wanglab/gogpt-training-data huggingface dataset:
Protein: Pleckstrin homology domain containing A7 (A0A8I6A229)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MNLRSAWATVYHNQQTTTFRHPVTGQFSSENSEYVLREEPHPHMSKQERNQRPSSMVSETSTAGTTSTLEAKPGPKIIKSSSKVHSFGKRDQAIRRNLNVPVVVRGWLHKQDSSGMRLWKRRWFVLADYCLFYYKDSREEAVLGSIPLPSYVISPVAPEDRISRKYSFKAVHTGMRALIYSTTTAGSQAEHSGMRTYYFSADTLEDMNAWVRAMNQAAQVLSRSSLKRDKVERQAMPQANHTDACQECGHVGPGHSRDCPRRGYEDAIVFDRREQEEERFRSQRDTLEGRRDRSKARSPYLPAEEDALFVDLPGGPRGQQAQPQRAERNGLPPYGLGEQNGTSGYSRTAPPRANLEKHSQRKTNLAQTEHWAKAQKGDGRSLPLDQTLPRQGPSQPPSFLENYQTLPRNTRYPSGSSSPPPRNLPSDYKYAQDRASHLKMSSEERRAHRDGTVWQLYEWQQRQQFRHGSPTAPIGAGSPEFTEQGRSRSLLEVPRSISVPPSPSDIPPPGPPRPFPPRRPHTPAERVTVKPPDQRRSVDISLGGSPRKARGHAVKNSSHVDRRSMPSMGYMTHTVSAPSLHGKSADDTYLQLKKDLEYLDLKMTGRDLLKDRSLKPMKIAESDTDVKLSIFCEQDRILQDLEDKIRALKENKDQLESVLEVLHRQTEQYRDQPQHLEKITCQQRLLQEDLVHIRAELCRESTEMENAWNEYLKLEKDVEQLKQTLQEQHRRAFFFQEKSQIQKDLWRIEDVMAGLSVNKENYRVLVGSVKNPERKTVPLFPHPSVPSLSPTESKPALQPSPPTSPVRTPLEVRLFPQLQTYVPYRPHPPQLRKVVSPLQSPTKATPQAEDEAPPRPPLPELYSPEDQPPAVPPLPREATIIRHTSVRGLKRQSDERKRDREQGQCVNGDLKVELRSYVSEPELASFSGDVPRPSLGLVGSESRYQTLPGRGLSGSTSRLQQSSTIAPYVTLRRGLNAENSSVTFSRPKSALERLYSGDHQRGKMSAEEQLERMKRHQKALVRERKRTLSQGERTGLLSARYLSQPLPGDLGSVC
Protein: RH02809p (Stathmin, isoform C) (Stathmin-14) (Q9GQR5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVNNTVDTEATEIRCQEKSRGGLSYEVILAEPAPNVAVPKRPVTPGKNVSVEEIEQKLKAAEERRISLEAKKMADISTKLAKVEEATRKKDEITNEFITQTKEQLESKMELHVEKREAIISDMKEKLKIHAQDIEKTRETLEQQKANEQKAIEEKLKIAQSLRDENIKKMLDRLKEHNTIKIAEIKSQNDQLECQKIEEKARIYENKLFAAEQKREKELQKKIEKVQKLERRAELVRQNKAQAQDLDGQQSAIASSG
Protein: Cholecystokinin (CCK) [Cleaved into: Cholecystokinin-58 (CCK58); Cholecystokinin-58 desnonopeptide ((1-49)-CCK58); Cholecystokinin-39 (CCK39); Cholecystokinin-33 (CCK33); Cholecystokinin-25 (CCK25); Cholecystokinin-18 (CCK18); Cholecystokinin-12 (CCK12); Cholecystokinin-8 (CCK8); Cholecystokinin-7 (CCK7); Cholecystokinin-5 (CCK5)] (P41520)
Organism: Bos taurus (Bovine)
Function: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P09240}.
