wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclin-O protein A (Q32NJ2)
Organism: Xenopus laevis (African clawed frog)
Function: Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of mcidas to promote mother centriole amplification and maturation in preparation for apical docking.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0C242}. Note=Localizes to the apical part of cytoplasm. {ECO:0000250|UniProtKB:P0C242}.
Interaction partners:
Sequence:
MVTCSMRCTEEHLLGAPAAFSSGKRKRDSGYSPGDATPGDRGEGGPDWPSAGIKKRVKYSRHRKQRLELRSCDSGVADLYETPSPSPVAPTPTNEPYDSPCTSMPDRLGLQSFSDYGHDCYLFNKSLEDKFLTVNCLKNQPQIKAESRCKLISWLIPVHKHLKLGFESLCLTVNILDRFLACTPVASDCFQLVGVTSLLIACKQVESRPPRVKQLLALCCDAFSREQLCNLECIILLKLCFRIGAPTINFFLQHFSLLRVTSVESPDTELIEATKSMTVARGIAELSLADYAFNAYSPSLVAACCLELADRMLCLRNPIGVRVSGYHQSLIKECVGKIDLLVSLNQDSLHRLLPSQFSVKSIKADN
Protein: Lysocardiolipin acyltransferase 1 (EC 2.3.1.-) (1-acylglycerol-3-phosphate O-acyltransferase 8) (1-AGP acyltransferase 8) (1-AGPAT 8) (EC 2.3.1.51) (Acyl-CoA:lysocardiolipin acyltransferase 1) (Q6NYV8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (By similarity). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors (By similarity). Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities (By similarity). Required for establishment of the hematopoietic and endothelial lineages.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6UWP7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tafazzin
- Lysophosphatidylcholine acyltransferase 4
- Phosphatidate cytidylyltransferase
- Phosphatidate cytidylyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Lysophospholipid acyltransferase 2
- Membrane-bound O-acyltransferase domain-containing 2b
- Lysophospholipid acyltransferase 1
- Cardiolipin synthase 1.
- Phospholipid phosphatase 5.
Sequence:
MVSPRGVCFLLFLLLGSVFGSVFMLGPLLPLMLLSPSRYRWITDRIVATWLTLPVALLELVLGVKVVVTGDGFIPGERSVIIMNHRTRLDWMFLWCCLLRYSYLRQEKICLKAALKSVPGFGWAMQVASFIFIQRRWEDDRTHMSNMLQYFCRIREPVQLLLFPEGTDLTENTRARSDEFAEKNGLQKYEYVLHPRTTGFTFIVDTLRGGDNLDAVHDITVAYPQNIPQTERHLLAGVFPREIHFHVQRFTVASVPAGAAGLQAWCQERWREKERRLQRFYETVPRRFDAPAVGVCVREPCCQSGQCVCVPRCKSEGRVRIILVASLLYWSVFITAACASLCLCPPAQFYFLFMVVFFLCQQRFTGGLELMELACHRYWSRRSADKQE
Protein: Probable enoyl-CoA hydratase EchA8 (EC 4.2.1.17) (P9WNN9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Could possibly oxidize fatty acids using specific components.
