wanglab/gogpt-training-data huggingface dataset:
Protein: Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha) (Q99MR8)
Organism: Mus musculus (Mouse)
Function: Biotin-attachment subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q96RQ3}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Peroxisomal bifunctional enzyme
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Methylglutaconyl-CoA hydratase, mitochondrial
- Biotin--protein ligase
- Propionyl-CoA carboxylase alpha chain, mitochondrial
Sequence:
MAAAALLAAVDRNQLRRVPILLLQPREWAWKLRTMKYGTTPGGSITKVLIANRGEIACRVIRTAKKMGVQSVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLAMEKIIQVAKSSAAQAIHPGYGFLSENMEFAELCKQEGIIFIGPPSSAIRDMGIKSTSKSIMAAAGVPVVEGYHGKDQSDQCLREHAGKIGYPVMIKAVRGGGGKGMRIVRSEREFQEQLESARREAKKSFNDDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGINPEVRRKLGEAAVRAAKAVKYVGAGTVEFIMDSRHNFYFMEMNTRLQVEHPVTEMITGTDLVEWQLRIAAGEKIPLSQEEIPLQGHAFEARIYAEDPDNNFMPGAGPLVHLSTPSADMSTRIETGVRQGDEVSVHYDPMIAKLVVWASDRQSALSKLRYCLHQYNIVGLRSNVDFLLRLSGHPEFEAGNVHTDFIPQHHKDLLPSHSTIAKESVCQAALGLILKEKEMTSAFKLHTQDQFSPFSFSSGRRLNISYTRNMTLRSGKSDIVIAVTYNRDGSYDMQIDNKSFRVLGDLSSEDGCTYLKSSINGVARKSKFILLDNTVHLFSMEGSIEVGIPVPKYLSPVSAEGAQGGTIAPMTGTIEKVFVKAGDRVKAGDSLMVMIAMKMEHTIKAPKDGRIKKVFFSEGAQANRHAPLVEFEEEESDK
Protein: Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic (AtFTSHI1) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 1) (Protein ARC1) (Protein FTSH INACTIVE PROTEASE 1) (O22993)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis. Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:22900897}; Multi-pass membrane protein {ECO:0000269|PubMed:22900897}.
Interaction partners:
- Protein Ycf2
- ATP-dependent zinc metalloprotease FTSH 12, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic
- Defensin-like protein A
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic
- Exocyst complex component EXO70A1
- Malate dehydrogenase, chloroplastic
- U-box domain-containing protein 8
- Protein TIC 100
Sequence:
MASIDNVFSLGTRFSIPENPKRSILKHATTSSFSARTQTRWRAPILRRSFTVLCELKTGSSSSGETNNSPAADDFVTRVLKENPSQVEPRYRVGDKLYNLKEREDLSKGTNAATGAFEFIKRKFDSKKKTETDKSEESVYLSDILREYKGKLYVPEQVFGPELSEEEEFEKNVKDLPKMSLEDFRKAMENDKVKLLTSKEVSGVSYTSGYRGFIVDLKEIPGVKSLQRTKWSMKLEVGEAQALLKEYTGPQYEIERHMTSWVGKVADFPNPVASSISSRVMVELGMVTAVIAAAAVVVGGFLASAVFAVTSFAFVTTVYVVWPIAKPFLKLFVGVFLGVLEKSWDYIVDVLADGGIFSRISDFYTFGGVASSLEMLKPILLVVMTMVLLVRFTLSRRPKNFRKWDLWQGIAFSQSKAEARVDGSTGVKFADVAGIDEAVDELQELVKYLKNPDLFDKMGIKPPHGVLLEGPPGCGKTLVAKAIAGEAGVPFYQMAGSEFVEVLVGVGSARIRDLFKRAKVNKPSVIFIDEIDALATRRQGIFKENSDQLYNAATQERETTLNQLLIELDGFDTGKGVIFLGATNRRDLLDPALLRPGRFDRKIRVRPPNAKGRLDILKIHASKVKMSDSVDLSSYASNLPGWSGAKLAQLVQEAALVAVRKTHNSILQSDMDDAVDRLTVGPTRIGLELGHQGQCRRATTEVGVAITSHLLLRYENAKIERCDRVSIIPRGQTLSQVVFHRLDDESYMFGRLPQLLHRLQVLLGGRAAEEVIYGSDTSKASVDYLSDASWLARKILTIWNLENPMVIHGEPPPWRKRPQFVGPRLDFEGSLYDDYDLVEPPVNFNMDDEVAHRSEELISQMYNKTVSLLRQNQTALLKTVKVLLNQKEISGEAIDFILDHYPPQTPLNSLLQEQNPGSLPFVPEHLRRESGDFVLVNHSTDVNAQV
