位置:首页 > 蛋白库 > RUVB2_MOUSE
RUVB2_MOUSE
ID   RUVB2_MOUSE             Reviewed;         463 AA.
AC   Q9WTM5;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=RuvB-like 2;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9Y230};
DE   AltName: Full=p47 protein;
GN   Name=Ruvbl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=10220587; DOI=10.1093/oxfordjournals.jbchem.a022372;
RA   Gohshi T., Simada M., Kawahire S., Imai N., Ichimura T., Omata S.,
RA   Horigome T.;
RT   "Molecular cloning of mouse p47, a second group mammalian RuvB DNA
RT   helicase-like protein: homology with those from human and Saccharomyces
RT   cerevisiae.";
RL   J. Biochem. 125:939-946(1999).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC       dependent DNA helicase (5' to 3') activity; hexamerization is thought
CC       to be critical for ATP hydrolysis and adjacent subunits in the ring-
CC       like structure contribute to the ATPase activity (By similarity).
CC       Component of the NuA4 histone acetyltransferase complex which is
CC       involved in transcriptional activation of select genes principally by
CC       acetylation of nucleosomal histones H4 and H2A (By similarity). This
CC       modification may both alter nucleosome-DNA interactions and promote
CC       interaction of the modified histones with other proteins which
CC       positively regulate transcription (By similarity). This complex may be
CC       required for the activation of transcriptional programs associated with
CC       oncogene and proto-oncogene mediated growth induction, tumor suppressor
CC       mediated growth arrest and replicative senescence, apoptosis, and DNA
CC       repair (By similarity). The NuA4 complex ATPase and helicase activities
CC       seem to be, at least in part, contributed by the association of RUVBL1
CC       and RUVBL2 with EP400 (By similarity). NuA4 may also play a direct role
CC       in DNA repair when recruited to sites of DNA damage (By similarity).
CC       Component of a SWR1-like complex that specifically mediates the removal
CC       of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Proposed
CC       core component of the chromatin remodeling INO80 complex which exhibits
CC       DNA- and nucleosome-activated ATPase activity and catalyzes ATP-
CC       dependent nucleosome sliding (By similarity). Plays an essential role
CC       in oncogenic transformation by MYC and also modulates transcriptional
CC       activation by the LEF1/TCF1-CTNNB1 complex (By similarity). May also
CC       inhibit the transcriptional activity of ATF2 (By similarity). Involved
CC       in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway
CC       where it negatively regulates expression of ER stress response genes
CC       (By similarity). May play a role in regulating the composition of the
CC       U5 snRNP complex (By similarity). {ECO:0000250|UniProtKB:Q9Y230}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y230};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y230};
CC   -!- SUBUNIT: Forms homohexameric rings (Probable). Can form a dodecamer
CC       with RUVBL1 made of two stacked hexameric rings; however, even though
CC       RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status
CC       of each hexamer is not known. Oligomerization may regulate binding to
CC       nucleic acids and conversely, binding to nucleic acids may affect the
CC       dodecameric assembly. Interaction of the complex with DHX34 results in
CC       conformational changes of the N-terminus of the RUVBL2 subunits,
CC       resulting in loss of nucleotide binding ability and ATP hydrolysis of
CC       the complex (By similarity). Interacts with the transcriptional
CC       activation domain of MYC. Interacts With ATF2. Component of the RNA
CC       polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-
CC       CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase
CC       complex which contains the catalytic subunit KAT5/TIP60 and the
CC       subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC       RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
CC       MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4
CC       complex interacts with MYC and the adenovirus E1A protein. RUVBL2
CC       interacts with EP400. Component of a NuA4-related complex which
CC       contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC       RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.
CC       Interacts with NPAT. Component of the chromatin-remodeling INO80
CC       complex; specifically part of a complex module associated with the
CC       helicase ATP-binding and the helicase C-terminal domain of INO80.
CC       Component of some MLL1/MLL complex, at least composed of the core
CC       components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as
CC       the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC       LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC       RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC       TEX10. Interacts with IGHMBP2. Interacts with TELO2. Interacts with
CC       HINT1. Component of a SWR1-like complex. Component of the R2TP complex
CC       composed at least of RUVBL1, RUVBL2, RPAP3 and PIHD1. Component of the
CC       PAQosome complex which is responsible for the biogenesis of several
CC       protein complexes and which consists of R2TP complex members RUVBL1,
CC       RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT
CC       and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. Interacts with
CC       ITFG1. Interacts with ZMYND10. Interacts with WAC; WAC positively
CC       regulates MTOR activity by promoting the assembly of the TTT complex
CC       composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of
CC       RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the
CC       dimerization of the mTORC1 complex and its subsequent activation. Forms
CC       a complex with APPL1 and APPL2 (By similarity). Interacts with ZNHIT2
CC       (via HIT-type zinc finger) in the presence of ATP or ADP; shows a
CC       stronger interaction in the presence of ADP (By similarity). The
CC       RUVBL1/RUVBL2 complex interacts with ZNHIT1 (via HIT-type zinc finger),
CC       ZNHIT3 (via HIT-type zinc finger), ZNHIT6 (via HIT-type zinc finger)
CC       and DDX59/ZNHIT5 (via HIT-type zinc finger) in the presence of ADP (By
CC       similarity). Interacts with NOPCHAP1; the interaction is direct and
CC       disrupted upon ATP binding (By similarity). Interacts with SMG1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9Y230, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9WTM5; P60122: Ruvbl1; NbExp=3; IntAct=EBI-2549911, EBI-1634999;
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q9Y230}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y230}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9Y230}. Membrane
CC       {ECO:0000250|UniProtKB:Q9Y230}. Dynein axonemal particle
CC       {ECO:0000250|UniProtKB:Q9DE27}. Note=Mainly localized in the nucleus,
CC       associated with nuclear matrix or in the nuclear cytosol. Although it
CC       is also present in the cytoplasm and associated with the cell
CC       membranes. {ECO:0000250|UniProtKB:Q9Y230}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB013912; BAA76297.1; -; mRNA.