Interaction partners:
- 3-hydroxybutyryl-CoA dehydrogenase
- Probable 3-hydroxybutyryl-CoA dehydrogenase FadB3
- 3-hydroxyisobutyryl-CoA hydrolase
- Conserved protein
- Probable acyl-CoA dehydrogenase FadE23
- Probable acyl-CoA dehydrogenase FadE4
- Probable acyl-CoA dehydrogenase FadE1
- Probable acyl-CoA dehydrogenase FadE2
- Possible acyl-CoA dehydrogenase FadE19
- Acyl-CoA dehydrogenase FadE7
Sequence:
MTYETILVERDQRVGIITLNRPQALNALNSQVMNEVTSAATELDDDPDIGAIIITGSAKAFAAGADIKEMADLTFADAFTADFFATWGKLAAVRTPTIAAVAGYALGGGCELAMMCDVLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLILTGRTMDAAEAERSGLVSRVVPADDLLTEARATATTISQMSASAARMAKEAVNRAFESSLSEGLLYERRLFHSAFATEDQSEGMAAFIEKRAPQFTHR
Protein: Phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) (Phosphotransferase system, enzyme I) (P08839)
Organism: Escherichia coli (strain K12)
Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- PTS system glucose-specific EIIA component
- Phosphocarrier protein HPr
- Multiphosphoryl transfer protein
- PTS system glucose-specific EIICB component
- PTS system fructose-specific EIIB'BC component
- Phosphocarrier protein NPr
- PTS system N-acetylglucosamine-specific EIICBA component
- PTS system mannitol-specific EIICBA component
- Adenylate cyclase
- Hexose-6-phosphate:phosphate antiporter
Sequence:
MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC
Protein: 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) (NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase) (P9WGT1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably involved in steroid metabolism. Catalyzes the oxidation of androsterone (3alpha-hydroxy-5alpha-androstan-17-one) and 20beta-hydroxyprogesterone (4-pregnen-20beta-ol-3-one), and the reduction of progesterone (4-pregnen-3,20-dione). Shows a preference for NADH. Has no detectable activity for oxidation of L-3-hydroxybutyric acid and only an insignificant activity for reduction of acetoacetyl-CoA.
Interaction partners:
- Ribose-5-phosphate isomerase B
- Probable fatty acid synthase Fas
Sequence:
MSGRLIGKVALVSGGARGMGASHVRAMVAEGAKVVFGDILDEEGKAVAAELADAARYVHLDVTQPAQWTAAVDTAVTAFGGLHVLVNNAGILNIGTIEDYALTEWQRILDVNLTGVFLGIRAVVKPMKEAGRGSIINISSIEGLAGTVACHGYTATKFAVRGLTKSTALELGPSGIRVNSIHPGLVKTPMTDWVPEDIFQTALGRAAEPVEVSNLVVYLASDESSYSTGAEFVVDGGTVAGLAHNDFGAVEVSSQPEWVT
Protein: Uncharacterized protein C530.07c (O59743)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable thiamine biosynthetic bifunctional enzyme
- GPN-loop GTPase 3
- Bromodomain-containing protein C631.02
Sequence:
MDPYTVAIIKKLGIEEQVETAATKSPFIEGLANGTAPPGAFKRWLYEDRIYVQGCSLCLAKAINAITHEKGFPKEALDLFLGAYNVITPELAHFEARCKESNVEMPKLKPVPTSWEQALQDNKPEEYYHLSAPDCKSYIQFMTQELFEIPGTSGIDYFMAFYLNEVIYHRAWKFVRESKQFQKNCPEEMEFVKWWGQPSFGKFVENLARSIQDVPFTSATVDIAKKICNFEYRFFSTAFEKA
Protein: SKU5 similar 3 (F4K1P9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Carbohydrate-binding X8 domain superfamily protein
- Carbohydrate-binding X8 domain superfamily protein
- Carbohydrate-binding X8 domain superfamily protein
- At2g03505
- Non-specific lipid transfer protein GPI-anchored 11