Protein: Inorganic pyrophosphatase 2 (AtPPsPase2) (PPi phosphatase 2) (Pyrophosphate-specific phosphatase 2) (EC 3.6.1.1) (Q9FZ62)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the specific cleavage of pyrophosphate.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit PDX1.3
- Inorganic pyrophosphatase 1
- Transmembrane protein
- Pyridoxal 5'-phosphate synthase-like subunit PDX1.2
- Pyridoxal 5'-phosphate synthase subunit PDX1.1
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Pyridoxal kinase
- Thiamine phosphate phosphatase-like protein
- Probable pyridoxal 5'-phosphate synthase subunit PDX2
- Pyridoxal reductase, chloroplastic
Sequence:
MAKNNNIVIVFDFDKTIIDVDSDNWVVDELGFTDLFNQLLPTMPWNSLMNRMMKELHDHGKTIEEIKQVLRRIPIHPRVIPAIKSAHALGCELRIVSDANTLFIETIIEHLGIGEFFSEINTNPGLVDEQGRLIVSPYHDFTKSSHGCSRCPPNMCKGLIIDRIQASLTKEGKTSKMIYLGDGAGDYCPSLGLKAEDYMMPRKNFPVWDLISQNPMLVKATVRDWTDGEDMERILMEIINEIMSSEEGEENDKMLSSENCKISVGIVHEPIQVPLNLVK
Protein: Nuclear pore complex-interacting protein family member B11 (E5RHQ5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVKLSIVLTPQFLSHDQGQLTKELQQHVKSVTCPCEYLRKVINTLADHHHRGTDFGGSPWLHIIIAFPTSYKVVITLWIVYLWVSLLKTIFWSRNGHDGSTDVQQRAWRSNRRRQEGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKALCNWVRMAAAEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHCITDNSLSLKTPLECLLTPLPPSADDNLKTPPECLLTPLPPSADDNLKTPPECLLTPLPPSAPPSAPPSADDNLKTRAECLLHPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTTAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAEHLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAEHLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTTAEHLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAEHLQFRFHPQRMIISRDLPSVSSLPFHPQLHPQQMIISRYLLSICGFRFHRQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQPMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQPMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQPMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQPMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQPMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGERLWVPLPPSADDNLKTPSKRQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSKRQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPTSADDNIKTPAERLRGPLPPSADDNLKTPPLATQEAEAEKPRKPKRQRAAEMEPPPEPKRRRVGDVEPSRKPKRRRAADVEPSSPEPKRRRVGDVEPSRKPKRRRAADVEPSSPEPKRRRLS
