wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q7ZVG8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Striatin
- Programmed cell death protein 10-A
- TRAF2 and NCK-interacting kinase b.
- Striatin-interacting protein 1 homolog
- Striatin, calmodulin-binding protein 4.
- Striatin-interacting protein 1 homolog isoform X2
- Krev interaction trapped protein 1
- Striatin, calmodulin-binding protein 3.
- Protein FAM65A isoform X5
- Calcium-binding protein 39.
Sequence:
MAHLRDMQNQNSRLDPEEYFTKQERIGKGSFGEVYKGINNRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLEYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNTPPTLEGSYSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSYLTELIDRYRRWKSEGHGDESSSDDSDMDGDGDDRDHCPVWTFPTVRPSSMNKLQKGYTNTDSEAAETVKRQPKSQCLSALVSPIFRELKEKRRACGGGMGAIEELENAFNLAEESCPGISDLLVTHIMERVCRFALNGNTTPSSR
Protein: GPI-anchor transamidase (GPI transamidase) (EC 3.-.-.-) (P49018)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- GPI transamidase component GAA1
- GPI transamidase component GPI16
- GPI transamidase component GPI17
- GPI transamidase component GAB1
- GPI ethanolamine phosphate transferase 3
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- GPI inositol-deacylase
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI mannosyltransferase 2
- GPI mannosyltransferase 3
Sequence:
MRIAMHLPLLLLYIFLLPLSGANNTDAAHEVIATNTNNWAVLVSTSRFWFNYRHMANVLSMYRTVKRLGIPDSQIILMLSDDVACNSRNLFPGSVFNNKDHAIDLYGDSVEVDYRGYEVTVENFIRLLTDRWTEDHPKSKRLLTDENSNIFIYMTGHGGDDFLKFQDAEEIASEDIADAFQQMYEKKRYNEIFFMIDTCQANTMYSKFYSPNILAVGSSEMDESSYSHHSDVEIGVAVIDRFTYYCLDFLEQIDKNSTLTLQDLFDSFTFEKIHSHVGVRTDLFDRNPSEVLITDFFANVQNVIPDDSKPLSVSHYHHYKDHIDTAQYELNNNVLDLALETYRKNNQSSKIEKKIKDIKSTSVLDVDIDSNECFFTSFKQSATIILALIVTILWFMLRGNTAKATYDLYTN
Protein: Protein C2-DOMAIN ABA-RELATED 8 (O49303)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the GTPase/ATPase activities of Obg-like ATPases (By similarity). Mediates the transient calcium-dependent interaction of PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and thus regulates ABA sensitivity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FHP6}. Nucleus {ECO:0000250|UniProtKB:Q9FHP6}.
Interaction partners:
- Probable E3 ubiquitin-protein ligase BAH1-like
- Serine/threonine-protein kinase BSK
- Protein RALF-like 27
- Protein RALF-like 9
- Epimerase family protein SDR39U1 homolog, chloroplastic
- Protein CLMP1
- Probable histone H2A.2
- Cysteine-rich receptor-like protein kinase 24
Sequence:
MENLVGLLRIRVKRGINLVSRDSNTSDPFVVVTMGSQKLKTRGVENSCNPEWDDELTLGINDPNQHVTLEVYDKDTFTSHDPMGDAEIDIKPFFEVQGTDIQELTNGTEIRRVKPSGDNCLAEESRIIFSNGKILQDMILQLRNVESGEVEIQIEWINVTGSSDF
Protein: Kinesin-like protein KIN-4A (GhKINESIN-4A) (A0A068FIK2)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: Kinesin-like motor protein involved in the control of the oriented deposition of cellulose microfibrils.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25600279}. Note=Localizes with vesicle-like structures associated with cortical microtubules (PubMed:25600279). {ECO:0000269|PubMed:25600279}.
