wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-1 receptor-like 1 (EC 3.2.2.6) (Interleukin-33 receptor alpha chain) (Lymphocyte antigen 84) (Protein ST2) (Protein T1) (P14719)
Organism: Mus musculus (Mouse)
Function: Receptor for interleukin-33 (IL-33); signaling requires association of the coreceptor IL1RAP. Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8 (By similarity). Possibly involved in helper T-cell function (By similarity). Upon tissue injury, induces UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages.
Subcellular location: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform B]: Secreted.
Interaction partners:
- Interleukin-33
- Interleukin-1 receptor accessory protein
- Myeloid differentiation primary response protein MyD88
- Thymic stromal lymphopoietin
- TNF receptor-associated factor 6
- Somatostatin receptor type 2
- Interleukin-1 beta
- Interleukin-13
- Interleukin-1 receptor-associated kinase 1
- Mast/stem cell growth factor receptor Kit
Sequence:
MIDRQRMGLWALAILTLPMYLTVTEGSKSSWGLENEALIVRCPQRGRSTYPVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRSPNLNKTGYLNVTIHKKPPSCNIPDYLMYSTVRGSDKNFKITCPTIDLYNWTAPVQWFKNCKALQEPRFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTNYIVTATRSFTVEEKGFSMFPVITNPPYNHTMEVEIGKPASIACSACFGKGSHFLADVLWQINKTVVGNFGEARIQEEEGRNESSSNDMDCLTSVLRITGVTEKDLSLEYDCLALNLHGMIRHTIRLRRKQPIDHRSIYYIVAGCSLLLMFINVLVIVLKVFWIEVALFWRDIVTPYKTRNDGKLYDAYIIYPRVFRGSAAGTHSVEYFVHHTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFAYEQEIALHSALIQNNSKVILIEMEPLGEASRLQVGDLQDSLQHLVKIQGTIKWREDHVADKQSLSSKFWKHVRYQMPVPERASKTASVAAPLSGKACLDLKHF
Protein: Oo18 RNA-binding protein, isoform C (Oo18 RNA-binding protein, isoform E) (Q8IMZ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKVLRVNLLSVNSNKIPHQQQQQQQQQQQQQQQQQQNQQQLQVQQQHQLQQQFVNLNRNYEQQISANLGSQQHGFEHNGVGVGASSSGNENCFSQYNLENITSVDMELAKLQNLQRINTLKLLHAQAQQMPLINQLLQSYAGNAIGSVGGSNLGNLMSAGGSSLMTEMAGNVGGIITTNDGHLDRVAKFYKSSAALCDATCTWSGHLPPRSHRMLNYSPKVFLGGIPWDISEQSLIQIFKPFGSIKVEWPGKEQQAAQPKGYVYIIFESDKQVKALLSACVLQVDDSHCGRNYFFKISSRRIKSKDVEVIPWIIADSNFVRSSSQKLDPTKTVFVGALHGKLTAEGLGNIMDDLFDGVLYAGIDTDKYKYPIGSGRVTFSNFRSYMKAVSAAFIEIRTTKFTKKVQVDPYLEDALCSICGVQHGPYYCRELSCFRYFCRSCWQWQHSCDIVKNHKPLTRNSKSQSLVGIGPSSSNVSLPFSGQRSIRDNRMGNGQHQQHQQHQYQQQKHRQLQEYSQPHSLNVMGNSGAANAAATSMVTLQQRQIHKVRIQRQQHQAI
Protein: Transmembrane protein 106B (Q80X71)
Organism: Mus musculus (Mouse)
Function: In neurons, involved in the transport of late endosomes/lysosomes. May be involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking. May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (By similarity). In motoneurons, may mediate the axonal transport of lysosomes and axonal sorting at the initial segment. It remains unclear whether TMEM106B affects the transport of moving lysosomes in the anterograde or retrograde direction in neurites and whether it is particularly important in the sorting of lysosomes in axons or in dendrites (Probable). In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress. Required for proper lysosomal acidification.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:25066864}; Single-pass type II membrane protein. Lysosome membrane {ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:25066864}; Single-pass type II membrane protein. Cell membrane {ECO:0000250|UniProtKB:Q9NUM4}; Single-pass type II membrane protein {ECO:0000255}. Note=Colocalizes with LAMP1. A small fraction resides on the cell surface (By similarity). {ECO:0000250|UniProtKB:Q9NUM4, ECO:0000269|PubMed:23136129, ECO:0000269|PubMed:25066864}.
