wanglab/gogpt-training-data huggingface dataset:
Protein: Pleckstrin homology domain containing A7 (A0A8I5ZXL6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAAVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMIRSDLPRGWEEGFTEEGASFFIDHNQQTTTFRHPVTGQFSSENSEYVLREEPHPHMSKQERNQRPSSMVSETSTAGTTSTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNLNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYSTTTAGSQAEHSGMRTYYFSADTLEDMNAWVRAMNQAAQVLSRSSLKRDKVERQAMPQANHTDACQECGHVGPGHSRDCPRRGYEDAIVFDRREQEEERFRSQRDTLEGRRDRSKARSPYLPAEEDALFVDLPGGPRGQQAQPQRAERNGLPPYGLGEQNGTSGYSRTAPPRANLEKHSQRKTNLAQTEHWAKAQKGDGRSLPLDQTLPRQGPSQPPSFLENYQTLPRNTRYPSGSSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPIGAGSPEFTEQGRSRSLLEVPRSISVPPSPSDIPPPGPPRPFPPRRPHTPAERVTVKPPDQRRSVDISLGGSPRKARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPMKIAESDTDVKLSIFCEQDRILQDLEDKIRALKENKDQLESVLEVLHRQTEQYRDQPQHLEKITCQQRLLQEDLVHIRAELCRESTEMENAWNEYLKLEKDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVMAGLSVNKENYRVLVGSVKNPERKTVPLFPHPSVPSLSPTESKPALQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDREQGQCVNGDLKVELRSYVSEPELASFSGDVPRPSLGLVGSESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAENSSVTFSRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLSQGERTGLLSARYLSQPLPGDLGSVC
Protein: Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1) (P97588)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). Has been shown to be also activated by TGF-beta (transforming growth factor) type I receptor kinase in rat intestinal epithelial cells (IEC 4-1). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q15797}. Nucleus {ECO:0000250|UniProtKB:Q15797}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4. Co-localizes with LEMD3 at the nucleus inner membrane (By similarity). Exported from the nucleus to the cytoplasm when dephosphorylated (By similarity). {ECO:0000250|UniProtKB:P70340, ECO:0000250|UniProtKB:Q15797}.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- E3 ubiquitin-protein ligase
- Mothers against decapentaplegic homolog 5
- Bone morphogenetic protein receptor type-1A
- Mothers against decapentaplegic homolog
- Bone morphogenetic protein receptor type-2
- Activin receptor type-1
- Serine/threonine-protein kinase receptor
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 9
Sequence:
MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPHSHPFAQYPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMAQDGSQPMDTNMTNMTAPTLPAEINRGDVQAVAYEEPKHWCSIVYYELNNRVGERFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETEYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Protein: Carbamoyl phosphate synthase large chain (EC 6.3.4.16) (EC 6.3.5.5) (Carbamoyl phosphate synthetase ammonia chain) (P00968)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Carbamoyl phosphate synthase small chain
- Aspartate carbamoyltransferase catalytic subunit
- Amidophosphoribosyltransferase
- Argininosuccinate synthase
- Ornithine carbamoyltransferase subunit F
- Aspartate carbamoyltransferase regulatory chain
- Orotidine 5'-phosphate decarboxylase
- Allantoinase
- Dihydroorotate dehydrogenase
- Orotate phosphoribosyltransferase
Sequence:
MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATADAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGGIAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATGFDPKVSLDDPEALTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGITGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDLAAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGRRAIEDSRVIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISVQEMHAQIK
Protein: Thymidylate kinase (EC 2.7.4.9) (Thymidine monophosphate kinase) (dTMP kinase) (TMPK) (P9WKE1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.