Interaction partners:
Sequence:
MEVGGGSEECCVKVAVHVRPLIGDEKVQGCKDCVTVIPGKPQVQIGTHSFTFDHVYGSTSSPSWMFEECIVPLVDGLFQGYNATVLAYGQTGSGKTYTMGTGFKGGSQTGIIPQVMNALFSKIENLKHQIEFQLHVSFIEILKEEVRDLLDPTFLNKSDTASANTGKVNVPGKPPIQIRESSDGVITLAGSTEVSVSTLKEMGACLEQGSLSRATGSTNMNNQSSRSHAIFTITLEQMRKLNPVSGDGNPNDSMSEEYLCAKLHLVDLAGSERAKRTGSDGMRFKEGVHINKGLLALGNVISALGDEKKRKEGVHVPYRDSKLTRLLQDSLGGNSRTVMIACISPADINAEETLNTLKYANRARNIQNKPVVNRDPMSNEILKMRQQLEYLQAELCARGGSGEVQVLNERIAWLEAANEDLCRELYEYRSRCTIVEQREMDAQDGSPCSVESDGLKRNLRSRESRDNQIVETMIGGDSREIEEGAAKEWEHMLLQNTMDKELHELNRQLEEKESEMKVFGGHTVALKQHFGKKIQELEEEKRAVQQERDRLLAEIENLSAGSEGQALKVHDIHAQKLKSLEAQIMDLKKKQENQVQLLKKKQKSDEAAKRLQDEIQYIKAQKVQLQHRIKQEAEQFRQWKASREKELLQLRKEGRRNEYERHKLQALNQRQKLVLQRKTEEAAMATKRLKELLEARKSAARDNLAIANGNGTNGKINEKGLQRWLDHELEVMVNVHEVRFEYEKQSQVRAALAEELAVLKQVDELDSKGPSPSRGKNGCARGSSLSPNARVARISSLEHMLGISSNSLVAMASQLSEAEERERAFTNRGRWNQLRSMGDAKNLLQYMFNSLGDSRYQLWEKGIEIREMKEQLKELVGLLRQSELQRKEVENELKLREQAVAIALATSATGNSPISLKHIDDDVKSSSSPMSVPAQKQLKYSPGIVNGPARESAAFIGQTRKMIPLGQLPMKNLVANGQAGNGKLWRWKRSHHQWLVQFKWKWQKPWRLSEWIRHSDETIIRARPRSQVLTYRV
Protein: Probable cation-transporting ATPase F (EC 7.2.2.-) (P9WPS9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Putative zinc metalloprotease Rip3
- Putative NAD
- ATP-dependent 6-phosphofructokinase isozyme 2
- Universal stress protein Rv2028c
- Probable nitrate/nitrite transporter NarK2
- Uncharacterized protein Rv2004c
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Uncharacterized glycosyl hydrolase Rv2006
- Nitrate reductase-like protein NarX
- Uncharacterized protein Rv2030c
Sequence:
MSASVSATTAHHGLPAHEVVLLLESDPYHGLSDGEAAQRLERFGPNTLAVVTRASLLARILRQFHHPLIYVLLVAGTITAGLKEFVDAAVIFGVVVINAIVGFIQESKAEAALQGLRSMVHTHAKVVREGHEHTMPSEELVPGDLVLLAAGDKVPADLRLVRQTGLSVNESALTGESTPVHKDEVALPEGTPVADRRNIAYSGTLVTAGHGAGIVVATGAETELGEIHRLVGAAEVVATPLTAKLAWFSKFLTIAILGLAALTFGVGLLRRQDAVETFTAAIALAVGAIPEGLPTAVTITLAIGMARMAKRRAVIRRLPAVETLGSTTVICADKTGTLTENQMTVQSIWTPHGEIRATGTGYAPDVLLCDTDDAPVPVNANAALRWSLLAGACSNDAALVRDGTRWQIVGDPTEGAMLVVAAKAGFNPERLATTLPQVAAIPFSSERQYMATLHRDGTDHVVLAKGAVERMLDLCGTEMGADGALRPLDRATVLRATEMLTSRGLRVLATGMGAGAGTPDDFDENVIPGSLALTGLQAMSDPPRAAAASAVAACHSAGIAVKMITGDHAGTATAIATEVGLLDNTEPAAGSVLTGAELAALSADQYPEAVDTASVFARVSPEQKLRLVQALQARGHVVAMTGDGVNDAPALRQANIGVAMGRGGTEVAKDAADMVLTDDDFATIEAAVEEGRGVFDNLTKFITWTLPTNLGEGLVILAAIAVGVALPILPTQILWINMTTAIALGLMLAFEPKEAGIMTRPPRDPDQPLLTGWLVRRTLLVSTLLVASAWWLFAWELDNGAGLHEARTAALNLFVVVEAFYLFSCRSLTRSAWRLGMFANRWIILGVSAQAIAQFAITYLPAMNMVFDTAPIDIGVWVRIFAVATAITIVVATDTLLPRIRAQPP
Protein: Muscle-specific homeobox protein tinman (Msh-2) (NK-4) (P22711)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the development of heart and visceral muscle; for the formation of somatic muscles. Has a crucial function in the early mesodermal subdivisions.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Myocyte-specific enhancer factor 2
- LP04777p
- GATA-binding factor A