Interaction partners:
- Progranulin
- Microtubule-associated protein 6
- Charged multivesicular body protein 2b
- TAR DNA-binding protein 43
Sequence:
MGKSLSHLPLHSNKEDGYDGVTSTDNMRNGLVSSEVHNEDGRNGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSGLAVFFLFPRSIEVKYIGVKSAYVSYDAEKRTIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLNNITNIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLLSIKVHNIVLMMQVTVTTAYFGHSEQISQERYQYVDCGRNTTYQLAQSEYLNVLQPQQ
Protein: Circadian clock oscillator protein KaiA (Q79PF6)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator.
Interaction partners:
- Circadian clock oscillator protein KaiB
- Circadian clock oscillator protein KaiC
- Light dependent period A
- Circadian input-output histidine kinase CikA
- Low amplitude and bright protein LabA
- Protein RecA
- Amidophosphoribosyltransferase
- Photosystem I reaction center subunit PsaK
- DUF3285 domain-containing protein
- Circadian phase modifier
Sequence:
MLSQIAICIWVESTAILQDCQRALSADRYQLQVCESGEMLLEYAQTHRDQIDCLILVAANPSFRAVVQQLCFEGVVVPAIVVGDRDSEDPDEPAKEQLYHSAELHLGIHQLEQLPYQVDAALAEFLRLAPVETMADHIMLMGANHDPELSSQQRDLAQRLQERLGYLGVYYKRDPDRFLRNLPAYESQKLHQAMQTSYREIVLSYFSPNSNLNQSIDNFVNMAFFADVPVTKVVEIHMELMDEFAKKLRVEGRSEDILLDYRLTLIDVIAHLCEMYRRSIPRET
Protein: Cell surface glycoprotein CD200 receptor 1 (CD200 cell surface glycoprotein receptor) (Cell surface glycoprotein OX2 receptor 1) (OX102 antigen) (Q9ES58)
Organism: Rattus norvegicus (Rat)
Function: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of pro-inflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- CD200 receptor 1-like
- OX-2 membrane glycoprotein
Sequence:
MLCFWRTSHVAVLLIWGVFAAESSCPDKNQTMQNNSSTMTEVNTTVFVQMGKKALLCCPSISLTKVILITWTITLRGQPSCIISYKADTRETHESNCSDRSITWASTPDLAPDLQISAVALQHEGRYSCDIAVPDGNFQNIYDLQVLVPPEVTHFPGENRTAVCEAIAGKPAAQISWTPDGDCVAKNESHSNGTVTVRSTCHWEQSHVSVVFCVVSHLTTGNQSLSIELGRGGDQLLGSYIQYIIPSIIILIIIGCICLLKISGCRKCKLPKSGATPDIEEDEMQPYASYTEKSNPLYDTVTTTEAHPASQGKVNGTDCLTLSAMGI
Protein: GRF-interacting factor 1 (ZmGIF1) (Protein ANGUSTIFOLIA 3 homolog) (A5HEH4)
Organism: Zea mays (Maize)
Function: Transcription coactivator that plays a role in the regulation of meristematic function in leaves, stems and inflorescences. Regulates shoot architecture and meristem determinacy. Binds to the inflorescence architecture gene UB3 (unbranched3). Regulates the expression of several genes involved in inflorescence architecture. Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (Probable). Associates with the core SWI/SNF chromatin-remodeling complex and specific GRFs to tightly regulate the transition between cell division and cell expansion in growing leaves.