- Beta-glucosidase 24
- Alpha-L-fucosidase 1
- Probable pectate lyase 18
- Metalloendoproteinase 5-MMP
- Serine carboxypeptidase-like 46
Sequence:
MRCFPPPLWCTSLVVFLSVTGALAADPYVFFDWTVSYLSASPLGTRQQVIGINGQFPGPILNVTTNWNVVMNVKNNLDEPLLLTWNGIQHRKNSWQDGVLGTNCPIPSGWNWTYEFQVKDQIGSFFYFPSTNFQRASGGYGGIIVNNRAIIPVPFALPDGDVTLFISDWYTKSHKKLRKDVESKNGLRPPDGIVINGFGPFASNGSPFGTINVEPGRTYRFRVHNSGIATSLNFRIQNHNLLLVETEGSYTIQQNYTNMDIHVGQSFSFLVTMDQSGSNDYYIVASPRFATSIKASGVAVLRYSNSQGPASGPLPDPPIELDTFFSMNQARSLRLNLSSGAARPNPQGSFKYGQITVTDVYVIVNRPPEMIEGRLRATLNGISYLPPATPLKLAQQYNISGVYKLDFPKRPMNRHPRVDTSVINGTFKGFVEIIFQNSDTTVKSYHLDGYAFFVVGMDFGLWTENSRSTYNKGDAVARSTTQVFPGAWTAVLVSLDNAGMWNLRIDNLASWYLGQELYLSVVNPEIDIDSSENSVPKNSIYCGRLSPLQKDQAQRVNFSGSQRSIFVTSRGILLALFAILVNINRLCNTKKILDSTAKAQTDLSLVETDRISEKNRDRISY
Protein: Integrator complex subunit 8 (Int8) (Protein kaonashi-1) (Q75QN2)
Organism: Homo sapiens (Human)
Function: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:34004147, ECO:0000269|PubMed:39032490}. Chromosome {ECO:0000269|PubMed:34004147}. Note=Associates with chromatin and transcription pause-release checkpoint. {ECO:0000269|PubMed:34004147}.
Interaction partners:
- Integrator complex subunit 5
- Integrator complex subunit 1
- Integrator complex subunit 7
- Integrator complex subunit 6
- Integrator complex subunit 3
- Integrator complex subunit 2
- Integrator complex subunit 11
- Integrator complex subunit 9
- Integrator complex subunit 4
- Integrator complex subunit 10
Sequence:
MSAEAADREAATSSRPCTPPQTCWFEFLLEESLLEKHLRKPCPDPAPVQLIVQFLEQASKPSVNEQNQVQPPPDNKRNRILKLLALKVAAHLKWDLDILEKSLSVPVLNMLLNELLCISKVPPGTKHVDMDLATLPPTTAMAVLLYNRWAIRTIVQSSFPVKQAKPGPPQLSVMNQMQQEKELTENILKVLKEQAADSILVLEAALKLNKDLYVHTMRTLDLLAMEPGMVNGETESSTAGLKVKTEEMQCQVCYDLGAAYFQQGSTNSAVYENAREKFFRTKELIAEIGSLSLHCTIDEKRLAGYCQACDVLVPSSDSTSQQLTPYSQVHICLRSGNYQEVIQIFIEDNLTLSLPVQFRQSVLRELFKKAQQGNEALDEICFKVCACNTVRDILEGRTISVQFNQLFLRPNKEKIDFLLEVCSRSVNLEKASESLKGNMAAFLKNVCLGLEDLQYVFMISSHELFITLLKDEERKLLVDQMRKRSPRVNLCIKPVTSFYDIPASASVNIGQLEHQLILSVDPWRIRQILIELHGMTSERQFWTVSNKWEVPSVYSGVILGIKDNLTRDLVYILMAKGLHCSTVKDFSHAKQLFAACLELVTEFSPKLRQVMLNEMLLLDIHTHEAGTGQAGERPPSDLISRVRGYLEMRLPDIPLRQVIAEECVAFMLNWRENEYLTLQVPAFLLQSNPYVKLGQLLAATCKELPGPKESRRTAKDLWEVVVQICSVSSQHKRGNDGRVSLIKQRESTLGIMYRSELLSFIKKLREPLVLTIILSLFVKLHNVREDIVNDITAEHISIWPSSIPNLQSVDFEAVAITVKELVRYTLSINPNNHSWLIIQADIYFATNQYSAALHYYLQAGAVCSDFFNKAVPPDVYTDQVIKRMIKCCSLLNCHTQVAILCQFLREIDYKTAFKSLQEQNSHDAMDSYYDYIWDVTILEYLTYLHHKRGETDKRQIAIKAIGQTELNASNPEEVLQLAAQRRKKKFLQAMAKLYF
Protein: AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) (P0C1X8)
Organism: Rattus norvegicus (Rat)
Function: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues (By similarity). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (By similarity). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (By similarity). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:F1MH24}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11877461}. Presynapse {ECO:0000269|PubMed:11877461}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells. {ECO:0000269|PubMed:11877461}.