- FI14601p
- Forkhead box protein biniou
- Protein twist
- Protein decapentaplegic
- Steroid receptor seven-up, isoform A
- Insulin gene enhancer protein ISL-1
- Zinc finger protein 1
Sequence:
MLQHHQQQAQSGGYYDHYTQSPSPGSLTNADALNTTPFSVKDILNMVNQTEAYEGSYGHIDGAATASALFAAGEYQNPHQYLNHQQHQQSELPIPQQQLHHQHLDDGATTSSSLSPLLPPPPHQLYGGYQDYGMPAHMFQHHHGHPHQSFQHSASAYNMSASQFYAGASATAYQTPATYNYNYAGSGEVYGGATPSAVGIKSEYIPTPYVTPSPTLDLNSSAEVDSLQAPTQKLCVNPLSQRLMETASNSSSLRSIYGSDEGAKKKDNSQVTSSRSELRKNSISGNSNPGSNSGSTKPRMKRKPRVLFSQAQVLELECRFRLKKYLTGAEREIIAQKLNLSATQVKIWFQNRRYKSKRGDIDCEGIAKHLKLKSEPLDSPTSLPPPIPNHVMWPPTMQQSQQQQQHHAQQQQMQHM
Protein: Nitric oxide synthase-interacting protein homolog (Q9VWV8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Negatively regulates nitric oxide production by inducing nitric oxide synthase translocation to actin cytoskeleton and inhibiting its enzymatic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Nitric oxide synthase
Sequence:
MTRHARNCTAGAVYTYNEKKRDAAESGYGTNAQRLGKDSVKSFDCCSLTLQPCRRPVITKDGYLFDKEAILQYIVTKKNEYSRRLKEYERLRRAEEDKLSQEANSKQQARMERFVNAEKPAMTPAHSSAAASEKPSTSSAAAAASSESSSASSISNMTNGHEKKLPSFWLPSECPNAGLAKAQKPDATIYCPVSQKPLRVKDLIDVKFTLLKDGDTKRSLIAKEARYMCPITHDVLSNAVPCAVLRPTGDVVTMECVERLIRKDMIHPLTDRKLKEKDIIPLQRGGTGYATTNDHLQAKEKRPMLQA
Protein: A-type potassium channel modulatory protein KCNIP1 (Kv channel-interacting protein 1) (KChIP1) (Potassium channel-interacting protein 1) (Q8R426)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. Modulates KCND2/Kv4.2 currents. In vitro, modulates KCND1/Kv4.1 currents (By similarity). Increases the presence of KCND2 at the cell surface.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:15356203}; Peripheral membrane protein {ECO:0000269|PubMed:14980206}. Cytoplasm {ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:15356203}. Cell projection, dendrite {ECO:0000269|PubMed:15356203}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- Potassium voltage-gated channel subfamily A member 4
- A-type potassium channel modulatory protein DPP6
- Voltage-gated potassium channel KCNC1
- A-type voltage-gated potassium channel KCND1
- Inactive dipeptidyl peptidase 10
- Kv channel-interacting protein 4
Sequence:
MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDDLEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM
Protein: Guanine nucleotide-binding protein G(olf) subunit alpha (EC 3.6.5.-) (Adenylate cyclase-stimulating G alpha protein, olfactory type) (P38405)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(olf) alpha mediates signal transduction within the olfactory neuroepithelium and the basal ganglia. May be involved in some aspect of visual transduction, and in mediating the effect of one or more hormones/neurotransmitters.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8CGK7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8CGK7}.