Interaction partners:
- Gastrin/cholecystokinin type B receptor
- Cholecystokinin A receptor
- Pro-neuropeptide Y
- Gastrin
- Somatostatin
- Appetite-regulating hormone
- Promotilin
- Pro-glucagon
- Annexin A5
- Agouti-related protein
Sequence:
MNRGVCLCLLMAVLAAGALAQPMPHADPTGPRAQQAEEAPRRQLRAVPRVDDEPRAQLGALLARYIQQARKAPSGRMSVIKNLQSLDPSHRISDRDYMGWMDFGRRSAEEFEYTS
Protein: Vesicle-associated membrane protein 723 (AtVAMP723) (Q8VY69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
Interaction partners:
- Syntaxin-81
- Syntaxin-73
- Syntaxin-72
- 25.3 kDa vesicle transport protein SEC22-1
- SNAP25 homologous protein SNAP33
- Putative SNAP25 homologous protein SNAP30
- SNAP25 homologous protein SNAP29
- At3g24315
- Syntaxin-23
- Syntaxin-22
Sequence:
MAQQSLFYSFIARGTVILVEFTDFKGNFTSVAAQYLENLPSSNNKFTYNCDGHTFNDLVENGFTYCVVAVDSAGREIPMAFLERVKEDFYKRYGGEKAATDQANSLNKEFGSNLKEHMQYCMDHPDEISNLAKAKAQVSEVKSLMMENIEKVLARGVICEMLGSSESQPQAFYIKRTQMKRKKWFQNMKIKLIVLAIIIALILIIILSVCGGFNCGK
Protein: Inositol-3-phosphate synthase (MIP synthase) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (IPS) (MI-1-P synthase) (Q8NLE6)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3-phosphate in a NAD-dependent manner. Plays a key role in oxidative stress resistance as its product is the precursor of the protective antioxidant mycothiol (MSH or AcCys-GlcN-Ins).
Interaction partners:
- Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family
- Inositol-1-monophosphatase
- Phosphoglucomutase
- Glucokinase
- Transcriptional regulators
- Phosphatidylinositol phosphate synthase
- Dystroglycan-type cadherin-like domain-containing protein
Sequence:
MSTSTIRVAIAGVGNCATSLIQGVEYYRNADPSETVPGLMHVKFGDYHVGDIEFVAAFDVDAEKVGIDLADATEASQNCTIKIADVPQTGINVLRGPTLDGLGDHYRATIDESTAEPVDVVQALIDAKADVLVSYLPVGSEEADKFYAQAAIDAGCAFVNALPVFIASDPEWAKKFTDAGIPIVGDDIKSQIGATITHRVLARLFEERGVRVDRTMQLNVGGNMDFKNMLDRNRLESKKVSKTQAVTSNIPDGPLSGKVEDRNVHIGPSDHVQWLDDRKWAYVRLEGTAFGGVPLNLEYKLEVWDSPNSAGIIIDAVRAAKIALDRGIGGPIMPASSYLMKSPPEQLPDDVARERLEAFIIEA
Protein: Heat shock transcription factor, Y-linked (Heat shock transcription factor 2-like protein) (HSF2-like) (Q96LI6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:15044259}. Cytoplasm {ECO:0000269|PubMed:15044259}.