Protein: Probable oxidoreductase (Q9I3F2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- GS catalytic domain-containing protein
- Probable aldehyde dehydrogenase
- Aminoacetaldehyde dehydrogenase
- Sarcosine oxidase alpha subunit
- Probable glutamine synthetase
- Probable glutamine synthetase
- Probable glutamine synthetase
- Probable glutamine synthetase
- GS catalytic domain-containing protein
Sequence:
MNAAIHPRPAAERAPSYYAATLNEETDYPTLLGAVTVDIAIIGGGFTGVATAVELAERGYKVALVETHRIGWGASGRNGGQVTGSLSGDAAMHKQMRQWLGAEVEDFIWHLRWRGHEIIRQRVEKYGIACDLRHGHLHAAMKASHMGELQASYEEAVRRGMGDQVVLLDKAGVQAHLETELYCGALKNTRNMHLHPLNLCIGEARAAAGLGALIFEHSEVLDIVHGPRPAVITREGRIEAQQILLAGDVYHKLERRQLKGMIFPAMGGIVTTRPLGELAREINPQGLAVYDCRFVLDYYRPTADGRLLFGGGANYSGRDSRDITAELRPCIERTFPRLKGVEIEFQWSCAMGIVMNRIPQLGKLSDNVWYCQGYSGHGVATSHIMGEIMAKAMSGSLEQFDTFARCKHLRVPLGDLFGNPMLAAGMWYYQLMEKLR
Protein: Transcription initiation factor IIF subunit alpha (TFIIF-alpha) (TFIIF large subunit) (Transcription factor G 105 kDa subunit) (P105) (P41895)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: TFIIF is a general transcription initiation factor that binds to RNA polymerase II. Its functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 14
- DNA-directed RNA polymerase II subunit RPB1
- RNA polymerase II subunit A C-terminal domain phosphatase
- Transcription initiation factor IIE subunit alpha
- Transcription initiation factor IIE subunit beta
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB2
- Transcription initiation factor IIF subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MSRRNPPGSRNGGGPTNASPFIKRDRMRRNFLRMRMGQNGSNSSSPGVPNGDNSRGSLVKKDDPEYAEEREKMLLQIGVEADAGRSNVKVKDEDPNEYNEFPLRAIPKEDLENMRTHLLKFQSKKKINPVTDFHLPVRLHRKDTRNLQFQLTRAEIVQRQKEISEYKKKAEQERSTPNSGGMNKSGTVSLNNTVKDGSQTPTVDSVTKDNTANGVNSSIPTVTGSSVPPASPTTVSAVESNGLSNGSTSAANGLDGNASTANLANGRPLVTKLEDAGPAEDPTKVGMVKYDGKEVTNEPEFEEGTMDPLADVAPDGGGRAKRGNLRRKTRQLKVLDENAKKLRFEEFYPWVMEDFDGYNTWVGSYEAGNSDSYVLLSVEDDGSFTMIPADKVYKFTARNKYATLTIDEAEKRMDKKSGEVPRWLMKHLDNIGTTTTRYDRTRRKLKAVADQQAMDEDDRDDNSEVELDYDEEFADDEEAPIIDGNEQENKESEQRIKKEMLQANAMGLRDEEAPSENEEDELFGEKKIDEDGERIKKALQKTELAALYSSDENEINPYLSESDIENKENESPVKKEEDSDTLSKSKRSSPKKQQKKATNAHVHKEPTLRVKSIKNCVIILKGDKKILKSFPEGEWNPQTTKAVDSSNNASNTVPSPIKQEEGLNSTVAEREETPAPTITEKDIIEAIGDGKVNIKEFGKFIRRKYPGAENKKLMFAIVKKLCRKVGNDHMELKKE
Protein: BcDNA.LD26050 (Windei, isoform A) (Windei, isoform B) (Q7KMH9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Histone-lysine N-methyltransferase eggless