Interaction partners:
- AP-2 complex subunit sigma
- AP-2 complex subunit mu
- Clathrin heavy chain 1
- Epsin-2
- Epidermal growth factor receptor pathway substrate 15
- AP-2 complex subunit beta
- Synergin gamma
- Clathrin light chain B
- Clathrin light chain A
- RALBP1 associated Eps domain containing 1
Sequence:
MKKFFDSRREQGSSGLGSGSSGGGGSSSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFALVFLVRTSNGVKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQAEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGSFTIPDNSRYSQDMHCLIYMLEPDPDKRPDIYQVSYFSFKLLKKECPVPNVQNSPIPTKLPEPVKASEAAVKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPLPQATGPSNQPSLLASVSQPKAQATPSQPLQSSQPKQPQAPPTPQQTPAPQTQGLPTQAQATPQHQQQLLLKQQQQQQQQQQQQQPQQPTAPPQPSGTFYQQQQPQQQQAQTQQQFQAVHPAAQQSVTAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQLMAQQAALQQKTAVVVPQPQAQPATAPQAAAAQEPQIQAPARQQPKVQTTPPPTIQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLHAAAAEASLSKSKSATTTPSGSPRTSQQNVSNASEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKLPEKLGGSAESLIPGFQATQGDAFATSSFSAGTAEKRKGGQAVDSGIPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADAAVESLIPGLEPPVAQRLPSHTESVTSNRTDSLTGEDSLLDCSLLSNPTADLLDEFAPIALSASTHKAAEDSNLISGFGVAEGSEKVAEDEFDPIPVLITKNTQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
Protein: Solute carrier family 15 member 1 (Intestinal H(+)/peptide cotransporter) (Oligopeptide transporter, small intestine isoform) (Peptide transporter 1) (P36836)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P46059}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium/glucose cotransporter 1
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Excitatory amino acid transporter 3
- Amino acid transporter
- Amino acid transporter
- Amino acid transporter
- Solute carrier family 22 member 7
Sequence:
MGMSKSLSCFGYPLSIFFIVVNEFCERFSYYGMRALLILYFRNFIGWDDNLSTVIYHTFVALCYLTPILGALIADAWLGKFKTIVWLSIVYTIGQAVTSLSSVNELTDNNHDGTPDSLPVHVAVCMIGLLLIALGTGGIKPCVSAFGGDQFEEGQEKQRNRFFSIFYLAINAGSLLSTIITPMVRVQQCGIHVKQACYPLAFGIPAILMAVSLIVFIIGSGMYKKFKPQGNILSKVVKCICFAIKNRFRHRSKQFPKRAHWLDWAKEKYDERLIAQIKMVTRVLFLYIPLPMFWALFDQQGSRWTLQATTMSGRIGILEIQPDQMQTVNTILIIILVPIMDAVVYPLIAKCGLNFTSLKKMTIGMFLASMAFVAAAILQVEIDKTLPVFPKANEVQIKVLNVGSENMIISLPGQTVTLNQMSQTNEFMTFNEDTLTSINITSGSQVTMITPSLEAGQRHTLLVWAPNNYRVVNDGLTQKSDKGENGIRFVNTYSQPINVTMSGKVYEHIASYNASEYQFFTSGVKGFTVSSAGISEQCRRDFESPYLEFGSAYTYLITSQATGCPQVTEFEDIPPNTMNMAWQIPQYFLITSGEVVFSITGLEFSYSQAPSNMKSVLQAGWLLTVAVGNIIVLIVAGAGQINKQWAEYILFAALLLVVCVIFAIMARFYTYVNPAEIEAQFEEDEKKKNPEKNDLYPSLAPVSQTQM
