wanglab/gogpt-training-data huggingface dataset:
Protein: Catalase-peroxidase (CP) (EC 1.11.1.21) (Hydroperoxidase I) (HPI) (Peroxidase/catalase) (P13029)
Organism: Escherichia coli (strain K12)
Function: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Also displays NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activities.
Interaction partners:
- Catalase HPII
- Superoxide dismutase
- Superoxide dismutase
- Superoxide dismutase
- Alkyl hydroperoxide reductase C
- Alkyl hydroperoxide reductase subunit F
- Histidinol-phosphate aminotransferase
- DNA-binding transcriptional dual regulator OxyR
- Aspartate aminotransferase
- Aromatic-amino-acid aminotransferase
Sequence:
MSTSDDIHNTTATGKCPFHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLTHRHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSPAGAIQFEAVDAPEIIPDPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKSRYIGPEVPKEDLIWQDPLPQPIYNPTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRGGDKRGGANGARLALMPQRDWDVNAAAVRALPVLEKIQKESGKASLADIIVLAGVVGVEKAASAAGLSIHVPFAPGRVDARQDQTDIEMFELLEPIADGFRNYRARLDVSTTESLLIDKAQQLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRVGVLSNDFFVNLLDMRYEWKATDESKELFEGRDRETGEVKFTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWVKVMNLDRFDLL
Protein: Adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (A0A1D8PR83)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ras-like protein 1
- cAMP-dependent protein kinase
- Guanine nucleotide-binding protein subunit alpha
- Ras2p
- cAMP-dependent protein kinase
- Phosphodiesterase
- Pho81p
- 3'\5'-cyclic-nucleotide phosphodiesterase PDE1
- Gpr1p
- Adenylyl cyclase-associated protein
Sequence:
MSFLRRDKSKANFRDGSATGLEEPVSPTTHFSPNAPPPLDGNHGDHYHDPDSPRSSVVSLPQLIHNSATHHLKENYRGFHANKRPKGIANVPPLAQPIKPRFKKKSNSLLNKLIYSTKKEDDETATSGKESRSSSIISDEKRKSASSASSGSSRQKFRFSSFDSNLSTSSSSPPKDKKASISDTVSDSSTVTASMSNMPTISIDLNLDEMHDIIKSPETPAPTVGLPTQKAEKKASPTAIKNWQAPESWDVKAPIKKEEPHAPKIEEVAENDVAIDNVLEKKRLPVLYGTHQVPHVTNSKDIKSSHIIRVFKEDNTFTTILCPLETTTSELLAIVQKKFFLESTTNFQLSVCIGNCVKVLEDFEKPLKIQMGLLLLSGYTEEDKLRMLGREDLSFVCKFVVENIFLRSLTHDEEVLLSRNYVDVNISSLNLKNVPIIFHQHTYEIEKLNVANNPSIYLPLDFIQGCTSLAYVDFSHNGCSKFPNNLLEAPQLTHLNLEMNFLDEIPQRISCLSNLTNLKLSSNQLYSLPHSFSTLTNLKQLDLSSNYFDSYPEAVNKLTNLVELNFSYNDLSIIPESIANLINLQKLNLCTNKLSGTLPGYLSQLKALKRLDIRYNYISNVDVLGIIPNLEVAYASKNAISTFSDQMKCLRLLHFDRNPITELKFNTQMQMLSVLDLSRAKITAFPAEFVEKVPNIEKLVLDKNHLVSLPNELCQLSKLVSLSVHANNLQSLPANIGDLRFLKYLDLHSNNLKSLPDQIWDLCHLTSLNVASNNLTSFPKAPYSVVKRLSSSLVDVHLESSQTLSLADSLLILILSDNRLSDDCFDEISFLIALKSLNVSYNDLIEIPQGTLSRLTRLNELYLSGNELTTLPADDLEVLKSLKLLYMNNNKLVSLPAELSRIANLQHLDVSSNQLKYNISNWPYDWSWHWNKNLKYLNFSGNKRFEIKQSHIKNPETGEDFDSLLVLKQLRVLGLIDVTLTTTNVPEQAVDLRLRTTASEFDNFGYGVSDSLGMRDHVSARDLFVQKFRGKENEMLLCAFDGKHGATNQGHRISLVAKNMFVRNFTKELDEIKNDDEIENALRKAFLNFNKEINGILTAKKNKSFTPVPNMSKEALELNLVDDGNAGCTVSVIYIKDKKLYSANIGDIEALLCRNNGDQFLLTEKHDPTNREEFERIRASGGYVSGGGELDGQLSVSRGVGFFNFLPHTHCGPTIRRFKITNDDDMIILGSKQLWDFISYESAVDIIRKDKNDPMVAAQKLRDFAICYGATDKICVIVLTFGNRQKQAANMYSNYGVDRRRRDKQQVVGGDSNLRKLEQEIEPPIGPLALVFTDIKNSTLLWDSYPAPMRSAIKIHNTIMRRQLRITGGYEVKTEGDAFMVAFPSPTAALLWCFQVQQNLVTADWPSEILETDQCCVVSDSENNTIFRGLSVRMGIHWGSPVCEPDVITGRMDYFGPMVNRASRISAIADGGQIAVSSDFLDVLNSLTVKHNNIKNNVESLIDAYQGNENAGMTIERELNALEDLGCNYFKIGERKLKGLETPEPITLVFTNRLKLRYDIFQKRLDANHSTRVAGTLPVEIIYGLRTVSLRLENLCSSINNGGNYCSEGFESSSGVISQKMNSSFKDSDLISLLNHVTTRIESCTTTLFLRQQLSQIKGNGGLIETNNSPSLDVIMDEIADIMKTVNELK
Protein: Cytosolic carboxypeptidase-like protein 5 (ATP/GTP-binding protein-like 5) (Protein deglutamylase CCP5) (Q583K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMVEAKVQKSLINSESLAGAARGTALGDAREEDPANWAPSPPPNNQREFEFPEDGLSFSSKFDSGNLIQVERTGPFRYLMYTAPDCGNSPQQTNNRQWFHFAIRGGTKGCVLAFTFVGMMHCKMFTYGWMPVVSVCPGKPQYCRLPGRAIVTPLEVMPPTPGYPGFVLKPWAKKGGDGEPEAYGGDEDAEAKGCSEGGMPEINDLTVAGGQTGTKKKKKDQYVAMNLTFDVRIDAETPLKSPYPLGHPQCPAIYVASNHPYSYTTLQQNIKVWKQLASGIMDTTDVSELSGSGKATPYTTDVYFSHEILCKSLDGLNVDLLTITDYLGVSEKRVPLFSNGEAPYSSVRGETSRPHLFSGKLAVVLTARVHPGECPSSHMMHGCIEFLLNKGDPRAEALRSHFVFYIVPMINPDGVARGHTRVDTEGVNLNRAYRTPSKRRHPAPYHIRGLLDSLSETKGKLALFIDMHAHSNKRGMFFYGNSMDAPELLQCLLYTKLVSLNTPYFEFQSCNFSEANMFATGKTGEGRDNSSRVTLYQRTGMIHSYTIEASHVVGNALNGVAALMNSPVEEAEVQQNGTCPRYTTAMFGDVGKALLVALLDLKGWNPMSRLTATAYHNPRGLLMALQRQLQIEIAERYFKLAFMNGGQVALARDSTGDPLVTVMDAMKAEELPEAITIKDGRVFPPLTVKGVPSFLPYDQAVQLLSHTHPSMPPRSFVCGMVRRAMIVSGGSGSGPLRSFCNPNTGIVVAGSGTSVATAAGRRGLLGANRTSFS
Protein: Circadian-associated transcriptional repressor (ChIP-derived repressor of network oscillator) (Chrono) (Computationally highlighted repressor of the network oscillator) (Q8N365)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor which forms a negative regulatory component of the circadian clock and acts independently of the circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a histone deacetylase-dependent manner represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Abrogates the interaction of BMAL1 with the transcriptional coactivator CREBBP and can repress the histone acetyl-transferase activity of the CLOCK-BMAL1 heterodimer, reducing histone acetylation of its target genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on circadian gene promoters and its occupancy shows circadian oscillation antiphasic to BMAL1. Interacts with the glucocorticoid receptor (NR3C1) and contributes to the repressive function in the glucocorticoid response (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Co-localizes with the CLOCK-BMAL1 heterodimer in the PML body. {ECO:0000250}.