Interaction partners:
- Adenylate cyclase type 9
- D
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 3
- Adenylate cyclase type 5
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 2
- Adenylate cyclase type 8
- Adenylate cyclase type 7
Sequence:
MGCLGGNSKTTEDQGVDEKERREANKKIEKQLQKERLAYKATHRLLLLGAGESGKSTIVKQMRILHVNGFNPEEKKQKILDIRKNVKDAIVTIVSAMSTIIPPVPLANPENQFRSDYIKSIAPITDFEYSQEFFDHVKKLWDDEGVKACFERSNEYQLIDCAQYFLERIDSVSLVDYTPTDQDLLRCRVLTSGIFETRFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIYVAACSSYNMVIREDNNTNRLRESLDLFESIWNNRWLRTISIILFLNKQDMLAEKVLAGKSKIEDYFPEYANYTVPEDATPDAGEDPKVTRAKFFIRDLFLRISTATGDGKHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLKQYELL
Protein: F-box only protein 8 (Q9QZN3)
Organism: Mus musculus (Mouse)
Function: May promote guanine-nucleotide exchange on an ARF. Promotes the activation of ARF through replacement of GDP with GTP (Potential).
Interaction partners:
- Centrosomal protein of 44 kDa
Sequence:
MGQGLWRVARNHHLQQEAYSETGYLSREQSRRVASSNISHTSHRKQAQGGIDIYHLLKARKSKEQEGFINLEMLPPELSFTILSYLNATDLCLASCVWQDLANDELLWQGLCKSTWGHCSIYNKNPPLGFSFRKLYMQLDEGSLTFNANPEEGVSYFMSKGILDDSPKEIAKFIFCTRTLNWKKLRIYLDERRDVLDDLVTLHNFRNQFLPNALREFFRHIHAPEERGEYLETLITKFSHRFCACNPDLMRELGLSPDAVYVLCYSLILLSIDLTSPHVKNKMSKREFIRNTRRAAQNISEDFVGHLYDNIYLIGHVAA
Protein: Copine-6 (Copine VI) (Neuronal-copine) (N-copine) (Q9Z140)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Binds phospholipid membranes in a calcium-dependent manner. Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:9886090}. Cell membrane {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110}. Endosome {ECO:0000269|PubMed:21087455}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:21087455}. Perikaryon {ECO:0000269|PubMed:9886090}. Cell projection, dendrite {ECO:0000269|PubMed:9886090}. Note=Mainly cytoplasmic in absence of calcium. Associated predominantly with membranes in presence of calcium (PubMed:9886090). Translocates to the cell membrane in a calcium-dependent manner (PubMed:21087455, PubMed:26175110). Colocalized with transferrin in intracellular clathrin-coated membrane vesicles in a calcium-dependent manner (PubMed:21087455). {ECO:0000269|PubMed:21087455, ECO:0000269|PubMed:26175110, ECO:0000269|PubMed:9886090}.