- Uncharacterized protein, isoform C
- Protein panoramix
- Small ubiquitin-related modifier
Sequence:
MMGVNQTMELKELSTEEALMRTLSTELGNEVEPLSTPAILNESSQTSVDEVDLCELTNGVDSSDNVKVIDKPKKISDRERNPGSDLDALLDKISSIVDCSPRNSDDIDSLDRDEECDSASAKKRTAADTDENLKEQREKPEEEEEGEEVLSSLEGEECIDPDSELKTEEKLDETEEHASAKESTQKTEDLADSDEILKSKEEDEVPANTADNIEKDRKNTSTDDVFMYALDCISSADEFDAFASQDSKKAKPSKKLNTENNSSVNDLEDISSDDDDIIKETEKPNTEVIDLDSSSECVPCEAESEVEETEANTEDTEVLTHGKVSTKKSLNLQNNISEKSASAAEYESVKADQHLTEGKEPMLVGDEVTEKSKESIPIQSEESIQVDEPEESKESEELEEHKEKEEPDYCKETKDSEEATEKEKSEIKIIKASKVAQILGDTKEEEDPSPTQEVEDVKETEEPENKKEIEDTEELEEPVVIEGEETEDPQKKVQKEFDVRTADHEMNYTTIDDKLDEAVKDVVEIEEKKAAEDELGVIPKGDKEPTTNGACEISTDGNLKDLESNESTVVEEETKETESDDEVIFFEPLDKTENVGTTANPTNENSVKPQAKDDEVVLVSEDEDETPQNGISEKEVQTIQKETALKGLPNESTTESVEAKNLQIDNSDNACDQFEKLKTHDMVKQTTTEDGNSNSSNLLRPAEYAEESVPKRLRLSTDEKNEFEAETNQESLPILSRAEGGLKDVTKRSHEHLDSSPQEEIPNKKAKTEDSDSNSSHEGTLQIDMGGQEDKEESPKKDTQKKLDFDLNPVPEIKQNVKPLRLEFFKTFRRSFDTMTRDDLEELVLQKVVEAMMVKSDFAEIRMQLDKCESTLANYRRKIAEVSKQFLDLETVHKRVLKDLEAKNSHFTAPVRITRAVGLQVGIPFKAIKPTVAAPESTHAAGSVLAPPSGTPPKASTSPTRATVRPRPPPPTFGPSTSSSETGAGVSVTPNSNHQQQQPAARSSQSLTTASVTPPVRRGCLQKVTPHRPVPTNLQPAPMLMNQSSVQRLQSSPPIAQRTMHASKHTGTPGSTPSSVANAINKTVMRARNSEAAFLAQKQQQKQHQQQQQQQQQHLQQQQKQQQAQQQFLLPRPSPGPTPGSSPAKQVPKCTTKVRAKQPPLSGATVSVPISSSSSGSELGSYGQQQESSLAPAKPKEKAVIDLTDEDDAAAAAAARAAQAQNARLRMEMLKRNAQTAAATRGGRGGGNVVRASPMQLPRVNARQIVHNNGGGQQSPLGSNVTMQIRSENTPPPASRLRYSHPAPLPTSPPQPFNPSWKVPPSRPVIRISLLDTGIVISWTLEDSSPRFAECVMYQIYAYQETINEPSTDSWRHVGDVSAMLLPMAVTLNQFQENQRYYFAVRGVDSHERFGPFSVPKTWS
Protein: Transcription factor MafK (Erythroid transcription factor NF-E2 p18 subunit) (O60675)
Organism: Homo sapiens (Human)
Function: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they act as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear factor erythroid 2-related factor 2
- Transcription regulator protein BACH1
- Transcription factor NF-E2 45 kDa subunit
- Transcription regulator protein BACH2
- Transcription factor MafG
- Nuclear factor erythroid 2-related factor 3
- Endoplasmic reticulum membrane sensor NFE2L1
- Transcription factor MafF
- Heme oxygenase 1
- Histone deacetylase 3
Sequence:
MTTNPKPNKALKVKKEAGENAPVLSDDELVSMSVRELNQHLRGLTKEEVTRLKQRRRTLKNRGYAASCRIKRVTQKEELERQRVELQQEVEKLARENSSMRLELDALRSKYEALQTFARTVARGPVAPSKVATTSVITIVKSTELSSTSVPFSAAS
Protein: Transcription factor E2F8 (E2F-8) (Q58FA4)
Organism: Mus musculus (Mouse)
Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene.
Subcellular location: Nucleus {ECO:0000269|PubMed:15722552}.