Interaction partners:
- Basic helix-loop-helix ARNT-like protein 1
- Period circadian protein homolog 3
- Cryptochrome-2
- Class E basic helix-loop-helix protein 41
- Period circadian protein homolog 2
Sequence:
MDSPSSVSSYSSYSLSSSFPTSPVNSDFGFPSDSEREDKGAHGPRPDTVGQRGGSRPSPGPIRCRHRSKVSGNQHTPSHPKQRGSASPMAGSGAKRSRDGELETSLNTQGCTTEGDLLFAQKCKELQGFIPPLTDLLNGLKMGRFERGLSSFQQSVAMDRIQRIVGVLQKPQMGERYLGTLLQVEGMLKTWFPQIAAQKSSLGGGKHQLTKHFPSHHSDSAASSPASPMEKMDQTQLGHLALKPKQPWHLTQWPAMNLTWIHTTPICNPPLSSPGTISFSHGPLGTGTGIGVILFLQHGVQPFTHSAPTTPVPPTTASPVIPGEPMKLSGEGPRCYSLPVTLPSDWSYTLSPPSLPTLARKMTIGHREQQRSHPPVAADAHLLNL
Protein: Catenin beta 1 (cDNA FLJ57878, highly similar to Beta-catenin) (B4DGU4)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}.
Interaction partners:
Sequence:
MELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
Protein: Guanine nucleotide-binding protein alpha-3 subunit (G5EB53)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- G-protein beta subunit
- Guanine nucleotide-binding protein subunit gamma
- Adenylate cyclase
- Regulator of G protein signaling domain protein
- Developmental regulator flbA
- Guanine nucleotide-binding protein subunit alpha
- DUF7582 domain-containing protein
- cAMP-dependent protein kinase
Sequence:
MGSCFSSESAGDVEQKKRSQAIDRKLEEDSRRLRRECKILLLGSGESGKSTIVKQMKIIHQNGYTVEELALYRLTVYKNLLECAKALIGAYHQFNLEPTSQKVRDNIEFLANYNIDPDPNIPLDPAVGDAITYIWNDPCTSTALERQNEFYLMDSAPYFFEEAKRITSPDYIPNVNDVLRARTKTTGIYETRFTMGQLSIHMFDVGGQRSERKKWIHCFENVTSIIFCVALSEYDQVLLEEGNQNRMMESLVLFDSVVNSRWFMRTSIILFLNKVDLFRQKLPRSPLSNYFPDYSGGNDVNRAAKYLLWRFNQVNRAHLNLYPHLTQATDTTNIRLVFAAVKETILQNALKDSGIL
Protein: Acidic leucine-rich nuclear phosphoprotein 32 family member B (Q5ZMN0)
Organism: Gallus gallus (Chicken)
Function: Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription. Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis. Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes. Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92688}.
Interaction partners:
- Histone H2A.Z
- tRNA-dihydrouridine
- Secretory carrier-associated membrane protein.
Sequence:
MEMKKRLTLELRNKKPGEVKELVLDNCRSDDGKIVGLSSDFENLEFLSMINVNLLSISNLPKLNKLRKLELSDNRISGGLEVLAERTPNLTHLNLSGNKIKDINTLEPLKKLPNLHSLDLFNCEVTMLINYRESVFTLLPQLTYLDGFDADEQEAPDSDPEADGDGLEDEYENGEGEEEEDDDEEDDLDEEVIDEEDDEDDDLEGEEEEDGVDDEEEDEEEDGEDEEDDEADDDLPRGEKRKRNLEDEGEEDPEDEEDDEDD
Protein: Carbonic anhydrase 6 (EC 4.2.1.1) (Carbonate dehydratase VI) (Carbonic anhydrase VI) (CA-VI) (Salivary carbonic anhydrase) (Secreted carbonic anhydrase) (P18761)
Organism: Mus musculus (Mouse)
Function: Reversible hydration of carbon dioxide. Its role in saliva is unknown.
Subcellular location: Secreted.
