wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase PSK1 (EC 2.7.11.1) (PAS kinase 1) (P31374)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase involved in the control of sugar metabolism and translation. Phosphorylates UGP1, which is required for normal glycogen and beta-(1,6)-glucan synthesis. This phosphorylation shifts glucose partitioning toward cell wall glucan synthesis at the expense of glycogen synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase
- Protein BMH2
Sequence:
MPYIGASNLSEHSFVNLKEKHAITHKGTSSSVASLQTPPSPDQENHIDNELENYDTSLSDVSTPNKKEGDEFEQSLRDTFASFRKTKPPPPLDFEQPRLPSTASSSVDSTVSSPLTDEDIKELEFLPNESTHSYSYNPLSPNSLAVRLRILKRSLEIIIQNPSMLLEPTPDDLPPLKEFAGRRSSLPRTSASANHLMNRNKSQIWNTTSATLNAFVNNTSSSSAASSALSNKKPGTPVFPNLDPTHSQTFHRANSLAYLPSILPEQDPLLKHNNSLFRGDYGNNISPERPSFRQPFKDQTSNLRNSSLLNERAYQEDETFLPHHGPSMDLLNEQRANLKSLLNLLNETLEKNTSERASDLHMISLFNLNKLMLGDPKKNNSERDKRTEKLKKILLDSLAEPFFEHYNFIGDNPIADTDELKEEIDEFTGSGDTTAITDIRPQQDYGRILRTFTSTKNSAPQAIFTCSQEDPWQFRAANDLACLVFGISQNAIRALTLMDLIHTDSRNFVLHKLLSTEGQEMVFTGEIIGIVQPETLSSSKVVWASFWAKRKNGLLVCVFEKVPCDYVDVLLNLDDFGAENIVDKCELLSDGPTLSSSSTLSLPKMASSPTGSKLEYSLERKILEKSYTKPTSTENRNGDENQLDGDSHSEPSLSSSPVRSKKSVKFANDIKDVKSISQSLAKLMDDVRNGVVFDPDDDLLPMPIKVCNHINETRYFTLNHLSYNIPCAVSSTVLEDELKLKIHSLPYQAGLFIVDSHTLDIVSSNKSILKNMFGYHFAELVGKSITEIIPSFPKFLQFINDKYPALDITLHKNKGLVLTEHFFRKIQAEIMGDRKSFYTSVGIDGLHRDGCEIKIDFQLRVMNSKVILLWVTHSRDVVFEEYNTNPSQLKMLKESELSLMSSASSSASSSKKSSSRISTGTLKDMSNLSTYEDLAHRTNKLKYEIGDDSRAHSQSTLSEQEQVPLENDKDSGEMMLADPEMKHKLELARIYSRDKSQFVKEGNFKVDENLIISKISLSPSTESLADSKSSGKGLSPLEEEKLIDENATENGLAGSPKDEDGIIMTNKRGNQPVSTFLRTPEKNIGAQKHVKKFSDFVSLQKMGEGAYGKVNLCIHKKNRYIVVIKMIFKERILVDTWVRDRKLGTIPSEIQIMATLNKKPHENILRLLDFFEDDDYYYIETPVHGETGCIDLFDLIEFKTNMTEFEAKLIFKQVVAGIKHLHDQGIVHRDIKDENVIVDSKGFVKIIDFGSAAYVKSGPFDVFVGTIDYAAPEVLGGNPYEGQPQDIWAIGILLYTVVFKENPFYNIDEILEGDLKFNNAEEVSEDCIELIKSILNRCVPKRPTIDDINNDKWLVI
Protein: Cilia- and flagella-associated protein 20 (Basal body up-regulated protein 22) (Transcription factor IIB) (Q9Y6A4)
Organism: Homo sapiens (Human)
Function: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the regulation of the size and morphology of cilia. Required for axonemal microtubules polyglutamylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:24414207}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:24414207}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24414207}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:24414207, ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q8BTU1}.