Interaction partners:
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Ribonucleoside-diphosphate reductase subunit alpha
- Thymidylate synthase ThyA
- Flavin-dependent thymidylate synthase
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Nucleoside diphosphate kinase
- R2-like ligand binding oxidase
- Ribonucleoside-diphosphate reductase subunit beta nrdF1
- Ribonucleoside-diphosphate reductase subunit beta nrdF2
- Adenosylhomocysteinase
Sequence:
MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLASSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWVQRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYAELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS
Protein: Tyrosine aminotransferase (TAT) (EC 2.6.1.5) (L-tyrosine:2-oxoglutarate aminotransferase) (Q8QZR1)
Organism: Mus musculus (Mouse)
Function: Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine.
Interaction partners:
- 4-hydroxyphenylpyruvate dioxygenase
- Phenylalanine-4-hydroxylase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Putative aspartate aminotransferase, cytoplasmic 2
- S-adenosylmethionine synthase isoform type-1
- Aromatic-L-amino-acid decarboxylase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Acireductone dioxygenase-requiring))
- S-adenosylmethionine synthase isoform type-2
Sequence:
MDSYVIQTNVNDSLPSVLDVRVNIGGRSSVQGRAKGRKARWNVRPSDMSNKTFNPIRAIVDNMKVKPNPNKTVISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGYLSSREEVASYYHCPEAPLEAKDVILTSGCSQAIELCLAVLANPGQNILIPRPGFSLYRTLAESMGIEVKLYNLLPEKSWEIDLKQLESLIDEKTACLVVNNPSNPCGSVFSKRHLQKILAVAERQCVPILADEIYGDMVFSDCKYEPMATLSTNVPILSCGGLAKRWLVPGWRLGWILIHDRRDIFGNEIRDGLVKLSQRILGPCTIVQGALKSILQRTPQEFYQDTLSFLKSNADLCYGALSAIPGLQPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLIAEQSVHCLPATCFEYPNFFRVVITVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
Protein: Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase (THBPA hydratase-aldolase) (EC 4.1.2.45) (2'-hydroxybenzalpyruvate aldolase) (Q9X9Q6)
Organism: Sphingobium xenophagum
Function: Involved in the naphthalene and naphthalenesulfonate catabolic pathway. Catalyzes the transformation of trans-O-hydroxybenzylidenepyruvate (THBPA) to salicylaldehyde and pyruvate. The reaction is reversible. Can also use 2,4-dihydroxybenzalpyruvate (2,4-DHBP) and 2,6-dihydroxybenzalpyruvate (2,6-DHBP).
Interaction partners:
Sequence:
MARTLMKPDDVKGAWAIIPTPAKDDASDWRATKTVDLDETARVVNGLIDAGINGILSMGTLGEAATMTHDEKLDFIKALVDAAAGRVPIFVGTTCLNTRDTIALTRQALDIGADGTMLGVPMWCAPSVDVAVQFYKDLAEAVPEMNIAIYANPEAFKFDFPRSFWAQVAEIPQVVTAKYIGVAHLLPDLAAIRGRIKLLPIDFDYYGAARMDESIDAFWSSGAVCDPLVTTTLRDLVSQARATGDWSAARAFMGRLGPTAAPLFPNGSFKEFSTYNIALEKARMNAGGWMNAGPVRPPYHLCPEPYLEGARLSGRMWAELGKALAAEK
Protein: Prokineticin receptor 2 (PK-R2) (G-protein coupled receptor 73-like 1) (Q8K458)
Organism: Mus musculus (Mouse)
Function: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8NFJ6}; Multi-pass membrane protein.
Interaction partners:
- Prokineticin-2
- Prokineticin-1
- Metastasis-suppressor KiSS-1
- NMDA receptor synaptonuclear signaling and neuronal migration factor
- Progonadoliberin-1
Sequence:
MGPQNRNTSFAPDLNPPQDHVSLNYSYGDYDLPLGEDEDVTKTQTFFAAKIVIGVALAGIMLVCGIGNFVFIAALARYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWAHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAVPSAYFTTETILVIVKNQEKIFCGQIWSVDQQLYYKSYFLFVFGLEFVGPVVTMTLCYARISQELWFKAVPGFQTEQIRKRLRCRRKTVLLLMGILTAYVLCWAPFYGFTIVRDFFPTVVVKEKHYLTAFYVVECIAMSNSMINTICFVTVKNNTMKYFKKMLRLHWRPSHYGSKSSADLDLKTSGVPATEEVDCIRLK
Protein: Transposon Ty3-G Gag polyprotein (Gag3) (Transposon Ty3-1 protein A) (TY3A) [Cleaved into: Capsid protein (CA) (p24); Spacer peptide p3; Nucleocapsid protein p9 (NC) (NCp9) (p7)] (Q12173)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1371165}.