Interaction partners:
- Growth-regulating factor
- Growth-regulating factor
- Growth-regulating factor
- Growth-regulating factor
- Growth-regulating factor
- Growth-regulating factor
- Putative homeobox DNA-binding domain superfamily protein
- GW2
- GW2
- GW2
Sequence:
MQQQHLMQMNQNMMGGYTSPAAVTTDLIQQYLDENKQLILAILDNQNNGKAEECERHQAKLQHNLMYLAAIADSQPPQTAPLSQYPSNLMMQPGPRYMPPQSGQMMNPQSLMAARSSMMYAHPSLSPLQQQQAAHGQLGMAPGGGGGGTTSGFSILHGEASMGGGGAGAGAGNNMMNAGMFSGFGRSGSGAKEGSTSLSVDVRGGTSSGAQSGDGEYLKVGTEEEGS
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (E2K) (Q01205)
Organism: Rattus norvegicus (Rat)
Function: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P36957}. Nucleus {ECO:0000250|UniProtKB:P36957}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P36957}.
Interaction partners:
- 2-oxoadipate dehydrogenase complex component E1
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
Sequence:
MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPDSRKMVINNSSVFSVRFFQTTAVCKNDVITVQTPAFAESVTEGDVRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPATAYKAAPEAPAAPPPPVAPVPTQMPPVPSPSQPPSSKPVSAIKPTAAPPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
Protein: Scinderin (Adseverin) (E9PU64)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, podosome {ECO:0000256|ARBA:ARBA00004188}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Gelsolin
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
Sequence:
MAQELQHPEFARAGKQAGLQVWRVEKLELVPVPQGAYGDFYVGDAYLVLHTTKSSRGFSYRLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQSRELQGYESTDFVGYFKGGLKYKAGGVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWQSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKASQVATGIRDNERKGRSQLIVVEEGSEPPELMKVLGRKPELPDGDNDDDVIADISNRKMAKLYMVSDASGSMKVTLVAEENPFSMGMLLPEECFILDHGAAKQIFVWKGKNANPQERKTAMKTAEEFLHKMNYSANTQIQVLPEGGETPIFKQFFKDWKDKDQSDGFGKVYITEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGGVEIWRVENSGRVQIDPSSYGEFYGGDCYIILYTYPRGQIIYTWQGADATRDELTMSAFLTVQLDRSLGGQAVQVRVSQGKEPAHLLSLFKDKPLIIYKNGTSKKGGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDTFVLKLPRNNGFIWIGKGASQEEEKGAEYVADVLKCKTTRIQEGKEPDEFWNSLGGRGDYQTSPLLETQAEDHPPRLYGCSNKTGRFIIEEVPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESVKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSKW
Protein: c-Myc-binding protein (A0A087WV05)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- c-Myc-binding protein
- Leucine-rich repeat and guanylate kinase domain-containing protein
Sequence:
MVCFSDLPKLRKAADSKREQFRRYLEKSGVLDTLTKVLVALYEEPEKPNSALDFLKHHLGAATPENPEIELLRLELAEMKEKYEAIVEENKKLKAKLAQYEPPQEEKRAE
Protein: Tectonic family member 2 (Tectonic-2) (F1R5E2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MRHFSSFHIGFYFTCIIFTFLNDGTVCNVVFQPAFIQASGPKISSFLVGNVSGISFSLSAVSSSNATGSILPPSCLPVYQPQWNLSYELIGKNAFLVHVSLNRSLQLCGNETSISDCCLELLCVQETLLVSACVDETPKASLIIQTQIYAQIHPSKPPSVNKTVIPNQVFQPLGQCPCDVSPGECDIRCCCDQDCTREVLGLFATQCFLGPYGGSFSPVPEYQCSAQPSENDPDWFPFLCVISPSYNNPFLGLFYHGGTVSPKPSPSFQAPQMTATLPPINYRQGDPIFTKDDKYFTIPQNTGTGQCVENAPVAFLENFEFQCVRRLQFCPSPSDDLRVDVKDGQGGVIAVSVVDDVADNIRLFVSNSPEVTSEPQQCDNVVVSLRYTFYWRENGLTAIAVTRTTANITVPVTLTSRYSAVFVNGNETSQSYSGYQVMRPVIGGVLDSETGVVQRTQISLWQPAGDGLCSSAKLRSALFGINSTSGCVVPVSLMNMTQCSLLRETLRSLLDGLVTATLVSTSGKPDFYNLTDWVNITTSQQNQSQSAEGSKGECSAVPTHLHIHVKSSIMEIVQGVPQMFIQSMQISFIERTWKIECGVGMMDPCLNPELMQNFPVTSSVTFTDLSLYSQPPRSRFSINFTEFDCDRNDVCWPELAFPFTTYYTGEPYSEALAKGLTLVFFFIAASVLGTPWRQIRQAWRNA
Protein: Nuclear factor 1 (C9JWJ8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MLPACRLQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKPEIKQKWASRLLAKLRKDIRPEFREDFVLTITGKKPPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLYKSPQCSNPGLCVQPHHIGVTIKELDLYLAYFVHTPESGQSDSSNQQGDADIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLESPSYYNINQVTLGRRSITSPPSTSTTKRPKSIDDSEMESPVDDVFYPGTGRSPAAGSSQSSGWPNDVDAGSPRATASALHFPSTSIIQQSSPYFTHPTIRYHHHHGQDSLKEFVQFVCSDGSGQATGQPNGSGQGKVPGSFLLPPPPPVARPVPLPMPDSKSTSTAPDGAALTPPSPSFATTGASSANRFVSIGPRDGNFLNIPQQSQSWFL
Protein: Adenine permease AdeP (P31466)
Organism: Escherichia coli (strain K12)
Function: High-affinity transporter for adenine.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:24214977}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:24214977}.
Interaction partners:
- Uric acid transporter UacT
- Xanthine permease XanP
- Uracil permease
- Xanthine permease XanQ
- Phosphoribosylformylglycinamidine synthase
- Putative purine permease YbbY
- Putative pyrimidine permease RutG
- Guanine/hypoxanthine permease GhxP
Sequence:
MSHQHTTQTSGQGMLERVFKLREHGTTARTEVIAGFTTFLTMVYIVFVNPQILGVAGMDTSAVFVTTCLIAAFGSIMMGLFANLPVALAPAMGLNAFFAFVVVQAMGLPWQVGMGAIFWGAIGLLLLTIFRVRYWMIANIPVSLRVGITSGIGLFIGMMGLKNAGVIVANPETLVSIGNLTSHSVLLGILGFFIIAILASRNIHAAVLVSIVVTTLLGWMLGDVHYNGIVSAPPSVMTVVGHVDLAGSFNLGLAGVIFSFMLVNLFDSSGTLIGVTDKAGLADEKGKFPRMKQALYVDSISSVTGSFIGTSSVTAYIESSSGVSVGGRTGLTAVVVGLLFLLVIFLSPLAGMVPGYAAAGALIYVGVLMTSSLARVNWQDLTESVPAFITAVMMPFSFSITEGIALGFISYCVMKIGTGRLRDLSPCVIIVALLFILKIVFIDAH