Interaction partners:
- TATA-box-binding protein
- Parkin coregulated gene protein
- EF-hand domain-containing protein 1
- EF-hand domain-containing family member B
- EF-hand domain-containing family member C2
- Enkurin
- Transcription initiation factor IIB
- Protein broad-minded
- Tubulin beta-4B chain
- Cilia- and flagella-associated protein 45
Sequence:
MFKNTFQSGFLSILYSIGSKPLQIWDKKVRNGHIKRITDNDIQSLVLEIEGTNVSTTYITCPADPKKTLGIKLPFLVMIIKNLKKYFTFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDDGWNQIQFNLLDFTRRAYGTNYIETLRVQIHANCRIRRVYFSDRLYSEDELPAEFKLYLPVQNKAKQ
Protein: Probable glutamate carboxypeptidase AMP1 (EC 3.4.17.21) (Probable glutamate carboxypeptidase 2) (Probable glutamate carboxypeptidase II) (Protein ALTERED MERISTEM PROGRAM 1) (AtAMP1) (Protein CONSTITUTIVE MORPHOGENESIS 2) (Protein HAUPTLING) (Protein MULTIFOLIA) (Protein PRIMORDIA TIMING) (Q9M1S8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May modulate the level of one or more small signaling molecules that have a role in regulating meristem function. May play a role in balancing and restricting the meristem-promoting activity of auxin signaling. Involved in ethylene and giberellin (GA) signaling pathways or in a parallel pathway controlling cell and hypocotyl elongation and cellular organization. Involved in abscisic acid (ABA) signaling pathway. Plays a negative role in ABA-mediated seed germination and seedling development. Acts in association with LAMP1 to suppress ectopic stem cell niche formation in the shoot apical meristem (SAM) independently of cytokinin signaling pathway. Modulates responses to ABA, oxidative stress and abotic stress. Acts as negative regulator of the ABA signaling pathway to modulate freezing and drought stress responses. Mediates carbon and amino acid metabolism. May be involved in the acquisition and/or maintenance of seed dormancy. Involved in the regulation of response to heat shock and plant defense.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:25673776}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Histidine kinase 1
- Histidine kinase 2
- Histidine kinase 5
- Histidine kinase 4
- Histidine-containing phosphotransfer protein 3
- Protein SUO
- Histidine kinase 3
- Ninja-family protein AFP2
- Probable N-acetyltransferase HLS1
- Histidine-containing phosphotransfer protein 4
Sequence:
MSQPLTTRPTVTGISIIPFRQPPPLCSFLFVIVLFVATFYTLHHPDAVTPPLLFSRNAYNALRLRRLFLSSASNATISSYLRELTRHPHLAGTKPSLDTLHYVFNHFQSLGLETHVAEYEALLSYPTHISVTASFSNTTTLEFDLNDVPGDSPVVRPYHAYSPSGSAQGNVVFVNHGEERDYHALESIGVSVKGCVVLARKGENLGRGAIVKIAEAKGALGVLIYAENDGGGFGGIERGTVMRGIGDPVSPGWPGVVGGEKLSLDDELVTRRFPKIPSLPLSLRNAEIILASLGGARAPLEWRNSGRVGPGQRVGPGRMVINMTFQGEMKMKKINNVVVTIRGSEEADRYVILGNHRDAWTYGAVDPNSGTSALLDISRRFALLLKSGWRPRRTILLCSWDAEEFGMIGSTEWIEENVLNLGASAVAYLNVDCAVQGSGFFAGATPQLDGLLVDVLKLVQDPDAVGLTVEETFKSQNNIIQRLSRVDSDFSGFLHHAGIPSIDMYYGADYPVYHTAFDSYDWMIHNADPLFHRHVAMAGIWGLLGILLADEPLIPFDYISYADQLQAHRDKLSKLLEGKVSVNPLSMAIQEFSLVAKEAADEAKKLKGKSYSKNDVAAAAKRRELNDRLMLVERGFLDAEGIKGKEWFKHLVYGPAAEPESKLGFFPGIADAIAMNASEGIIEHEIWRVARAIQRASKALKGGFT
Protein: Myosin light chain 3 (Myosin alkali light chain 1, ventricular) (MLClV) (Myosin light chain 1, slow-twitch muscle B/ventricular isoform) (MLC1SB) (Ventricular myosin light chain 1) (rVMLC1) (P16409)
Organism: Rattus norvegicus (Rat)
Function: Regulatory light chain of myosin. Does not bind calcium.
