wanglab/gogpt-training-data huggingface dataset:
Protein: Copper-transporting ATPase ccc2 (EC 7.2.2.8) (Cu(2+)-ATPase) (O59666)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone atx1 and incorporates it into trans-Golgi vesicles (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Metal homeostasis factor atx1
- Cytochrome c oxidase copper chaperone
- Metal-binding regulatory protein cuf1
- Iron transport multicopper oxidase fio1
- Copper transport protein ctr4
- Protein sco1
- Rsm22-cox11 tandem protein 2
- Uncharacterized protein C3B8.11
- Superoxide dismutase 1 copper chaperone
- Rsm22-cox11 tandem protein 1
Sequence:
MYTTTLSVQGMTCTSCVASIQSMLEGVEGIEQFTISLLLERAIAVHDPSIISPDQIAEKIEDCGFDASVISSTEGEHGVMANYLLLSPMQAEQWTKVHNHINELQGVLSVNCSSSPDAAIRVIYDSEITGPRSIMKEILSMGVKCTFQPVDSSTSRILSLQRGSQIRVWKIRFIISISFSLAVMFLPQIFDSCDSMRAAFLVPHYFGICAGHIISLVLSLPVQFGVGRVYYSAAYHALKRGTANMDVLVSLGSTVAFAASIFFMILYSARHADNPAPIFFDTADMLLTFVTLGRYLESKAKGSTSAALSQLLSLAPSSATIIEDNEQIEILADLIERGDLILVKPGEIIPVDGTVVEGSSYVDESSVSGEPVPVHKTIDDELLSGTANGNGRLLVKATKSPRESQLAVIVDLVQRAQISHAPIQQFADRVAGIFVPVIVALSISTFTFWFLFTKYSSKYPSVFDDPMGKFAVCLKLTISVVVVACPCALGLSTPTAVMVGTGVGALNGIIIKGGEILERLNQVDTVVFDKTGTLTVGKLSVTDISIVDNLEELLDIPKNIFWAFVKASESSSEHPIGKAITEKASEFTDVSEIGIESFNAVPGEGVDVVLRWKERTFHALLGNSLLLEHNNVSIPDDFDSKLKLSSSSGLTCVRIAIDGQFVGFLGCMDQVRPDSYQTVSALKQLGKKVCLLTGDQKATARRVAQGLEIDFSDVYAEAVPSQKAEIIQKLKDQKHCVAMVGDGINDSPSLVLADVGIAPINGSGIALESADVILVRKGVLLDTAVSFDLSRVIVKRIKMNLVWACIYNFVMIPIAMGFFLPWGIYLNPMWASAAMMFSSLSVLASSLLLRRWKKPKSLIFSEADDVETESSTNSSVLQKVYTATRSIFGRNKSSNKYQPVANEV
Protein: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC 5.3.1.16) (5-proFAR isomerase) (Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase) (Q10184)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Imidazole glycerol phosphate synthase hisHF
- Histidine biosynthesis bifunctional protein his7
- Histidinol dehydrogenase
- Imidazoleglycerol-phosphate dehydratase
- ATP phosphoribosyltransferase
- Histidinol-phosphate aminotransferase
- Multifunctional tryptophan biosynthesis protein
- ATP-dependent helicase rhp16
- Tryptophan synthase
- Anthranilate phosphoribosyltransferase
Sequence:
MEKSQHTLFRPCIDIHQGQVKQIVGGTLGNDADVKTNYVSLKPSSYYAELYKLNHLEGAHVIMLGPNCEEAAKTALHTWPGALQIGGGINISNAQNWLQEGASKVIVTSWLFPDAQFDLDRLKAISSKIGKDRLVVDVSCRRKDNRWFAAINKWQVMTAFELNEENLDLLSQYCSEFLIHAADVEGLCKGIDEDLVIKLGEWVKIPTTYAGGGRSIEDLDLVDKLSKGKVDLTIGSALDIFGGVLEFTRVVAWNRRFTPLPLQD
Protein: At1g35210 (Q8GY45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTQIDEEMASLSTSLLGIRRGSSNKNKAEDKTKNAVFCKKHPKHRQSPGVCSLCLNERLSLFIKAASSRRPRSRQILSTSSSTTSSLSSDGSSSVSSCPSPIVDRRRYLLMSGGSGRGEKVISWMTKSRSVAYKVDDEKRRKKKTKTNSGFFFGLVMGTKKRQ
Protein: At5g63130 (Octicosapeptide/Phox/Bem1p family protein) (Q9FML0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pyrroline-5-carboxylate reductase
- C2 and GRAM domain-containing protein At5g50170
- Plant intracellular Ras-group-related LRR protein 9
