wanglab/gogpt-training-data huggingface dataset:
Protein: N-terminal kinase-like protein (Coated vesicle-associated kinase of 90 kDa) (SCY1-like protein 1) (Telomerase regulation-associated protein) (Telomerase transcriptional element-interacting factor) (Teratoma-associated tyrosine kinase) (Q96KG9)
Organism: Homo sapiens (Human)
Function: Regulates COPI-mediated retrograde protein traffic at the interface between the Golgi apparatus and the endoplasmic reticulum. Involved in the maintenance of the Golgi apparatus morphology. Has no detectable kinase activity in vitro.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18556652}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:18556652}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18556652}. Note=Localized to the Endoplasmic reticulum-Golgi intermediate and cis-Golgi in an ARF1-independent manner.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Note=Cytoplasmic throughout the cell cycle.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Cytoplasmic throughout the cell cycle.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic during interphase and centrosomal during mitosis, it localizes to the centrosomes in a microtubule-independent manner.; SUBCELLULAR LOCATION: [Isoform 6]: Nucleus {ECO:0000269|PubMed:15504359}.
Interaction partners:
- RAB6-interacting golgin
- Coatomer subunit gamma-2
- Coatomer subunit alpha
- Coatomer subunit beta'
- Coatomer subunit delta
- Coatomer subunit zeta-1
- Coatomer subunit epsilon
- Divergent protein kinase domain 2A
- Coatomer subunit zeta-2
- Transmembrane emp24 domain-containing protein 7
Sequence:
MWFFARDPVRDFPFELIPEPPEGGLPGPWALHRGRKKATGSPVSIFVYDVKPGAEEQTQVAKAAFKRFKTLRHPNILAYIDGLETEKCLHVVTEAVTPLGIYLKARVEAGGLKELEISWGLHQIVKALSFLVNDCSLIHNNVCMAAVFVDRAGEWKLGGLDYMYSAQGNGGGPPRKGIPELEQYDPPELADSSGRVVREKWSADMWRLGCLIWEVFNGPLPRAAALRNPGKIPKTLVPHYCELVGANPKVRPNPARFLQNCRAPGGFMSNRFVETNLFLEEIQIKEPAEKQKFFQELSKSLDAFPEDFCRHKVLPQLLTAFEFGNAGAVVLTPLFKVGKFLSAEEYQQKIIPVVVKMFSSTDRAMRIRLLQQMEQFIQYLDEPTVNTQIFPHVVHGFLDTNPAIREQTVKSMLLLAPKLNEANLNVELMKHFARLQAKDEQGPIRCNTTVCLGKIGSYLSASTRHRVLTSAFSRATRDPFAPSRVAGVLGFAATHNLYSMNDCAQKILPVLCGLTVDPEKSVRDQAFKAIRSFLSKLESVSEDPTQLEEVEKDVHAASSPGMGGAAASWAGWAVTGVSSLTSKLIRSHPTTAPTETNIPQRPTPEGVPAPAPTPVPATPTTSGHWETQEEDKDTAEDSSTADRWDDEDWGSLEQEAESVLAQQDDWSTGGQVSRASQVSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDGTRLASEYNWGGPESSDKGDPFATLSARPSTQPRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPMKLGARKLD
Protein: Methyl-CpG-binding domain protein 6 (X1WFM6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Host cell factor C1b.
- ASXL transcriptional regulator 2.