Interaction partners:
- Chorion-specific transcription factor GCMb
- Testis-specific Y-encoded protein 1
- RNA-binding motif protein, Y chromosome, family 1 member A1
- Testis-specific basic protein Y 2
- Testis-specific chromodomain protein Y 2
- Testis-specific basic protein Y 1
- Testis-specific chromodomain protein Y 1
- Deleted in azoospermia protein 1
Sequence:
MAHVSSETQDVSPKDELTASEASTRSPLCEHTFPGDSDLRSMIEEHAFQVLSQGSLLESPSYTVCVSEPDKDDDFLSLNFPRKLWKIVESDQFKSISWDENGTCIVINEELFKKEILETKAPYRIFQTDAIKSFVRQLNLYGFSKIQQNFQRSAFLATFLSEEKESSVLSKLKFYYNPNFKRGYPQLLVRVKRRIGVKNASPISTLFNEDFNKKHFRAGANMENHNSALAAEASEESLFSASKNLNMPLTRESSVRQIIANSSVPIRSGFPPPSPSTSVGPSEQIATDQHAILNQLTTIHMHSHSTYMQARGHIVNFITTTTSQYHIISPLQNGYFGLTVEPSAVPTRYPLVSVNEAPYRNMLPAGNPWLQMPTIADRSAAPHSRLALQPSPLDKYHPNYN
Protein: EMBRYO SURROUNDING FACTOR 1.3 (Maternally expressed family protein 1.3) (Maternally expressed gene 1.3) (A8MQA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Maternally-contributed central cell peptide regulating suspensor development and correct auxin distribution in early developing embryos.
Interaction partners:
- EMBRYO SURROUNDING FACTOR 1-like protein 6
- F-box associated ubiquitination effector family protein
- Similarity to tapetum-specific protein
- At4g20420
- EMBRYO SURROUNDING FACTOR 1-like protein 9
- EMBRYO SURROUNDING FACTOR 1-like protein 8
- EMBRYO SURROUNDING FACTOR 1-like protein 10
- Uncharacterized protein AT4g11020
- Transmembrane protein
- Transmembrane protein
Sequence:
MKSSHTTLICIIMLSLFALHECEKMEVKEIGRSSKIILPACMHETCSGGFSLKNDCWCCLRLKTKQARCWKEKEFPNAKELCFANCPPLE
Protein: Cyclic AMP-dependent transcription factor ATF-7 (cAMP-dependent transcription factor ATF-7) (Activating transcription factor 7) (Transcription factor ATF-A) (Q8R0S1)
Organism: Mus musculus (Mouse)
Function: Stress-responsive chromatin regulator that plays a role in various biological processes including innate immunological memory, adipocyte differentiation or telomerase regulation. In absence of stress, contributes to the formation of heterochromatin and heterochromatin-like structure by recruiting histone H3K9 tri- and di-methyltransferases thus silencing the transcription of target genes such as Htr5b, STAT1 in adipocytes, or genes involved in innate immunity in macrophages and adipocytes. Phosphorylation of ATF7 disrupts interactions with histone methyltransferase and enhances the association with coactivators containing histone acetyltransferase and/or histone demethylase, leading to disruption of the heterochromatin-like structure and subsequently transcriptional activation. In response to TNF-alpha, which is induced by various stresses, phosphorylated ATF7 and telomerase are released from telomeres leading to telomere shortening. Also plays a role in maintaining epithelial regenerative capacity and protecting against cell death during intestinal epithelial damage and repair.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:19893493}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P17544}. Chromosome, telomere {ECO:0000269|PubMed:29490055}. Note=Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear peiphery. {ECO:0000250|UniProtKB:P17544}.