- Gag-Pol-related retrotransposon family protein
- Gag-Pol-related retrotransposon family protein
- Helicase with zinc finger protein
- Uncharacterized mitochondrial protein AtMg00300
- Probable long-chain-alcohol O-fatty-acyltransferase 5
- Uncharacterized mitochondrial protein AtMg00750
- General transcription and DNA repair factor IIH subunit TFB1-3
Sequence:
MVAVDYTEKNSGSSLKFLCSYGGRILPRSTDGKLRYVGGHTRVLSVDRSISFSELMKKLYEFCGYSVDLRCQLPNGDLETLISVKSEEELAEIVEEYDRICGAKIRAVLSPPRSSHKTESSPSSSGDRSPKSPFSVTPSPPNSPSPAYGRYLQSRYCLPSTDLPPRRYIQRAEESHCCYACRVHKDSRLVWH
Protein: Hepatocyte nuclear factor 4-gamma (HNF-4-gamma) (Nuclear receptor subfamily 2 group A member 2) (Q9WUU6)
Organism: Mus musculus (Mouse)
Function: Transcription factor. Has a lower transcription activation potential than HNF4-alpha (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
Sequence:
MNTTDSGVNCLCAICGDRATGKHYGASSCDGCKGFFRRSIRKSHVYSCRFSRQCVVDKDKRNQCRYCRLRKCFRAGMKKEAVQNERDRISTRRSTYEGSNIPSINTLAQAEVRSCQISVPSPSSSTDINIKKIASISDVCESMKQQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGATKRSMMYKDILLLGNHYVIHRNSCEVEVSRVANRVLDELVRPFQEIQIDDNEYACLKAIVFFDPDAKGLSDPVKIKNMRFQVQISLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFVKLFGMVKIDNLLQEMLLGGAANDGSHLHHPMHPHLSQDPLTGQTILLGPMSTLVHTDQIATPETPLPSPPQGSGQEPYKITANQASVISHQSLSKQKQL
Protein: Uncharacterized protein (Q38E19)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLQTTLIQSIKEVNPCIVLFASVVQVAFAALWYKLIVKTIVDYHLAADKGVRRVEHILQRYPPYVHWIVTLLSACFRIVFIATIVGICKGNSLHDYQNAALLVAGISCVSQHLSIQHQRPLPLLAADVGYEVIAALLASLTYYAIMTVNVF
Protein: Ganglioside-induced differentiation-associated protein 1 (GDAP1) (Q8TB36)
Organism: Homo sapiens (Human)
Function: Regulates the mitochondrial network by promoting mitochondrial fission.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:15772096, ECO:0000269|PubMed:16172208, ECO:0000269|PubMed:16857173}; Multi-pass membrane protein {ECO:0000269|PubMed:16172208}. Cytoplasm {ECO:0000250|UniProtKB:O88741}.
Interaction partners:
- Mitofusin-2
- Mitofusin-1
- Mitochondrial fission 1 protein
- mRNA cap guanine-N
- Myelin P2 protein
- Myelin protein zero-like protein 1
- SH3 domain and tetratricopeptide repeat-containing protein 2
- Ras-related protein Rab-6B
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Myotubularin-related protein 13
Sequence:
MAERQEEQRGSPPLRAEGKADAEVKLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSTGEVPVLIHGENIICEATQIIDYLEQTFLDERTPRLMPDKESMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGQQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGNGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVLGTTLVVGLLAGVGYFAFMLFRKRLGSMILAFRPRPNYF
Protein: Cornifin-A (19 kDa pancornulin) (SPRK) (Small proline-rich protein IA) (SPR-IA) (P35321)
Organism: Homo sapiens (Human)
Function: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.
Subcellular location: Cytoplasm.