Sequence:
MTGGSESVAGEKDGGTTLIAQVPVGWRRKVEDGAVSYISPSGTVLQSVDEVRVYLRTDGTCKCGLECPLVPNKVFNFDPAAMVQAPGHQSGKVEEDMTKLCNHRRKVDAMTALCQSMHPSHLAPLAQATGGVVCSVDGRESRGSMLTHGDGAHCTYPQPRHSQPKPNMGFPLSSSRSVLQNGSVNLSPISRPPDQGSPLKKSQAPVYAKQQWSPHPPLIQNTPQRTAHNPTSPNNVKPTQAHPPDSINSFSFSSSLSNRTIPPMSQGASVKSPSPLSPSRTRDSFSPHQRSRHSSTSSLSDHQIFIQGAKPLHPTMPCSSPKLPNAPLSPCSRLEGILQHYKDCSTSSSISTSANQSIHQASLVALPNASDKRNGAMLGQILNQKQKSHINNSFPASSLLSAAAKAQLANQKTEGLSALPLAGLDKEQQSKVLISTLNSSVHNTSSRPQALTALLLPHSPASPSEKNLRRKRQRRSPTVLSMLKDTQLGRTVLDLSSPPQLIPPCSSPPVHNSSDNLRLPVNPPNCRLQDSEECKKPGIANSLPSASPSQPLSALLHLLSMQNANQQCIGAKPGNMHANTSPRPITPLTPQGDGQSVLRIHNPQPQSTTPTLDPQQPASQAFPIMGDETTANLKAASSNTILNLSQPHVGTTTPDLSGSIISMINQMSSNSCLPTFAEKVCGSKMTEAYPEHSTYQINQPNHSPDVEDKGPVETIDSDTRLLAGCEPDHGLSLSTAPTSDLTNPATDPAISLPLAEAFPFMTQEQLLQLLSSNAGLPSLLPPFLGSLPLGLWTGSQPSTPGSNQSQHPPIGNQGSPLNLLNQAELPLNLLSLLNPAGSAAALPPVAGVETGEKPPGLQALLMASLLLGQNPAAMLPLPALNLELPTPPQQVFADGVSLEKPPALLDSVLMGPGLLEALQTLAPGADGQSLLLSAPLAAPPPAFLSLNPALLAAALAQTEPLPNHTPSPPPHSQGTLSSPALVSTSVSCGPLVSAGPEVCDPLAEQDKNSQTHHFLSPLLAPGVLGDLAALGNINSLHGLLGAGPLLLPQGVPLTQNQTTLNPLTCLQLTMAPALMGEKPVALHETPPPQDAAAPPHDSLSQQREAPGLFDPYGSFMDTIYTSFLQVSERGSDSNPLTFPALLQQASAPPSLSPRRACSVHNPDLSRLGPDVAQSPARGTPKPSGDSPPPPCRPAGAHALTVEEAKTHTSKHCVFSNGLRSEGGEEEEEEDEDEDAGVQEYLSPTQRTSRDEDEDISHAEQIRAEDVHTGSRRGRKRKQTLQMGSDLPGGIDSIIEEPSASAILVSRSSRSSRGKRRRVLR
Protein: Protein WVD2-like 1 (AtWDL1) (Q8GYX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Microtubule-associated protein (MAP) that regulates the orientation of interphase cortical microtubules. Modulates both rotational polarity and anisotropic cell expansion during organ growth. Promotes clockwise root and etiolated hypocotyls coiling, clockwise leaf curling, but left-handed petiole twisting.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17319849}.
Interaction partners:
- GDSL esterase/lipase 2
- Protein TPX2
- GDSL esterase/lipase 1
- GDSL esterase/lipase CPRD49
- Alpha-L-fucosidase 3
- GDSL esterase/lipase At1g28670
- GDSL esterase/lipase LTL1
Sequence:
MGREVVEVLMDRNADVSSARVHVAPKIAAEETDEEFEVKECTEEKSLSENAPNVGSAERVGAQKSPKTRNGNAKVSKQDAPLLAVRKPLQPENKKHIDDEDNCSIASSVATSMRMGKSGLTYGSAPTFRSAQRAEKRKEYYQKLEEKNQALEAERNELEQRQKDEQEAALKQLRKNLKFKAKPVPNFYYEAPPAKPELKKLPLTRPKSPKLILSRRKSFSDAVSSSSREEILKTVSNRNRHSTGTVQNKDDDHRNKNTNAAHDSPRVRSGKGKSGLKPVNESSEEA
Protein: Neuropeptide-like protein 7 (Q19569)
Organism: Caenorhabditis elegans
Function: May regulate lifespan in response to food availability and oxidative stress.