Interaction partners:
- Myosin-7
- Myosin-6
- Actin, alpha cardiac muscle 1
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain kinase 2, skeletal/cardiac muscle
- Troponin I, slow skeletal muscle
- Similar to OTTMUSP00000000621
- Myosin light chain kinase 3
- Myosin light chain 4
- Myosin-binding protein C, cardiac-type
Sequence:
MAPKKPEPKKDDAKTAAPKAAPAPAAAPAAAPEPERPKEAEFDASKIKIEFTPEQIEEFKEAFQLFDRTPKGEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPKQEELNSKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMAS
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (E7ET49)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA
Protein: Uncharacterized protein (Q38CF6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIGTRRSTKSTSFQHLYGSQNRTLRGANGQKGFSHQRNGTAREEQQSTKPPGPRNSVLINRVVDVLPLFSINGTVRYIEAVGGRSAWTAEADGCIRVRSVPKGTEVRTLEGREGCFCTCILYVESTNAMWTTFSDGFIRVFDFNTHALLSEFIKHDKAIECIWEVEGYVFTGGRDWQIYQWKPDTYVCERRLSGHNNTVRCLCQYAGDTGAVLFSGSDDGTVRAWDPYLPARKGKDGGPMMHIFTGHTQGVLSLELVTVSNQLWSGGEDTTIRVYDLQTLGCVSVLKHHRAPVSSIKLIGIRVWSADKYGKTLLWDPKTLTPLKDLTTHMATDPGSMLSICKVKQLVSWKVWTACSGGKIYCWNADSIPIAFDGPTAGKDAVDVSDAVQLLTENKGLRGEIEKLRRQLMGEAEDGGSSANRGSASVSPSRAKSVPSHPRHHESKMGRGTSPSATPPGKRRSPPAFSAEYANDTPIHERANTASREGDDARGCTTCHERFFYGDAWEFIFRQDTEELCAVIRHEVATVLGIPADQVQITQMELGSAGQGCVVKLNIQHSASLPPSEIDTMLSNYPFIDVYELYGRYLAKKYGDPNEVHVSESGSGTLGGQVHRSLCVDDSRGEEEMANGYDDPTPLQNMINTLLKENEELRGQLMPKAETPPDENNAEVRTALTNYEEERMKPRIAQLEKALAERDETLHRKDERIRQLERELEATKSDTGMKEVMKDLRKREKKLLTEVEALTSQVEAMEEDKRRAEDDASFYRRENELLRNRISAMNEQMAKASGSEAEEMQKVLTSYEEENVKPRIARLEEVIAEKDENLQSRDEKIKKLEDELEAAKQEAKFASGESVKSNGKAGSETETSLLTEVQVLRDQVEAMEEDKRRVEDDASFYRRENELLRNRISAMNEQMAKASGSEAEEMQKVLTSYEEENVKPRIARLEEAVSQRDEVLRSQDERIKELTREIEENRREDKKGSYHVTDEAVVASKEEVQALKNQMKAMKKEKEKLENESKLYRKENESLKERLSETNDQLKKSSPLHEEEKQKVLSRYEEENMKARVARLEEAVTQRDEALRAKSERIRQLEKELRAAHREVKAALEESKKSSSRLHSDSTQTSAEELRSLMTKAREREKEKLKNESKLYRKENESLKERLSETDDQLKKSSSLDEEEKQKVLSRYEEEDVKPRVARLEEAVTQRDEALRAKDERIRQLEKELRAAHREAKSALEDGRRNSSRLHSDSTQTSAEELRSLKTKMDEMENDKRRLNEEIVLLRKENETLKRNLGDVMRRLKNPSSFIASEKQKLLSSYEEEHVKPRITRLEHAVTLRDERLQAKEDRIRQLERELDALRYGGKNDVDNNAVEDGKTFRQLEEALLVEIQGVKDQMRAMAKSNQKMQEEAVCLMRENQMLRDRLAEACEQLGKTPSIEARETSRELVKCEDVSPNPRIAQLEQAVTERDEILHTKDERIRQLERELEMFQHENRAICGNRDCRDAGRKLAAENQELRNLVKYIENDKQKLEHEASFFKHENDALIGRIAELESTPRAPSLSPTKTHTLSGDREALMSRLGTAIEQVHNVQKEREAAERKIAVLQEDCRDLRMRLQHASDTPVRNEALFPSSTNCDGTYQTGLHSGEDAHLIESARGAPHSSSDAIVELLPDRLTALEDTMASLNTGLHDAIRRLSSVSDNSALLRTQIADMLSQRSSHNLITDPHERS