Interaction partners:
- BPI fold-containing family A member 2
- Mucin-like protein 2
Sequence:
MRALVSVVSLFFLGIQAHSDWSYSGDDGVGESQWSEQYPSCGGERQSPIDVKTEEVMFNPSLKPLSLVNYEKENLEFTMTNNGHTVSIDLPPSMYLETSDGTEFISKAFHFHWGGRDWELSGSEHTIDGIRSIMEAHFVHFNKEYGTYENAKDQKNGLAVLAVLFKIDEYAENTYYSDIISALKNIEKPGETTTLKDTTIRNLLPKDVHHYYTYPGSLTTPPCTENVQWFVLRDKVTLSKAQVVTIENSVMDHNNNTIQNGYRSTQPNNHRVVEANFLNVQDMYSSYHLYLKNMQKEILQPKKQKKTKKNRHFWSRK
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (Q00141)
Organism: Aspergillus niger
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
Sequence:
MAQLDTLDLVVLAVLLVGSVAYFTKGTYWAVAKDPYASTGPAMNGAAKAGKTRNIIEKMEETGKNCVIFYGSQTGTAEDYASRLAKEGSQRFGLKTMVADLEEYDYENLDQFPEDKVAFFVLATYGEGEPTDNAVEFYQFFTGDDVAFESASADEKPLSKLKYVAFGLGNNTYEHYNAMVRQVDAAFQKLGPQRIGSAGEGDDGAGTMEEDFLAWKEPMWAALSESMDLEEREAVYEPVFCVTENESLSPEDETVYLGEPTQSHLQGTPKGPYSAHNPFIAPIAESRELFTVKDRNCLHMEISIAGSNLSYQTGDHIAVWPTNAGAEVDRFLQVFGLEGKRDSVINIKGIDVTAKVPIPTPTTYDAAVRYYMEVCAPVSRQFVATLAAFAPDEESKAEIVRLGSHKDYFHEKVTNQCFNMAQALQSITSKPFSAVPFSLLIEGITKLQPRYYSISSSSLVQKDKISITAVVESVRLPGASHMVKGVTTNYLLALKQKQNGDPSPDPHGLTYSITGPRNKYDGIHVPVHVRHSNFKLPSDPSRPIIMVGPGTGVAPFRGFIQERAALAAKGEKVGPTVLFFGCRKSDEDFLYKDEWKTYQDQLGDNLKIITAFSREGPQKVYVQHRLREHSELVSDLLKQKATFYVCGDAANMAREVNLVLGQIIAAQRGLPAEKGEEMVKHMRRRGRYQEDVWS
Protein: Leucine zipper putative tumor suppressor 2 (Protein LAPSER1) (Q3LUD4)
Organism: Rattus norvegicus (Rat)
Function: Negative regulator of katanin-mediated microtubule severing and release from the centrosome. Required for central spindle formation and the completion of cytokinesis. May negatively regulate axonal outgrowth by preventing the formation of microtubule bundles that are necessary for transport within the elongating axon. Negative regulator of the Wnt signaling pathway. Represses beta-catenin-mediated transcriptional activation by promoting the nuclear exclusion of beta-catenin.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Preferentially localized to the mother centriole. Also localized to the midbody in cells undergoing cytokinesis. Within neurons, enriched in cell bodies and localized to branch points and the tips of axonal branches.
Interaction partners:
Sequence:
MAIVQTLPVPLEPARETATAPQTPAMGSVSSLISGRPCPGGPAPQRHHGVPGPTFFRQQDGLLRGGYEAQEPLCPAVPPRKTVPGNSFTYVNEDFRTESPPSPSSDVEDPREHQAHNAHLRGPPPKLIPVSGKLEKNMEKILIRPTAFKPVLPKPRGAPSLPGFLGPRAAGLSGSQGSLTQLFGGPASSSSSSSSSSAADKPLALSGWASGCPSGTLSDSGRNSLSSLPTYSTGGAEPTANSPGGHLPSHGPGRGPLPGPARGVPTGPSHSDSGRSSSSKSTGSLGARVAGGLLGSGARASPGSSSGGDRSPPPPPPPPPSDEALLHCVLEGKLRDREAELQQLRDSVDESEAAVCQAFGARQRRWPGEREDCASHAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQQELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAALRVSEGHARGLQEAARARELELEACSQELQRYRQEAEQLREKARHLDAEAAGLREPPVPPATTDPFLLAESDEAKVQRAAAGTGGSLRAQVERLRQELQREQRRGDEQRNSFEGERLAWQAEKEQVIRYQKQLQHNYVQMYRRNRQLEQELQQLSLELEARELADLGLSEPAPCICLEEITATEI
Protein: Alcohol O-acetyltransferase 2 (AATase 2) (EC 2.3.1.84) (Acetyl-CoA:pregnenolone acetyltransferase) (APAT) (P53296)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Can use acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate. ATF2 seems to play only a minor role in the acetate ester synthesis, compared to ATF1. Plays an active role in the detoxification hydroxysteroids and possibly certain phytochemicals, in association with the efflux pumps PDR5 and SNQ2.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:25093817}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25093817}; Peripheral membrane protein {ECO:0000269|PubMed:25093817}. Note=Traffics to lipid droplets during the stationary phase (PubMed:25093817). {ECO:0000269|PubMed:25093817}.