Interaction partners:
- Protein c-Fos
- Transcription factor Jun
Sequence:
MGDDRPFVCSAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKASDDDEKKGAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTTKPVVISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQIGSPTGSLPLVMHLANGQTMPMLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNNSGSISPSGHPMPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQNQILIQHPDAPSPAQPQVSPAQPTPSTGGRRRRTVDEDPDERRQRFLERNRAAASRCRQKRKLWVSSLEKKAEELTSQNIQLSNEVTLLRNEVAQLKQLLLAHKDCPVTALQKKTQGYLGK
Protein: GH06387p (Syntaxin 17, isoform A) (Q9VZC9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTRDEKLPLKQAEVSIQRFQDVAVPHHLSLLKNHRSNIEKSLALGDWQKIKKEELNAMRVIKQIKNLLLEMDALREKVREEDLERFDDLMKPGRDTAFAGMKEFAELQLKSPTSTLSSQYDDDLDNQPQEVDMNSLPAHRHMPQLQLNFQLEEHQLAQRQACLDQMENLQQEIYDLHGMFQGMRQLTAEQSVAVEKIADNAEEALENVQQGELNLRRALTYKKAMYPVVGALLGTCVGGPIGLVAGMKAGGLAAVGCGILGFTGGSVLKANPNVMHGNIEEEQVEPDSESTERLELKEKPE
Protein: Undifferentiated embryonic cell transcription factor 1 (Q6J1H4)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional coactivator of ATF2.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein NANOG
- Steroid hormone receptor ERR2
- POU domain, class 5, transcription factor 1
- Developmental pluripotency-associated protein 3
- Sal-like protein 4
- Developmental pluripotency-associated protein 4
- Myc proto-oncogene protein
- Transcription factor SOX-2
- Developmental pluripotency-associated protein 5A
- Zinc finger protein 42
Sequence:
MLLRPRRLPAFSPPSPASPDAELRSAGDVPVTTSDAFATSGGMAEPGSPKAPVSPDSAQRTPWSARETELLLGTLLQPAMWRSLLLDRRQTLPTYRRVSAALARQQVRRTPAQCRRRYKFLKDKLRDSQGQPSGPFDNQIRQLMGLLGDDGPPRVRRRSTGPGRPQRRGRSSLSALAPAPAPVEQEAELPLAAENDEPAPALRFSSSTTKSAGAHRITSSPPLTSTDTLPPEPGHTFESSPTPTPDHDVETPNEPPGLSQGRASSPQVAPQSLNTALLQTLTHLGDISTVLGPLRDQLSTLNQHVEHLRGSFDQTVSLAVGFILGSAASERGILGDLRQ
Protein: Beta-1,6-glucan synthesis-associated protein KEG1 (KRE6-binding ER protein responsible for glucan synthesis protein 1) (P43614)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the biosynthesis of (1->6)-beta-D-glucan polymers of the cell wall. Required for viability. Involved in maintaining chromosome stability.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17893149}; Multi-pass membrane protein {ECO:0000269|PubMed:17893149}.
Interaction partners:
- Beta-glucan synthesis-associated protein KRE6
- Protein ROT1
- Killer toxin-resistance protein 5
- Calnexin homolog
Sequence:
MAGIKLTHKLYQYYQLATSFLYAALLIRWLILMPLVGSRFLPGGIHEFLIYLMFYSSIMEVIWLLRFHGFKYGLLSRTFLKDLNFIYLVSVIHFYDDYEHALILKNASYSSFIISLSLSQAYCHWCKLFKRKGVKERTLVWKVNTFVTLPILYLSEFALLLLNIQVKNYHSTPTLDIINRVVLLAYFPVLLTAYKKLLTK
Protein: Elongator complex protein 4 (A0A1W2PP47)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQQIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIERLHLPPDLSDTVSRSSKMDLAESAKRLGPGCGMMAGGKKHLDF
Protein: Ubiquitin-like-specific protease 1D (EC 3.4.22.-) (Protein OVERLY TOLERANT TO SALT 1) (Q2PS26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins. Cleaves precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2 from conjugates, but unable to cleave SUM3. Protease activity mainly directed at deconjugating SUM1 and SUM2 from their target proteins. Regulates salt stress responses and flowering time. Redundant with ULP1C.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:18849491}.