Protein: 5'-deoxyadenosine deaminase (5'-dA deaminase) (EC 3.5.4.41) (5'-methylthioadenosine deaminase) (MTA deaminase) (EC 3.5.4.31) (Adenosine deaminase) (EC 3.5.4.4) (S-adenosylhomocysteine deaminase) (SAH deaminase) (EC 3.5.4.28) (Q8PUQ3)
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Function: Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Interaction partners:
Sequence:
MADIIIKNAYVLTMDPDAGDIKKGTVVIEDGKITEIGVKTKESADTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLQLAEWLEKHIWPAEAQLTAEDVYRGSLLACLEMIRSGTTSFADMYFFMDETAKAVEASGLRASLSHGLIELWNEEKGENDLKEGKRFVRAWQGAAKGRIKTMYGPHAPNTCSDEFLAKVKEAARQDGAGLHIHVLETEAELLAMKERYGKCSVHMLDDIGFFGPDVLAAHCVWLSDGDIEVLREKGVNVSHNPISNMKLASGTAPVYKMLERGVNVSLGTDGCASNNNLDLFEEMKTAALLHKLSTCNPTALPARQVLQMATVNGAKALGTETGMLKTGMKADMIIVDMKKPHLTPCFDVPSHLVYSAGGSDVRTTIVDGKILMQDYRVMVLDEQKVIEEAQKAAEELVARVNS
Protein: Protocadherin alpha-8 (PCDH-alpha-8) (Q9Y5H6)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin alpha-2
Sequence:
MDYHWRGELGSWRLLLLLLLLAAWKVGSGQLHYSVPEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKRHRDLLEVSLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVDVEVKDVNDNPPVFRVKDQKLFVSESRMPDSRFPLEGASDADVGANSVLTYRLSSHDYFMLDVNSKNDENKLVELVLRKSLDREDAPAHHLFLTATDGGKPELTGTVQLLVTVLDVNDNAPTFEQSEYEVRIFENADNGTTVIKLNASDPDEGANGAISYSFNSLVETMVIDHFSIDRNTGEIVIRGNLDFEQENLYKILIDATDKGHPPMAGHCTVLVRILDKNDNVPEIALTSLSLPVREDAQFGTVIALISVNDLDSGANGQVTCSLMPHVPFKLVSTFKNYYSLVLDSALDRERVSAYELVVTARDGGSPSLWATASLSVEVADVNDNAPAFAQPEYTVFVKENNPPGCHIFTVSARDADAQENALVSYSLVERRVGERSLSSYISVHTESGKVYALQPLDHEELELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLEPRVGGTGGAASKLVPRSVGAGHVVAKVRAVDADSGYNAWLSYELQPAASSPRIPFRVGLYTGEISTTRVLDEADSPRHRLLVLVKDHGEPALTATATVLVSLVESGQAPKASSRQSAGVLGPEAALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSALPTEGGCRAGKPTLVCSSAVGSWSYSQQQPQRVCSGEGPPKTDLMAFSPCLPPDLGSVDVGEEQDLNVDHGLKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit) (Q86KI1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity).