Interaction partners:
- Transcription factor E2F7
- Cyclin-A2
- Kinesin-like protein KIF11
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division control protein 6 homolog
- DNA topoisomerase 2-alpha
- Disks large-associated protein 5
- Proliferation marker protein Ki-67
- Transcription factor Dp-2
- Transcription factor E2F6
Sequence:
MENQKENLFSEPHKRGLMKSPLHPSSKANMVLAEIQPDLGPLTTPTKPKEVSQGEPWTPTANLKMLISAVSPEIRSRDQKRGLSDNRSALPEARDCLHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPKYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLTKTLGTLKSVGEENKYAEQIMMIKRKEYEQEFDFIKSCGIEDHVIKSHTGQNGHSDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEIAAKILIGEDHVEDLDKSKYKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNNSGSSPIMPLPASLEAEQSAKENCAKNLFSTRGKPSFTRHPSLIKLVKSIENDRRKISSAPSSPVKSNKAESSQNSPPVPNKMAQLAAICKMQLEEQSSEPRKKVKVNLARSGHYKPLAPLDPTVNTELELLTPSLIQPLGVVPLIPSPLSSAVPVILPQAPSGPSYAIYLQPAQAQMLTPPPGLSPTVCPTQPSNATGSKDPTDAPAEKTATDAATTGSLQPAPERHGAKHRSKETTGDRGTKRMITAEDSGPSSVKKPKEDLKALENVPTPTPLFPSGYLIPLTQCSSLGPDSVLSNTENSGTPSPNHRIYGSPIAGVIPVASSELTAVNFPPFHVTPLKLMVSPTSMAAVPVGNSPALNSGHPAPAQNPSSAIVNFTLQHLGLISPGVQMSASPGPGAGTVPVSPRVEADNLSSRQRRATNHDSPVLGQSQLNGQPVAGTGAQQPVPVTPKGSQLVAENFFRTPGGPTKPTSSPYTDFDGANKTSFGTLFVPQRKLEVSTEDIH
Protein: GDSL esterase/lipase At2g04570 (EC 3.1.1.-) (Extracellular lipase At2g04570) (Q9SJB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Probable long-chain-alcohol O-fatty-acyltransferase 5
- Probable lysophospholipase BODYGUARD 3
- At1g62510
- GDSL esterase/lipase At5g62930
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Peroxidase 29
- At2g10940/F15K19.1
- CHY-type/CTCHY-type/RING-type Zinc finger protein
- At1g12030
- Non-specific lipid transfer protein GPI-anchored 31
Sequence:
MGHLKSLFTILFLIAMSSTVTFAGKIPAIIVFGDSSVDAGNNNYIPTVARSNFEPYGRDFVGGKPTGRFCNGKIATDFMSEALGLKPIIPAYLDPSYNISDFATGVTFASAATGYDNATSDVLSVLPLWKQLEYYKEYQTKLKAYQGKDRGTETIESSLYLISIGTNDFLENYFAFPGRSSQYSVSLYQDFLAGIAKEFVKKLHGLGARKISLGGLPPMGCMPLERATNIGTGGECVGRYNDIAVQFNSKLDKMVEKLSKELPGSNLVFSNPYEPFMRIIKNPSSFGFEVVGAACCATGMFEMGYGCQRNNPFTCTNADKYVFWDSFHPTQKTNHIMANALMNSTFPHFL
Protein: Subtilisin BPN' (EC 3.4.21.62) (Alkaline protease) (Subtilisin DFE) (Subtilisin Novo) (P00782)
Organism: Bacillus amyloliquefaciens (Bacillus velezensis)
Function: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.
Subcellular location: Secreted.
Interaction partners:
- Bacillolysin
- Extracellular metalloprotease.
