wanglab/gogpt-training-data huggingface dataset:
Protein: MYND-type zinc finger protein C31F10.10c (P87311)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized transcriptional regulatory protein C3C7.04
- LisH domain-containing protein C1711.05
- Putative splicing factor C222.18
- Uncharacterized RNA-binding protein C126.11c
- Transposon Tf2-1 polyprotein
- Uncharacterized oxidoreductase C663.08c
Sequence:
MRESNVSIVWNNKASVTINTVLYDRRALDCDSEMSLMNSLSHLVYLTSTSPKIREILTMDGGLMRLMNILRAGRGQTFARMTIWQLALQCVVNVGIRGSEAIRIRVVEAGIVPIVVTLLDDFLFALESVVSHHSRFQFSLTPSTTPPPSSASAPFPINSNISNSLDSVSQHNSSADSLFVNGDVPSPFGASTASSSSRRVYSVDLRDSGDVQLPNQSTFRHSVNRDLLGSSSTTSHDRSSGSIYSNDSFQDPRVQANSPLTIQRISSAAPSTPTSTENVNYNMTTPSSPSYSRQTGPASETINDEIDSPNFFFPTPLNIMTTTQDSSRDVQLSLNNVQSQALNNRQRRNQLLPGVPSTSALLDGRRPENVVDYHGIASFFDNFDKKINKLPREEDILFGLQILAYTSKNYFHMRPYFESSKDVPSLRMSPLRSGSKTWNIFQLVEQFTLKFYPPQVQYWARAIMNNYCRKDESHGGIRRCANLLCNKWEEHSRQFAKCRRCRRTKYCSKECQHQAWPGHSRWCRVIHKDGRNSKRESSKINSVTESESTASPAASVIPVGTESVTSSTQSDSRL
Protein: Fatty acid synthase (EC 1.1.1.100) (EC 1.3.1.39) (EC 2.3.1.41) (EC 2.3.1.85) (EC 3.1.2.14) (M9PB21)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Acetyl-CoA carboxylase, isoform A
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Probable malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- ATP-citrate synthase
- long-chain-fatty-acid--CoA ligase
- 3-oxoacyl-[acyl-carrier-protein] synthase
- Long-chain-fatty-acid--CoA ligase
- Fatty acid synthase
- Very long-chain-fatty-acid--CoA ligase bubblegum
- Long-chain-fatty-acid--CoA ligase heimdall
Sequence:
MPSRKKAQGESAAGEDADIVISGLSGKLPESSNIEEFKYNLLNGIDMVTDEPRRWEAGIYGLPERMAKMKDSDLEKFDDKFFSVHQKQAELMDPCMRMLLELTHEAIIDAGINPVQLRGSRTGVYIGLSFVETEHEIPNMEPSSINGYCLTGCARAMFANRISYTFDFKGPSFIVDTACSSSLVALNHAFADMRAGRCDYALVAGVNLILKPIFALQFLRLGIVSHDGSCKTFDAAANGYARADTCAVVLLQRRKEAKRVYASILNVRTNTDGFKEQGVTFPDGRMQQALLEETYSEIGLNPDEVVYVEAHGSGTPVGDDQEANMLSNFFCRPSRSTPLLIGSVKSNMGHAEPASGVSALAKMIIAMEEGIIPKNLHYRTPNPSVPALVEGKLKVVDRNLPWQGGIVGLNSFGFGGANAHVVLKSHTKAKEPKACPKAGEAEQSLSLVTCSGRTEDAVNQLLKVATEQRHDQELLTLINDIHSHPIPLHPFRGYAVLGTSGCVKEEVLPYEEEERPIWFVYAGMGSQWARMAKDLMQLEVFRNSIQHCAEVLAQVDFDLIDVLTRSTERTFDNMLYSFVSVSAVQVALTDLLRVLDIRPDGIIGHSAGELGAAYMDGCLTAEQTVLAAYWRGRSVLDTPDLPRGKMAAVGLSWEQIGSQIPKDCYPVCHNSDDNCTVSGPPSSMDAMIEDLTAKGIFVREVGSGGYAFHSPYIEGAAPMLRRSLERLITEPKKKSIRWLSTSVKEAEWDSEKNHLASAGYFINNLISPVLFHQAVKRIPQNALIVEIAPHGLFRAILRSLSPQISYVSLMQRGHANNFEFLLSQLGRLYAAGGQPQILKISPSIPYPVSRGTPMLGSLVGWDHTQKWNYPKFKGGRQAGQLSVELDLGKEENVYLAGHTIDGRVLFPATGYMTLAWMSLAQQQGLDYLRTPVLFEDVVFHRATILSVGTVVKLTLNFFPGSSSFEICEGTSLVTSGKIRLVSNVQQEQLQLSSLPGIAGSNKLSTKDIYKELRLRGYDYTGVFQGILESDISAVTGQLQWADNWISFMDTMLQFRILSNDIRELYVPTGIERALIDPLKHLELAKKHQQKLTVNWHRNISVVKCGGVEIHKMKTAQTQRRSGGQSPPSLERYRFWPHSQHLGQREEQEKSRSTALAVAIQLIIENSGGAVKLKGVELAGSRSTLDALSAVQLLELIEREPILVGDMAVVTSSSNESELGEQLKEHGIRVIVKDIKAGAVEQQCHFVYSVNMLAQNSVKDLQHCLDSLKSDSGFLLLEEAASRYNIIGKEKLNKLKLVSVLEQFFGTDRVLVLVRKLSKVQSSQALTLHLTNKQFKWVNELKNSIAKAQAEEKNLYLVAQGEPNSGALGLMNCLKREAGGHFLRLYLILDEGVPQFSLDDPFYAAQLAKDLVVNVYRNGSWGSYRHLKMESRPPMLPVEQAYVNTLVKGDLSSLRWIESPRSSPIQSQLEPCTVYYAPLNFRDVMLASGKLGVDALPGDLAYQDCVLGLEFAGRDSCGRRVMAMVTAKSLATNCLANRNLLWEVPSKWTMEQASTVPCVYATVYYALVVRGQMKEGERILIHAGSGGVGQAAISVALAHGLTVFTTVGSKEKREFLLKRFPKLKAKNIGNSRDTSFEQLIMSETHGNGVELVLNSLSEEKLQASIRCLALNGRFLEIGKFDLSNNTPLGMSVFLKNTSFHGILLDSVMEGEEEMQLMVAKLVAEGIKSGAVQPLPTTVFAEQEIEKAFRFMASGKHIGKVVIKVRLEEEQQAALPRLRQIQAIPRSYMHPEKSYILVGGLGGFGLELANWLVSRGARFLVLSSRSGVKSGYQALMIRRWHDRGVQVQIDTNDVTTAVGCQRLLEVSNKLALVGGIFNLAAVLRDGLIEDQSPKNFEKVSAPKLLATIHLDKISREICPALEYFVCFSSLSCGRGNMGQTNYGLANSTMERICEQRQEYGYPGTAIQWGAIGDTGLIIEHMGNNETVVGGTLPQRMISCLETLDLFLQQPHPVMASMVVAEKRKTEQANRLSLIATIANIMGLRDVKSVSDKTTLFDLGMDSLMSTEIKQTLERHFDLVLSAQEIRQLTFSALRQIDAQEPPSASVSSPSASSTLSRIKEEACVEVQPQSDETRKVFAKEVLPQEVMVRLRSKAPVASEDPAVFFLAPIEGFTIAVEALAASLTCPAYGLQCTEQVPLDSIEACAAYYLRQIQKLQPLGPYHIVGYSYGCLLAHAIAVALEQRRFGVKVIMLDGAPTMASGYVQEAKKQTDDLNRQQSMTLAYFGALLADVDYNQVLLQLLDGVQTWPSKLDKLADTLAGYTQQTREVIKKAACMFKQKLLLSESYKGAKQLHSDVVLIKSAEHNAIMAQDYGLKEICSAQIDMHVVEGTHRTFLKEPHTLQIIERVLRKRP
Protein: Unconventional myosin-VIIb (Q6PIF6)
Organism: Homo sapiens (Human)
Function: Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli (Probable).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, microvillus {ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:32209652}. Note=Enriched in the microvilli of the intestinal brush border. {ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:32209652}.