Interaction partners:
- Cornifin-B
- Involucrin
- Small proline-rich protein 2A
- Loricrin
- Small proline-rich protein 3
- Late cornified envelope protein 3D
- Trichohyalin
- Filaggrin
- Small proline-rich protein 2E
- Small proline-rich protein 2D
Sequence:
MNSQQQKQPCTPPPQPQQQQVKQPCQPPPQEPCIPKTKEPCHPKVPEPCHPKVPEPCQPKVPEPCQPKVPEPCPSTVTPAPAQQKTKQK
Protein: Ankyrin 1 (A0A8I5ZS64)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAERPRRSGSDPAADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTSMVKLLLENDASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVQLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGTAHISLTGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKPMKYEDAQHILCHLNVTMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPDRRHGDREYSLSPSQVNGYSSLQDELLSPASLHYALPSPLCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSSGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKSQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTVDWYKQGSAASYPQEAAQSSWQEEVTQGPQSFQRRITTIQGPEPGTLQEYEQVVVSTREHVQRGPPESDSPKAGKDPSLWASESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: L-erythrulose 1-kinase (EC 2.7.1.209) (A0R758)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Kinase that has a preference for L-erythrulose, producing L-erythrulose-1P. Involved in the degradation pathway of L-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source. Is also able to phosphorylate D-erythrulose and dihydroxyacetone in vitro.
Interaction partners:
- Phosphocarrier protein HPr
- D-erythrulose-4-phosphate isomerase 2
- L-erythrulose-1-phosphate isomerase
- AP endonuclease, family protein 2
Sequence:
MTYLLNSPDDFADEAVRGLVAANPDLLTEVPGGVVRSTETPKGQPALVIGGGSGHYPAFAGWVGPGMGHGAPCGNIFSSPSASEVYSVVRNAENGGGVILGFGNYAGDVLHFGLAAEKLRHEGIDVRIVTVSDDIASNSPENHRDRRGVAGDLPVFKIAGAAIEAGADLDEAERVAWKANDATRSFGLAFEGCTLPGATEPLFHVEKGWMGVGLGIHGEPGVRDNRLGTAAEVADMLFDEVTAEEPPRGENGYDGRVAVILNGLGTVKYEELFVVYGRIAERLAQQGFTVVRPEVGEFVTSLDMAGVSLTMVFLDDELERLWTAPVETPAYRRGAMPAVDRTPRTTTWDAAETTIPEASEGSRECARNIVAVLETFQQVCADNEAELGRIDAVAGDGDHGQGMSFGSRGAAQAARDAVDRNAGARTTLLLAGQAWADAAGGTSGALWGAALTSAGGVFSDTDGADEQAAVDAICAGIDAILRLGGAQPGDKTMVDAAVPFRDALVKAFDTQAGPAITSAARVAREAAEKTADITARRGRARVLGEKSVGTPDPGALSFAMLMKALGEHLTR
Protein: Phospholipid-transporting ATPase IH (EC 7.6.2.1) (ATPase IS) (ATPase class VI type 11A) (P4-ATPase flippase complex alpha subunit ATP11A) (P98197)
Organism: Mus musculus (Mouse)
Function: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (By similarity). Does not show flippase activity toward phosphatidylcholine (PC) (By similarity). Contributes to the maintenance of membrane lipid asymmetry with a specific role in morphogenesis of muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho GTPases signal transduction, subsequently leading to the assembly of cortical actomyosin fibers and myotube formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29799007}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000250|UniProtKB:P98196}. Recycling endosome {ECO:0000250|UniProtKB:P98196}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P98196}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. {ECO:0000250|UniProtKB:P98196}.