Sequence:
MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ
Protein: Glycosyltransferase WbpL (G3XD50)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Probable NAD-dependent epimerase/dehydratase WbpK
- O-antigen polymerase
- UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase
- O-antigen chain length regulator
- Probable glycosyl transferase WbpJ
- O-antigen translocase
- UDP-N-acetyl-D-glucosamine 6-dehydrogenase
- LPS biosynthesis protein WbpG
- Probable glycosyltransferase WbpH
- UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase
Sequence:
MMIWMIACLVVLLFSFVATWGLRRYALATKLMDVPNARSSHSQPTPRGGGVAIVLVFLAALVWMLSAGSISGGWGGAMLGAGSGVALLGFLDDHGHIAARWRLLGHFSAAIWILLWTGGFPPLDVVGHAVDLGWLGHVLAVFYLVWVLNLYNFMDGIDGIASVEAIGVCVGGALIYWLTGHVAMVGIPLLLACAVAGFLIWNFPPARIFMGDAGSGFLGMVIGALAIQAAWTAPSLFWCWLILLGVFIVDATYTLIRRIARGEKFYEAHRSHAYQFASRRYASHLRVTLGVLAINTLWLLPLALMVALGWISGFIGILVAYAPLCLLAVGYKAGSLEKS
Protein: C-Mpl binding protein (La ribonucleoprotein 4) (Q96J85)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYSSSCETTRNTTGIEESTDGMILGPEDLSYQIYDVSGESNSAVSTEDLKECLKKQLEFCFSRENLSKDLYLISQMDSDQFIPIWTVANMEEIKKLTTDPDLILEVLRSSPMVQVDEKGEKVRPSHKRCIVILREIPETTPIEEVKGLFKSENCPKVISCEFAHNSNWYITFQSDTDAQQAFKYLREEVKTFQGKPIMARIKAINTFFAKNGYRLMDSSIYSHPIQTQAQYASPVFMQPVYNPHQQYSVYSIVPQSWSPNPTPYFETPLAPFPNGSFVNGFNSPGSYKTNAAAMNMGRPFQKNRVKPQFRSSGGSEHSTEGSVSLGDGQLNRYSSRNFPAERHNPTVTGHQEQTYLQKETSTLQVEQNGDYGRGR
Protein: Mitogen-activated protein kinase kinase kinase 14 (EC 2.7.11.25) (NF-kappa-beta-inducing kinase) (Serine/threonine-protein kinase NIK) (Q9WUL6)
Organism: Mus musculus (Mouse)
Function: Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner.
Subcellular location: Cytoplasm.
Interaction partners:
- TNF receptor-associated factor 2
- TNF receptor-associated factor 3
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- TNF receptor-associated factor 6
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor superfamily member 3
- Mitogen-activated protein kinase kinase kinase 7
- Mitogen-activated protein kinase kinase kinase 8
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
Sequence:
MAVMEVACPGTPGSAVGQQKELAKAKEKTQSLGKKQSCIFKLEAVEKSPVFCGKWEILNDVITKGTAKDGSEGGPPAISIIAQAECENSQEFSPTFSERIFIAGSQQYSQSESLDQIPNNVAHATEGKMARVCRRGKRHGKARKKRRKKRSKSLAQAGVALAKPLPRTPEQESCTIPVQEDESPLGNLYARNVSQFTKPLGGPGLGHLCFKKQDEGLRPVLPRPELHKLISPLQCLNHVWKLHHPQATGPRPHPTHPFPYSGMPHPFPFYPLEPWKPYMLDSAVLDKLAGVSGQRPLPGPPHLSQLAHGDSQKPLPGPHLESSCPSRGALEKVPVEEYLVHALQGSVSSGQAHSLASLAKTWSSGSAKLQRLGPETEDNEGVLLTEKLKPVDYEYREEVHWMTHQPRVGRGSFGEVHRMKDKQTGFQCAVKKVRLEVFRVEELVACAGLSSPRIVPLYGAVREGPWVNIFMELLEGGSLGQLIKQMGCLPEDRALYYLGQALEGLEYLHTRRILHGDVKADNVLLSSDGSRAALCDFGHALCLQPDGLGKSLLTGDYIPGTETHMAPEVVMGKPCDAKVDIWSSCCMMLHMLNGCHPWTQYFRGPLCLKIASEPPPIREIPPSCAPLTAQAIQEGLRKEPVHRASAMELRRKVGKALQEVGGLKSPWKGEYKEPRPPPQDQATCHQTLPTPPRENPPAKANTDGAPEPQPPLPPEPPEPSKAPALNLSKEESGTWEPLPLSSLDPATAKGPSFPDRRATLPELELQQLEIELFLNSLSQPFSLEEQEQILSCLSIDSLSLSDDSEKNPSKASQSSRDTLSSGVHSWNSQAEARTCSCSTALARGRPTDIPSYFNGVKVQIQSLNGEHLHIREFHRVKVGDIATGISSQIPATAFSLVTKDGQPVCYDMEVPDSGIDLQCTLAPDGSFAWTWRVKHGQLENRP
Protein: Microtubule-associated protein (P90973)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU000686}.