Protein: Docking protein 6 (Downstream of tyrosine kinase 6) (Q6PKX4)
Organism: Homo sapiens (Human)
Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK6 promotes Ret-mediated neurite growth. May have a role in brain development and/or maintenance.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Glial cell line-derived neurotrophic factor
Sequence:
MASNFNDIVKQGYVKIRSRKLGIFRRCWLVFKKASSKGPRRLEKFPDEKAAYFRNFHKVTELHNIKNITRLPRETKKHAVAIIFHDETSKTFACESELEAEEWCKHLCMECLGTRLNDISLGEPDLLAAGVQREQNERFNVYLMPTPNLDIYGECTMQITHENIYLWDIHNAKVKLVMWPLSSLRRYGRDSTWFTFESGRMCDTGEGLFTFQTREGEMIYQKVHSATLAIAEQHERLMLEMEQKARLQTSLTEPMTLSKSISLPRSAYWHHITRQNSVGEIYSLQGHGFGSSKMSRAQTFPSYAPEQSEEAQQPLSRSSSYGFSYSSSLIQ
Protein: Protein OS9-like domain-containing protein (Q38E25)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Derlin
- Derlin
- RING-type E3 ubiquitin transferase
- E3 ubiquitin-protein ligase CHFR
- RING-type domain-containing protein
- UBX domain-containing protein
Sequence:
MAEPVLAGRAALTLASLYLLLKIVSAKECEWAQRLREYEVEVFSRTNPSGSESEVQSGCISWKTGYWTYEVCPGRWIRQFHKDGNVIVDENFLGVQHRWHLADEIGSKRLRYRDGIHTIPERLNASGAPINNTEATYTCSKDVSVSNVQVDVLYSHGTMCGRGYRRSSQLHLVCNEDVKKADVKLKELELCKYDITVVASTVCDAIYGRSRAYRELSDADMIFAL
Protein: LD16387p (Will decrease acetylation) (Q9VCN9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Transcriptional adaptor 3, isoform C
- SAGA complex subunit Spt20
- Ubiquitin carboxyl-terminal hydrolase nonstop
- Transcription-associated protein 1
- histone acetyltransferase
- SAGA-associated factor 29kDa
- Ataxin-7
- Transcription initiation factor TFIID subunit 10b
- Transcriptional adapter 2b
- SAGA complex subunit Spt7
Sequence:
MSLPSASNHAHAASPVYSNSNNNKSSASSKKTSSKNDLLRCAVGLLLKQKNYVSNERFRRSDFLLLQNKQQFAVNKMLDTDLHGGNSFTFSNVQVITNNQHTVDQQFGRFSQFVEAQAEPLRLEMKRFYGPMLCHFYLDLLKAREPRGAVELLRKYAHLVAPVDMYDAPPPTKINGCSTTANESTFNIRFAKEAQDTGDTELDYFMRLVQTLSGYTRLEAAESDDTVAHFRSSKYELHTTAVVVNRICAYLQRRGHVLIMNLLYTWLHVHIVENEQRAFSEDHLLGLTDDLEGEDGEDDVVSKPAVTLNTRGDIRPSKSLTEKSNRKRPAEEPNIMLETDIKQEVETDESAELSKLQLNIDACLDTLKSATEQILKSQVELPRFLRISERSRGLTSAHLDPSECHMLAGFDNSAVQLWQLNQSYCRGKSFYRRYPQKRCPWELNNCANQEEETDEDSSDEDVKCSEEERRERNRARHCKYADNSYNEYGGFQLRGHTKGVTDVRFSAHYPLMYSVSKDATMRCWRAHNLHCAAIYRSHNYPIWCLDESPVGQYVVTGSKDLSARLWSLEKEHALIIYAGHTQDVECVAFHPNGNYIATGSADHSVRLWCATSGKLMRVFADCRQAVTQLAFSPDGKMLAAAGEETKVRIFDLAAGAQLAELKDHSASISSLSWSTHNRHLATACSDGTLRLWDIKKLSPMSDNSSAGSSSSATTNRVLTVNSSCQRLVDVFYGTSKTLYCIGT
