPGAIMVGIYIHIFTVARKHARKIGPGPRTKRALSESKMKATSGKESKATKTLSIVMGVFVLCWLPFFVLTITDPFIGFTTPEDLYNVFLWLGYFNSTFNPIIYGMFYPWFRKALRMIVTGTIFRSDSSTSSLHPAHP
Protein: Endoplasmic reticulum-Golgi intermediate compartment protein (F8W0R1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU369013}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369013}.
Interaction partners:
Sequence:
MRRLNRKKTLSLVKELDAFPKVPESYVETSASGGTVYQDTWMKYEYEVDKDFSSKLRINIDITVAMKCQYVGADVLDLAETMVASADGLVYEPTVFDLSPQQKEWQRMLQLIQSRLQEEHSLQDVIFKSAFKSTSTALPPREDDSSQSPNACRIHGHLYVNKVAGNFHITVG
Protein: DnaJ homolog subfamily C member 5B (Cysteine-string protein isoform beta) (CSP-beta) (Q9UF47)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000269|PubMed:17034881}; Lipid-anchor {ECO:0000269|PubMed:17034881}. Note=May be associated with the trans-Golgi network. {ECO:0000269|PubMed:17034881}.
Interaction partners:
- Cell division cycle 5-like protein
- Tuftelin-interacting protein 11
- Crooked neck-like protein 1
- Pleiotropic regulator 1
- Pre-mRNA-processing factor 19
- Protein BUD31 homolog
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 1-like
- SNW domain-containing protein 1
- Heat shock 70 kDa protein 4
Sequence:
MACNIPNQRQRTLSTTGEALYEILGLHKGASNEEIKKTYRKLALKHHPDKNPDDPAATEKFKEINNAHAILTDISKRSIYDKYGSLGLYVAEQFGDENVNTYFMLSSWWAKALFVIVGLLTGCYFCCCLCCCCNCCCGHCRPESSVPEEDFYVSPEDLEEQIKSDMEKDVDFPVFLQPTNANEKTQLIKEGSRSYCTDS
Protein: Ubiquitin E2 variant 1D-4 (F4J6Z1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTLGSGGSSVVVPRNFRLLEELERGEKGIGDGTVSYGMDDGDDIYMRSWTGTIIGPHNIMPLLLLLVVTEINFMSQTVHEGRIYQLKLFCDKDYPEKPPTVRFHSRVNMACVNHETGVVDPKKFGLLANWQREYTMEDILVQLKKEMSTSHNRKLVQPPEGTCF
Protein: Aspartic proteinase A1 (EC 3.4.23.-) (O65390)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles (By similarity). Possesses aspartic protease activity in vitro.
Subcellular location: Vacuole {ECO:0000269|PubMed:17012602}. Note=Located in protein storage vacuoles (PSV) of the embryo.
Interaction partners:
- PRA1 family protein F3
- PRA1 family protein B6
- PRA1 family protein F2
- PRA1 family protein F4
- PRA1 family protein D
- RNA-binding
- PRA1 family protein B3
- AP-2 complex subunit sigma
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- PRA1 family protein E
Sequence:
MKIYSRTVAVSLIVSFLLCFSAFAERNDGTFRVGLKKLKLDSKNRLAARVESKQEKPLRAYRLGDSGDADVVVLKNYLDAQYYGEIAIGTPPQKFTVVFDTGSSNLWVPSSKCYFSLACLLHPKYKSSRSSTYEKNGKAAAIHYGTGAIAGFFSNDAVTVGDLVVKDQEFIEATKEPGITFVVAKFDGILGLGFQEISVGKAAPVWYNMLKQGLIKEPVFSFWLNRNADEEEGGELVFGGVDPNHFKGKHTYVPVTQKGYWQFDMGDVLIGGAPTGFCESGCSAIADSGTSLLAGPTTIITMINHAIGAAGVVSQQCKTVVDQYGQTILDLLLSETQPKKICSQIGLCTFDGTRGVSMGIESVVDKENAKLSNGVGDAACSACEMAVVWIQSQLRQNMTQERILNYVNELCERLPSPMGESAVDCAQLSTMPTVSLTIGGKVFDLAPEEYVLKVGEGPVAQCISGFIALDVAPPRGPLWILGDVFMGKYHTVFDFGNEQVGFAEAA
Protein: Hematopoietic cell signal transducer (DNAX-activation protein 10) (Membrane protein DAP10) (Transmembrane adapter protein KAP10) (Q9QUJ0)
Organism: Mus musculus (Mouse)
Function: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilization and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells.