Interaction partners:
- Acetylcholine receptor-like protein cup-4
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- FMRFamide-like neuropeptides 11
Sequence:
MYIKAALLIVVLFGVASQITSALYLKQADFDDPRMFTSSFGKRSAIESEPQAYPKSYRAIRIQRRSMDDLDDPRLMTMSFGKRMILPSLADLHRYTMYDKRGSDIDDPRYFLFSNRLTCRC
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9W3N8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cell division cycle protein 27 homolog
- Cell division cycle 16
- Shattered
- Fizzy-related protein homolog
- Anaphase-promoting complex subunit 4
- Cyclosome subunit 8
Sequence:
MSGEESAGMDFSQKTLQDYEVLAVMGNGSFGTCYKVRDKSTGELFAWKGMNYDELDEAKCDALVSEISVLRQLQHPNIVQYYHHLVNREAKSVYIVMECCAGGDLAQIVQRARSQRQRFEEPYIWRVLFQLCRALQVCHNKIPNGTILHRDIKPANIFLDAAGNAKLGDFGLARMLRRDQSFAASFVGTPHYMSPELVKGRKYDRKSDVWAVGCLVYEMCALRPPFRGRAFDQLSEKIAQGEFSRIPAIYSTDLQEIIAFMLAVDHEQRPGIEVIIRHPLVVRNISELDGKFPILVDSGEDFYTLPSGARLFEDEEEDGVHPELSSTMFTEQYSFNEGYGQRRLSVTGVFTPDLRSELFYSAKRKIFPAKKLQLSDPSLYESIRREERAEERQVELAEERRRKKDQEQQKRDQELLKEAPSSPRALTQNIFDEVLKTRLHAIRAQESLLQQKLEELQTREQELQLAEQRVQTLERQMQEKLLQQEKHTCSCRQPIAPPIPPRKPAKSHHDDTYCTIELNETSPTVAKLNLATLPAPKSLNTLRKVTFKSPQKFVTYGIENMPPPAVKPAVNPPPTGVPMQMSVSSNDSGDSQASSTRRKSILSLFGLSRGSKATSKSLPSVNQVAQAAATRVQRPPLAVKPPITQEQPAEVPPVANLWTKEQKKQAFELLAAMNAAEREASGGGVVGSGPGGARRQHLRQSVRERNSTLQRNRMRRSLVVATGHQKLTTRDQMVI
Protein: Major fimbrial subunit of aggregative adherence fimbria II (D3H539)
Organism: Escherichia coli O44:H18 (strain 042 / EAEC)
Interaction partners:
Sequence:
MKKIRMFVIATLLSSGAAINATAVAKTATSTITVVNNCDITITPATNRDVNVDRSANIDLSFTIRQPQRCADAGMRIKAWGEGNHGQLLIKPQGGNKSAGFTLASPRFSYIPNNPTNIMNGFVLTNPGVYQLGMQGSITPAMPLRPGIYEVVLNAELVTN
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (C3U1W4)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
Sequence:
KRSLLVRRLWRSRAPGGGEEETGDGGAPAEPRPHSCGGGGRGCCPAKPPRGGGRGAAEGELKALTHAVLKRCKERQLEGLLRAVESRGAARTPCVLLPARGEARLGAQRDALPALLCRVFRWPELRHGAPLKRLRGCCQADGAAPTELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTAGCPDSVPSSTETGGTNCLAPGGLSDSQVLQESGDHSHWCVVAYWEEKTRVGRLYSVQEPSLDIFYDLPQGNGFCLGQLNSDNRSQLVQKVRSKIGYGIQLTKEVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNNR
Protein: Steryl-sulfatase (EC 3.1.6.2) (Arylsulfatase C) (ASC) (Steroid sulfatase) (Steryl-sulfate sulfohydrolase) (P15589)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of sulfated steroid precursors, such as dehydroepiandrosterone sulfate (DHEA-S) and estrone sulfate to the free steroid.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P08842}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08842}; Multi-pass membrane protein {ECO:0000305}. Note=The sequence shows several membrane-spanning domains that could serve to anchor the protein in the microsomal membrane.