Interaction partners:
Sequence:
MSFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIGATTHLQEEYDSDYDSEDNLTQNGYVHTVRTRRSYNKPMSNHRNRRNNNPSREECIKNRLCFYCKKEGHRLNECRARKASSNRS
Protein: Transmembrane protein (DUF2215) (F4K567)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004575}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004575}; Nucleoplasmic side {ECO:0000256|ARBA:ARBA00004575}.
Interaction partners:
Sequence:
MGDYRLLRNSGVVIGIILLHLFTFASLVSSDELQFGVVVNFLWPYGTVVGESGELQVTPSLEVKGSPGLKPDRTSLCERIHIHGLGRFKHLDKYAHSLKLIVNASISGKTNNIDVCFHRNLSRGIGMCPHSRWEKASKGSWVQTMSPFDHKILDVRVPSSNKVSLEVSAVEELFMHRIVFLLLGAVLLASASTLSQSLAFYYSSAMAVGIILVVLLVLFQGMKLLPTGRSSFALFIYSTLLGLGGFLLRYLPGLFESLLTEMGIDEEMYTPAAIFVGAFLSLGGAFFGFWTVRKLILTEDGSIDVSTSLFVSWSIRIMAAVLILQSSVDPLLAGGALISVILMSSTLKKITRLKFLLRLFEIPLNLLLGIWEAIRDTDIPSVPGYLHDFMQKSPDASGFRNRVTSASPSGGINNGMRESPPSESDTFPSSFHKTPERSQLTKEEWKKLTKDSTTKAVQELVSSPDFGKWAAVNADRINVTPRKGSSSKNQPRKWMRWF
Protein: FI04474p (Sanpodo) (Q8IMI5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein numb
- LD31322p
- Nucleolar protein 14 homolog
- Bystin
- LD47749p
- LD10780p
- LD38375p
- Lethal
- U3 small nucleolar ribonucleoprotein protein MPP10
- KRR1 small subunit processome component homolog
Sequence:
MSQHNYTNPAFCQNSEYYPVPSGNSSRVESIYNRSLQMNFGAAPPRATRDPREGPLRMQRSMSTRSVTRKQHQQQQQQQHQQQIHQQHLAQQQQHQPQSSSGRYALVPLEELNSSRASRYAIVPGQAAQRLARSQDNLDRYGSRHGLHEEEEPHSFHEEPHQETQFASLPPILNLPPKPRNINNNTNANQTQIKHAFSSDFGSKTFLIVDKNSNQRYQMVPTAEDEELVDENQEIIQMHNGRAHRYAVVPTDADDDDLAEEQEQQETCLSNMELSRQYAARTSTPQQKNAAAATRALHELLTTPRKMQPPPRLAHSTPRNAAHHEQLQLERRLEIYKSQQIYQSQQVGAVVGVPPTLPLRQNRLSPQRLHYETVKPLPMQIADRSMAVISPRVQEQGQEQEREQDMSSIQGKGKKNSSYPQKMANATITLAVVSLMLVLGSTMNAGLIIYMIAHLGKSFYLQFSLVASFSGMGLGFLGFKSRHCEWLPNRSYSSGYILVTVFCLFKSCGLLVILVVDPFPGFPVHDVTTGVILGLSTFTMFFIGLGVLGSLWCHRPPPDNRVNVV
Protein: Neuraminidase (EC 3.2.1.18) (Q6DPL2)
Organism: Influenza A virus (strain A/Vietnam/1203/2004 H5N1)
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000255|HAMAP-Rule:MF_04071}.