Interaction partners:
Sequence:
MSDPEMGWVPEPPAMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERTEVLRSCSSPVFSRVLAIEYFFEEKQPLQFHVFDAEDGATSPSSDTFLGSTECTLGQIVSQTKVTKPLLLKNGKTAGKSTITIVAEEVSGTNDYVQLTFRAHKLDNKDLFSKSDPFMEIYKTNGDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDIHRPLKFLVYDYDSSGKHDFIGEFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTFLDYIMGGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRTVGGICQDYDSDKRFPAFGFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPIINRVAEPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNADFSDMRLLDGDDGPLRCPKGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYASQGISPGAPRPSTPAMTPSPSP
Protein: Homeobox protein Hox-A9 (Homeobox protein Hox-1.7) (P09631)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P31269}. Cytoplasm {ECO:0000250|UniProtKB:P31269}.
Interaction partners:
- Homeobox protein Meis1
- Pre-B-cell leukemia transcription factor 1
- Pre-B-cell leukemia transcription factor 3
- Homeobox protein Hox-A10
- Homeobox protein Hox-A7
- Protein AF-9
- Nuclear pore complex protein Nup98-Nup96
- Btk-PH-domain binding protein translocated to, 1)
- Pre-B-cell leukemia transcription factor 2
- Histone-lysine N-methyltransferase 2A
Sequence:
MATTGALGNYYVDSFLLGADAADELGAGRYAPGTLGQPPRQAAALAEHPDFSPCSFQSKAAVFGASWNPVHAAGANAVPAAVYHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPGALSFAGLPSSRPYGIKPEPLSARRGDCPTLDTHTLSLTDYACGSPPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE
Protein: Arginine-specific demethylase JMJ20 (EC 1.14.11.-) (Arginine-specific histone demethylase JMJ20) (Jumonji domain-containing protein 20) (AtJMJ20) (Protein JUMONJI 20) ([histone H4]-dimethyl-L-arginine(3) monodemethylase JMJ20) (Q67ZB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone demethylase that demethylates 'Arg-3' (H4R3me) of histone H4 with a specific activity for H4R3me2. Involved in the positive regulation of gene expression. Together with JMJ22, regulates positively seed germination by promoting the removal of repressive histone arginine methylations (e.g. H4R3me2) at GA3ox1 and GA3ox2 to trigger gibberellic acid (GA) biosynthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:22483719}.
Interaction partners:
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 1
- Dof zinc finger protein DOF3.7
- Histone deacetylase 15
Sequence:
MGIQIIGQIERINGKELSYGDFAERYLAKNQPVVISDLTEDWRAREDWVSENGNPNLHVFATHFGKSRVQVADCDTREFTDQKRLEMSVTEFVEQWTNKDSIEESVLYLKDWHFVKEYPDYTAYQTPPLFSDDWLNVYLDNYQMHEDRDSFQKYDQISCSDYRFVYMGGKGSWTPLHADVFRSYSWSANVCGKKRWLFLPPPQSHLVYDRYMKNCVYDIFEEVNETKFPGFKKTTWLECIQEPGEIIFVPSGWHHQVYNLEDTISINHNWLNAYNLSWVWDLLWKDYKDTEESIEDIRDICDDFEAICQRNLAANTGMNLNDFFLFMSRFSLGNMVLLQSYSDKHKNLNSCSLAMAQNLLMNLSTILKVMMKMISAGGVTAEEVYLDLRETLEDPQFLRFVRDMGRTYARIHMEEEDQFLSSKELLQKLSGLAGPNMQICSPKDLVEMINHHNTFSSQIYFI
Protein: Monocarboxylate transporter 1 (MCT 1) (Solute carrier family 16 member 1) (P53986)
Organism: Mus musculus (Mouse)
Function: Bidirectional proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (By similarity). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis. Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart. Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 302-Asp is essential for the conformational transition (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21792931, ECO:0000269|PubMed:8603082}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53987}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Apical cell membrane {ECO:0000250|UniProtKB:P53985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53985}. Note=Expression at the cell surface requires the ancillary proteins BSG and EMB. {ECO:0000250|UniProtKB:P53985}.