Protein: Protein cycle (Brain and muscle ARNT-like 1) (BMAL1) (MOP3) (O61734)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative transcription factor involved in the generation of biological rhythms. Activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Circadian locomoter output cycles protein kaput
- Cryptochrome-1
- Protein timeless
- Period circadian protein
- Crystallin, isoform A
- 
- GH23983p
- Timeout
- Discs overgrown protein kinase
- NAD-dependent histone deacetylase sirtuin-1
Sequence:
MEVQEFCENMEEIEDENYDEEKSARTSDENRKQNHSEIEKRRRDKMNTYINELSSMIPMCFAMQRKLDKLTVLRMAVQHLRGIRGSGSLHPFNGSDYRPSFLSDQELKMIILQASEGFLFVVGCDRGRILYVSDSVSSVLNSTQADLLGQSWFDVLHPKDIGKVKEQLSSLEQCPRERLIDAKTMLPVKTDVPQSLCRLCPGARRSFFCRMKLRTASNNQIKEESDTSSSSRSSTKRKSRLTTGHKYRVIQCTGYLKSWTPIKDEDQDADSDEQTTNLSCLVAIGRIPPNVRNSTVPASLDNHPNIRHVLFISRHSGEGKFLFIDQRATLVIGFLPQEILGTSFYEYFHNEDIAALMESHKMVMQVPEKVTTQVYRFRCKDNSYIQLQSEWRAFKNPWTSEIDYIIAKNSVFL
Protein: Phenylalanine-4-hydroxylase (PAH) (EC 1.14.16.1) (Phe-4-monooxygenase) (Tryptophan 5-hydroxylase) (TRH) (EC 1.14.16.4) (Tryptophan 5-monooxygenase) (Q54XS1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the hydroxylation of L-phenylalanine. Hydroxylates L-tryptophan to 5-hydroxy-L-tryptophan but does not hydroxylate L-tyrosine to L-DOPA. It uses D-threo-tetrahydrodictyopterin (DH4), also known as dictyoperin, as a cofactor.
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Dihydropteridine reductase
- Sepiapterin reductase
- 4a-hydroxytetrahydrobiopterin dehydratase
- Tyrosine aminotransferase
- Homogentisate 1,2-dioxygenase
- dihydrofolate reductase
- Aldose reductase C
Sequence:
MESNTNSQGQGIIPQSYHSSIFFSISKGSDKIGGLLEYLEIIKKHNINITRIESRPSKTEKKDYDFFLDLEYPTENNKEVEKVIKDLEEKGVKATTLQESSNQTYAPWFPRKISDLDLFANKVLEMGSDLTSDHPGASDPVYRERRREIAKIASTYKHGDEIPRIDYTEEEIKTWGVVYNRLKELFPTNACHQHAYIFPLLEQNCGYSPDNIPQLQDISNFLQECTGWRIRPVQGLLSARDFLNGLAFRVFHATQYIRHPSVPLYTPEPDCCHELLGHVPLLADPDFADFSQEIGLASIGASDEDIQLLSTCYWFTVEFGLCKEGDTIRAYGAGILSSTGEMEHFLTDKAKKLPFNPFDACNTEYPITTFQPLYYVAESFQKAKEQMRQFADSFKKPFSIRYNPYTQSIEILDNKDKLLNICNDIRNQSEILADAISKLKA
Protein: LexA repressor (EC 3.4.21.88) (C1F978)
Organism: Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB 13165 / 161)
Interaction partners:
- Protein RecA