Interaction partners:
- Cell cycle control protein 50A
- Cell cycle control protein 50B
- Phospholipid-transporting ATPase IF
- Phospholipid-transporting ATPase VA
- Phospholipid-transporting ATPase IB
- Phospholipid-transporting ATPase IA
- Cell cycle control protein 50C
- Phospholipid-transporting ATPase VB
- Phospholipid-transporting ATPase ID
- Phospholipid-transporting ATPase IC
Sequence:
MDCSLLRTLVRRYCAGEENWVDSRTIYVGHKEPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRIANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRADGTCHVTTASLDGESSHKTHYAVQDTKGFHTEADVDSLHATIECEQPQPDLYKFVGRINVYNDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNTFLIVYLCILVSKALINTVLKYVWQSEPFRDEPWYNEKTESERQRNLFLRAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEEMGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMAFKECCIEGHVYVPHVICNGQVLPDSSGIDMIDSSPGVCGREREELFFRAICLCHTVQVKDDHCGDDVDGPQKSPDAKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENDIERFELLEVLTFDSVRRRMSVIVKSTTGEIYLFCKGADSSIFPRVIEGKVDQVRSRVERNAVEGLRTLCVAYKRLEPEQYEDACRLLQSAKVALQDREKKLAEAYEQIEKDLVLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETASATCYACKLFRRSTQLLELTTKKLEEQSLHDVLFDLSKTVLRCSGSMTRDSFSGLSTDMHDYGLIIDGAALSLIMKPREDGSSSGNYRELFLEICRNCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDIAKNALLRWRVFIYWTFLGVFDALVFFFGAYFIFENTTVTINGQMFGNWTFGTLVFTVMVLTVTLKLALDTHYWTWINHFVIWGSLLFYIAFSLLWGGVIWPFLSYQRMYYVFISMLSSGPAWLGIILLVTVGLLPDVLKKVLCRQLWPTATERTQNIQHQDSISEFTPLASLPSWGAQGSRLLAAQCSSPSGRVVCSRWESEECPVLPLHPGLPHKARYGCCRSSLEMPT
Protein: Proteinase-activated receptor 4 (PAR-4) (Coagulation factor II receptor-like 3) (Thrombin receptor-like 3) (Q96RI0)
Organism: Homo sapiens (Human)
Function: Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prothrombin
- Proteinase-activated receptor 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Proteinase-activated receptor 3
- Angiotensinogen
- Guanine nucleotide-binding protein G
- Cathepsin G
- Aryl hydrocarbon receptor repressor
- Guanine nucleotide-binding protein G
Sequence:
MWGRLLLWPLVLGFSLSGGTQTPSVYDESGSTGGGDDSTPSILPAPRGYPGQVCANDSDTLELPDSSRALLLGWVPTRLVPALYGLVLVVGLPANGLALWVLATQAPRLPSTMLLMNLAAADLLLALALPPRIAYHLRGQRWPFGEAACRLATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGRRLALGLCMAAWLMAAALALPLTLQRQTFRLARSDRVLCHDALPLDAQASHWQPAFTCLALLGCFLPLLAMLLCYGATLHTLAASGRRYGHALRLTAVVLASAVAFFVPSNLLLLLHYSDPSPSAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSAEFRDKVRAGLFQRSPGDTVASKASAEGGSRGMGTHSSLLQ
Protein: Uncharacterized protein (Q38EM4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLATQTKTWVAGAATKAQQPCVRRGSTLATPSSPLWYNPLCVACRLQASDQFHRYLHNPHIVQPDGIDSLPRTKGDQQQWLNVEQWDGYSDTYLKQHMQYPPTNEHPNNHLNFSHNLLSECLRSCYEYYGKPADQLQRLHEDPLHPHFHQMIAGIKKDREKIAEELDRVYANLHPTVKTVYDAYLVRRYYQLGDWIERVEQKRHDLLCQLSPEYIRQAERARGVAAHFLSRLKQLQSAFTHNPTLGLLDDAMEGQYTHDELVMLRQKAAYFRNMRQLGANQQDADVHTH
Protein: UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) (Squashed vulva protein 4) (Q19905)
Organism: Caenorhabditis elegans
Function: Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.
Interaction partners:
- UDP-glucuronate decarboxylase
- dTDP-D-glucose 4,6-dehydratase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- UDP-glucose 4-epimerase
- UTP--glucose-1-phosphate uridylyltransferase
- dTDP-D-glucose 4,6-dehydratase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- Putative UDP-glucuronosyltransferase ugt-48
Sequence:
MTDQVFGKVSKVVCVGAGYVGGPTCAMIAHKCPHITVTVVDMNTAKIAEWNSDKLPIYEPGLDEIVFAARGRNLFFSSDIPKAIAEADLIFISVNTPTKMYGRGKGMAPDLKYVESVSRTIAQYAGGPKIVVEKSTVPVKAAESIGCILREAQKNNENLKFQVLSNPEFLAEGTAMKDLANPDRVLIGGESSPEGLQAVAELVRIYENWVPRNRIITTNTWSSELSKLVANAFLAQRISSINSISAVCEATGAEISEVAHAVGYDTRIGSKFLQASVGFGGSCFQKDVLSLVYLCESLNLPQVADYWQGVININNWQRRRFADKIIAELFNTVTDKKIAIFGFAFKKNTGDTRESSAIHVIKHLMEEHAKLSVYDPKVQKSQMLNDLASVTSAQDVERLITVESDPYAAARGAHAIVVLTEWDEFVELNYSQIHNDMQHPAAIFDGRLILDQKALREIGFRTFAIGTSPDQAYNLFGTAGY
Protein: Protein chibby homolog 1 (Cytosolic leucine-rich protein) (PIGEA-14) (PKD2 interactor, Golgi and endoplasmic reticulum-associated 1) (Q9D1C2)
Organism: Mus musculus (Mouse)
Function: Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q9Y3M2}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9Y3M2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y3M2}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y3M2}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9Y3M2}.