Subcellular location: Cell membrane. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-1 complex subunit beta
- Clathrin heavy chain
- AP-4 complex subunit beta
- Epidermal growth factor receptor substrate 15 homolog
- ANTH domain-containing protein
- AP-3 complex subunit beta
- Clathrin light chain
- AP-3 complex subunit mu
Sequence:
MSMNVTNPNIAKTSMRGLTNFISDLRNSPSKENEEKRVTKEMAHIRKEFKENKNIDGYQRRKYVCKLVYMYMLGYELDFGHMEAVTLLSSTKFSEKQIGYIALGILLNEQHEMLPLIINSFKEDLLARSDYFQSLALAAICNIGGKEVAEFLSPLIQKLLIANTSSPMVKKRCALAILRMNRKHIGLVTPDSWVERLVSVLDEPDFGVLTSLMSLLIELASENPIGWEPAIPKVIHLLKKIIINKEFPKEYVYYHVTCPWLQVKLLKFLRYFPAPDDSQGGKVLGEILTAVFAQSESAKAGTVNHKNSLNAVLFEAINLIIHLDNDPVLLKQTSLLLGRFITVKETNIRYLGLEAMSHFASLSNETSIMIKKYQDTVLLSLKDSDISIRRRALDLLYGMCDKNTCKHIVAELLSYLQTADYAIREELVIKIANLAEKFASNYSWYVDVILQLITTAGDFVSDDIWFRVVKIVTNHEDIQAYAASTVFNALQSRNCHETLIKVGGYILGEFGHLIADNPQSSPLVQFNILHSKFNTCGAPTKALLLSTYAKFVNLFPELTQQTQEVFKQHQSYIDAEIQQRACEYLNLTSLNEDLMQTVLDVIPAFIDAKDNSNTTSNTANNSNMINSQDSKISSGGFNQSPQPSQQQQQQQPPQQQQAQLQQNVSSNGLDLLDPFGLGLGNQQQQQQQPVQQAQPVYQQQQQAESFSPVQSDTVSSFGQQQQQQQGGFSSPTIQASSSPISSGGSDPMQIKILASYKRLCLVSEGVLYEDSMLQVGLKSEYQSGQGRLMLYYGNSSAFPLTNFNVTLNSIAGLTLQPQSIAPVIQPKAQLQQPVTFSCTSEFTESPVITINFLTPGKPITITLRLPIVISKFFEPLRLSSGDFFARWKTISGKPLEIQEIFKSTKPIDIQSYNRVIQEGLNITVLKQVDPNPNNIVASCLFPFGSNGQPINSYIRIETNPQANMCRLTIRSQSATLTNTIKNLLISHLQ
Protein: Always early (Q2PNP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRIKPGVASKRTENFTKKPSNISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGNSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0R4IIN0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 6
- HIRA-interacting protein 3.
- PAXIP1-associated glutamate-rich protein 1
- Aspartate beta-hydroxylase domain-containing protein 2
- Seizure-related 6 homolog
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- Double C2-like domain-containing protein alpha isoform X2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- TLC domain-containing 3Ba.
Sequence:
MPSSVRAGSLKDPEVAELFYKEDPEKLFTDLREIGHGSFGAVYFAHDIRTNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTVEYRGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLVYLHSHNMIHRDVKAGNILLTEPGQVKLGDFGSASIVAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPVLQSNHWSDYFRNFVDSCLQKISQDRPTSDVLLKHHFLCRERPVTVVMDLIARTKDAVRELDNLQYRKMKKILFQETHNGPATEGTEEEEDVEQYMLRTGTVNSMESSHSLPSMSISASSQSSSVNSLADGSDDSGEMAMMQEGEHTVTSNSSVLHKALNHDNIYDDPYQPEMDSQQQQQQGPSGGRRRRGRDHFATIRTASLVTRQIQEHEQGSALREQMSGYKRMRRQHQKQLMALENKLKAEMDEHQLRLDKELETQRNNFGSEADKLSKKHQAILEKETKGAIAEEKKFQQHILGQQKKELTSLLESQKRHYRQRKEQLKEELNENQSTPKREKQEWLVQQKECLQQVQAEEEAGLLRRQRQYYELQGRQYKRKMLLSRHNLEQDLLREDLNKKQTLKDLECAMLLRHHESTQELEFRQLALVQRTRADLIRTQHQTELTNQMEYNKRREQELRQKHAVEVRQQPKSLRSKELQIKRQFQDTCKIQTRQYKALRNHLLENTPKSDHKAVLKRLKDEQTRKLAILAEQYDHSINDMLSTQALRLDETQEAEYQVLRMQLQQELELLNAYQSKIKMHTDTQHEREGKDLEQRVSIRRALLEQRIEEEMLALQNERSERIRSLLERQASEIEAFDSESLRLGFSSLALTGIPSEAHPKQGYPSSQTPRPSGHWSHGGGPHPHPRRGPSRAESTSSSSVSHALGLARDGPLHHSSRSSSSSSSSSSSSHHNRHHLPQHYHHQSTPQLYRDREREREREREKEKEWGGGGSRADHPHLFPHHLPSRSSSQSLALLPPPPPAPMLSASSAQSSGSQGVYGGGGGGLVVRGPSLMALRNSPQPLRRTASGGPGAPAGADGVLSRSTSVTSHISNGSHLSYS