Interaction partners:
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Sulfotransferase 2B1
- Aldo-keto reductase family 1 member C15
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Cholesterol side-chain cleavage enzyme, mitochondrial
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Steroid 21-hydroxylase
- Cytochrome P450 2E1
- Cytochrome P450 7A1
- 25-hydroxycholesterol 7-alpha-hydroxylase
Sequence:
MLWPCLLALLLSQLNFLCAARPGPGPNFLLIMADDLGIGDLGCYGNRTLRTPHIDRLALEGVKLTQHLAAAPLCTPSRAAFLTGRYPVRSGMASHGRLGVFLFSASSGGLPPNEVTFAKLLKGQGYTTGLVGKWHLGLSCQAASDFCHHPGRHGFDRFLGTPTTNLRDCKPGGGTVFGSAQQVFVVLPMNILGAVLLAMALARWAGLARPPGWVFGVTVAAMAAVGGAYVAFLYHFRPANCFLMADFTITQQPTDYKGLTQRLASEAGDFLRRNRDTPFLLFLSFMHVHTAHFANPEFAGQSLHGAYGDAVEEMDWAVGQVLATLDKLGLANNTLVYLTSDHGAHVEELGPNGERHGGSNGIYRGGKANTWEGGIRVPGLVRWPGVIVPGQEVEEPTSNMDVFPTVARLAGAELPTDRVIDGRDLMPLLLGHVQHSEHEFLFHYCNAYLSAVAWRPHNSSSVWKAFYFTPNFDPPGSNGCFSTHVCMCHGHHVTHHDPPLLFDIARDPRERHPLTPETEPRHGEILRNMDAAARAHVATLEEAPNQLSMSNVAWKPWLQLCLPSKPHPLACRCAGDG
Protein: High affinity cationic amino acid transporter 1 (CAT-1) (CAT1) (Ecotropic retroviral leukemia receptor homolog) (Ecotropic retrovirus receptor homolog) (Solute carrier family 7 member 1) (System Y+ basic amino acid transporter) (P30825)
Organism: Homo sapiens (Human)
Function: High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q09143}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Estrogen-related receptor gamma
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Peroxisome proliferator-activated receptor gamma coactivator 1-beta
- Steroid hormone receptor ERR1
- Steroid hormone receptor ERR2
- Nuclear receptor-interacting protein 1
- Neutral amino acid transporter A
- Neutral amino acid transporter B
- Large neutral amino acids transporter small subunit 1
- Cell cycle checkpoint protein RAD1
Sequence:
MGCKVLLNIGQQMLRRKVVDCSREETRLSRCLNTFDLVALGVGSTLGAGVYVLAGAVARENAGPAIVISFLIAALASVLAGLCYGEFGARVPKTGSAYLYSYVTVGELWAFITGWNLILSYIIGTSSVARAWSATFDELIGRPIGEFSRTHMTLNAPGVLAENPDIFAVIIILILTGLLTLGVKESAMVNKIFTCINVLVLGFIMVSGFVKGSVKNWQLTEEDFGNTSGRLCLNNDTKEGKPGVGGFMPFGFSGVLSGAATCFYAFVGFDCIATTGEEVKNPQKAIPVGIVASLLICFIAYFGVSAALTLMMPYFCLDNNSPLPDAFKHVGWEGAKYAVAVGSLCALSASLLGSMFPMPRVIYAMAEDGLLFKFLANVNDRTKTPIIATLASGAVAAVMAFLFDLKDLVDLMSIGTLLAYSLVAACVLVLRYQPEQPNLVYQMASTSDELDPADQNELASTNDSQLGFLPEAEMFSLKTILSPKNMEPSKISGLIVNISTSLIAVLIITFCIVTVLGREALTKGALWAVFLLAGSALLCAVVTGVIWRQPESKTKLSFKVPFLPVLPILSIFVNVYLMMQLDQGTWVRFAVWMLIGFIIYFGYGLWHSEEASLDADQARTPDGNLDQCK
Protein: Transcriptional repressor of nicotinamide riboside utilization NrtR (Q8EFJ3)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
- Nicotinamide phosphoribosyltransferase
- Ribose phosphate pyrophosphokinase NadR
- Transcriptional repressor NrdR
- Transcriptional repressor of branched chain amino acid degradation LiuR
- Arginine repressor
- Transcriptional repressor of fatty acid degradation PsrA
Sequence:
MTEAEYLANYDPKAFKAQLLTVDAVLFTYHDQQLKVLLVQRSNHPFLGLWGLPGGFIDETCDESLEQTVLRKLAEKTAVVPPYIEQLCTVGNNSRDARGWSVTVCYTALMSYQACQIQIASVSDVKWWPLADVLQMPLAFDHLQLIEQARERLTQKALYSLVPGFALSEPFTLPELQHVHEVLLGKPIQGKSFRRRVEQADLLIDTGLKRTERGRPANLYCLKPDTASYRFLRNLEC