Interaction partners:
Sequence:
MSTPQSEPGSEPGSPGENENSMETQYSQGSFPEVAVEPEPEPEPEPEPEPEPEPEPEPEPEPKPKPEVEPVPQPEPEPEYQPEPEPEPEVEPEPEPEPVPEPEPEPEPEPEPVVEKEEEVVVESPPREQEPEKSGKSKPSSPIPDAPTMEDIAPRELESLNFSETSGTSDQQADRIMQNNENERVEEKKQMSPTPSQPQHKTPQRSGIRPPTAILRQPKPIPASLPRPATATPSSQRAISTPRQTASTAPSPRPISKMSRERSDVQKSTSTRSIDNVGRMTPKVNAKFVNVKSKVGSVTNHKAGGGNVEIFSEKRLYNAQSKVGSLKNATHVAGGGNVQIENRKLDFSAASPKVGSKTNYQPAKSDVKIVSEKLTWQAKSKVGSMDNAAHKPAGGNVQRSGSKSTKNDDGHNN
Protein: Nop14-like (Nucleolar protein 14) (Q6DRP8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MKKQQQKGVRGLADKVRRSKAAPEIQRNPFEVKINRKKFDVLGRKSKHDVGLPGVSRSRANQKRKETLLKELKVKGKSNKFIDRRFGEYDSKLNPEEKILQRFTLERQRLHDRRDVFNLNEDEQLTHYGQSLAELEKMPDLQDSDSDSEEKGLLSAELTATHFGGGGGLLRKKSSADGDEEQKPRSRQQLIEELILKSKQEKRERQTQKEEAQELTEKLDQQWRDIQSLLAHKTPNAERREQPDKPQLDPYDMAVRELGFEMKAQPSEKLKSAEEEAREQQRRLQDLEADRLKRMMGESEASAHTHTHISADDINDGFILDGDKRNTLTYKDGKWSMGGEEEEEEEDETAARGGEEEEEEEDEDAEGEEEEEEDEDGEDDGDLQSEGAEDDDDDGDDDEEQLRDEDEEDPPAETEEQKTEAQEAARAELPYTFTAPESYSELQCVLQGRSSEQQRLIVDRIVKCHHPSLATANKSKLQRLFGFLLEYISELTTHNPPDLRTVNTLIPQLCSLCQMFPDAACKAVQTLISDTTHTMEETLEVKGRAAMPGLDMLVLLKITALLFPTSDFRHPVTTPAFLYISQTLTKCAVVSLEDVCKGLILCCLALEFVSLSQRFFPELINFLLGLLNLAVPDKTSTGYTVVTACRARGKNCDLLLLTDTDASHSWRRKPLSLHTTHTSAEDRDHCRLSVIDSCLDLLKRCVSLYKELPSFSHIFQPIRALLHKHLPVEKYPACIQDLHREVLDAIPDQPSQHAPLVFKKKKPIPLKLFTPKIVQILDYGKKRGNTREEKERERLKHKYKREFKGALREIRKDTRFLAQEKLNHIISRDTERKRKVKELYGSLATQEGEWKALKRNKRK
Protein: Tetratricopeptide repeat protein 21B (TPR repeat protein 21B) (Intraflagellar transport 139 homolog) (Tetratricopeptide repeat-containing hedgehog modulator 1) (Q0HA38)
Organism: Mus musculus (Mouse)
Function: Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs). Essential for retrograde trafficking of IFT-1, IFT-B and GPCRs (By similarity). Negatively modulates the SHH signal transduction.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:18327258}. Note=In polarized epithelial inner medullary collecting ducts cells and in the nodes of mice at 8.0 dpc, colocalizes with alpha-tubulin in cilia. Expressed in a punctate manner throughout the axoneme from the cilia base to the tip.