Subcellular location: Membrane {ECO:0000269|PubMed:17100879}; Single-pass type I membrane protein {ECO:0000269|PubMed:17100879}.
Interaction partners:
- NKG2-D type II integral membrane protein
- Growth factor receptor-bound protein 2
- TYRO protein tyrosine kinase-binding protein
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Proto-oncogene vav
- Tyrosine-protein kinase SYK
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- C-type lectin domain family 5 member A
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Sequence:
MDPPGYLLFLLLLPVAASQTSAGSCSGCGTLSLPLLAGLVAADAVMSLLIVGVVFVCMRPHGRPAQEDGRVYINMPGRG
Protein: Reduced viability upon starvation protein 161 (P25343)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Reduced viability upon starvation protein 167
- Nuclear fusion protein FUS2
- Proline-rich protein LAS17
- Clathrin heavy chain
- Actin
- Actin cytoskeleton-regulatory complex protein SLA1
- Protein BZZ1
- Altered inheritance of mitochondria protein 3
- Actin cytoskeleton-regulatory complex protein END3
- GTPase-activating protein GYP5
Sequence:
MSWEGFKKAINRAGHSVIIKNVDKTIDKEYDMEERRYKVLQRAGEALQKEAKGFLDSLRAVTASQTTIAEVISNLYDDSKYVAGGGYNVGNYYLQCVQDFDSETVKQLDGPLRETVLDPITKFSTYFKEIEEAIKKRDHKKQDFDAAKAKVRRLVDKPAKDASKLPRAEKELSLAKDIFENLNNQLKTELPQLVSLRVPYFDPSFEALIKIQLRFCTDGYTRLAQIQQYLDQQSRDDYANGLLDTKIEELLGQMTSLDICALGIK
Protein: Short chain dehydrogenase helC (EC 1.1.1.-) (Helvolic acid biosynthesis cluster protein helC) (Q4WR19)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Interaction partners:
Sequence:
MNTAIITGAAQGVGLCIAEALAQRNYRIVLSDIDTEKGPAAASKLNLTHGEGTAAFFHCDLSNLREIDALLSFTIETMGGFSVLINNAGYLRAPFLALSAQDIQDMITVNLTAPIYATQQAIKYWDGLHQGQAGCVVSVTSSSSFKTYASIAPYGAAKAGAAMFTFAAGAFHPRVRVNAVAPTAIATGFDKNRMRVETDRTGPGYTPEEEMRAMGLKRLQPQEVAEAVVRCVEDKGLYGKVLYLDAVEGIKIHDGYT
Protein: Transmembrane protein 41B (Protein stasimon) (Q5BJD5)
Organism: Homo sapiens (Human)
Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by ATG2 (ATG2A or ATG2B) to mediate autophagosome assembly. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required. Required for normal motor neuron development (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30093494, ECO:0000269|PubMed:30126924, ECO:0000269|PubMed:30352685, ECO:0000269|PubMed:30933966, ECO:0000269|PubMed:33338421, ECO:0000269|PubMed:34015269, ECO:0000269|PubMed:34043740}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:34015269}. Note=Localized to specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. {ECO:0000269|PubMed:30352685}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33338421}. Note=(Microbial infection) Upon infection with infection with flaviviruses, diffuse reticular-like pattern to a large cytosolic aggregate that colocalizes with viral non-structural proteins, NS4A (ZIKV) and NS4B (YFV). {ECO:0000269|PubMed:33338421}.