Protein: D-erythrulose-4-phosphate isomerase 2 (EC 5.3.1.34) (A0R757)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the isomerization of D-erythrulose-4P to D-erythrose-4P. Involved in the degradation pathways of L-threitol, D-threitol and erythritol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Transketolase, N-subunit
- Ribose-5-phosphate isomerase B
- Transketoloase, C half
- Transketolase
- Transketolase
- Ribose-phosphate pyrophosphokinase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Ribokinase
- 6-phosphogluconate dehydrogenase, decarboxylating
Sequence:
MALKIVIGGDNAGFNYKEALRKDLEADDRVASVEDVGVGGVDDTTSYPNVAVAAAEKVARGEADRALLICGTGLGVAIAANKVKGIRAVTAHDVYSVQRSVLSNNAQVLCMGERVVGLELARALVKEWLGLEFDPQSASAAKVNDICAYEGA
Protein: 3-isopropylmalate dehydrogenase 1, chloroplastic (3-IPM-DH 1) (AtIMDH1) (IMDH 1) (EC 1.1.1.85) (Beta-IPM dehydrogenase 1) (Isopropylmalate dehydrogenase 1) (AtIMD1) (Methylthioalkylmalate dehydrogenase 1) (Q9FMT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in both glucosinolate and leucine biosynthesis; catalyzes the oxidative decarboxylation step in both leucine biosynthesis (primary metabolism) and methionine chain elongation of glucosinolates (specialized metabolism). Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate, 3-IPM) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Required during pollen development and involved in embryo sac development. More active on 3-isopropylmalate and NAD(+) than towards D-malate.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19674406}.
Interaction partners:
- 3-isopropylmalate dehydratase small subunit 2
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- 3-isopropylmalate dehydratase small subunit 3
- 3-isopropylmalate dehydratase small subunit 1
- Methylthioalkylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 3, chloroplastic
- Methionine aminotransferase BCAT4
- 3-isopropylmalate dehydrogenase 2, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- Probable sodium/metabolite cotransporter BASS5, chloroplastic
Sequence:
MAAFLQTNISLNAIKIVPGKYSSLTDHQFRAPYRIRCAAASPGKKRYNIALLPGDGIGPEVISVAKNVLQKAGSLEGLEFDFKEMPVGGAALDLVGVPLPEETFTAAKLSDAILLGAIGGYKWDKNEKHLRPEMALFYLRRDLKVFANLRPATVLPQLVDASTLKKEVAEGVDMMIVRELTGGIYFGEPRGITINENGEEVGVSTEIYAAHEIDRIARVAFETARKRRGKLCSVDKANVLDASILWRKRVTALASEYPDVELSHMYVDNAAMQLIRDPKQFDTIVTNNIFGDILSDEASMITGSIGMLPSASLGESGPGLFEPIHGSAPDIAGQDKANPLATILSAAMLLKYGLGEEKAAKRIEDAVVDALNKGFRTGDIYSPGNKLVGCKEMGEEVLKSVESKVPATV
Protein: tRNA (guanine(9)-N(1))-methyltransferase (EC 2.1.1.221) (D6R954)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEMLPAFIETSNVDKKQGINEDQEESQKPRLGEGCEPISKRQMKKLIKQKQWEEQRELRKQKRKEKRKRKKLERQCQMEPNSDGHDRKRVRRDVVHSTLRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMDENDKGWVNWKDIHIKPEHYSELIKKEDLIYLTSDSPNILKELDE
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR14 (EC 3.1.3.95) (HCV NS5A-transactivated protein 4 splice variant A-binding protein 1) (NS5ATP4ABP1) (Myotubularin-related protein 14) (Phosphatidylinositol-3-phosphate phosphatase) (hJumpy) (Q8NCE2)
Organism: Homo sapiens (Human)
Function: Lipid phosphatase which efficiently dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2; inactive toward PtdIns4P, PtdIns(3,4)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17008356}. Note=Found in reticular structures and plasma membrane ruffles. Concentrated near the nucleus. {ECO:0000269|PubMed:17008356}.