Interaction partners:
- Catenin beta-1
- 14-3-3 protein zeta/delta
- Exportin-1
- CBY1-interacting BAR domain-containing protein 1
Sequence:
MPLFGSIFSPKKTPPRKSASLSNLHSLDRSTRELELGLDYGTPTMNLAGQSLKFENGQWVADSVISGGVDRRETQRLRKRNQQLEEENNLLRLKVDILLDMLSETTAESHLKDKELDELKVTNRRRK
Protein: Ent-kaurene synthase 1, chloroplastic (IeKS1) (EC 4.2.3.19) (A0A3G1QTS7)
Organism: Isodon eriocalyx (Plectranthus eriocalyx)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-kaurene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLLLSNSVLVGPKFRSSRISHASASLDIGLQRATSPQNASVPTCFEETKGRIAKLFHKNELSVSTYDTAWVAMVPSPTSSEEPCFPACLNWLLENQCHDGSWARPHHHHMLKKDVLSSTLACILALKKWGVGEEQINRGLHFVELNFASATEKGQITPMGFDIIFPAMLDNARGLSLNLQLEPTMLNDLIYKRDLELKRCNQSNSAEKEVYWAHIAEGMGKLHDWESVMKYQRKNGSLFNCPSTTAAAFTALRNSDCLNYLCLALEKFGSAVPAVYPLDIYSQLCTVGNLERLGISRYFLTEIQSVLDETYRSWLQGDEEIFMDASTCALAFRTLRMNGYNVTSDPITKILQECFSSSFRGNMTDNNTTLEIYRASELILYPEERDLVQHNLRLKTFLEQELSSNGFIQSCQLGRNINAEVNQAIEYPFYAIMDRMAKRKNIENYNIDNTRILKTSYRSPNFGNKDFLSLSVEDFNRCQVIHREELRELERWVIENRLDELKFARSKAAYCYFSAAATIFSPELSDARMSWAKNGVLTTVVDDFFDVGGSVEELKNLIQLVELWDVDVSTQCCSPNVQIIFSALKHTICEIADKGFKLQGRSITDHIISIWLDLLYSMMKETELGIDKSFPTMDEYMSNAYVSFALGPIVLPALYLVGPKLSEEMVNHSEYHTLFKLMSTCGRLLNDIRGYERELKDGKISAVSLYIMNNGGEITTEAAISEMRSWIERDRRELLRLVLEENKSVLPKACKKLFWHMCTVVHVFYSKDDGFTSLNLHGVVNAIINEPIVLNQF
Protein: DNA-directed RNA polymerase III subunit rpc4 (RNA polymerase III subunit C4) (RNA polymerase III subunit C53) (O74857)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Essential for tRNA synthesis. The RPC53/RPC4-RPC37/RPC5 subcomplex is required for terminator recognition and reinitiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-directed RNA polymerase III subunit rpc9
- DNA-directed RNA polymerases I and III subunit RPAC2
- Probable DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerase III subunit rpc3
- DNA-directed RNA polymerase III subunit rpc5
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase III subunit rpc31
- DNA-directed RNA polymerase III subunit rpc8
- DNA-directed RNA polymerase III subunit rpc1
Sequence:
MRKFTPKFVPRRKNGPVEEKDVDERVKIEFDVESQKKWKASRPKPEIKLTASGPFALGPNASSSGTGRPIGSVYVPPPNVKNEEKDDALSKLAASSGHDEGHDEDMVDILKLRELNGQEQGKTDIGGKDLLVPIITDRMLPESNDEKLKHHAESAIHTTVINKEDEEQERVALDLQSLAQHLGLTEQEGMEDHFKDQMVLMQFPDKLPRFMGDADVDPVWPSSEVKEEEAGEKTDVEEKKDPDKHGRENGNIDDLTSLPYPAFHPPAGQIGVLRVHQSGKTTLEMGGVNFVVQSGSDCLFLQEIAVVDYDSKRIWNLGSFERRMIVSPDF