Interaction partners:
- Steryl acetyl hydrolase 1
- N-acetyltransferase SLI1
Sequence:
MEDIEGYEPHITQELIDRGHARRMGHLENYFAVLSRQKMYSNFTVYAELNKGVNKRQLMLVLKVLLQKYSTLAHTIIPKHYPHHEAYYSSEEYLSKPFPQHDFIKVISHLEFDDLIMNNQPEYREVMEKISEQFKKDDFKVTNRLIELISPVIIPLGNPKRPNWRLICLPGKDTDGFETWKNFVYVTNHCGSDGVSGSNFFKDLALLFCKIEEKGFDYDEEFIEDQVIIDYDRDYTEISKLPKPITDRIDYKPALTSLPKFFLTTFIYEHCNFKTSSESTLTARYSPSSNANASYNYLLHFSTKQVEQIRAQIKKNVHDGCTLTPFIQACFLVALYRLDKLFTKSLLEYGFDVAIPSNARRFLPNDEELRDSYKYGSNVGGSHYAYLISSFDIPEGDNDKFWSLVEYYYDRFLESYDNGDHLIGLGVLQLDFIVENKNIDSLLANSYLHQQRGGAIISNTGLVSQDTTKPYYVRDLIFSQSAGALRFAFGLNVCSTNVNGMNMDMSVVQGTLRDRGEWESFCKLFYQTIGEFASL
Protein: Protein regulator of cytokinesis 1 (Q54VM5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Kinesin-related protein 13
- Uncharacterized protein
- Kinesin-related protein 8
- Probable serine/threonine-protein kinase PLK
- Cell division control protein 45 homolog
- Probable serine/threonine-protein kinase mps1
- SAP domain-containing protein
- Uncharacterized protein
Sequence:
MTIESEIIKEVLVKVAKIWDELGIDQAYRKNQIDTASEKIIEIYNSLLKKEEQYKEDIIKDIISGLESLCSMSTELGETVNDNHQTLSSMTLFQRLEYIEIEKSKLRKRTEDRMAIIEELEAGIDDYSKEMELKDLHQSTIDESAMQGNDYSMDKISSLGRKLKILKTQRDELFFEVQKISNEIVQLWEELRVSPDTELEKSILLMTQSTIDKVSPIPLGQATLTALEQKRYRLYIIKAEHEEMVCKYATQITLLWNKLEIPTDERDSFFAKTSGLGFDVIEACREELERVEEIRNNCLSDLIKKVVEKIQTFYNHLHLPIEKLKKLVIDNNLDINNDSEELLELYELELTRVGKLYEISKPLLLLIEKRETIRNYKIEYEQTILGDKERLLSKKFDRARFEKEKELSTAFQKLPVIEDNLKKQLLIWDKTYGQPFTYEGFNYLEVMQQQADNEKKLKETEKLRKEREKQNKVDEMKSNAINCNNGNNVNINGNGNGVGGPIKKSTSTTFNNNNNINSSNISSNNNNNNNNNGPKTPTSSRVFKSVQTPSTPKTPKSKSTLENLTQSPYSSALSTKTLLKKRSPLSPLPIKSLTNTPGTNSNRSTAASKLSPNNKKKIQFSLNTNLNNNNNNNNNNNNQQNIVNNKSSTTAAVKRPISRISPTITENKQQQLQHQQLQHHSNVSMVPIVSPTSSVSSQSSRSSQTSSHSNGNGSYIIHQPPQQQQQQQQQQQHMHPNPTLNNGIYKSNSNDSIMINNHQYNDDLIMDDTMI
Protein: Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1) (P04268)
Organism: Gallus gallus (Chicken)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P04692}.