Interaction partners:
- Intraflagellar transport protein 43 homolog
- Intraflagellar transport protein 122 homolog
- WD repeat-containing protein 19
- Intraflagellar transport protein 140 homolog
- WD repeat-containing protein 35
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 80 homolog
Sequence:
MDSQGLKTLINYYCQERYYHHVLLVASEGMKKYSSDPVFRFYHAYGTLMEGKAQEALREFEAIKNKQDVSLCSLMALMYVHKMSPNPDREAILELDTKMKEQRKEAGRKALYHAGLFLWHIGRHDKAREYIDRMSKMPHDSNEGPILKAWLDITRGKEPYAKKALRYFEEGLQDGNDIFALLGKVLCLEIRQNYSGALETVSQIIVNFPSFLPAFEKKMKLQLALQDWDQTVETAQRLLLQDNHNVEALRMLALYYLCREGDVEKAATKLENLGNALDVMEPQNAQLFYKITLAFSRTCGRNQLILQKVQSFLEKAFSLTPQQAEIATELGYQMILQGKVKEAWKWYRTAMTLNESNISAVTGLIRCQLIEGQLQDADQQLEFFSEFQQSMGKSAELMYLHAVLATKKNNRQDEVINLLNDVVNTHFSHLEDLPLGIQYFEKLNPDFLLEVVTEYLNLCPIQPAGPGQPLSPVLRRCSSVLETIIRSVPGLPQAVFLMAKVKYLSGDTEAAYNNLQHCLEHSPSYAEAHLLMAQVYLSQDKVKLCSQSLELCLSYNFNVREYPLYHLIKAQSQKKMGEVAEAIKTLHMAMNLPGMRRSRASSKSKHRTEVDASHRLSIFLELVEVHRLNGEQHEAAKVLQDAIHEFSGTCEELRVTIANADLALAQGDTDRALSMLRNVTTEQPYFIEAKEKMADIYLKHRKEKMLYITCYREIAERMPSPRSFLLLGDAYMNIQEPEEAIVAYEQALNQNPKDGTLARKIGKALVKTHNYSKAITYYEAALKSGQQNCLCYDLAELLLRLKLYEKAEKVLQHSLAHEPVSELSALMVDGRSQVLLAKVYSKMERPSDAIAALQQARELQARILKRVQMEQPDAVPSQKHFAAEICAEIAKHSAAQRDYEKAITFYREALVHCETDSKIMLELAQLYLAQEDLDASLRHCALLLQRDQDNEPATMLMADLMFRKQDYEQAVYHLQQLLDRKPDNFMTLSRLIDLLRRCGKLEDVPRFFLMAEKHNSRTKLEPGFQYCKGLHFWYTGEPNDALRHFNKARKDSDWGQNALYNMIEICLNPDNETIGGEVFENLNGDLGTSPEKQESVQLAVRTAEKLLKELKPQTVQGRLQLRIMENCCLMATKQKSSVEQALNTFTEIAASEKDHIPALLGMATAYMILKQTPKARNQLKRIAKMPWNPIEAEDLEKSWLLLADIYIQSAKYDMAEELLKRCLCHNRSCCKAYEYMGYIMEKEQAYTDAAFNYEMAWKHSNQTNPAVGYKLAFNYLKAKRYVDAIDVCHQVLEAHPTYPKIRKDILDKARASLRP