Interaction partners:
- Harmonin
- Ankyrin repeat and SAM domain-containing protein 4B
- Cadherin-related family member 2
- Cadherin-related family member 5
- pre-mRNA splicing regulator USH1G
Sequence:
MSGFRLGDHVWLEPPSTHKTGVAIGGIIKEAKPGKVLVEDDEGKEHWIRAEDFGVLSPMHPNSVQGVDDMIRLGDLNEAGMVHNLLIRYQQHKIYTYTGSILVAVNPFQVLPLYTLEQVQLYYSRHMGELPPHVFAIANNCYFSMKRNKRDQCCIISGESGAGKTETTKLILQFLATISGQHSWIEQQVLEANPILEAFGNAKTIRNDNSSRFGKYIDIYFNPSGVIEGARIEQFLLEKSRVCRQAPEERNYHIFYCMLMGVSAEDKQLLSLGTPSEYHYLTMGNCTSCEGLNDAKDYAHIRSAMKILQFSDSESWDVIKLLAAILHLGNVGFMASVFENLDASDVMETPAFPTVMKLLEVQHQELRDCLIKHTILIRGEFVTRSLNIAQAADRRDAFVKGIYGHLFLWIVKKINAAIFTPPAQDPKNVRRAIGLLDIFGFENFENNSFEQLCINFANEHLQQFFVQHVFTMEQEEYRSENISWDYIHYTDNRPTLDLLALKPMSIISLLDEESRFPQGTDLTMLQKLNSVHANNKAFLQPKNIHDARFGIAHFAGEVYYQAEGFLEKNRDVLSTDILTLVYSSKNKFLREIFNLELAETKLGHGTIRQAKAGNHLFKSADSNKRPSTLGSQFKQSLDQLMKILTNCQPYFIRCIKPNEYKKPLLFDRELCLRQLRYSGMMETVHIRKSGFPIRYTFEEFSQRFGVLLPNAMRMQLQGKLRQMTLGITDVWLRTDKDWKAGKTKIFLRDHQDTLLEVQRSQVLDRAALSIQKVLRGYRYRKEFLRQRRAAVTLQAWWRGYCNRRNFKLILVGFERLQAIARSQPLARQYQAMRQRTVQLQALCRGYLVRQQVQAKRRAVVVIQAHARGMAARRNFQQRKANAPLVIPAEGQKSQGALPAKKRRSIYDTVTDTEMVEKVFGFLPAMIGGQEGQASPHFEDLESKTQKLLEVDLDTVPMAEEPEEDVDGLAEYTFPKFAVTYFQKSASHTHIRRPLRYPLLYHEDDTDCLAALVIWNVILRFMGDLPEPVLYARSSQQGSSVMRQIHDTLGREHGAQVPQHSRSAQVASQLNIGEEALEPDGLGADRPMSNLEKVHFIVGYAILRPSLRDEIYCQICKQLSENFKTSSLARGWILLSLCLGCFPPSERFMKYLLNFIGQGPATYGPFCAERLRRTYANGVRAEPPTWLELQAVKSKKHIPIQVILATGESLTVPVDSASTSREMCMHIAHKQGLSDHLGFSLQVAVYDKFWSLGSGRDHMMDAIARCEQMAQERGESQRQSPWRIYFRKEFFTPWHDSREDPVSTELIYRQVLRGVWSGEYSFEKEEELVELLARHCYVQLGASAESKAVQELLPSCIPHKLYRTKPPDRWASLVTAACAKAPYTQKQVTPLAVREQVVDAARLQWPLLFSRLFEVITLSGPRLPKTQLILAVNWKGLCFLDQQEKMLLELSFPEVMGLATNREAQGGQRLLLSTMHEEYEFVSPSSVAIAELVALFLEGLKERSIFAMALQDRKATDDTTLLAFKKGDLLVLTKKQGLLASENWTLGQNDRTGKTGLVPMACLYTIPTVTKPSAQLLSLLAMSPEKRKLAAQEGQFTEPRPEEPPKEKLHTLEEFSYEFFRAPEKDMVSMAVLPLARARGHLWAYSCEPLRQPLLKRVHANVDLWDIACQIFVAILRYMGDYPSRQAWPTLELTDQIFTLALQHPALQDEVYCQILKQLTHNSNRHSEERGWQLLWLCTGLFPPSKGLLPHAQKFIDTRRGKLLAPDCSRRIQKVLRTGPRKQPPHQVEVEAAEQNVSRICHKIYFPNDTSEMLEVVANTRVRDVCDSIATRLQLASWEGCSLFIKISDKVISQKEGDFFFDSLREVSDWVKKNKPQKEGAPVTLPYQVYFMRKLWLNISPGKDVNADTILHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDRSQLASVPKILRELVPENLTRLMSSEEWKKSILLAYDKHKDKTVEEAKVAFLKWICRWPTFGSAFFEVKQTSEPSYPDVILIAINRHGVLLIHPKTKDLLTTYPFTKISSWSSGSTYFHMALGSLGRGSRLLCETSLGYKMDDLLTSYVQQLLSAMNKQRGSKAPALAST
Protein: At3g44100 (MD-2-related lipid recognition domain-containing protein) (Q9LXQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAISQAQPLLLLLLSVFFLPALHATSFTYCDKRLDPVKVTGVKISPDPVVSGAAATFKIFGSTGEDISGGKVVIRVLYVGIPVHTETHDLCDETACPVAPGSFVLSHSQTLPSITPPGTYTLKMTINDKNGGRLTCISFKFKITVGSAVFAS
Protein: Putative zinc protease mug138 (EC 3.4.24.-) (Meiotically up-regulated gene 138 protein) (O14077)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable ubiquitin carboxyl-terminal hydrolase 12
- Protein rax1
- Polarized growth protein rax2
Sequence:
MDGKPQVEVIVNGQVVPNLDDREYRLIKLENDLEVLLVRDPETDNASAAIDVHIGSQSNPRELLGLAHFCEHLLFMGTKKYPDENEYRKYLESHNGISNAYTASNNTNYYFEVSHDALYGALDRFAQFFIDPLFLEECKDREIRAVDSEHCKNLQSDSWRFWRLYSVLSNPKSVFSKFNTGNIETLGDVPKELGLDVRQELLKFYDKYYSANIMKLVIIGREPLDVLQDWAAELFSPIKNKAVPIPKFPDPPYTDNEVRKICYVKPVKNLRRLDIVFPIPGQYHKYKCRPAEYVCHLLGHEGEGSYLAYLKSLGLATSLIAFNVSITEDADIIVVSTFLTEEGLTDYQRVIKILFEYIRLLDQTNAHKFLFEETRIMSEAQFKTRQKTPAYQYAHVVASKLQREYPRDKVLYYSSVLTEFDPKGIQEVVESLRPNNFFAILAAHSIEKGLDNKEKFYGIDYGLEDLDSQFIDSLLHIKTSSELYLPLANEFIPWSLEVEKQPVTTKLKVPNLVRNDKFVRLWHKKDDTFWVPKANVFINFISPIARRSPKVSVSTTLYTRLIEDALGEYSYPASLAGLSFSLSPSTRGIILCISGFTDKLHVLLEKVVAMMRDLKVHPQRFEILKNRLEQELKDYDALEAYHRSNHVLTWLSEPHSWSNAELREAIKDVQVGDMSDFISDLLKQNFLESLVHGNYTEEDAKNLIESAQKLIDPKPVFASQLSRKRAIIVPEGGNYIYKTVVPNKEEKNSAIMYNLQISQLDDERSGALTRLARQIMKEPTFSILRTKEQLGYIVFTLVRQVTPFINLNIFVQSERSSTYLESRIRALLDQFKSEFLEMSDEDFSKHKSSLINFMLEKHTNLKEESSMYWLRICDGFYDFTRLEKQAEIVSTITKDEFYSFFINNIHYEGENTKKISVHVVSQRCEDEVYEIPNVTIIENGNMFKESMTLSKAAFPLKPFDEIDRSLLFN
Protein: Uncharacterized protein (Q389X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSAEAVADLERRAAAAETAIGELSLRLQTMGSSVGAGIEPRLRELLKLMHEDRAEFEAVRAQRDELKEENERLKIQVAKHEYRIKHLLRTIEEISPEENS
Protein: Protein PTST, chloroplastic (PROTEIN TARGETING TO STARCH) (Q94AX2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in targeting GBSS1 to the starch granule. Was originally thought to be a carbohydrate-binding scaffold protein, but it has been shown that it is mainly found as a soluble protein and that interaction with GBSS1 is a pre-requisite for subsequent starch granule binding. Dissociation from starch as a function of pH, Mg(2+) concentration or redox state is not observed. Interacts primarily with amylopectin and is required for amylose synthesis.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19038037, ECO:0000269|PubMed:25710501}. Note=The vast majority of PTST is soluble and only a small amount is granule-bound. No localization to the starch granules in the absence of GBSS1. {ECO:0000269|PubMed:25710501}.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- MAR-binding filament-like protein 1
- Probable starch synthase 4, chloroplastic/amyloplastic
- Isoamylase 1, chloroplastic
- Phosphoglucan phosphatase DSP4, chloroplastic
- Isoamylase 2, chloroplastic
- Phosphoglucan phosphatase LSF2, chloroplastic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Isoamylase 3, chloroplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
Sequence:
MGCVPRIEFGCSSQSLTLSWNLRAWNLCRLNTISHFQKLPYPLVASTRKHYKNSLLLKRFLVGVGTEESSLSEDLLDESLSRPLTSDELKSLLIDTERSKLVKKLSEANQQNRFLKRQLKTQEHEITNIKTELALMELEVQALVKLAEEIANLGIPQGSRKISGKYIQSHLLSRLDAVQKKMKEQIKGVEAAQSKEVHVFWIGMAESVQVMGSFDGWSQREDLSPEYSALFTKFSTTLFLRPGRYEMKFLVDGEWQISPEFPTSGEGLMENNVLVVE
Protein: Cysteine desulfurase IscS (EC 2.8.1.7) (NifS protein homolog) (ThiI transpersulfidase) (TusA transpersulfidase) (P0A6B7)
Organism: Escherichia coli (strain K12)
Function: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to an acceptor protein. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Transfers sulfur onto 'Cys-456' of ThiI and onto 'Cys-19' of TusA in transpersulfidation reactions.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305}.
Interaction partners:
- Sulfur carrier protein TusA
- HTH-type transcriptional regulator IscR
- Iron-sulfur cluster assembly scaffold protein IscU
- 2Fe-2S ferredoxin
- Co-chaperone protein HscB
- Iron-binding protein IscA
- tRNA sulfurtransferase
- Iron-sulfur cluster assembly protein CyaY
- Molybdopterin-synthase adenylyltransferase
- 3-mercaptopyruvate sulfurtransferase
Sequence:
MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH
Protein: Phage protein (Q729C4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Protein RecA
- DNA 3'-5' helicase
- Thiamine-monophosphate kinase
Sequence:
MNPPPSGAGFSCHGTTADGPHFPSDGGYHMLDPRDCILYSGGATGTEAHFGGIAEKYGLEEVNYSFEGHQIERTRGVRVLTSEELALKDVSLTYVSRLMNRQYTRAPLFRKVLQSICWQVSCGHEVWVVGSIQEDDTVTGGTGWGAEFAKICNKPLYVFDQTRNGWYMWDKSAWSPVSEPRIGHRHFTATGTRFLEDNGRAAIEALFARSFNV
Protein: Receptor expression-enhancing protein (A1Z9M2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362006}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362006}.
Interaction partners:
- Reticulon-like protein
- Protein transport protein Sec61 subunit beta
- Protein YIPF
- Translocon-associated protein subunit delta
- Transmembrane emp24 domain-containing protein bai
Sequence:
MATQVKQFLNGYKDDVSKSLRDASKPWTKVFDTVEEKTGVDRVNIFVGAVGLCAIYLIFGWGAQLLCNIIGVLYPAYISIHAIESSTKQDDTKWLIYWVTFGIFTVIEFFSSLLTSVIPFYWLLKCAFLIWCMLPTEQNGSTIIYNKLVRPYFLKHHESVDRIIDDGMKKAAGVLKHD
Protein: FAST kinase domain-containing protein 1, mitochondrial (Q53R41)
Organism: Homo sapiens (Human)
Function: Involved in the down-regulation of mitochondrial MT-ND3 mRNA levels which leads to decreased respiratory complex I abundance and activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:28238724, ECO:0000269|PubMed:28335001}. Note=Preferentially localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly (PubMed:28335001). {ECO:0000269|PubMed:28335001}.
Interaction partners:
- Fas-activated serine/threonine kinase
Sequence:
MKKTPVFLESLVTNMLRLRAICPFSWRVFQFRPISCEPLIIQMNKCTDEEQMFGFIERNKAILSEKQVGCAFDMLWKLQKQKTSLLKNAEYVRDHPQFLTLHNLATNKFKLMNDDTLVNVLYVTQQFAGEAHDPLVEALVTEAWRRLERFDIKLLSEFSSCLADQHLYFSPLMGKIADIVHRNLETTQDLSSLSVLMVNISSLISRHFQQQLVNKTELLFDTIDSSEVNVAKSIAKFLRNVRYRYQPLLERCNNVFLSNVDHLDLDSISKILSVYKFLQFNSFEFIIMAKKKLTEMIPLCNHPASFVKLFVALGPIAGPEEKKQLKSTMLLMSEDLTGEQALAVLGAMGDMESRNSCLIKRVTSVLHKHLDGYKPLELLKITQELTFLHFQRKEFFAKLRELLLSYLKNSFIPTEVSVLVRAISLLPSPHLDEVGISRIEAVLPQCDLNNLSSFATSVLRWIQHDHMYLDNMTAKQLKLLQKLDHYGRQRLQHSNSLDLLRKELKSLKGNTFPESLLEEMIATLQHFMDDINYINVGEIASFISSTDYLSTLLLDRIASVAVQQIEKIHPFTIPAIIRPFSVLNYDPPQRDEFLGTCVQHLNSYLGILDPFILVFLGFSLATLEYFPEDLLKAIFNIKFLARLDSQLEILSPSRSARVQFHLMELNRSVCLECPEFQIPWFHDRFCQQYNKGIGGMDGTQQQIFKMLAEVLGGINCVKASVLTPYYHKVDFECILDKRKKPLPYGSHNIALGQLPEMPWESNIEIVGSRLPPGAERIALEFLDSKALCRNIPHMKGKSAMKKRHLEILGYRVIQISQFEWNSMALSTKDARMDYLRECIFGEVKSCL
Protein: 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase (AONS/AKB ligase) (EC 2.3.1.29) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) (Alpha-oxoamine synthase) (Glycine acetyltransferase) (Q5SHZ8)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide (By similarity). Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate. It also converts 2-amino-3-ketobutyrate and CoA to glycine and acetyl-CoA. Activity is also observed with the following combinations of substrates: acetyl-CoA and either L-alanine or L-serine, pimeloyl-CoA and either glycine or L-serine, and palmitoyl-CoA with L-alanine.
Interaction partners:
Sequence:
MSLDLRARVREELERLKREGLYISPKVLEAPQEPVTRVEGREVVNLASNNYLGFANHPYLKEKARQYLEKWGAGSGAVRTIAGTFTYHVELEEALARFKGTESALVLQSGFTANQGVLGALLKEGDVVFSDELNHASIIDGLRLTKATRLVFRHADVAHLEELLKAHDTDGLKLIVTDGVFSMDGDIAPLDKIVPLAKKYKAVVYVDDAHGSGVLGEKGKGTVHHFGFHQDPDVVQVATLSKAWAGIGGYAAGARELKDLLINKARPFLFSTSHPPAVVGALLGALELIEKEPERVERLWENTRYFKRELARLGYDTLGSQTPITPVLFGEAPLAFEASRLLLEEGVFAVGIGFPTVPRGKARIRNIVTAAHTKEMLDKALEAYEKVGKRLGIIR
Protein: Extracellular serine/threonine protein kinase CeFam20 (CeFam20) (EC 2.7.11.1) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK) (Q9XTW2)
Organism: Caenorhabditis elegans
Function: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IXL6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IXL6}. Secreted {ECO:0000250|UniProtKB:Q5MJS3}. Note=Resides in the Golgi apparatus membrane and is secreted following propeptide cleavage. {ECO:0000250|UniProtKB:Q8IXL6}.
Interaction partners:
- Galectin
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- NADPH--cytochrome P450 reductase
- N-acetyltransferase 9-like protein
- C-type lectin domain-containing protein
Sequence:
MRCNIKRLFTLAIGVFAATLVIISFSKDNYEREWKQGPQSNEARAVGHQSPDLFPVGQNSLPHQPIPPSLGEKDLSDPFNFLFSSNKITLRKLYDLTKNVDFDQLRQNECKKNITLSKFWEKSEQRNVPEDDNWERFYSNIGSCSVYSDDQMIDNLLHDLNTSPIKHVHIMDGGTQVKFVFTFKNDKQAVFKPMRFGRDYESDPNHFYFSDFERHHAEIATFHLDRVLGFRRAIPTVGRVLNMTTELFEKAEKKLKKTFFFSPAKNFCFVSRCDYYCDTTHAICGLPDMKEGSVQVFLPDESAVPRKHNRSPYRRTYSKKNQVAEWQSSMNYCTDKVKTKRQYAHGRRLLDLVDIHILDYLIGNQDRHHFESFNVFNDLPSYAIHLDHGRAFGRSDFDDDDIILPLRQCCILRPSTFQTLMNFYSTPKSLTKALHESLSKDPAHPILAYKHYPAMERRLAKIMSHILECFESRGVAEVLVAEYNNPDVSDAEQNDEEQSEEHQDKKDDKKTV
Protein: Methyl-CpG-binding domain protein 3 (Methyl-CpG-binding protein MBD3) (O95983)
Organism: Homo sapiens (Human)
Function: Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Acts as transcriptional repressor and plays a role in gene silencing. Does not bind to methylated DNA by itself. Binds to a lesser degree DNA containing unmethylated CpG dinucleotides. Recruits histone deacetylases and DNA methyltransferases.
Subcellular location: Nucleus {ECO:0000269|PubMed:15701600, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}. Chromosome {ECO:0000269|PubMed:27732854}. Note=Nuclear, in discrete foci. Detected on chromatin, at promoter regions of active genes. {ECO:0000269|PubMed:27732854}.
Interaction partners:
- Histone deacetylase 1
- Metastasis-associated protein MTA2
- Histone-binding protein RBBP7
- Chromodomain-helicase-DNA-binding protein 4
- Metastasis-associated protein MTA1
- Histone-binding protein RBBP4
- Metastasis-associated protein MTA3
- Histone deacetylase 2
- Transcriptional repressor p66-alpha
- Chromodomain-helicase-DNA-binding protein 3
Sequence:
MERKRWECPALPQGWEREEVPRRSGLSAGHRDVFYYSPSGKKFRSKPQLARYLGGSMDLSTFDFRTGKMLMSKMNKSRQRVRYDSSNQVKGKPDLNTALPVRQTASIFKQPVTKITNHPSNKVKSDPQKAVDQPRQLFWEKKLSGLNAFDIAEELVKTMDLPKGLQGVGPGCTDETLLSAIASALHTSTMPITGQLSAAVEKNPGVWLNTTQPLCKAFMVTDEDIRKQEELVQQVRKRLEEALMADMLAHVEELARDGEAPLDKACAEDDDEEDEEEEEEEPDPDPEMEHV
Protein: RNA-binding motif protein, Y chromosome, family 1 member E (A6NEQ0)
Organism: Homo sapiens (Human)
Function: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis.