Protein: CAP, isoform F (A1Z869)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MFAPKFKARAPPGSGVWTPYGSSGDLNQSGATSATPPPPPPPSLPVWTPQPSPVLSGRKEFRPVRFESPTLPRRYTAQQQQKTTTTIPPWSSAENGEGGPPPTAPASLNSVNSNSDYAETDCSGHFGPVAPSASVSDKIRTFERSSSNSELQRPFVRRQLSDASRPAYRPNEVIYKVKHEYMSEPETGSDRPRKMAQLGRRQYDGIGPVTNDGMPIILRSEVKEPHQHEWYKRLYQTIHKQKNGDDFVIRYKCPRARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Oligodendrocyte transcription factor 3 (Oligo3) (Class B basic helix-loop-helix protein 7) (bHLHb7) (Class E basic helix-loop-helix protein 20) (bHLHe20) (Q7RTU3)
Organism: Homo sapiens (Human)
Function: May determine the distinct specification program of class A neurons in the dorsal part of the spinal cord and suppress specification of class B neurons.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Tumor necrosis factor alpha-induced protein 3
Sequence:
MNSDSSSVSSRASSPDMDEMYLRDHHHRHHHHQESRLNSVSSTQGDMMQKMPGESLSRAGAKAAGESSKYKIKKQLSEQDLQQLRLKINGRERKRMHDLNLAMDGLREVMPYAHGPSVRKLSKIATLLLARNYILMLTSSLEEMKRLVGEIYGGHHSAFHCGTVGHSAGHPAHAANSVHPVHPILGGALSSGNASSPLSAASLPAIGTIRPPHSLLKAPSTPPALQLGSGFQHWAGLPCPCTICQMPPPPHLSALSTANMARLSAESKDLLK
Protein: 26S proteasome non-ATPase regulatory subunit 10 (26S proteasome regulatory subunit p28) (Gankyrin) (Q9Z2X2)
Organism: Mus musculus (Mouse)
Function: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module (By similarity). Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 8
- 26S proteasome regulatory subunit 4
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 6A
Sequence:
MEGCVSNIMICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLGLILKRLAESEEASM
Protein: Aromatic amino acid aminotransferase C1773.13 (EC 2.6.1.57) (O94570)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has aromatic amino acid transaminase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Tryptophan synthase
- Aspartate aminotransferase, mitochondrial
- Putative prephenate dehydratase
- Probable prephenate dehydrogenase [NADP
- Aspartate aminotransferase, cytoplasmic
- Chorismate mutase
- Homoisocitrate dehydrogenase
- L-2-aminoadipate reductase
- Multifunctional tryptophan biosynthesis protein
- Chorismate synthase
Sequence:
MIRNSEDFSHHLSRESKAREKGPFQMLGRIKSSTGIDAISFSSGLPHPNKFAIRELSIKFPQLGCFKEENGTYAKEVNVTFNIKADPSEGLLNFSQSLQYGQCQGISELVGFIKEHIRRIHAPRYENWDIKMSNGNTSGLEYCLRLLVNYGDHVLTEKYTYPAAITAMRALGVQFVSVDMDSEGMLPESLEEIMRDWDISLGPRPHVLYTVPTGQNPTGSTLSLSRRKKLLALARKYDIIIVEDEPYYFLQMEDYNGSLNPAQQKCDGSTFLKSLVPSLLSLDTEGRVLRLDSFSKLIAPGTRLGYITGNSMFIDHITRIAEVCTESPSGICQSVLYAMLHNWGQEGFCAWLQELQYSYTVRRNAFLNVANKYLPNSVCIYHVPRAGLFLWVELNLNHYRFSDTKKSVSQIEMEIFLALVEKGVKTVCGQFFMANPERSTKIFFRFAYSIADFEDFEEGIKRFTSVINEHFNVESRVRICP