Interaction partners:
- Basigin
- Embigin
- Sodium-coupled monocarboxylate transporter 1
- Carbonic anhydrase 2
- L-lactate dehydrogenase A chain
Sequence:
MPPAIGGPVGYTPPDGGWGWAVLVGAFISIGFSYAFPKSITVFFKEIEVIFSATTSEVSWISSIMLAVMYAGGPISSILVNKYGSRPVMIAGGCLSGCGLIAASFCNTVQELYLCIGVIGGLGLAFNLNPALTMIGKYFYKKRPLANGLAMAGSPVFLSTLAPLNQAFFDIFDWRGSFLILGGLLLNCCVAGSLMRPIGPEQVKLEKLKSKESLQEAGKSDANTDLIGGSPKGEKLSVFQTINKFLDLSLFTHRGFLLYLSGNVVMFFGLFTPLVFLSSYGKSKDFSSEKSAFLLSILAFVDMVARPSMGLAANTKWIRPRIQYFFAASVVANGVCHLLAPLSTTYVGFCVYAGVFGFAFGWLSSVLFETLMDLIGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVILIIAGIYLFIGMGINYRLLAKEQKAEEKQKREGKEDEASTDVDEKPKETMKAAQSPQQHSSGDPTEEESPV
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FUH0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MSFLKNLLFGGVKTSEDPTGITDSGSGNAKASQDVNEPIVEGRFTPRTLSKFNGHDDEKIFIAIRGKVYDCTAGRQFYGPSGPYSNFAGHDASRGLALNSFEMEVVPDWDKPMDDLKDLTPQQIDSLNEWEQHFANKYPVVGTLEAEPGVNV
Protein: Protein STE50 (P25344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in growth arrest during conjugation. May interact with the G protein alpha subunit.
Interaction partners:
- High osmolarity signaling protein SHO1
- Cell division control protein 42
- Serine/threonine-protein kinase STE11
- Protein OPY2
- Mitogen-activated protein kinase HOG1
- Serine/threonine-protein kinase STE20
- Mitogen-activated protein kinase FUS3
- MAP kinase kinase PBS2
- Serine/threonine-protein kinase STE7
- Osmolarity two-component system protein SSK1
Sequence:
MEDGKQAINEGSNDASPDLDVNGTILMNNEDFSQWSVDDVITWCISTLEVEETDPLCQRLRENDIVGDLLPELCLQDCQDLCDGDLNKAIKFKILINKMRDSKLEWKDDKTQEDMITVLKNLYTTTSAKLQEFQSQYTRLRMDVLDVMKTSSSSSPINTHGVSTTVPSSNNTIIPSSDGVSLSQTDYFDTVHNRQSPSRRESPVTVFRQPSLSHSKSLHKDSKNKVPQISTNQSHPSAVSTANTPGPSPNEALKQLRASKEDSCERILKNAMKRHNLADQDWRQYVLVICYGDQERLLELNEKPVIIFKNLKQQGLHPAIMLRRRGDFEEVAMMNGSDNVTPGGRL
Protein: Zinc finger and BTB domain-containing protein 25 (Zinc finger protein 46) (Zinc finger protein KUP) (P24278)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus.