Interaction partners:
- Vacuole membrane protein 1
- WD repeat-containing protein 46
Sequence:
MAKGRVAERSQLGAHHTTPVGDGAAGTRGLAAPGSRDHQKEKSWVEAGSARMSLLILVSIFLSAAFVMFLVYKNFPQLSEEERVNMKVPRDMDDAKALGKVLSKYKDTFYVQVLVAYFATYIFLQTFAIPGSIFLSILSGFLYPFPLALFLVCLCSGLGASFCYMLSYLVGRPVVYKYLTEKAVKWSQQVERHREHLINYIIFLRITPFLPNWFINITSPVINVPLKVFFIGTFLGVAPPSFVAIKAGTTLYQLTTAGEAVSWNSIFILMILAVLSILPAIFQKKLKQKFE
Protein: Probable transketolase (TK) (EC 2.2.1.1) (Q9URM2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
- Fructose-bisphosphate aldolase
- ATP-dependent 6-phosphofructokinase
- Fructose-1,6-bisphosphatase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Phosphoglucomutase
Sequence:
MTSSSYTDIDTLAINTIRTLAVDTTAHAKSGHPGAPMGLAPAAHVLFSRIMKFNPAHPKWLNRDRFILSNGHACVLQYIMCHLLGYKLTIEDLKQFRQVGSKTPGHPETHNPDLNIETGAGPLGQGIASAVGLAIGKAHSAAVYNKPGFDLFSNYTFCFLGDGCLQEGVSSEACSLAGHLKLSNLIAVWDNNKITIDGATSMSFDEDVEKRFEAYGWNIVRVANGDTDLDGIEKGFREAMSCTDKPTLINLKTTIGYGSELQGTHSVHGSPLKPEDCVHVKKLFGFDPTKTFQVPPEVYAYYKERVAIASSAEEEYKKMYASYKQSYPDLSNQLERILSRKFPEGWEKHLPVYKPGDKAVATRKLSEIVLDALCPVLPELVGGSADLTPSNLTRWEGAADFQPPSSKLGTYAGRYIRYGIREHGMAGIMNGLAVYGPIIPYGGTFLNFVSYAAGAVRMAALNNSRVIYVATHDSIGLGEDGPTHQPIETFAHFRAMPNINCWRPADGNETSAAYYSALTSDSTPSILALTRQNLPQLENSTIENALKGGYVMLENKEADITLVGTGSEVSLCIDTVKTLETEYNLKARVVSLPCWEVFEQQPESYRLSVIPDGIPAMSVEVWATNGWRRYVHEAFGMHTFGDSGPAPKLYEKFHFTTSGVAQRAKKTVDAYKDIPYIRSPVRRAF
Protein: ADP-ribosylation factor GTPase-activating protein 2 (Zinc finger protein 289) (E9PIY6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}.