- Protein RecA
- Protein RecA
- DNA repair protein RecN
- Arginine repressor
Sequence:
MTKRQKEVLDFITGFVQRNGYSPSFEEIARGLNLKSLATVHKHITNLQNKGLLARAHNRSRSLDVLPPRSRGRSVDRLPLMGRIAAGRPVEAAENAESISLGDIIGNREVFALQVHGESMRDEHIVDGDYVLVERTNTARQGEIIVALVRGAETTLKRFYLEGSMVRLQPSNAEMNPIIVPAAQVAIQGRVLGMLRKY
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4KH40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MTNLSPIKSLNPIGFDLIRKCQHLFDLVSKLTPLYKSEFLTNYNDRDIYRESGYVLVSTVDGSISLVDMSSQKLDWTFHTNEPIYSSYQAPHYHYTTDEERSSVLGDDFYMDCDKDWRLYNSSVRKGKRVNEIVDASEFIGTLPYTSTDRIVLGKKDTSVFLLDWKTGKLVKRYRMDELYSNTVVENDKEKAIVLSKEAPLLFGSGFKKSEDFPELVYIERKDFKIQCISKFGDVLWSVSYAKMEAKLQNHESVQFISGLSSSVGKNQFPLSYTTSVPMVQLRNVKYETLFPRLGFLDEALYLPFQDRKPNQLAIGDGNQLTLPGNKEAEEVLSLPLPETVISQITDIIDGSTKQAGFASKFSGLIVLIFGFCVTMLSVCGLFFYRLRQSIRIKEPYVSEVPIATPKKKKSKKNGTTKAVHKKENGFISGGNKDPSHEENEKRLLTAFPGLNNSSAEGYRVGKLFVSNKEIAKGSNGTVVLEGSYEGRLVAVKRLVQSHHDVAQKEILNLMASDKHSNIVRWYGVDQDEHFIYISLELCACSLNDLIYASSALLESPMASSSIHSIQINPIFENGKGVELWKENGHPSPVLLKLMRDIVAGLVHLHDIGIVHRDLKPQNVLIVKNSSLCAKLSDMGISKRLPADTSALTRNSTGLGSGSSGWQAPEQLRNERQTRAVDLFSLGCVLFFCMTGGKHPYGDNYERDVNVLNDQKDLFLIESLPEAVHLLTGLLNPDPNLRPRAQDVMHHPLFWNSDMRLSFLRDASDRVELENREEGSQLLAALESTAAVTLNGRWDEKLDSIFLDNIGRYRRYKFDSIRDLLRVIRNKLNHYRELPKELQELLGSVPEGFERYFSSRFPKLLIQVYTVLFDYCNNEEFFFKYSKTTVF
Protein: 26S proteasome regulatory subunit rpn12 (P50524)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- Probable 26S proteasome regulatory subunit rpn9
- 26S proteasome regulatory subunit rpn1
- 26S proteasome regulatory subunit rpn2
- Probable 26S proteasome regulatory subunit rpn3
- 26S proteasome regulatory subunit rpn10
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn502
Sequence:
MSTLDLNHLADLYDRKDWNACKKELLKLKVELAKQNLFVPTSDKEKASFARNVFEYGVLVSIQTCDIESFARYASQVIPFYHDSLVPSSRMGLVTGLNLLYLLSENRIAEFHTALESVPDKSLFERDPYVEWVISLEQNVMEGAFDKVASMIRSCNFPEFSYFMKIVMSMVRNEIATCAEKVYSEIPLSNATSLLYLENTKETEKLAEERGWDIRDGVIYFPKEANALETEDGMLIDEEDELELPPTASKHTISSIRQLLSYTSELEQIV
Protein: Replicase large subunit (EC 2.1.1.-) (EC 2.7.7.-) (EC 2.7.7.48) (EC 3.6.4.13) (183 kDa protein) (RNA-directed RNA polymerase) [Cleaved into: Replicase small subunit (EC 2.1.1.-) (EC 2.7.7.-) (EC 3.6.4.13) (126 kDa protein) (Methyltransferase/RNA helicase) (MT/HEL)] (P89657)
Organism: Pepper mild mottle virus (strain Japan) (PMMV-J)
Function: Is an RNA-dependent RNA polymerase active in viral RNA replication.