Interaction partners:
Sequence:
MNPNQKIITIGSICMVTGIVSLMLQIGNMISIWVSHSIHTGNQHQSEPISNTNFLTEKAVASVKLAGNSSLCPINGWAVYSKDNSIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPHRTLMSCPVGEAPSPYNSRFESVAWSASACHDGTSWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTVMTDGPSNGQASHKIFKMEKGKVVKSVELDAPNYHYEECSCYPNAGEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGVFGDNPRPNDGTGSCGPVSSNGAYGVKGFSFKYGNGVWIGRTKSTNSRSGFEMIWDPNGWTETDSSFSVKQDIVAITDWSGYSGSFVQHPELTGLDCIRPCFWVELIRGRPKESTIWTSGSSISFCGVNSDTVGWSWPDGAELPFTIDK
Protein: Ubiquitin-conjugating enzyme E2 Z (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Z) (Uba6-specific E2 conjugating enzyme 1) (Use1) (Ubiquitin carrier protein Z) (Ubiquitin-protein ligase Z) (Q3UE37)
Organism: Mus musculus (Mouse)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H832}. Nucleus {ECO:0000250|UniProtKB:Q9H832}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-conjugating enzyme E2 Q1
- Ubiquitin-conjugating enzyme E2 variant 1
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 J1
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin-conjugating enzyme E2 K
- Ubiquitin-conjugating enzyme E2 H
- Ubiquitin-conjugating enzyme E2 W
Sequence:
MAESPTEEAATATAGAGAAGPGSSGVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLGLIRQKVLERLHNENAEMDSDSSSSGTETDLHGSLRV
Protein: EFR3 homolog B (E7ESK9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKLTFYALSAPEKLDRIGAYLSERLIRDVGRHRYGYVCIAMEALDQLLMACHCQSINLFVESFLKMVAKLLESEKPNLQILGTNSFVKFANIEEDTPSYHRSYDFFVSRFSEMCHSSHDDLEIKTKIRMSGIKGLQGVVRKTVNDELQANIWDPQHMDKIVPSLLFNLQHVEEAESRSPSPLQAPEKEKESPAELAERCLRELLGRAAFGNIKNAIKPVLIHLDNHSLWEPKVFAIRCFKIIMYSIQPQHSHLVIQQLLGHLDANSRSAATVRAGIVEVLSEAAVIAATGSVGPTVLEMFNTLLRQLRLSIDYALTGSYDGAVSLGTKIIKEHEERMFQEAVIKTVGSFASTLPTYQRSEVILFIMSKVPRPSLHQAVDTGRTGENRNRLTQIMLLKSLLQVSTGFQCNNMMSALPSNFLDRLLSTALMEDAEIRLFVLEILISFIDRHGNRHKFSTISTLSDISVLKLKVDKCSRQDTVFMKKHSQQLYRHIYLSCKEETNVQKHYEALYGLLALISIELANEEVVVDLIRLVLAVQDVAQVNEENLPVYNRCALYALGAAYLNLISQLTTVPAFCQHIHEVIETRKKEAPYMLPEDVFVERPRLSQNLDGVVIELLFRQSKISEVLGGSGYNSDRLCLPYIPQLTDEDRLSKRRSIGETISLQVEVESRNSPEKEERVPAEEITYETLKKAIVDSVAVEEQERERRRQVVEKFQKAPFEEIAAHCGARASLLQSKLNQIFEITIRPPPSPSGTITAAYGQPQNHSIPVYEMKFPDLCVY
Protein: Endothelin-1 receptor (Endothelin receptor type A) (ET-A) (ETA-R) (hET-AR) (P25101)
Organism: Homo sapiens (Human)
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.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Endothelin-2
- Endothelin-3
- Endothelin-1
- Endothelin receptor type B
- Angiotensinogen
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-11
- Kininogen-1
- Guanine nucleotide-binding protein subunit alpha-13
Sequence:
METLCLRASFWLALVGCVISDNPERYSTNLSNHVDDFTTFRGTELSFLVTTHQPTNLVLPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYRGEQHKTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYNEMDKNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQWKNHDQNNHNTDRSSHKDSMN
Protein: ADP-ribosylation factor GTPase activating protein, putative (Q384B0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ADP-ribosylation factor GTPase activating protein 1, putative
- ADP-ribosylation factor GTPase activating protein, putative
Sequence:
MSNANAAQKRRIDALLRLPENKVCFECLENQPRWASTNLGVFLCLRCAGLHRSAGTHVSKVRSATMDTWEEEMIRCCENIGNARGRVLYEYNMPDSVRPNASTNGALAERLIREKYEQRRYFNVEYDSLLKKFMSEGASQGSSTPKDEKRDVVASVPAPPSLWVGNSQQTAQPTLTAGQTKQSASANGISIDDLFSTPNAKTNPNVGTPVSPQPVGVVPQGQFQQTSGMFHPAGMTPFGMEVRGPSQGNFQAPAVDAKQEIMSLFTPSNQGPPHVYSAWAPSGSSKCFSPQ
Protein: Polycystin family receptor for egg jelly (PKD and REJ homolog) (Polycystic kidney disease and receptor for egg jelly-related protein) (Q9Z0T6)
Organism: Mus musculus (Mouse)
Function: May have a central role in fertilization. May generate a Ca(2+) transporting channel directly involved in initiating the acrosome reaction of the sperm.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16261614}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:16261614}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q9NTG1}.
Interaction partners:
Sequence:
MWPGPALLLLGLGLGLGSQPPPTGPRGLPGVLRGAPGLGQGAESSVRGGDTGGLSPRAAPRHASPTPPRRCPSGAAARVLLKVNSSDPAAAKANVSCQTAPCIMQPVKINRKDQNAPLILSRDEEATLNITVRWYCPDALVIRKSWVYFSVASVNDTPDWNRPVLLPQVAVSKGFSLHIPKYALPYGVYVFNFTLSIFRWDLAWPTVTGSDIIYIWVRKRPLKAVLLGAPRVTVKFSDELILNGSMSYDPEADIPTWGLQFFWYCTTNPRYYSGNYVLVINQAVCHPEQDSLNWPWAVGSVLTIPPKTLRGNGVYYFRMVVQKQNRTAFSDKTVHVLQGLQPKAHISCIENCGPTLGVSDRFSLFLNCPSCGRQDLYSWSILSLTGHEVMFDWAGQAITRRNGPYLSIKAFAFRNFLENRVWVSLILKSWSGMTTTLRHPVVINHGPRVGKCKINPASGISMVTKFAVECSDFKDENLPLKYKIIVSELDSIGAISSVEENTLGSVVYSGAEPITPAFFLPVGTVTDEYNVRLYVQVYDSLGTFSQVTLQATVTAPTVRDSSKDVLQQLLNVTMKPTSLLSTLLQKQDWLQAGYLTYVVISVLNNIKGEQELQDDRARLLEHLVKQSLTFAMNTADEIGQSVMVITKLTQKASDLSQADLEATSFRLRQASQDLQEYQHRHKHLQQVEVVGTGILTSLSNLLKLINPYYTLQDPLFVVESLSDTILANKVPGSKTTALRTSNFNMYVEKVENWNVFKAFRNDSLCPNCLRATLNASTVPRLPAKAPISMMFCEFADDPFPWLTYPENISVDVVGFRMTGVADNNKVIEITPDIAEVYLVRKDLTPSSFNLTVGPGIKSDGFSKVTTGGISFEVDSRWTGELLIHIVTNVTVLFEALVYEGCQLTPTNLMATFLVPNDIPPIVKWSGLFDPTCSVKEARVVCLSSSLLRSIAQRRFSFKYNISMVLQASRFVLKPTNKLVRIALFMVHCLDMYGIQSDWQQSTCVLGEKTTWKTVHCVCRNGRRSRRQLTSVKLTYHHLHTHFVTAKVIVVPNPVDLRLAIISNLTQNPATFLAVLFIMILYAILAFWALHRDVIDLYFRDNVVILTDNDPFDTLCYLVTIFTGSRWGSGTRANVFIQLMGTEGTSDVHCLSHPYFKTLYRGSINTFLLTTKNDLGDIHSIRVWHDNSGEAPSWYLSRIKVENLFNKRIWLFVCRRWLSVDTTLDATFSVTNPDEPLKRTDFFMIDVRDKLRKNHMWISIFTEIVPKPFNRLQRLSCCLAMLLSSLVCNIMFFNLNQKEKIESRHMHIIRSMLIGIESVVITIPVQLLITFFFTYSQKNLKMNLDKVAPQKHPLMSEEGLSWKERLHKWHEYEMKALPRRAAVSTSAPEEKEAFETSQKHEKADTQMSNKNSSNNNQEASEGVPPKAFSSQPHTTESVQKKTQIILPRWCVYIAWFLVFATSGISSFFIVFYGVTYGYAKSIEWLFASFCSFCQSVFLVQPCNILLRSGTRSYKPKYCKNLSWSSKYHYSEIRLQGLTMTQEEMEQLHEDIAYVRSLSMYQPITEDKIQILRRENRIRRRSFLFLSYLVTHFIFLTLLLLLIFSLRHNDSFYYNQFIRHRFSVDLATVMKLGDIYTWLHGVFLPLLHNDPNPTFLPDSSSKILGLPLVRQVRARPSNKTCLLAKKFVQSSVAGEIHCHPQYGIDPEDTQHYSSVWSKAGKQSTDKASHGFTYKPPGKRWVYHSYGVLNTYGSGGYVFYFFPGQQMFNSTVRLKELEGKNWLDELTWAVIVELTTLNPDTSLMCSISVVFEVSPLGVVNSSLSVYSFSLADFNRKTSSEIYLYAAILIFFCAYVVDEGYIIRQERASYIRSVYNLLNFSLKCMFALLIVLFFWKYFLATKMVQLYLADPEAFIPFHAVSRVDHFMRIILAFLLFLTILKTLRYSRFFYNVRLAQKAIQAALPGICHTALVVSIYSFMYVAFGYLVFGQHEWNYSNMIHATQTIFSYCVSAFQNTEFSGNKVLGVLFLSSFMLVMICIFINLFQAVILSAYDEMKQPVYEEPSDEAEAVTYLCNRLKSGFDFLTTRSRDKDQSNFFVDMLYGQPEKNTRRFLGLKARNINGKKMIYLVV
Protein: Mas-related G-protein coupled receptor member X2 (Q96LB1)
Organism: Homo sapiens (Human)
Function: Mast cell-specific receptor for basic secretagogues, i.e. cationic amphiphilic drugs, as well as endo- or exogenous peptides, consisting of a basic head group and a hydrophobic core. Recognizes and binds small molecules containing a cyclized tetrahydroisoquinoline (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs), including tubocurarine and atracurium. In response to these compounds, mediates pseudo-allergic reactions characterized by histamine release, inflammation and airway contraction (By similarity). Acts as a receptor for a number of other ligands, including peptides and alkaloids, such as cortistatin-14, proadrenomedullin N-terminal peptides PAMP-12 and, at lower extent, PAMP-20, antibacterial protein LL-37, PMX-53 peptide, beta-defensins, and complanadine A.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cortistatin
- Cathelicidin antimicrobial peptide
- Pro-adrenomedullin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Centromere protein S
- Protachykinin-1
- Pro-FMRFamide-related neuropeptide FF
- Guanine nucleotide-binding protein G
Sequence:
MDPTTPAWGTESTTVNGNDQALLLLCGKETLIPVFLILFIALVGLVGNGFVLWLLGFRMRRNAFSVYVLSLAGADFLFLCFQIINCLVYLSNFFCSISINFPSFFTTVMTCAYLAGLSMLSTVSTERCLSVLWPIWYRCRRPRHLSAVVCVLLWALSLLLSILEGKFCGFLFSDGDSGWCQTFDFITAAWLIFLFMVLCGSSLALLVRILCGSRGLPLTRLYLTILLTVLVFLLCGLPFGIQWFLILWIWKDSDVLFCHIHPVSVVLSSLNSSANPIIYFFVGSFRKQWRLQQPILKLALQRALQDIAEVDHSEGCFRQGTPEMSRSSLV
Protein: Casparian strip membrane protein 1 (AtCASP1) (Q9SIH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21593871, ECO:0000269|PubMed:24920445}; Multi-pass membrane protein {ECO:0000269|PubMed:21593871, ECO:0000269|PubMed:24920445}. Note=Very restricted localization following a belt shape within the plasma membrane which coincides with the position of the Casparian strip membrane domain.