Protein: DNA polymerase processivity factor (Polymerase accessory protein) (Q77CD8)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MLQPPSHLRADEGEARLTAGLSDGGNGNPIASASLIGRQLADVSALLSPFGASLRNAFLVFSREGMLVHSGLYDEQVYVAVPAEKFTSFQWAPARDDARAVFLANVDSRRGLLDAFRADKTRTVQNVAFLITGEPPASVLTQVTYFREADALLQASLVKHELGEYSIMLPTRGADLAVSLSRPQLSKLQAVAKDPNEAVVFAYRRARCLSAESASGRASFAARHEGGESGAELQLALAPSAGSERIFARAQGGGRRAALLEVRCSGGAPDFRLELESPSGFRRLLQKVRQVGGDALVRFYLAPASAAMMSVSTAAPEGLTVFFFCRPATATASADDADDCAEPAPRLPAKRPAASGQPRRGAGAGIQTDGAHPVAVSGGRARKRPRADAGAPGPSSGPDRGGEGGETP
Protein: Putative peptidyl-tRNA hydrolase PTRHD1 (EC 3.1.1.29) (Peptidyl-tRNA hydrolase domain-containing protein 1) (Q6GMV3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHRGVGPAFRVVRKMAASGAEPQVLVQYLVLRKDLSQAPFSWPAGALVAQACHAATAALHTHRDHPHTAAYLQELGRMRKVVLEAPDETTLKELAETLQQKNIDHMLWLEQPENIATCIALRPYPKEEVGQYLKKFRLFK
Protein: Tenascin C (A0A8I6AG89)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MGAVTWLLPGIFLALFALTPEGGVLKKVIRHKRESGLNLTLPEENQPVVFNHIYNIKLPMGSQCSVDLESTSGEKDLSPTPESSGSFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELEMLVSSLREQCTMGTGCCLQPAEGRLDSRPFCSGRGNFSAEGCGCVCEPGWKGPNCSEPECPGNCNLRGQCLDGQCICDQGFTGEDCSQLACPNDCNDQGKCVNGVCVCFEGYAGLDCGLEVCPVPCSEEHGMCVDGRCVCKDGFAGEDCNEPLCFNNCNNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGELTCPNNCQGHGQCEEGQCVCNEGFAGADCSEKRCPADCHHHGRCLNGQCECDDGFTGADCGELQCPNGCSGHGRCVNGQCVCDEGYTGEDCSQRRCPNDCHNRGHCVQGKCICEQGFKGFDCSEMSCPNDCHQHGRCVNGMCICDDDYTGEDCRDRRCPRDCSQRGRCVDGQCICEDGFTGSDCAELSCPGDCHGHGRCVNGQCICHEGFTGKDCKEQRCPSDCHGQGRCEDGQCICHEGFTGLDCGQRSCPNDCSNQGQCVAGRCICNEGYTGVDCSEVSPPKDLIVTEVTEETVNLAWDNEMRVTEYLIMYTPTHADGLEMQFRVPGDQTSTTIRELEPGVEYFIHVFAILENKRSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKKVTTTRLDAPSQIEVRDITDTTALITWSKPLAEIDSIELSYGIKDVPGDRTTIDLTHEDNQYSIGNLKPDTEYEVSLISRRVDMASNPAKETFITGLDAPRNLRRVSQTDNSITLEWRNVKADIDSYRIKYAPISGGDHAEIDVPKSQQATTKTTLTGLRPGTEYGVGVSAVKGDKEGDPATINAATEIDAPRDLQVSETTQDSLTLFWKTPLAKFDRYRLNYSLPTGQSIEIQLPKDATSHVLTDLEPGQEYTVLLTAEKGRHKSKPARVKASTEEVPSLENLTVTEAGWDGLRLNWTADDLAYEYFVIQVQEANKVETAHNFTVLGNLRTADIPGLKAATPYRVSIYGVARGYKTPVLSAETFTGKTPSLGEVTVAEVGWDALKLNWTAPEGAYTNFFIQVLEADMTQTVQNLTVPGGLRSVDLPGLKAATRYYITVRGVTQDFSTAPLSVEVLTEEIPQLGGLSVTEVSWDSLTLNWTTDDLAYKHFIIQVQEANNVEAAQNLTVSGSLRVVDIPGLKADTPYRVSIYGVIQGYRTPMLSADVSTAKEPEIGNLNISDVTPESFNLSWTATDGIFDMFTIEIIDSNRLLQTAEHNISGAERTAHISGLPPSTDFIVYLSGIAPSIRTKTISTTATTEAEPEVDNLLVSDATPDGFRLSWTADEGIFDSFVIRIRDTKKQSEPQEITLPSPDRTRDITGLREATEYEIELYGISRGRRSQPVSAIATTAMGSPKEIMFSDITENAATVSWRAPTAQVESFRITYVPVTGGPPSMVTVDGTDTETRLVRLTPGVEYHVSVIAMKGFEESDPVSGSLITALDGPSGLLTANITDSEALAMWQPAIATVDSYVISYTGERVPEITRTVSGNTVEFELHDLEPATEYTLSVFAEKGHQKSSTIATKFTTDLDSPRELTATEVQSETALLTWRPPRASVTGYLLVYESVDGTVKEVIVGPDTTSYSLADLSPSTHYTARIQALSGSLRSKLIQTIFTTIGLLYPFPRDCSQAMLNGDTTSGLYTIYINGDKTQALEVYCDMTSDGGGWIVFLRRKNGREDFYRNWKAYAAGFGDRREEFWLGLDNLSKITAQGQYELRVDLQDHGESAYAVYDRFSVGDAKSRYKLKVEGYSGTAGDSMNYHNGRSFSTYDKDTDSAITNCALSYKGAFWYKNCHRVNLMGRYGDNNHSQGVNWFHWKGHEYSIQFAEMKLRPSNFRNLEGRRKRA
Protein: Mkl1 variant 1 Mkl1_S (Myocardin related transcription factor A) (W0Z7M9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTLLEPEMLMMAVQSVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEAIIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLEARVSEPLLSATSASPTQVVSQLPMGRDSREMLFLAEQPPLPPPPLLPPSLTNGTTIPTAKSTPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDRGAPPMDSSYAKILQQQQLFLQLQILNQQQQQHHNYQAILPAPPKSAGEALGSSGTPPVRSLSTTNSSSSSGAPGPCGLARQNSTSLTGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQISPVPGAPKAPAATSILHKAGEVVVAFPAARLSTGPALVAAGLAPAEVVVATVASSGVVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDTFGEMVTSPLTQLTLQASPLQILVKEEGPRAGSCCLSPGGRAELEGRDKDQMLQEKDKQIEALTRMLRQKQQLVERLKLQLEQEKRAQQPAPAPAPLGTPVKQENSFSSCQLSQQPLGPAHPFNPSLAAPATNHIDPCAVAPGPPSVVVKQEALQPEPEPVPAPQLLLGPQGPSLIKGVAPPTLITDSTGTHLVLTVTNKNADSPGLSSGSPQQPSSQPGSPAPAPSAQMDLEHPLQPLFGTPTSLLKKEPPGYEEAMSQQPKQQENGSSSQQMDDLFDILIQSGEISADFKEPPSLPGKEKPSPKTVCGSPLAAQPSPSAELPQAAPPPPGSPSLPGRLEDFLESSTGLPLLTSGHDGPEPLSLIDDLHSQMLSSTAILDHPPSPMDTSELHFVPEPSSTMGLDLADGHLDSMDWLELSSGGPVLSLAPLSTTAPSLFSTDFLDGHDLQLHWDSCL
Protein: Protein NipSnap homolog 3B (NipSnap3B) (NipSnap-related protein) (Protein NipSnap homolog 3A) (NipSnap3A) (Q9CQE1)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol. Note=May be part of some vesicular structure distinct from lysosomal vesicles. {ECO:0000250}.
Interaction partners:
Sequence:
MLALRSGLRTALAPRVLTPQVCSPFATGPRQSNGTFYEFRTYFLKPSKTNEFLENFKNSVHLRTAHSEMIGYWTVEFGGRTNRVFHIWKYDNFAHRTAVRKALAKDKEWQERFLIPNLAFIDKQEVEITYLVPWCKIGTPPKEGVYELATFQMKPGGPALWGNAFKRAVNAHVELGYSTLVGVFHTEYGALNRVHVLWWNESADSRAAGRHWSHEDPRVVAAVRESVSYLESQQNTFLIPTSFSPLK
Protein: Ras-like protein family member 10A (EC 3.6.5.2) (Ras-like protein RRP22) (Ras-related protein on chromosome 22) (Q92737)
Organism: Homo sapiens (Human)
Function: Potent inhibitor of cellular proliferation.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus, nucleolus {ECO:0000269|PubMed:15833841}. Note=May cycle in and out of the nucleolus in a GTP-dependent manner.