Interaction partners:
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 3
- SUMO-conjugating enzyme SCE1
- SUMO-activating enzyme subunit 2
- E3 SUMO-protein ligase SIZ1
- E3 SUMO-protein ligase MMS21
- Small ubiquitin-related modifier 5
- E4 SUMO-protein ligase PIAL1
- Translation initiation factor IF-2
Sequence:
MTKRKKEVIDVDCSEKKDFVIDWSSAMDKEDEVPELEIVNTTKPTPPPPPTFFSDDQTDSPKLLTDRDLDEQLERKKAILTLGPGLPDKGEKIRLKIADLEEEKQRRVLEGSKMEVDRSSKVVSSTSSGSDVLPQGNAVSKDTSRGNADSKDTSRQGNADSKEVSRSTFSAVFSKPKTDSQSKKAFGKELEDLGCERRKHKAGRKPVTRLSNGWRLLPDVGKAEHSAKQFDSGLKESKGNKKSKEPYGKKRPMESSTYSLIDDDDDDDDDDDNDTSGHETPREWSWEKSPSQSSRRRKKSEDTVINVDEEEAQPSTVAEQAAELPEGLQEDICYPTRDDPHFVQVCLKDLECLAPREYLTSPVMNFYMRFLQQQISSSNQISADCHFFNTYFYKKLSDAVTYKGNDKDAFFVRFRRWWKGIDLFRKAYIFIPIHEDLHWSLVIVCIPDKKDESGLTILHLDSLGLHSRKSIVENVKRFLKDEWNYLNQDDYSLDLPISEKVWKNLPRRISEAVVQVPQQKNDFDCGPFVLFFIKRFIEEAPQRLKRKDLGMFDKKWFRPDEASALRIKIRNTLIELFRVSDQTE
Protein: Probable endo-beta-1,4-glucanase B (Endoglucanase B) (EC 3.2.1.4) (Carboxymethylcellulase B) (Cellulase B) (A2QPC3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MKFQSTLLLAAAAGSALAVPHGSGHKKRASVFEWFGSNESGAEFGTNIPGVWGTDYIFPDPSTISTLIGKGMNFFRVQFMMERLLPDSMTGSYDEEYLANLTTVVKAVTDGGAHALIDPHNYGRYNGEIISSTSDFQTFWQNLAGQYKDNDLVMFDTNNEYYDMDQDLVLNLNQAAINGIRAAGASQYIFVEGNSWTGAWTWVDVNDNMKNLTDPEDKIVYEMHQYLDSDGSGTSETCVSGTIGKERITDATQWLKDNKKVGFIGEYAGGSNDVCRSAVSGMLEYMANNTDVWKGASWWAAGPWWGDYIFSLEPPDGTAYTGMLDILETYL
Protein: CAD protein (EC 2.1.3.2) (Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) (U3JAV8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Amidophosphoribosyltransferase
- Dihydroorotate dehydrogenase
- ornithine carbamoyltransferase
- Glutamine synthetase
- Glutamine synthetase
- Glutamine synthetase
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase
- Argininosuccinate synthase
- Adenylosuccinate synthetase isozyme 1
Sequence:
MSLKMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEDGEFGLSKWFESSQIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIPFDNPDARNLVKEVSMKAPKVFNPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLDSNDFDGLFISNGPGNPEYCKETVENIRKVACVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVRDVKENKAGKSVKQRLMEHLTFPGSPDPNAFVRPRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVLLTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHTSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVGFDHTIKPESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDESAMPPEIMRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVFEQPHVMVIGSGVYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPNNIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGEVIAIAVSEHVENAGVHSGDATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVGLMRGNGIVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEEESDCPNKDKQRNIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRMAIDFSVPLITDIKCTKLFVQALKQIGQAPRVKTHVDSMTSQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNAALLPSIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWPKHLPIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDKAQVRPMLGTREDMEALWENLDIIDCFATDHAPHSAEEKISEKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPGYGQDVKSWSATPTATTEVIMDAPKRVIEAMTPERPRQAAPVDVVRSRAPSPRRSAGDGRFILPPRIHRSSDPGLPPELALPAEAYAHPPPLARILSPQAGQPQILPHPQTSPLLHPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLARLLTQYRITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSSEKEYNACFGQFILTPHIMTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR
Protein: S-layer protein EA1 (P94217)
Organism: Bacillus anthracis
Function: The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria.
Subcellular location: Secreted, cell wall, S-layer.