Interaction partners:
- Dirigent protein 10
- LRR receptor-like serine/threonine-protein kinase GSO1
- Transcription factor MYB36
- Peroxidase 64
- Magnesium dechelatase SGR1, chloroplastic
- Non-specific lipid transfer protein GPI-anchored 16
- Uclacyanin 1
- GDSL esterase/lipase At4g30140
- Glycerol-3-phosphate acyltransferase 5
- CASP-like protein 4C1
Sequence:
MAKESTTIDVGEPSTVTKSSSHVVKDAKKKGFVAVASRGGAKRGLAIFDFLLRLAAIAVTIGAASVMYTAEETLPFFTQFLQFQAGYDDLPAFQYFVIAVAVVASYLVLSLPFSIVSIVRPHAVAPRLILLICDTLVVTLNTSAAAAAASITYLAHNGNQSTNWLPICQQFGDFCQNVSTAVVADSIAILFFIVLIIISAIALKRH
Protein: JmjC domain-containing protein (Q386V9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAQSWFKRHPLGIYPRGNAKNLDELVSPRFGILSTLQFASKGRAGKCCILGSQPAEEAFVDVMLHLLSFVAVDDMCRLSAVCTGWYCFIHASDAFKQAHGLLSPTYTCFEGSWKETAIRRFIKLRSKQRLNTAKRMRLEGGTPGVGETVNLSHRPVMVKRAFYNDQLFQAWMCTILPCHYHLRQSSIAGTATANRQPSVLSARGRYRSPLKEVPRCSGLSVDEFRTRFEETNLPVIIADVATEWPIYKILQEKFENLAVMQKKLFRPGTRPDVPMCCEHTTMSVADYVRYARDQTDERPIYLFDSEFGTFMDVESLYTVPEYFSRDDFFKVLGGARPKYRWIIAGPRRGGSSFHVDPNYTSAWNANLTGLKRWILLPPGHTPAGVFPSEDMSEVVTPVSLTEWLLNHYDATVEKWRDVAYECVCGPGDIMFIPCGWWHFVINLEDSVAITQNYVSKCNLSSVLKFLSVMKSSISGIDEDVDNCDTSRMVETRRANFAEEFAAAMHLSYPELMQTVAGEAKREAEERHEKKKMRAALPLLDVGSNGFAFSF
Protein: Latexin (Endogenous carboxypeptidase inhibitor) (ECI) (Tissue carboxypeptidase inhibitor) (TCI) (P70202)
Organism: Mus musculus (Mouse)
Function: Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Carboxypeptidase A4
- Cytosolic carboxypeptidase 2
Sequence:
MEIPPTHYAASRAASVAENCINYQQGTPHKLFLVQTVQQASKEDIPGRGHKYHLKFSVEEIIQKQVTVNCTAEVLYPQMGQGSAPEVNFTFEGEIGKNPDEEDNTFYQSLMSLKRPLEAQDIPDNFGNVSPQMKPVQHLAWVACGYVMWQNSTEDTWYKMLKIQTVKQVQRNDDFIELDYTILLHDIASQEIIPWQMQVLWHPQYGTKVKHNSRLPKEGQAE