Subcellular location: Nucleus.
Interaction partners:
- RNA-binding motif protein, Y chromosome, family 1 member B
- RNA-binding motif protein, Y chromosome, family 1 member D
- RNA-binding motif protein, Y chromosome, family 1 member A1
- Testis specific protein Y-linked 8
Sequence:
MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSQEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTAHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY
Protein: Envelope glycoprotein UL132 (F5HGU6)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Subcellular location: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPAPRGPLRATFLALVAFGLLLQIDLSDVTNVTSSTKVPTSTSNRNSVDNATSSGPTTGINMTTTHESSVHNVRNNEIMKVLAILFYIVTGTSIFSFIAVLVAVVYSSCCKHPGRFRFADEEAVNLLDDTDDSGGSSPFGSGSRRGSQIPAGFCSSSPYQRLETRDWDEEEEASAARERMKHDPENVIYFRKDGNLDTSFVNPNYGRGSPLTIESHLSDNEEDPIRYYVSVYDELTASEMEEPSNSTSWQIPKLMKVAMQPVSLRDPEYD
Protein: Probable envelope ADP,ATP carrier protein, chloroplastic (Envelope ADP/ATP translocase) (O65023)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transports adenine nucleotides.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|Ref.4}; Multi-pass membrane protein {ECO:0000269|Ref.4}.
Interaction partners:
- Peter Pan-like protein
- NADH dehydrogenase iron-sulfur protein 5-B
- At5g65925
- Histone deacetylase complex subunit
- Protein SHI RELATED SEQUENCE 8
- Probable lysophospholipase BODYGUARD 2
- Putative galacturonosyltransferase 2
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MEEDRAILTFHRIPSLNSSLITTSSPAKSGAEQFRRRVLRNPARGDFGLGRFACISLVEKCEQREFAPTTAQLLNNPLAILALVPKDAAIFAAGALAGAAAKTVTAPLDRIKLLMQTHGIRLGQQSAKKAIGFIEAITLIAKEEGVKGYWKGNLPQVIRVLPYSAVQLLAYESYKNLFKGKDDQLSVIGRLAAGACAGMTSTLLTYPLDVLRLRLAVEPGYRTMSQVALSMLRDEGIASFYYGLGPSLVGIAPYIAVNFCIFDLVKKSLPEEYRKKAQSSLLTAVLSAGIATLTCYPLDTVRRQMQMRGTPYKSIPEAFAGIIDRDGLIGLYRGFLPNALKTLPNSSIRLTTFDMVKRLIATSEKQLQKISDDNRNRDQAQ
Protein: Secretoglobin, family 2B, member 27 (A0A087WRN7)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKGTLLLLALLVTGELGFQTTEACAPFVGAYVKILGGNRLALNAYLSMFQATAAERVAFEKIQDCFNEEPLTTKLKSPQIMT
Protein: Oxidoreductase NAD-binding domain-containing protein 1 (EC 1.-.-.-) (Q96HP4)
Organism: Homo sapiens (Human)
Interaction partners:
- Calpain-7
- Xin actin-binding repeat-containing protein 1
- Dihydropyrimidine dehydrogenase [NADP
- Dihydroorotate dehydrogenase
- Uridine 5'-monophosphate synthase
- Diphthamide biosynthesis protein 3
Sequence:
MACAAVMIPGLLRCSVGAIRIEAASLRLTLSTLRHLTLTSIMKSKRKTDHMERTASVLRREIVSAAKVCGAASESPSVKSLRLLVADQDFSFKAGQWVDFFIPGVSVVGGFSICSSPRLLEQERVIELAVKYTNHPPALWVHNTCTLDCEVAVRVGGEFFFDPQPADASRNLVLIAGGVGINPLLSILRHAADLLREQANKRNGYEIGTIKLFYSAKNTSELLFKKNILDLVNEFPEKIACSLHVTKQTTQINAELKPYITEGRITEKEIRDHISKETLFYICGPPPMTDFFSKQLENNHVPKEHICFEKWW