Interaction partners:
- Polysaccharide pyruvyl transferase CsaB
- Transcriptional regulator, ArsR family
- N-acetylmuramoyl-L-alanine amidase
Sequence:
MAKTNSYKKVIAGTMTAAMVAGIVSPVAAAGKSFPDVPAGHWAEGSINYLVDKGAITGKPDGTYGPTESIDRASAAVIFTKILNLPVDENAQPSFKDAKNIWSSKYIAAVEKAGVVKGDGKENFYPEGKIDRASFASMLVSAYNLKDKVNGELVTTFEDLLDHWGEEKANILINLGISVGTGGKWEPNKSVSRAEAAQFIALTDKKYGKKDNAQAYVTDVKVSEPTKLTLTGTGLDKLSADDVTLEGDKAVAIEASTDGTSAVVTLGGKVAPNKDLTVKVKNQSFVTKFVYEVKKLAVEKLTFDDDRAGQAIAFKLNDEKGNADVEYLNLANHDVKFVANNLDGSPANIFEGGEATSTTGKLAVGIKQGDYKVEVQVTKRGGLTVSNTGIITVKNLDTPASAIKNVVFALDADNDGVVNYGSKLSGKDFALNSQNLVVGEKASLNKLVATIAGEDKVVDPGSISIKSSNHGIISVVNNYITAEAAGEATLTIKVGDVTKDVKFKVTTDSRKLVSVKANPDKLQVVQNKTLPVTFVTTDQYGDPFGANTAAIKEVLPKTGVVAEGGLDVVTTDSGSIGTKTIGVTGNDVGEGTVHFQNGNGATLGSLYVNVTEGNVAFKNFELVSKVGQYGQSPDTKLDLNVSTTVEYQLSKYTSDRVYSDPENLEGYEVESKNLAVADAKIVGNKVVVTGKTPGKVDIHLTKNGATAGKATVEIVQETIAIKSVNFKPVQTENFVEKKINIGTVLELEKSNLDDIVKGINLTKETQHKVRVVKSGAEQGKLYLDRNGDAVFNAGDVKLGDVTVSQTSDSALPNFKADLYDTLTTKYTDKGTLVFKVLKDKDVITSEIGSQAVHVNVLNNPNL
Protein: Small ribosomal subunit protein uS12cz/uS12cy (30S ribosomal protein S12, chloroplastic) (P12149)
Organism: Oryza sativa subsp. japonica (Rice)
Function: With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity).
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Os01g0220300 protein
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein uS2c
- Large ribosomal subunit protein bL27c
- Os10g0411700 protein
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein bS16c
- Small ribosomal subunit protein uS9c
- Os02g0102400 protein
- Os07g0658200 protein
Sequence:
MPTVKQLIRNARQPIRNARKSAALKGCPQRRGTCARVYTINPKKPNSALRKVARVRLTSGFEITAYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYRIIRGALDAVAVKNRQQGRSKYGVKKPKK
Protein: Tyrosine-protein kinase Btk (EC 2.7.10.2) (Dsrc28C) (Dsrc29a) (P08630)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for proper ring canal development. Also required for the development of male genitalia and for adult survival.