Interaction partners:
- Myotubularin
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate-4-phosphatase type I A
- Phosphatidylinositide phosphatase SAC2
- Dynamin-2
- Inositol polyphosphate 4-phosphatase type II
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
Sequence:
MAGARAAAAAASAGSSASSGNQPPQELGLGELLEEFSRTQYRAKDGSGTGGSKVERIEKRCLELFGRDYCFSVIPNTNGDICGHYPRHIVFLEYESSEKEKDTFESTVQVSKLQDLIHRSKMARCRGRFVCPVILFKGKHICRSATLAGWGELYGRSGYNYFFSGGADDAWADVEDVTEEDCALRSGDTHLFDKVRGYDIKLLRYLSVKYICDLMVENKKVKFGMNVTSSEKVDKAQRYADFTLLSIPYPGCEFFKEYKDRDYMAEGLIFNWKQDYVDAPLSIPDFLTHSLNIDWSQYQCWDLVQQTQNYLKLLLSLVNSDDDSGLLVHCISGWDRTPLFISLLRLSLWADGLIHTSLKPTEILYLTVAYDWFLFGHMLVDRLSKGEEIFFFCFNFLKHITSEEFSALKTQRRKSLPARDGGFTLEDICMLRRKDRGSTTSLGSDFSLVMESSPGATGSFTYEAVELVPAGAPTQAAWRKSHSSSPQSVLWNRPQPSEDRLPSQQGLAEARSSSSSSSNHSDNFFRMGSSPLEVPKPRSVDHPLPGSSLSTDYGSWQMVTGCGSIQERAVLHTDSSLPFSFPDELPNSCLLAALSDRETRLQEVRSAFLAAYSSTVGLRAVAPSPSGAIGGLLEQFARGVGLRSISSNAL
Protein: Transcription factor MYB34 (Myb-related protein 34) (AtMYB34) (Protein ALTERED TRYPTOPHAN REGULATION 1) (ATR1) (O64399)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in tryptophan gene activation and in indole-3-acetic acid (IAA) and indolic glucosinolates (IG) biosynthesis. Acts as a direct transcriptional activator of both Trp synthesis genes and Trp secondary metabolism genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Tryptophan N-monooxygenase 2
- Tryptophan N-monooxygenase 1
- Transcription factor MYC2
- Cytosolic sulfotransferase 16
- Methylthioalkylmalate synthase 3, chloroplastic
- Transcription factor MYC4
- Transcription factor MYC3
- Cytosolic sulfotransferase 18
- Methylthioalkylmalate synthase 1, chloroplastic
- Cytosolic sulfotransferase 17
Sequence:
MVRTPCCKEEGIKKGAWTPEEDQKLIAYLHLHGEGGWRTLPEKAGLKRCGKSCRLRWANYLRPDIKRGEFSPEEDDTIIKLHALKGNKWAAIATSLAGRTDNEIKNYWNTNLKKRLKQKGIDAITHKPINSTGQTGFEPKVNKPVYSSGSARLLNRVASKYAVELNRDLLTGIISGNSTVAEDSQNSGDVDSPTSTLLNKMAATSVLINTTTTYSGFSDNCSFTDEFNEFFNNEEISDIYTTVDNFGFMEELKSILSYGDASAGVIENSPEVNVADAMEFIDSWNEDDNMVGVFV
Protein: DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.38) (Deoxycytidine deaminase) (Q7YR25)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also simian foamy virus (SFV). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. May inhibit the mobility of LTR retrotransposons.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9HC16}. Nucleus {ECO:0000250|UniProtKB:Q9HC16}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9HC16}. Note=Mainly cytoplasmic, small amount are found in the nucleus. {ECO:0000250|UniProtKB:Q9HC16}.