Interaction partners:
Sequence:
MAYTQQATNAALASTLRGNNPLVNDLANRRLYESAVEQCNAHDRRPKVNFLRSISEEQTLIATKAYPEFQITFYNTQNAVHSLAGGLRSLELEYLMMQIPYGSTTYDIGGNFAAHMFKGRDYVHCCMPNMDLRDVMRHNAQKDSIELYLSKLAQKKKVIPPYQKPCFDKYTDDPQSVVCSKPFQHCEGVSHCTDKVYAVALHSLYDIPADEFGAALLRRNVHVCYAAFHFSENLLLEDSYVSLDDIGAFFSREGDMLNFSFVAESTLNYTHSYSNVLKYVCKTYFPASSREVYMKEFLVTRVNTWFCKFSRLDTFVLYRGVYHRGVDKEQFYSAMEDAWHYKKTLAMMNSERILLEDSSSVNYWFPKMKDMVIVPLFDVSLQNEGKRLARKEVMVSKDFVYTVLNHIRTYQSKALTYANVLSFVESIRSRVIINGVTARSEWDVDKALLQSLSMTFFLQTKLAMLKDDLVVQKFQVHSKSLTEYVWDEITAAFHNCFPTIKERLINKKLITVSEKALEIKVPDLYVTFHDRLVKEYKSSVEMPVLDVKKSLEEAEVMYNALSEISILKDSDKFDVDVFSRMCNTLGVDPLVAAKVMVAVVSNESGLTLTFERPTEANVALALQPTITSKEEGSLKIVSSDVGESSIKEVVRKSEISMLGLTGNTVSDEFQRSTEIESLQQFHMVSTETIIRKQMHAMVYTGPLKVQQCKNYLDSLVASLSAAVSNLKKIIKDTAAIDLETKEKFGVYDVCLKKWLVKPLSKGHAWGVVMDSDYKCFVALLTYDGENIVCGETWRRVAVSSESLVYSDMGKIRAIRSVLKDGEPHISSAKVTLVDGVPGCGKTKEILSRVNFDEDLVLVPGKQAAEMIRRRANSSGLIVATKENVRTVDSFLMNYGRGPCQYKRLFLDEGLMLHPGCVNFLVGMSLCSEAFVYGDTQQIPYINRVATFPYPKHLSQLEVDAVETRRTTLRCPADITFFLNQKYEGQVMCTSSVTRSVSHEVIQGAAVMNPVSKPLKGKVITFTQSDKSLLLSRGYEDVHTVHEVQGETFEDVSLVRLTPTPVGIISKQSPHLLVSLSRHTRSIKYYTVVLDAVVSVLRDLECVSSYLLDMYKVDVSTQYQLQIESVYKGVNLFVAAPKTGDVSDMQYYYDKCLPGNSTILNEYDAVTMQIRENSLNVKDCVLDMSKSVPLPRESETTLKPVIRTAAEKPRKPGLLENLVAMIKRNFNSPELVGVVDIEDTASLVVDKFFDAYLIKEKKKPKNIPLLSRASLERWIEKQEKSTIGQLADFDFIDLPAVDQYRHMIKQQPKQRLDLSIQTEYPALQTIVYHSKKINALFGPVFSELTRQLLETIDSSRFMFYTRKTPTQIEEFFSDLDSNVPMDILELDISKYDKSQNEFHCAVEYEIWKRLGLDDFLAEVWKHGHRKTTLKDYTAGIKTCLWYQRKSGDVTTFIGNTIIIAACLSSMLPMERLIKGAFCGDDSILYFPKGTDFPDIQQGANLLWNFEAKLFRKRYGYFCGRYIIHHDRGCIVYYDPLKLISKLGAKHIKNREHLEEFRTSLCDVAGSLNNCAYYTHLDDAVGEVIKTAPPGSFVYRALVKYLCDKRLFQTLFLE