Protein: Histocompatibility 2, M region locus 2 (MHC class Ib antigen) (Q6W9L1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- H2-O alpha
- Histocompatibility 2, class II antigen E beta2
- H-2 class II histocompatibility antigen, A-B alpha chain
- Beta-2-microglobulin
- Class II histocompatibility antigen, M alpha chain
- H-2 class II histocompatibility antigen, E-B beta chain
- H-2 class II histocompatibility antigen gamma chain
- Class II histocompatibility antigen, M beta 1 chain
- H2-M beta 2
- Tapasin
Sequence:
METSAFFTLLFTLYLLLGASLALAQTFKGSHSLRYFDIAVSRPGLEETHYMTVGYVDDTEFVHFDNEAENPRFEPRVPWMEQMGQKYWDDQTRIAKAAEQQIRVYFQKLRDYYNQSQNSSHTIQRMTGCYIGPDGHLLHAYRQFGYDGQDYLTLNEDLSTWTAADAAAEITRREWEATNVAEFWRVYLEGPCMVWLFKYLTVGNETLLRTEPPKAYVTHHPRPEGDVTLRCWALGFYPSDIIMIWQRDGEDQTQDMDVIETRPAGDGTFQKWVAVVVPSGKEQNYTCHVAHEGLPEPLTLRWSRPPQSFIFIIIVAVGLVLLGASVATLVMWKKSSGGERGSL
Protein: SET domain-containing protein (Q57Y34)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase complex I subunit
- NADH-ubiquinone oxidoreductase complex I subunit
- Uncharacterized protein
- Adrenodoxin reductase, putative
- NB-ARC domain-containing protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase subunit NI8M
- Uncharacterized protein
Sequence:
MNEQLRVALESVEPQAGSSLQAEEVQSTIRKKEMFAPRIATLAAVAPLAEEELPPAVYRKPKFSFLSDPSERHPPDALSVYEVPNNSPKAPLPMWASSLTSPQLGRQRIRVENWISTDSMGTVPEDHVQDFLAWFREELIKSSQTVLWNMLTDNVDFHLRSQYSRGLVARKPFHKGDMIFAVPLYGALGADSADEFVPSSPAPSVASEGNLTPWSLTINSENLQRHSVAAQRRGVPSYQSVEAIVGQRKSSFDPLPHPLFVDQVHFALLLACERAEGAKSPLFSYLRLLSPFDDDFIRELHLGVLDPATHLEYTDHCGRFSHYLRQIRNRWQQEYESAVCSGAGEVSSVDGSVSPNDGNDVVNARSPIEEGKTQCTTPGRLPPPSMDDLTWALRVVLSRQRLLPLRRHTEHFEDICSEEKVLQKLHLWTRLITKMHMGVMDNIFRVVDRNRVGVNDFQPHTIATIVPIVDMLQHPPGGMSNTSCSIEKISLSNDSNKVANTAGMCKEAVCAVVRANSRIEEGDELTQLYPRCYSVSYTLYRFGFLPLRRRAGDAADAVLRTQR
Protein: Adenosine 5'-monophosphoramidase HINT1 (EC 3.9.1.-) (Desumoylating isopeptidase HINT1) (EC 3.4.22.-) (Histidine triad nucleotide-binding protein 1) (Protein kinase C inhibitor 1) (Protein kinase C-interacting protein 1) (PKCI-1) (P49773)
Organism: Homo sapiens (Human)
Function: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Hydrolyzes adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. Hydrolyzes 3-indolepropionic acyl-adenylate, tryptamine adenosine phosphoramidate monoester and other fluorogenic purine nucleoside tryptamine phosphoramidates in vitro. Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide. In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1. Modulates p53/TP53 levels and p53/TP53-mediated apoptosis. Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex. Also exhibits SUMO-specific isopeptidase activity, deconjugating SUMO1 from RGS17. Deconjugates SUMO1 from RANGAP1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:8812426}. Nucleus {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:9770345}. Note=Interaction with CDK7 leads to a more nuclear localization. {ECO:0000269|PubMed:10958787}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Tripartite motif-containing protein 29