DR   CCDS; CCDS21243.1; -.
DR   RefSeq; NP_035434.1; NM_011304.3.
DR   RefSeq; XP_006540785.1; XM_006540722.1.
DR   RefSeq; XP_006540786.1; XM_006540723.3.
DR   AlphaFoldDB; Q9WTM5; -.
DR   SMR; Q9WTM5; -.
DR   BioGRID; 203037; 95.
DR   ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR   ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR   ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR   IntAct; Q9WTM5; 71.
DR   MINT; Q9WTM5; -.
DR   STRING; 10090.ENSMUSP00000103400; -.
DR   iPTMnet; Q9WTM5; -.
DR   PhosphoSitePlus; Q9WTM5; -.
DR   SwissPalm; Q9WTM5; -.
DR   REPRODUCTION-2DPAGE; Q9WTM5; -.
DR   EPD; Q9WTM5; -.
DR   jPOST; Q9WTM5; -.
DR   MaxQB; Q9WTM5; -.
DR   PaxDb; Q9WTM5; -.
DR   PRIDE; Q9WTM5; -.
DR   ProteomicsDB; 256663; -.
DR   Antibodypedia; 3244; 429 antibodies from 36 providers.
DR   DNASU; 20174; -.
DR   Ensembl; ENSMUST00000107771; ENSMUSP00000103400; ENSMUSG00000003868.
DR   Ensembl; ENSMUST00000211214; ENSMUSP00000147502; ENSMUSG00000003868.
DR   GeneID; 20174; -.
DR   KEGG; mmu:20174; -.
DR   UCSC; uc009gvc.1; mouse.
DR   CTD; 10856; -.
DR   MGI; MGI:1342299; Ruvbl2.
DR   VEuPathDB; HostDB:ENSMUSG00000003868; -.
DR   eggNOG; KOG2680; Eukaryota.
DR   GeneTree; ENSGT00940000153556; -.
DR   HOGENOM; CLU_028311_4_0_1; -.
DR   InParanoid; Q9WTM5; -.
DR   OMA; YDMGAKM; -.
DR   OrthoDB; 752343at2759; -.
DR   PhylomeDB; Q9WTM5; -.
DR   TreeFam; TF300469; -.
DR   BioGRID-ORCS; 20174; 44 hits in 110 CRISPR screens.
DR   ChiTaRS; Ruvbl2; mouse.
DR   PRO; PR:Q9WTM5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9WTM5; protein.
DR   Bgee; ENSMUSG00000003868; Expressed in epiblast (generic) and 243 other tissues.
DR   ExpressionAtlas; Q9WTM5; baseline and differential.
DR   Genevisible; Q9WTM5; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR   GO; GO:0000791; C:euchromatin; ISO:MGI.
DR   GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0097255; C:R2TP complex; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
DR   GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR   GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR   GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0140585; F:promoter-enhancer loop anchoring activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR   GO; GO:0001094; F:TFIID-class transcription factor complex binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR   GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0043486; P:histone exchange; IC:ComplexPortal.
DR   GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; ISO:MGI.
DR   GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR   GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR   GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR   GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR   GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR   GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR   GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR   GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR   Gene3D; 2.40.50.360; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
DR   InterPro; IPR041048; RuvB-like_C.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR037942; RUVBL2.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093; PTHR11093; 1.
DR   PANTHER; PTHR11093:SF2; PTHR11093:SF2; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ATP-binding; Chromatin regulator; Cytoplasm;
KW   DNA damage; DNA recombination; DNA repair; Helicase; Hydrolase;
KW   Isopeptide bond; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT   CHAIN           2..463
FT                   /note="RuvB-like 2"
FT                   /id="PRO_0000165645"
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT   CROSSLNK        9
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT   CROSSLNK        444
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT   CROSSLNK        456
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y230"
SQ   SEQUENCE   463 AA;  51113 MW;  419D779972933308 CRC64;
     MATVAATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL
     EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT
     QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE
     SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH
     TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE
     VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTS
     PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE
     VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024