Interaction partners:
Sequence:
MAAEPNKTEIQTLFKRLRAVPTNKACFDCGAKNPSWASITYGVFLCIDCSGVHRSLGVHLSFIRSTELDSNWNWFQLRCMQVGGNANATAFFRQHGCTANDANTKYNSRAAQMYREKIRQLGSAALARHGTDLWIDNMSSAVPNHSPEKKDSDFFTEHTQEWLTEASVIWPPFQPPAWDAPATEPSGTQQPAPSTESSGLAQPEHGPNTDLLGTSPKASLELKSSIIGKKKPAAAKKGLGAKKGLGAQKVSSQSFSEIERQAQVAEKLREQQAADAKKQAEESMVASMRLAYQELQIDRKKEEKKLQNLEGKKREQAERLGMGLVSR
Protein: Cell cycle associated protein MOB1, putative (D6XJ89)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MKRFKAKLFDSDRTYKPKKKHKEGTERYNLHKFAKSLVRSGDLSAAVKLPQGADLNHWLSVHTVDFYNITNVLYGSLTEFCTNSSCPVMSSGPRYEYLWRDPPEYPKATKVSAPEYVRLLMEWIERQINDERVFPSEDRNPYPPDFADRVKACFKRLFRVYAHVYYSHFAKIRELQEESHINTALKHFMYFVWEFDLIPREEVSPLRELLVNLMGQRAKEKLEVP
Protein: Gamma-aminobutyric acid receptor subunit alpha-6 (GABA(A) receptor subunit alpha-6) (GABAAR subunit alpha-6) (Q16445)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P30191}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P30191}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid receptor subunit delta
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid type B receptor subunit 2
Sequence:
MASSLPWLCIILWLENALGKLEVEGNFYSENVSRILDNLLEGYDNRLRPGFGGAVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWTDERLKFGGPTEILSLNNLMVSKIWTPDTFFRNGKKSIAHNMTTPNKLFRIMQNGTILYTMRLTINADCPMRLVNFPMDGHACPLKFGSYAYPKSEIIYTWKKGPLYSVEVPEESSSLLQYDLIGQTVSSETIKSNTGEYVIMTVYFHLQRKMGYFMIQIYTPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIEFAAVNYFTNLQTQKAKRKAQFAAPPTVTISKATEPLEAEIVLHPDSKYHLKKRITSLSLPIVSSSEANKVLTRAPILQSTPVTPPPLSPAFGGTSKIDQYSRILFPVAFAGFNLVYWVVYLSKDTMEVSSSVE
Protein: Ras-related GTP-binding protein C (G5EGB3)
Organism: Caenorhabditis elegans
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- GTP-binding protein
- DAF-15
- Target of rapamycin homolog
- Ragulator complex protein LAMTOR2 homolog
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- UDENN FNIP1/2-type domain-containing protein
- Target of rapamycin complex subunit lst8
- UDENN FLCN/SMCR8-type domain-containing protein.
- GATOR complex protein NPRL3
- WDR59/RTC1-like RING zinc finger domain-containing protein
Sequence:
MESDPDEDFDDYRYGIDEEDDYPDSRPTVILMGHKRSGKTSIRKVVFQKMSPNETMFVESTARITRDTICSSFINFETIEFPGQMCPFDDSLDPVGVFQKCEALLFIIDAQAELQEPIATLVEYFCRAYKINQNIKFEVFVHKADGLTEEARVETKFNIYHQVKETIKDQIDVDLQVTYHLTSIYDHSIFEAFSKVVQNLVKQLPTLERLLDVFNNSSKVTKSFLFDILSKIYIATDSEPVEMSIYELCCDMIDVTLDLSSIYGVAENGSNYDERSSSVIRLKSEQVMFLRQVNKHLALVFIMKEDGNEKAGFIDHNFGVFKAGIEQVFKVKNRGVNF
Protein: Ghrelin O-acyltransferase (EC 2.3.1.-) (Membrane-bound O-acyltransferase domain-containing protein 4) (O-acyltransferase domain-containing protein 4) [Cleaved into: 44,4 kDa fragment] (P0C7A3)
Organism: Mus musculus (Mouse)
Function: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity. In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18267071, ECO:0000269|PubMed:24045953}; Multi-pass membrane protein {ECO:0000269|PubMed:18267071}.