- Cytochrome b-c1 complex subunit 8
- Large ribosomal subunit protein eL27
- Cytochrome c oxidase subunit 7A2, mitochondrial
- Large ribosomal subunit protein eL33
- Adenosine 5'-monophosphoramidase HINT3
- Large ribosomal subunit protein uL22
- Regulator of G-protein signaling 20
- Lysosomal protective protein
Sequence:
MADEIAKAQVARPGGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHISQISVAEDDDESLLGHLMIVGKKCAADLGLNKGYRMVVNEGSDGGQSVYHVHLHVLGGRQMHWPPG
Protein: Membrane-anchored lipid-binding protein LAM6 (Lipid transfer at contact site protein 1) (Lipid transfer protein anchored at membrane contact sites 1) (Q08001)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in regulation of various organellar membrane contact sites. May be involved in sterol transfer between intracellular membranes. Selectively transports sterols between membranes in vitro. Involved in stress-dependent formation of sterol-enriched vacuolar membrane domains.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26001273}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to intracellular puncta representing endoplasmic reticulum-mitochondrion membrane contact sites (ERMES), nucleus-vacuole junctions (NVJ) and vacuole-mitochondria patches (vCLAMP) (PubMed:14562095, PubMed:25987606, PubMed:26001273, PubMed:26119743). Localization to ER-mitochondria contacts is dependent on TOM70/TOM71, and localization to ER-vacuole junctions on VAC8 (PubMed:25987606). {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25987606, ECO:0000269|PubMed:26001273, ECO:0000269|PubMed:26119743}.
Interaction partners:
- Vacuolar protein 8
- Protein TOM71
- Mitochondrial import receptor subunit TOM70
- Mitochondrial distribution and morphology protein 34
- Mitochondrial Rho GTPase 1
- Mitochondrial distribution and morphology protein 10
- Phosphatidylglycerol/phosphatidylinositol transfer protein
- Mitochondrial distribution and morphology protein 12
- Membrane-anchored lipid-binding protein LAM1
- Membrane-anchored lipid-binding protein SIP3
Sequence:
MWGDSMRELGDAMDNELNAVKPVVEEGGMDGARKFIKGKSFQKSSTEHMLISPGRDGSVPLNGLKSSPADPHLSDVNSILDNHRGGGETALTSVNNIIMATSTNGDSDGVDGDAKRPSISNCSSRSSFFDTVLSTFSLKSNSQDTVTNEVKNIEVQFASEEANKKFRQMFKPLAPNTRLITDYFCYFHREFPYQGRIYLSNTHLCFNSTVLNWMAKLQIPLNEIKYLDKVTTNSSAISVETVTNRYTFSGFIARDEVFQLITRVWSKENLTNINDVLEVDERVSKKKGISSTPSSIFNNVSTNAYNDFISTTTTEPTSRASYMSENDMLIEEAIRSVDDYMGTPRASPSSSSSSSSSSSSLGSSTTYYCRPVYRLKPNAPFQYEGPFHVQETMDFPYKPEANNEYVLLERQFSVPPGLLFIMMFNEDNPVFELSFLKTQDSSNISHIGTFEKVNKDGQHYREFQYTKQLHFPVGPKSTNCEVAEILLHCDWERYINVLSITRTPNVPSGTSFSTRTRYMFRWDDQGQGCILKISFWVDWNASSWIKPMVESNCKNGQISATKDLVKLVEEFVEKYVELSKEKADTLKPLPSVTSFGSPRKVAAPELTMVQPESKPEAEAEISEIGSDRWRFNWVNIIILVLLVLNLLYLMKLNKKMDKLTNLMTHKDEVVAHATLLDIPAKVQWSRPRRGDVL