Interaction partners:
- Troponin T, fast skeletal muscle isoforms
- Troponin T, cardiac muscle isoforms
- Actin, alpha cardiac muscle 1
- Uncharacterized protein
- ACTSB protein
- Actin, aortic smooth muscle
- Myosin regulatory light chain 2A, cardiac muscle isoform
- Actin, cytoplasmic 1
- Troponin I, fast skeletal muscle
- Myosin regulatory light chain 2B, cardiac muscle isoform
Sequence:
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATDAESEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAQKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERAEERAELSESKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: FI05912p (A1ZAU6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDEDILNAVESLFGKDVKIVDCETSSSLQQEEVLLVNGVPVKLDGLPADDASAIKAALLEGQMPSVEHLNQLLFRAGLAQQPIEVETSLTVKSSLTTTEEVLVSRNGQILDERTVETKENFNHQSHQKEIWHPVKQQSALARATPENALKYRTTSNSTFASQATDSDERPVDPLGRQLNQTFSNASLMSSSSAITGSDQVIGSVSSTTIGDKSSNISSCDSGHDGLFHSVSMSAPWSHPRDTLTDSLYCDIPSSADESDAVSILNTHLKITEPFDCQTAPVYAKDIPKKGNLDSVVNLLINNNTKDLRFAFLTTSRLFSPPHQLLSKIIAKIDNEEENVLRLLNEWLDTCPGDFSHELLLQELENKRNVKGLAAFLDGIPQALAQKDENGRSQLNNLLTKQSSASSLGRQSSIKSLKRFAANVYKTDNVLNNCSSAFELAHQLYAIEYAYLSQIRLEEFVEILEKDELKTCISQTKAGTLGSNCISQVTIDSYVQWFNQLSYLTATEILKLGKKSQRAQMIDFWVETALECFNTGNFNSLMAILTALNLTAIARLKKTWAKVQTTKFEGLEHQMDPSSNFLNYRSTMKAAVWRSEREMANEIERAIIPFFSLFLKDLHAINESHETKLANGYINFEKCLHLGTQLRNFGKWQRLDCPYEQLPSVVSYLLKAEVLSEDLLMKASYESEPPETGEEKDHYKTLKAARKSNT
Protein: Large ribosomal subunit protein uL15 (60S ribosomal protein L27a) (L29) (P14115)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS25
Sequence:
MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGMHHHRINFDKYHPGYFGKVGMRHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKTGVAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKGVGGACVLVA
Protein: Regulator of chromosome condensation domain-containing protein (Q55CR5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DNAJ heat shock N-terminal domain-containing protein
- BAR domain-containing protein
- Uncharacterized protein
Sequence:
MSQPPISNRPSTIAANGGSLVSPNSIVNSNSNSRGNLTGGRPLPSPPINTSSGSINVNNNNNSNNNTNGGVPVSSSPLKSPPPLKPRPKTLLTPVAPIGSQNPQPPSLQQQQQPQPQPQNTSSSNLLQQPSPSPSQQPPSQQPPSQQQQQQPPSQQPPKSTSPPALPRREWPPNNTSSGNLNSLNSSGGNVINRPQPVADNSNNNNSNKPVNVTTQPPQPQTTPIKPASTALQSTPIKETTTTATAATTTPVSVPTQTAVPVAQETSSTVTPIKINNLEASGQTTESGNNSTSTSTQSSPSTSTPPTPNSSTSTTPLSTSTTQLAPPPLAPPLFNTPPISVSQSTSSGNLNSLYSSSAPTNSGMANYKPISPNSSIISPSKPEPLVLPSSISTTTTPTNSTPNTPSTQQQQQQQSSPNNTNENKQKRNSLGEQTSITLEKMAQESSLTINEKDEEETNDSSGKKSKSKPKLFPHQWSMGKPSEKDAKKEEKERKENEKREEKERKELEKREKKERKEKEKLDKKGEKGDKTEKDKEKEKEKEKEKEKEKEKEKDIKSGIEKPPPLSRTSSSFASKLKHATLRGGKVNDIDDTDSNSGSSVGNSPSLTAQRDTRGSSVPHPPVNISTSTNSATTPSSSSSSTPISSPPPSLSSSSNIAISSCSASNLSNVLADNSGSSTGTTPTDGFSSSPPNGQSPSLSSTAHRSAIHLDTSRGLMTWGSASNCKLGFKVTAKDQSQPTPERLPNFNIPDICSISSGSYYSSVLTENGDVYLWGRGAVKTPAVPILGIPQIEDQLLPFKLESLSDVVSVSIGFCHGAAVRANGELLTWGVGENGQLGHGDTNNQIEPKIIQSLTSFWITQVQCGEKHTICLTKNGKVYSWGASEYGQLGLGDVTQHSSPMQVSALEKYNVLQIASGSTHCAVLTTSKEVLVFGNGAAMGAASVVSLPTLVPSLKYLHIDRLCCGHYSTAAITECGDVYTWGTGQELGHGGNSTETSPKLIEALRNQSIRQISCGGRHTAFLTDSGRIFTCGKDSFGQLGQMSGDQNKPKRIESLTKTTFISVSCGENYNVALFDTTRSFRDKFCWKLLETQRTYVRTLDIIQTIFLNPLRIRDRDLLPESMKHLPYIFLSEEEIRTIFGPIEKLYALNSTLLHVMNKRFANWSNKKKVGDVLLNHFKHSEDTFIQYMENLPLALTCLDNLCKKQTAPIIGYLKECEKLALDRKKIDTDDDSKEFNLRSLLIEPLNIISRYHKAINGMVKYTKTTHIDYSGLVDLDGIMEIKVNKVTNILNITQSPSSMASYTTSNPTVTAVSSSSSENSEFLKEYDIKLEALQNFKKTCTKIIKSSKKYYEVEPDSFKEQGHFSEHLINVKACFDGNIDPALAASIDQFSSSIKKIGYLRSELSTRTHTSFAQPLSTVADELENFLPLITEMRKRVFESHTEYENAVSKLYSLAKNLQPTEKKMIEAEKEVASLKKVLDKTLFEFDAIFKEGISIQTKSLKLFYACMKAQQEYYERGLQRFQAMKPSFDALDTYFRQQSRNTWAKSIFETVTTTFTQEKGAPTPSLTSIKSTPIIQSQSSASSTLQIPPSDIAAAPSSTPSSAPSPLVLATQLNSVNNTDMSANSSTPLSSTPKEQHPFALSENIEKTESSPSTKLQQPTINATTTNTTTSPVATTTATATTNNNTASLLDPHQIMTELEQSDWTFLMDPPASNEFTDTFIEEQYNGLVEILASPSLQVAQCVVSAAPSDQQSPTIESISRIFESFNKIRPIIHSGIEQEVLSTANPSTLFRSNTTATKLMTAFTKLKGMPYLQKHITPLVREIIDNPNGYEVDPAKINEGSEELMTNMMNLIQICEKFTDAIIDSVENLPASLREISSYLQQEVVKKFPDNKYSSVGGFIFLRFLCPSILAPHTSGLVEEQPGPEATRALVLIGKVLQNLANGIEFGQKESFMIPVNRFIIGNVTRLNNYFDKLTNVPMYTSSDSISTTSREEVQKDIRNIHLLIVKNLSKLVKQLALYKQKEIIGQLSKTLVFLGDPSSMYK
Protein: Tyrosine-protein kinase JAK1 (EC 2.7.10.2) (Janus kinase 1) (JAK-1) (P23458)
Organism: Homo sapiens (Human)
Function: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Kinase partner for the type I interferon receptor IFNAR2. In response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins. Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors.
Subcellular location: Endomembrane system; Peripheral membrane protein. Note=Wholly intracellular, possibly membrane associated.
Interaction partners:
- Interferon gamma receptor 1
- Interferon alpha/beta receptor 1
- Signal transducer and activator of transcription 5B
- Interleukin-10 receptor subunit alpha
- Tyrosine-protein kinase JAK3
- Suppressor of cytokine signaling 1
- Cytokine receptor common subunit gamma
- Interferon alpha/beta receptor 2
- Tyrosine-protein kinase JAK2
- Signal transducer and activator of transcription 1-alpha/beta
Sequence:
MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK