wanglab/gogpt-training-data huggingface dataset:
Protein: SET domain-containing protein 4 (EC 2.1.1.-) (EC 2.1.1.364) (P58467)
Organism: Mus musculus (Mouse)
Function: Histone-lysine N-methyltransferase that acts as a regulator of cell proliferation, cell differentiation and inflammatory response. Regulates the inflammatory response by mediating mono- and dimethylation of 'Lys-4' of histone H3 (H3K4me1 and H3K4me2, respectively), leading to activate the transcription of pro-inflammatory cytokines IL6 and TNF-alpha. Also involved in the regulation of stem cell quiescence by catalyzing the trimethylation of 'Lys-20' of histone H4 (H4K20me3), thereby promoting heterochromatin formation (By similarity). Involved in proliferation, migration, paracrine and myogenic differentiation of bone marrow mesenchymal stem cells (BMSCs).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:31376731}. Nucleus {ECO:0000269|PubMed:31376731}.
Interaction partners:
- Large ribosomal subunit protein mL39
Sequence:
MQRRRGRTERARKRRRRSSGSRAVNESYRSEFIELRKWLKERKFEDTDLVPASFPGTGRGLMSKASLQEGQVMISLPESCLLTTDTVIRSSLGPYIKKWKPPVSPLLALCTFLVSEKHAGCRSLWKSYLDILPKSYTCPVCLEPEVVDLLPSPLKAKAEEQRARVQDLFTSARGFFSTLQPLFAEPVDSVFSYRAFLWAWCTVNTRAVYLRSRRQECLSAEPDTCALAPFLDLLNHSPHVQVKAAFNEKTRCYEIRTASRCRKHQEVFICYGPHDNQRLLLEYGFVSVRNPHACVPVSADMLVKFLPAADKQLHRKITILKDHGFTGNLTFGWDGPSWRLLTALKLLCLEAERFTSWKKVLLGEVISDTNEKTSLGVAQKICSDVIEETHAVLRKVSDMKEGTVSLRSQLSLVEALRMEELRILQASAEILSGLLAPFS
Protein: Spore coat protein V (Q08309)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Spore coat protein W
- Spore coat protein X
- Spore coat protein Y
- Spore coat protein Z
- Spore protein CgeB
- Sporulation-specific transcription factor SpoVIF
- Spore coat protein T
- Spore coat protein G
- Spore coat protein F
- Spore coat polysaccharide biosynthesis protein SpsA
Sequence:
MSFEEKVESLHPAIFEQLSSEFEQQIEVIDCENITIDTSHITAALSIQAFVTTMIIVATQLVIADEDLADAVASEILILDSSQIKKRTIIKIINSRNIKITLSADEIITFVQILLQVLNSILSELDVL
Protein: Large ribosomal subunit protein eL30 (60S ribosomal protein L30) (Q55BS9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein eL36
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS25
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein eS1
Sequence:
MVSVKKVKKSQENIGSKLALVMKSGKSQLGYKSTLKTLRAGKSKLILLASNLPSIRRSEIEYYAMLSKTTVHLYSGNNVDLGTALGRHYRVSVMSITDAGDSDILTALNAKA
Protein: Tyrosine-protein kinase TXK (EC 2.7.10.2) (Protein-tyrosine kinase 4) (Resting lymphocyte kinase) (P42681)
Organism: Homo sapiens (Human)
Function: Non-receptor tyrosine kinase that plays a redundant role with ITK in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation leads to the recruitment of TXK to the cell membrane, where it is phosphorylated at Tyr-420. Phosphorylation leads to TXK full activation. Contributes also to signaling from many receptors and participates in multiple downstream pathways, including regulation of the actin cytoskeleton. Like ITK, can phosphorylate PLCG1, leading to its localization in lipid rafts and activation, followed by subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with PARP1 and EEF1A1. Within the complex, phosphorylates both PARP1 and EEF1A1. Phosphorylates also key sites in LCP2 leading to the up-regulation of Th1 preferred cytokine IL-2. Phosphorylates 'Tyr-201' of CTLA4 which leads to the association of PI-3 kinase with the CTLA4 receptor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17177976}. Nucleus {ECO:0000269|PubMed:17177976}. Cell membrane {ECO:0000269|PubMed:17177976}; Peripheral membrane protein {ECO:0000269|PubMed:17177976}. Note=Localizes in the vicinity of cell surface receptors in the plasma membrane after receptor stimulation. Translocates into the nucleus and enhances IFN-gamma gene transcription in T-cells.
Interaction partners:
- Proto-oncogene vav
- Guanine nucleotide exchange factor VAV3
- Tyrosine-protein kinase ITK/TSK
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Guanine nucleotide exchange factor VAV2
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3-kinase regulatory subunit beta
Sequence:
MILSSYNTIQSVFCCCCCCSVQKRQMRTQISLSTDEELPEKYTQRRRPWLSQLSNKKQSNTGRVQPSKRKPLPPLPPSEVAEEKIQVKALYDFLPREPCNLALRRAEEYLILEKYNPHWWKARDRLGNEGLIPSNYVTENKITNLEIYEWYHRNITRNQAEHLLRQESKEGAFIVRDSRHLGSYTISVFMGARRSTEAAIKHYQIKKNDSGQWYVAERHAFQSIPELIWYHQHNAAGLMTRLRYPVGLMGSCLPATAGFSYEKWEIDPSELAFIKEIGSGQFGVVHLGEWRSHIQVAIKAINEGSMSEEDFIEEAKVMMKLSHSKLVQLYGVCIQRKPLYIVTEFMENGCLLNYLRENKGKLRKEMLLSVCQDICEGMEYLERNGYIHRDLAARNCLVSSTCIVKISDFGMTRYVLDDEYVSSFGAKFPIKWSPPEVFLFNKYSSKSDVWSFGVLMWEVFTEGKMPFENKSNLQVVEAISEGFRLYRPHLAPMSIYEVMYSCWHEKPEGRPTFAELLRAVTEIAETW
Protein: Olfactory receptor (Q80ZX9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MAGTNHTEVIEYVLLGLQDHHGLEIALFVLCLGIYCMTLLGNSFLVGLIVLDTHLHSPMYFFISNLSLIDICGTSSFTPMMLLNFLDVQRTISFPSCALQMYLTLALGTTECLLLAVMAYDRYVAICQPLRYPELVNGPLCIQMAGISWGTGFANSLLHSILVWHLPFCGHYIINHFFCEILAVLKLACGDISLNALILTVATAVLTMTPLLLICLSYIFILAAILRVPSAAGRSKAFSTCSAHLTVVVIFYGTITFMYLKPKDQDPSVGKIITLLYAIVAPSLNAFIYSLRNSEVKAAVTALLWGGLLTRKMSHF
Protein: START domain-containing protein (Q57ZK9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTEDVFVESAGEKYRLQVLRDFRKFKELVLSTNAWTKQYSDSHTLVETRPPEDKSTGINIVRVKREMPGVTCEDLYDTLHDAGYRATWDENMLEGKNIATLSPHNDIGYYAVKLPWPLKNRDFCNLRSWMEFTNGEFVIFNHSVKHPNCPEKKQFVRARSIITGYLIQPFGDGGCLLSYITCSDPCGSIPHSVINFTTTRIVPKVMNQLQKCALKYGEYFAKNGKCPREELPWRTPKMNWSSTFNYPGEEEAATSGANVGLNDTREGTVNRDGERVMSLMEESSLAAGSQYSSPACDGLTGRCVGAESATPTTAEGDSPVVQQYKDIMHRLANVADDTFIVEGRAPAVAEYTSRVGVFVDGVRRTSPH
Protein: Probable LRR receptor-like protein kinase At1g51890 (EC 2.7.11.1) (C0LGG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Protein VACUOLELESS GAMETOPHYTES
- Cytochrome P450 81F2
- Similarity to unknown protein
- Transducin/WD40 repeat-like superfamily protein
- Acyl-CoA N-acyltransferases
- PLC-like phosphodiesterases superfamily protein
- Endochitinase CHI
- AT3g59080/F17J16_130
Sequence:
MRFLSFLIFVFAVLGLVQAQDQSGFISLDCGLVPTEITYVEKSTNITYRSDATYIDSGVPGKINEVYRTQFQQQIWALRSFPEGQRNCYNFSLTAKRKYLIRGTFIYGNYDGLNQLPSFDLYIGPNKWTSVSIPGVRNGSVSEMIHVLRQDHLQICLVKTGETTPFISSLELRPLNNNTYVTKSGSLIVVARLYFSPTPPFLRYDEDVHDRIWIPFLDNKNSLLSTELSVDTSNFYNVPQTVAKTAAVPLNATQPLKINWSLDDITSQSYIYMHFAEIENLEANETREFNITYNGGENWFSYFRPPKFRITTVYNPAAVSSLDGNFNFTFSMTGNSTHPPLINGLEIYQVLELPQLDTYQDEVSAMMNIKTIYGLSKRSSWQGDPCAPELYRWEGLNCSYPNFAPPQIISLNLSGSNLSGTITSDISKLTHLRELDLSNNDLSGDIPFVFSDMKNLTLINLSGNKNLNRSVPETLQKRIDNKSLTLIRDETGKNSTNVVAIAASVASVFAVLVILAIVFVVIRKKQRTNEASGPRSFTTGTVKSDARSSSSSIITKERKFTYSEVLKMTKNFERVLGKGGFGTVYHGNLDDTQVAVKMLSHSSAQGYKEFKAEVELLLRVHHRHLVGLVGYCDDGDNLALIYEYMEKGDLRENMSGKHSVNVLSWETRMQIAVEAAQGLEYLHNGCRPPMVHRDVKPTNILLNERSQAKLADFGLSRSFPVDGESHVMTVVAGTPGYLDPEYYRTNWLSEKSDVYSFGVVLLEIVTNQPVMNKNRERPHINEWVMFMLTNGDIKSIVDPKLNEDYDTNGVWKVVELALACVNPSSSRRPTMPHVVMELNECLALEIERKQGSQATYIKESVEFSPSSASDFSPLAR
Protein: Mediator of RNA polymerase II transcription subunit-like protein (T21P5.12 protein) (Q9SRQ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Serine/threonine-protein kinase ATR
- Minichromosome maintenance 10
- DNA replication licensing factor MCM6
- Probable DNA helicase MCM8
- Probable inactive protein kinase At3g63330
- Origin of replication complex subunit 5
Sequence:
MEESKQQQLQQQQLLLQMQQQQQMQQRQQQLFLMQHLQKQQQQQAAMSMFPPNADAHLRPPGLIPNRPVNPFLQNVNPNPNLIQQANKFQQQQQQQMMMMMQQQQLQQQQQQKLMRPSNQLEIQFAYQDAWRVCHPDFKRPFASLEDACERLLPYHVVADYEAEEDDSIFDSNTTSQTLPRCQQWDNNIAAKVAEFTATFEGQVQAFDRIIQKRSDGDRVEERLMMEQVLLNDERNACIQLDREMKAQDARLRMAALAQAAGQARAEESQQSHAEMMARNPLRANAIGNHGEQGRNMNPNEMMLLMNGWGNNNNNNNSQKEEKEPLEDFLNDEENENGEHEKWRRSGDFDLNIR
Protein: Alpha-crystallin A chain (Heat shock protein beta-4) (HspB4) (Heat shock protein family B member 4) [Cleaved into: Alpha-crystallin A(1-172); Alpha-crystallin A(1-168); Alpha-crystallin A(1-162)] (P02489)
Organism: Homo sapiens (Human)
Function: Contributes to the transparency and refractive index of the lens. In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14512969, ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:19503744, ECO:0000269|PubMed:26004348, ECO:0000269|PubMed:30340470}. Nucleus {ECO:0000269|PubMed:19464326}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Interaction partners:
Sequence:
MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q4GZE6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase, putative
- Glyceraldehyde-3-phosphate dehydrogenase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Phosphoglycerate kinase
- Phosphoglycerate kinase
- Pyruvate kinase
- Phosphotransferase
Sequence:
MSTAPNAKNNISLKKSVGDVWPLTAKRVLMRVDFNVPMQNGHITNDYRIRAAIPTIRRVIDQGGICILLSHLGRPRGVSMVAGVRDIRRRYHEAQFHDNKGKTAFFSVLPGEEKVKILAKSSAREEATHISPEVKSGKTMLFARLPEDEKKSLLMQYLNENKDSALPQMSVSAGYEEQYSLRPVAVRLAELLGQHVYFAHDCLDARVEVSRLKRGNVMLLENVRFYSEENGENAEEREAMAKILASYGDVYISDAFGAAHRDSATMTGIPKILGHGAAGYLMEKEISYFAKVLGNPPRPLVAIVGGAKVSEKIQLLDNMLQRIDYLLIGGAMAYTFLKAQGYSIGKSKCEESKLEFARSLLKKAEDRKVQIILPIDHVCHTEFKAVDSPLITEDQNIPEGHMALDIGPKTIEKYVQTIGKCKSAIWNGPMGVFEMVPYSKGTFAIAKAMGRGTQKRGLMSIIGGGESAGAAELCGEAARISHVSTGGGASLELLEGKTLPGVAVLDDKE
Protein: Acyl-CoA synthetase 7 (EC 6.2.1.-) (Q17577)
Organism: Caenorhabditis elegans
Function: Plays a role in ascaroside pheromones biosynthesis, which regulates development and behavior. Specifically, activates the side chain of medium-chain indol-3-carbonyl (IC)-ascarosides for shortening through beta-oxidation. Converts IC-asc-C7 and IC-asc-C9 into IC-asc-C7-CoA and IC-asc-C9-CoA, respectively. May play a role in fatty-acid metabolism by activating and converting nonanoate (C9) into nonanoyl-CoA (C9-CoA).
Subcellular location: Peroxisome {ECO:0000269|PubMed:29863473}.
Interaction partners:
- Fatty acid synthase
- Nsp1_C domain-containing protein
- Acyl-coenzyme A oxidase acox-1.1
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Carboxylic ester hydrolase
- Acyl-coenzyme A oxidase acox-3
- Non-specific lipid-transfer protein-like 2
- Carboxylic ester hydrolase
- Acyl-coenzyme A oxidase acox-1.3
- Enoyl-CoA Hydratase
Sequence:
MIFHGEQLENHDKPVHEVLLERFKVHQEKDPDNVAFVTAENEDDSLGFQQLGKKVLQISEWFVENGYKKGDVFLLASYNNWRCFAAALGAWRAGLIVSAAASQFTSFEMNYQIEDSQSQVILVDKHTLPVVQEACKNLKFVKQIISISANPPSPVIKFDVLTSRLVRNLKMPLIDPKNDIVFLPYSSGTTGKPKGVMISHLNFSMMLESSLRFFDANAKAIGLPPDFVLPYDLHFLPMYHAMGMFRTLLTSYRGTTQIMFTKFDMELMLKNIEKYSIMVLSLVPAIAVRMLNSPLLQKYDVSSLVSVTVGSAPFPESASKKLKQLLPNVNIVQGYGMTELTFATHLQSPGSPDGSVGRLVPGTSMKVKKEDGTLCGPHEIGELWIKGPQMMKGYWKKEQQTNELLDEHGFMRTGDIVYFDKNGETFICDRIKELIKVNAKQVAPAELESVILEHDDVADVCVFGVDDASSGERPVACVVSKRGRDMETSKAIMKHINQKLARYKHIKEIEFVSEIMRTGTGKLLRRAMKKAFLDAKKAKL
Protein: Acyl-CoA dehydrogenase, putative (P95097)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MGIALTDDHRELSGVARAFLTSQKVRWAARASLDAAGDARPPFWQNLAELGWLGLHIDERHGGSGYGLSELVVVIEELGRAVAPGLFVPTVIASAVVAKEGTDDQRARLLPALIDGTLTAGVGLDSQVQVTDGVADGEAGIVLGAGLAELLLVAAGDDVLVLERGRKGVSVDVPENFDPTRRSGRVRLDNVRVTTDDILLGAYESALARARTLLAAEAVGGAADCVDSAVAYAKVRQQFGRTIATFQAVKHHCANMLVAAESAIAAVWDAARAAAEDEEQFRLAAAVAAALAFPAYARNAELNIQVHGGIGFTWEHDAHLHLRRALVTVGLFGGDAPVRDVFERTAAGVTRAISLDLPAQAEELRARIRSDAAEIAALEKDAQRDKLIETGYVMPHWPRPWGRAAGAVEQLVIEEEFSAAGIERPDYSITGWVILTLIQHGTPWQIERFVEKALRQQEIWCQLFSEPDAGSDAASVKTRATRVEGGWKINGQKVWTSGAQYCARGLATVRTDPDAPKHAGITTVIIDMLAPGVEVRPLRQITGDSEFNEVFFNDVFVPDEDVVGAPNSGWTVARATLGNERVSIGGSGSYYEAMAAKLVQLVQRRSDAFAGAPIRVGAFLAEDHALRLLNLRRAARSVEGAGPGPEGNITKLKVAEHMIEGAAIAAALWGPEIALLDGPGRVIGRTVMGARGMAIAGGTSEVTRNQIAERILGMPRDPLIS
Protein: methylmalonyl-CoA mutase (EC 5.4.99.2) (A0A0E8UW09)
Organism: Mycobacterium tuberculosis
Interaction partners:
Sequence:
MTTKTPVIGSFAGVPLHSERAAQSPTEAAVHTHVAAAAAAHGYTPEQLVWHTPEGIDVTPVYIAADRAAAEAEGYPLHSFPGEPPFVRGPYPTMYVNQPWTIRQYAGFSTAADSNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVQGDVGMAGVAIDSILDMRQLFDGIDLSTVSVSMTMNGAVLPILALYVVAAEEQGVAPEQLAGTIQNDILKEFMVRNTYIYPPKPSMRIISDIFAYTSAKMPKFNSISISGYHIQEAGATADLELAYTLADGVDYIRAGLNAGLDIDSFAPRLSFFWGIGMNFFMEVAKLRAGRLLWSELVAQFAPKSAKSLSLRTHSQTSGWSLTAQDVFNNVARTCIEAMAATQGHTQSLHTNALDEALALPTDFSARIARNTQLVLQQESGTTRPIDPWGGSYYVEWLTHRLARRARAHIAEVAEHGGMAQAISDGIPKLRIEEAAARTQARIDSGQQPVVGVNKYQVPEDHEIEVLKVENSRVRAEQLAKLQRLRAGRDEPAVRAALAELTRAAAEQGRAGADGLGNNLLALAIDAARAQATVGEISEALEKVYGRHRAEIRTISGVYRDEVGKAPNIAAATELVEKFAEADGRRPRILIAKMGQDGHDRGQKVIATAFADIGFDVDVGSLFSTPEEVARQAADNDVHVIGVSSLAAGHLTLVPALRDALAQVGRPDIMIVVGGVIPPGDFDELYAAGATAIFPPGTVIADAAIDLLHRLAERLGYTLD
Protein: Nonspecific nucleoside hydrolase (Q4QDN1)
Organism: Leishmania major
Interaction partners:
- Guanine deaminase
- adenine phosphoribosyltransferase
- Xanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Adenine aminohydrolase
Sequence:
MPRKIILDCDPGIDDAVAIFLAHGNPEIELLAITTVVGNQSLEKVTQNARLVADVAGIVGVPVAAGCTKPLVRGVRNASHIHGETGMGNVSYPPEFKTKLDGRHAVQLIIDLIMSHEPKTITLVPTGGLTNIAMAVRLEPRIVDRVKEVVLMGGGYHTGNASPVAEFNVFIDPEAAHIVFNESWNVTMVGLDLTHQALATPAVQKRVREVGTKPAAFMLQILDFYTKVYEKEHDTYGKVHDPCAVAYVIDPTVMTTERVPVDIELNGALTTGMTVADFRYPRPKNCRTQVAVKLDFDKFWCLVIDALERIGDPQ
Protein: Twist-related protein (CeTwist) (Helix-loop-helix protein 8) (Q11094)
Organism: Caenorhabditis elegans
Function: Acts as a transcriptional regulator. Involved in postembryonic mesodermal cell fate specification. Activates ceh-24 and egl-15 during mesodermal patterning.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Myoblast growth factor receptor egl-15
- Delta-like protein
- Helix-loop-helix protein hlh-2
- Homeobox protein mab-5
- Protein PFC0760c-like
Sequence:
MVARRKGERVVRKNEVENVQQRACANRRERQRTKELNDAFTLLRKLIPSMPSDKMSKIHTLRIATDYISFLDEMQKNGCKLYGHSIFDEKRGYNLQSAFNMWRGNNGYTPIAGPSQLPPLQSAHIPPPAPSSIPPHCLMPQPWYQTCPPPKQEFHELCPISTPNPNSNPNQLTPIHWQ
Protein: Pre-rRNA-processing protein RIX1 (Involved in processing IST2 protein 2) (Ribosomal export protein 1) (P38883)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA and the nucleoplasmic transit of the pre-60S ribosomal subunits. Regulates pre-60S association of the critical remodeling factor MDN1.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15528184}.
Interaction partners:
- Pre-rRNA-processing protein IPI1
- Pre-rRNA-processing protein IPI3
- Protein SDA1
- Probable metalloprotease ARX1
- Nuclear GTP-binding protein NUG1
- Nucleolar GTP-binding protein 2
- Ribosome assembly protein 4
- Ribosome biogenesis protein NOP53
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
Sequence:
MSEEFIAVSTLARNLEIAKGNEFHTILATLRSPVYINEQLLKSELSFLVTKILKLIRSGNDFDLWKGCHTSVVTCAYNPLVLSTHGGQLLAAIYSRLEQKTGFYSSVISSSHGKQLFNTLISSVAIIIDLMKNKPTLSREALVPKLKAIIPTLITLSQYEPELVLPVLQRILKRNTTTFKPFTNKFRTVLINLIISDYASLGTKTQRLVCENFAYLHLLKIQVSDTSDDETQAHHKIYADSNWRTGLMSILSQFKPIIQLCGEILDFEQDNELYKLIKSLPVIDESNNKEEFLPSLKLDFNAPLTLWEIPQRLSLLADMLVAFISLPTPFPIRVPLGGINSLCEVLLGVSNKYLPLKKELRHDNELNGVINTILPQIQFQGIRLWEIMVSKYGKCGLSFFEGILSSIELFIPLKKKSNNEIDFNVVGSLKFEFATVFRLVNMILSHLGHQLNIISVISQLIEVALFLSHDKTLIDSLFKNRKSIMKQQTKTKQSKRSKSAEGAFSDIYTHPELFVCKNSMNWFNEINDFFITALNNWILPSTPHIQILKYSITQSLRLKERFGYIPESFVNLLRCEVLHPGSERVSILPIAISLLKNINDDMFELLCHPKVPVGMVYQLHKPLDLGEDGEVRDDINKKEVETNESSSNANTGLETLKALENLENVTIPEPKHEVPKVVDDTAIFKKRSVEEVIERESTSSHKKVKFVEETTVDNGEELIVKKAVSQTKEEEKPMEDSEDEEQEEFEIPAIELSDDEEEEEEEE
Protein: Cerberus (Cerberus-like protein) (Cer-l) (Cerberus-related protein) (O55233)
Organism: Mus musculus (Mouse)
Function: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part, through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak.
Subcellular location: Secreted {ECO:0000269|PubMed:9431803}.