Interaction partners:
- GAS2-like protein 1
- AP-1 complex subunit beta-1
- GAS2-like protein 2
- Growth arrest-specific protein 2
- Sperm surface protein Sp17
- Ras-related protein Rap-1b
- RNA-binding protein EWS
- Rap1 GTPase-GDP dissociation stimulator 1
Sequence:
MGGSLRVAVLGAPGVGKTAIIRQFLFGDYPERHRPTDGPRLYRPAVLLDGAVYDLSIRDGDVAGPGSSPGGPEEWPDAKDWSLQDTDAFVLVYDICSPDSFDYVKALRQRIAETRPAGAPEAPILVVGNKRDRQRLRFGPRRALAALVRRGWRCGYLECSAKYNWHVLRLFRELLRCALVRARPAHPALRLQGALHPARCSLM
Protein: tRNA endonuclease ANKZF1 (EC 3.1.-.-) (Ankyrin repeat and zinc finger domain-containing protein 1) (Zinc finger protein 744) (Q9H8Y5)
Organism: Homo sapiens (Human)
Function: Plays a role in the cellular response to hydrogen peroxide and in the maintenance of mitochondrial integrity under conditions of cellular stress. Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28302725}. Note=Translocates to the mitochondria upon exposure to hydrogen peroxide. {ECO:0000269|PubMed:28302725}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- E3 ubiquitin-protein ligase listerin
- Ribosome quality control complex subunit NEMF
- Nuclear protein localization protein 4 homolog
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Eukaryotic translation initiation factor 6
- Ribosome quality control complex subunit TCF25
- Ubiquitin conjugation factor E4 B
- Ubiquitin conjugation factor E4 A
- Outer mitochondrial transmembrane helix translocase
Sequence:
MSPAPDAAPAPASISLFDLSADAPVFQGLSLVSHAPGEALARAPRTSCSGSGERESPERKLLQGPMDISEKLFCSTCDQTFQNHQEQREHYKLDWHRFNLKQRLKDKPLLSALDFEKQSSTGDLSSISGSEDSDSASEEDLQTLDRERATFEKLSRPPGFYPHRVLFQNAQGQFLYAYRCVLGPHQDPPEEAELLLQNLQSRGPRDCVVLMAAAGHFAGAIFQGREVVTHKTFHRYTVRAKRGTAQGLRDARGGPSHSAGANLRRYNEATLYKDVRDLLAGPSWAKALEEAGTILLRAPRSGRSLFFGGKGAPLQRGDPRLWDIPLATRRPTFQELQRVLHKLTTLHVYEEDPREAVRLHSPQTHWKTVREERKKPTEEEIRKICRDEKEALGQNEESPKQGSGSEGEDGFQVELELVELTVGTLDLCESEVLPKRRRRKRNKKEKSRDQEAGAHRTLLQQTQEEEPSTQSSQAVAAPLGPLLDEAKAPGQPELWNALLAACRAGDVGVLKLQLAPSPADPRVLSLLSAPLGSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEKNPDAYDYNKAQVPGPLTPEMEARQATRKREQKAARRQREEQQQRQQEQEEREREEQRRFAALSDREKRALAAERRLAAQLGAPTSPIPDSAIVNTRRCWSCGASLQGLTPFHYLDFSFCSTRCLQDHRRQAGRPSS
Protein: GTP-binding protein rho4 (Q874R1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cell separation. Involved in the regulation of the septum degradation during cytokinesis and in the organization of F-actin patches and cytoplasmic microtubules.
Subcellular location: Membrane {ECO:0000269|PubMed:12653963, ECO:0000269|PubMed:12796297}. Note=Membrane-bound. Associates with the septum during mitosis.
Interaction partners:
- Probable Rho-type GTPase-activating protein 3
- Probable Rho-type GTPase-activating protein 4
- Septin ring organizing protein mid2
- Rho GDP-dissociation inhibitor
- Rho1 guanine nucleotide exchange factor 3
- Rho guanine nucleotide exchange factor gef3
- Primary septum glucan endo-1,3-beta-D-glucosidase
- Glucan endo-1,3-alpha-glucosidase agn1
- Rho-type GTPase-activating protein 1
- Exocyst complex component exo70
Sequence:
MSAFKKSGSKSETSKKLVVVGDGGCGKTCLLIVFSSGTFPERYVPTVFENYITDITYGPNSKVIELALWDTAGQEEYDRLRPLSYPNSNVILLCFSIDCPASLNNVTEKWYPEVQHFCPRTPIVLVGLKADLRKDRNATEVLRTQGLTPVTYQQAQSVALSMNAPYVECSAKENTGVNEVFQLAVGLTIKKSFSFSKKSCVIL