Interaction partners:
Sequence:
MNPQIRNMVEQMEPDIFVYYFNNRPILSGRNTVWLCYEVKTKDPSGPPLDANIFQGKLYPEAKDHPEMKFLHWFRKWRQLHRDQEYEVTWYVSWSPCTRCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQQALRILCQERGGPHATMKIMNYNEFQHCWNEFVDGQGKPFKPRKNLPKHYTLLHATLGELLRHVMDPGTFTSNFNNKPWVSGQRETYLCYKVERSHNDTWVLLNQHRGFLRNQAPDRHGFPKGRHAELCFLDLIPFWKLDDQQYRVTCFTSWSPCFSCAQKMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLHRDGAKIAVMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAI
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (E2) (P06959)
Organism: Escherichia coli (strain K12)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Interaction partners:
- Pyruvate dehydrogenase E1 component
- Dihydrolipoyl dehydrogenase
- 2-oxoglutarate dehydrogenase E1 component
- Citrate synthase
- Phosphate acetyltransferase
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Formate acetyltransferase 1
- Probable pyruvate-flavodoxin oxidoreductase
Sequence:
MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVSVGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVAGEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLITVEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKAEGKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILREDVQAYVKEAIKRAEAAPAATGGGIPGMLPWPKVDFSKFGEIEEVELGRIQKISGANLSRNWVMIPHVTHFDKTDITELEAFRKQQNEEAAKRKLDVKITPVVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYINIGVAVDTPNGLVVPVFKDVNKKGIIELSRELMTISKKARDGKLTAGEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMLPISLSFDHRVIDGADGARFITIINNTLSDIRRLVM
Protein: Protein phosphatase 1 regulatory subunit 3B (Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL) (Protein phosphatase 1 regulatory subunit 4) (PP1 subunit R4) (Protein phosphatase 1 subunit GL) (PTG) (Q8C767)
Organism: Mus musculus (Mouse)
Function: Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Glycogen [starch] synthase, liver
- Glycogen [starch] synthase, muscle
- Protein phosphatase 1 regulatory subunit 3A
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 3C
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1 regulatory subunit 3F
Sequence:
MAVDIQYSYSSMAPSLRRERFTFKISPKLSKPLRPCIQLGSKDEASGMVAPAVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDIPFNITELLDNIVSLTTAESESFVLDFPQPSADYLDFRNRLQTNHVCLENCVLKDKAIAGTVKVQNLAFEKVVKIRMTFDTWKSFTDFPCQYVKDTYAGSDRDTFSFDISLPEKIQSYERMEFAVCYECNGQAYWDSNKGKNYRITRAELRSSPGKIEPYNGPDFGISFDQFGSPRCSFGLFPEWPSYLGYEKLGPYY
Protein: Fibroblast growth factor (FGF) (B3DGE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MATGGITTLPAAPDAENSSFPAGSFRDPKRLYCKNGGFFLRINADGRVDGARDKSDPHIRLQLQATAVGEVLIKGICTNRFLAMNADGRLFGTKRTTDECYFLERLESNNYNTYRSRKYPDWYVALKRTGQYKSGSKTSPGQKAILFLPMSAKC