Interaction partners:
- Proto-oncogene Wnt-3
- Protein Wnt-11
- Protein Wnt-3a
- Protein Wnt-8a
- Protein Wnt-2b
- Protein Wnt-2
- Protein Wnt-9b
- Protein Wnt-4
- Protein Wnt-5a
- Protein Wnt-8b
Sequence:
MHLLLVQLLVLLPLGKADLCVDGCQSQGSLSFPLLERGRRDLHVANHEEAEDKPDLFVAVPHLMGTSLAGEGQRQRGKMLSRLGRFWKKPETEFYPPRDVESDHVSSGMQAVTQPADGRKVERSPLQEEAKRFWHRFMFRKGPAFQGVILPIKSHEVHWETCRTVPFNQTIAHEDCQKVVVQNNLCFGKCSSIRFPGEGADAHSFCSHCSPTKFTTVHLMLNCTSPTPVVKMVMQVEECQCMVKTERGEERLLLAGSQGSFIPGLPASKTNP
Protein: SERTA domain-containing protein 2 (Transcriptional regulator interacting with the PHD-bromodomain 2) (TRIP-Br2) (Q9JJG5)
Organism: Mus musculus (Mouse)
Function: Acts at E2F-responsive promoters as coregulator to integrate signals provided by PHD- and/or bromodomain-containing transcription factors. May act as coactivator as well as corepressor of E2F1-TFDP1 and E2F4-TFDP1 complexes on E2F consensus binding sites, which would activate or inhibit E2F-target genes expression. Modulates fat storage by down-regulating the expression of key genes involved in adipocyte lipolysis, thermogenesis and oxidative metabolism.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Exported out of the nucleus via its NES in a XPO1-dependent manner. Once in the cytoplasm, is degraded by the proteasome (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MLGKGGKRKFDEHEDGLEGKIVSPSDGPSRVSYTLQRQTIFNISLMKLYNHRPLTEPSLQKTVLINNMLRRIQEELKQEGSLRPAFTPSSQPSNSLSDSYQEAPPPAPHPCDLGSTTPLEACLTPASLLEDDNDDTFCTLQAVHPAAPTRLSSAALPAEKDSFSSALDEIEELCPTSTSTEAAHTAAPEGPKGTSSESSVQKPEGPEEGRTDDSRFMDSLPGNFEITTSTGFLTDLTLDDILFADIDTSMYDFDPCTSASGTASKMAPVSADDLLKTLAPYSNQPVAPSQPFKMDLTELDHIMEVLVGS
Protein: DNA repair endonuclease XPF (EC 3.1.-.-) (DNA excision repair protein ERCC-4) (Q9QZD4)
Organism: Mus musculus (Mouse)
Function: Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair, and which is essential for nucleotide excision repair (NER) and interstrand cross-link (ICL) repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92889}. Chromosome {ECO:0000250|UniProtKB:Q92889}. Note=Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q92889}.
Interaction partners:
- DNA excision repair protein ERCC-1
- Structure-specific endonuclease subunit SLX4
- DNA repair protein complementing XP-A cells homolog
- Structure-specific endonuclease subunit SLX1
- Structure-specific endonuclease subunit MUS81
- DNA excision repair protein ERCC-5
- Fanconi anemia core complex-associated protein 24
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- DNA repair protein RAD52 homolog
- Fanconi anemia group C protein homolog
Sequence:
MEPGLSGERRSMAPLLEYERQQVLELLDSDGLVVCARGLGTDRLLYHFLRLHCHPACLVLVLNTQPAEEEYFINQLKIEGVEHLPRRVTNEIASNSRYEVYTQGGIIFATSRILVVDFLTGRIPSDLITGILVYRAHRIIESCQEAFILRLFRQKNKRGFIKAFTDNAVAFDTGFCHVERVMRNLFVRKLYLWPRFHVAVNSFLEQHKPEVVEIHVSMTPAMLAIQTAILDILNACLKELKCHNPSLEVEDLSLENALGKPFDKTIRHYLDPLWHQLGAKTKSLVQDLKILRTLLQYLSQYDCVTFLNLLESLRATEKVFGQNSGWLFLDASTSMFVNARARVYRVPDVKLNKKAKTSEKTSSPEVQETKKELVLESNPKWEALTDVLKEIEAENKESEALGGPGRVLICASDDRTCCQLRDYLSAGAETFLLRLYRKTFEKDGKAEEVWVNVRKGDGPKRTTKSDKRPKAAPNKERASAKRGAPLKRKKQELTLTQVLGSAEEPPEDKALEEDLCRQTSSSPEGCGVEIKRESFDLNVSSDAAYGILKEPLTIIHPLLGCSDPYALTRVLHEVEPRYVVLYDAELTFVRQLEIYRASRPGKPLRVYFLIYGGSTEEQRYLTALRKEKEAFEKLIREKASMVVPEEREGRDETNLDLARGSAALDAPTDTRKAGGQEQNGTQSSIVVDMREFRSELPSLIHRRGIDIEPVTLEVGDYILTPELCVERKSVSDLIGSLHSGRLYSQCLAMSRYYRRPVLLIEFDPSKPFSLAPRGAFFQEMSSSDVSSKLTLLTLHFPRLRLLWCPSPHATAELFEELKQNKPQPDAATAMAITADSETLPESDRYNPGPQDFVLKMPGVNAKNCRSLMNQVKNIAELATLSLERLTTILGHSGNAKQLHDFLHTAYADLVSKGRVRK