Interaction partners:
- Downstream of kinase
- Protein vav
- Tyrosine-protein kinase Src64B
- Caspase-8
- Guanine nucleotide-binding protein subunit alpha homolog
- SH3 domain-binding protein 5 homolog
- Uncharacterized protein, isoform G
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MMGTKHRNSHVNGSIKSSSSLRSSSKSFQAKMDLMSERLYDVVKSGSMVKRAQNKKRFTPVNYKHRWFELTKRTFSYFDVENVERRRERGRIHLKGVRLVEEATVSGEGGDPFAPDGYPFQVGYCEISASANSHQLENGNGGGSGVGIEGQQSGRAVPQYTLYVIANSEKERSEWIRAIRQVCEDSNTPKSYRYHPGLWSGKKWSCCKGLSRTTFGCRAAAHWREANNNPSNGSSPAQNSTRSISPNSSTTNSQFSLQHNSSGSLGGGVGGGLGGGGSLGLGGGGGGGGSCTPTSLQPQSSLTTFKQSPTLLNGNGTLLDANMPGGIPTPGTPNSKAKDNSHFVKLVVALYPFKAIEGGDLSLEKNAEYEVIDDSQEHWWKVKDALGNVGYIPSNYVKPKALLGLERYEWYVGDMSRQRAESLLKQGDKEGCFVVRKSSTKGLYTLSLHTKVPQSHVKHYHIKQNARCEYYLSEKHCCETIPDLINYHRHNSGGLACRLKSSPCDRPVPPTAGLSHDKWEIHPMELMLMEELGSGQFGVVRRGKWRGSIDTAVKMMKEGTMSEDDFIEEAKVMTKLQHPNLVQLYGVCSKHRPIYIVTEYMKHGSLLNYLRRHEKTLIGNMGLLLDMCIQVSKGMTYLERHNYIHRDLAARNCLVGSENVVKVADFGLARYVLDDQYTSSGGTKFPIKWAPPEVLNYTRFSSKSDVWAYGVLMWEIFTCGKMPYGRLKNTEVVERVQRGIILEKPKSCAKEIYDVMKLCWSHGPEERPAFRVLMDQLALVAQTLTD
Protein: Electron transfer flavoprotein beta subunit lysine methyltransferase (EC 2.1.1.-) (ETFB lysine methyltransferase) (ETFB-KMT) (Protein N-lysine methyltransferase METTL20) (Q80ZM3)
Organism: Mus musculus (Mouse)
Function: Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8IXQ9}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IXQ9}. Note=Concentrated in cytoplasmic granular foci. {ECO:0000250|UniProtKB:Q8IXQ9}.
Interaction partners:
- Electron transfer flavoprotein subunit beta
- EEF1A lysine methyltransferase 2
- Protein N-lysine methyltransferase METTL21D
- Methyltransferase-like protein 22
- Histidine protein methyltransferase 1 homolog
- Protein N-lysine methyltransferase METTL21A
- DNA/RNA-binding protein KIN17
- Protein-lysine N-methyltransferase EEF2KMT
Sequence:
MAFSLCWKAPRSPWSFLQAVNNGSPLFLWRTVGSCLDPKMKAYLEENTEVTSSGSLTPEIQLRLLTPRCKFWWERADLWPYSDPYWAIYWPGGQALSRYLLDNPAVVRGKSVLDLGSGCGATAIAAKMSGASKILANDIDPIAGMAITLNCKLNGLNPFPVLTKNILNTQQGKFDLIVLGDMFYDEDLADSLHLWLQNYFWTHGTRVLIGDPGRPQFSGHSIRHQLYQLVEYTLPEPTQQENNGLTTSAVWDFHP
Protein: Pre-mRNA polyadenylation factor fip1 (Q09801)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- mRNA cleavage and polyadenylation specificity factor complex subunit pta1
- Protein cft1
- Polyadenylation factor subunit 2
- mRNA 3'-end-processing protein yth1
- Endoribonuclease ysh1
- Poly
- Cleavage factor two protein 2
- RNA polymerase II subunit A C-terminal domain phosphatase ssu72
- mRNA 3'-end-processing protein rna14
- Uncharacterized WD repeat-containing protein C824.04
Sequence:
MSNADQHMDVDEDEYLYGETIEERNDGVTVSNAKSPEQASEESDDSDIEFIIETKPGERAEPLGGSIATLGSTRPSAKPQVEKTAVEVKTTEPQDLSTAETAPKVDIDAVPTIDGKNIFEIDLESFDDKPWRKPGADISDYFNYGFDEFTWAAYCAKQTTLRDDFSPQKFMASLAQIPGPLPSGNVPSPAEFQAMMASGFPPFMPIPPPIGGPQEDMGYSRNFPVHASSNYNTTHTSGGGVHSGAATPNAYVNNNPSSSRRESESPANSPNITSSAGMTHAQPTHNPTSSYGNGASTNYNASRPPSNHPHSSNYPSSSRRKPSPDRYSNYSSRGSGGRYRRNRY