Interaction partners:
- Zinc finger protein 383
- Elongator complex protein 6
Sequence:
MDTASHSLVLLQQLNMQREFGFLCDCTVAIGDVYFKAHRAVLAAFSNYFKMIFIHQTSECIKIQPTDIQPDIFSYLLHIMYTGKGPKQIVDHSRLEEGIRFLHADYLSHIATEMNQVFSPETVQSSNLYGIQISTTQKTVVKQGLEVKEAPSSNSGNRAAVQGDHPQLQLSLAIGLDDGTADQQRACPATQALEEHQKPPVSIKQERCDPESVISQSHPSPSSEVTGPTFTENSVKIHLCHYCGERFDSRSNLRQHLHTHVSGSLPFGVPASILESNDLGEVHPLNENSEALECRRLSSFIVKENEQQPDHTNRGTTEPLQISQVSLISKDTEPVELNCNFSFSRKRKMSCTICGHKFPRKSQLLEHMYTHKGKSYRYNRCQRFGNALAQRFQPYCDSWSDVSLKSSRLSQEHLDLPCALESELTQENVDTILVE
Protein: Glycophorin (B8Q183)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MYGKIIFVLLLSAIVSISASSTTGVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ
Protein: Uncharacterized protein (Q381M4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKHCSACAGGATLLRATRMTGATFIQARCAHLVRGTNRSLGQHQGTNIPHYRLPLRRALRLIDSTGRHNASMVETEDCVSEEQLQHHSHDGEGVSQRQEDAARYAAYHCHHMLTSFRVERQRWGENTGTLSVEDLSRIVEYIFYASVLLHLTALYQTADKYCEDLIGAVISCSIFVSKNVEEILKSLSTASASGTLMAANKRLASQGSDMWNSLHWAAVHYSQGVCYWGLLDHTEPLFDMRRLHAPFRGLFSTYVKLVCKILAHAGMPREDKQLLSYVKSPEGCNRWFGEEVNGGLAVSTLCFPGSAAGTACSGVHDNHCFPQQRRLQLLPLIWVALLSCHCAVSNEENRFRSARHAFLHVLPLFSKEAKAENVVMLLARLLYIRPSTVLKANSVDVGMLLARAEQCNVFPPSSSVPSVTYAAFLRLWMCADVAQEKEPEVRGVHKAYAAFRAIPLCALQLDGEPHSPASGGDAFVRHLLLRALLQWSFRLTAFVSFRGEVEEILKSTQHVVQLLDHARRRPGWGGRKETIVVDLCEAVLRAFAVRVSVICGMDAPLKKEDYALIAEFDDVVRMMIRSGEDRSSLCTLPTVYECLRPRRGSRSYAREVEEDSFPSSLTPRNSPV
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Phosphatase and tensin homolog) (Q6TGR7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm {ECO:0000256|PIRNR:PIRNR038025}. Nucleus {ECO:0000256|PIRNR:PIRNR038025}. Nucleus, PML body {ECO:0000256|PIRNR:PIRNR038025}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
Sequence:
MAMTAKLKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDASKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDENHVAAIHCKAGKGRTGVMICAYLLHRKKFAEAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNKLDYKPVALLFHKMVFQTLPMFSGGTCNPQFVVYQLKVKIHTSNPAHTRREEKHMIFEFPQPLPVCGDIKVEFFHKQSKMMKKDKMFHFWINTFFIPGPEEAGDKVENGSVVNDVDSLSCQSQSSPAERDREKERAVAAAALDRERGEQRADGEKDYLILTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNSEASTSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEEQHAQITKV
Protein: Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.143) (Beta-1,2-N-acetylglucosaminyltransferase II) (GlcNAc-T II) (GNT-II) (Mannoside acetylglucosaminyltransferase 2) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II) (Q921V5)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in protein N-glycosylation. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q10469}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q10469}.
Interaction partners:
- Alpha-mannosidase 2
- Alpha-mannosidase 2x
- Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Sequence:
MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKSDALGPPLLDAEPVRGAGHLAVSVGIRRVSNESAAPLVPAVPRPEVDNLTLRYRSLVYQLNFDQMLRNVGNDGTWSPGELVLVVQVHNRPEYLRLLIDSLRKAQGIQEVLVIFSHDFWSAEINSLISRVDFCPVLQVFFPFSIQLYPNEFPGSDPRDCPRDLKKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHFVWERVKVLQDYTGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPGCDVLSLGTYTTIRSFYGIADKVDVKTWKSTEHNMGLALTRDAYQKLIECTDTFCTYDDYNWDWTLQYLTLACLPKIWKVLVPQAPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNSNKQYLFPETLVIGEKFPMAAISPPRKNGGWGDIRDHELCKSYRRLQ