Interaction partners:
- Appetite-regulating hormone
- Growth hormone secretagogue receptor type 1
Sequence:
MDWLQLFFLHPLSFYQGAAFPFALLFNYLCILDTFSTRARYLFLLAGGGVLAFAAMGPYSLLIFIPALCAVALVSFLSPQEVHRLTFFFQMGWQTLCHLGLHYTEYYLGEPPPVRFYITLSSLMLLTQRVTSLSLDICEGKVEAPRRGIRSKSSFSEHLWDALPHFSYLLFFPALLGGSLCSFRRFQACVQRSSSLYPSISFRALTWRGLQILGLECLKVALRSAVSAGAGLDDCQRLECIYLMWSTAWLFKLTYYSHWILDDSLLHAAGFGAEAGQGPGEEGYVPDVDIWTLETTHRISLFARQWNRSTALWLRRLVFRKSRRWPLLQTFAFSAWWHGLHPGQVFGFLCWSVMVKADYLIHTFANVCIRSWPLRLLYRALTWAHTQLIIAYIMLAVEGRSLSSLCQLCCSYNSLFPVMYGLLLFLLAERKDKRN
Protein: GRAS family protein RAM1 (Protein REQUIRED FOR ARBUSCULAR MYCORRHIZATION 1) (MtRAM1) (G7L166)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. AMT2;4, AMT2;5, EXO70I, STR, RAM2, LEC5, PT4, VPY, BCP1, SCP1 and RAD1) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis and Glomus versiforme). Promotes directly the expression of RAM2, EXO70I, STR and RAD1. Not necessary to enable hyphopodium formation or hyphal entry into the root but essential to support arbuscule branching. Involved in the phosphate-mediated suppression of AM fungi colonization in mycorrhiza. Also involved in restricting mycorrhizal colonization of the root meristem (By similarity). Required for Myc factor signaling from mycorrhizal fungi, but has no function in Nod factor signaling from rhizobial bacteria. Regulates the expression of RAM2, a glycerol-3-phosphate acyl transferase that promotes cutin biosynthesis to enhance mycorrhizal hyphopodia formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:23122845}. Cytoplasm {ECO:0000250|UniProtKB:A0A145P7T2}.
Interaction partners:
Sequence:
MINSLCGSSNSLKEKCLQPNSSNQTNTHSKKNATNSCGDLEQINVLTPQSLNLPSLKFDLDGDVEVQSPDSSMWEAFFNDHLDNDFMISSPIRNINPNSPQASTYNNCNYNYAQGMQIQSLSGCSPPRFASQIGSLNSNNQQKGKGLSPLHRVFNSPNNQYMQHVENLSLPAIEEFLEDFQGDVDHFSSTKVSSECFDMETPISTILDSLTMQNSSSYGASVNEESTLLHGGNSSSQISQESDIYHQMGSMASASLSQALQQERYQEKHQKMQAQQQSLTVPIQIGIEQEQDSGLQLVHLLLACAEAVAKGEYMLARRYLHQLNRVVTPLGDSMQRVASCFTESLSARLAATLTTKSSSTKKLAPSSLSSSSSSSCLSTFPSNPMEVLKIYQIVYQACPYIKFAHFTANQAIFEAFEAEERVHVIDLDILQGYQWPAFMQALAARPGGAPFLRITGVGPCIESVRETGRCLTELAHSLRIPFEFHPVGEQLEDLKPHMFNRRVGEALAVNTVNRLHRVPGNHLGNLLSMIRDQAPNIVTLVEQEASHNGPYFLGRFLEALHYYSAIFDSLDATFPVESAPRAKVEQYIFAPEIRNIVACEGEERIERHERLEKWRKIMEGKGFKGVPLSPNAVTQSRILLGLYSCDGYRLTEDKGCLLLGWQDRAIIAASAWRC
Protein: Dehydration-responsive element-binding protein 2C (OsDREB2C) (Q84ZA1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcriptional activator that binds to the DNA sequence 5'-[AG]CCGAC-3' of the cis-acting dehydration-responsive element (DRE).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:20049613}.
Interaction partners:
Sequence:
MEMDIGEGESCCGRRKQQQQQNISSSKSRKCCPLRRSRKGCMKGKGGPENQRCPFRGVRQRTWGKWVAEIREPNRGARLWLGTFNTALDAARAYDSAARALYGDCARLNLLLAAATAGAPPAAATPSVATPCSTNDDSNNSSSTTHQQQLTTMLQLDDDNYTLQPSSSDQEDFETYVTRLPKAEDFGLEGFQEVPLDVLDEAGGGISIWDLSICPADFMATAATTTAKSS