RUVB1_MOUSE
ID RUVB1_MOUSE Reviewed; 456 AA.
AC P60122; O35753;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=RuvB-like 1;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9Y265};
DE AltName: Full=49 kDa TATA box-binding protein-interacting protein;
DE Short=49 kDa TBP-interacting protein;
DE AltName: Full=DNA helicase p50;
DE AltName: Full=Pontin 52;
DE AltName: Full=TIP49a;
GN Name=Ruvbl1; Synonyms=Tip49, Tip49a;
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=Mammary gland;
RX PubMed=9843967; DOI=10.1073/pnas.95.25.14787;
RA Bauer A., Huber O., Kemler R.;
RT "Pontin52, an interaction partner of beta-catenin, binds to the TATA box
RT binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14787-14792(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 318-333.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 (3' to 5') 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). Essential
CC for cell proliferation (By similarity). May be able to bind plasminogen
CC at cell surface and enhance plasminogen activation (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y265}.
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:Q9Y265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9Y265};
CC -!- SUBUNIT: Forms homohexameric rings. Can form a dodecamer with RUVBL2
CC made of two stacked hexameric rings; however, even though RUVBL1 and
CC RUVBL2 are present in equimolar ratio, the oligomeric status of each
CC hexamer is not known. Oligomerization may regulate binding to nucleic
CC 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. Component of the RNA polymerase II holoenzyme
CC complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex and TBP.
CC Component of the NuA4 histone acetyltransferase complex which contains
CC the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400,
CC BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin,
CC ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41,
CC VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the
CC adenovirus E1A protein. RUVBL1 interacts with EP400. Component of a
CC NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP,
CC BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
CC ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Component of the BAF53 complex,
CC at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and
CC TRRAP/PAF400. Component of some MLL1/MLL complex, at least composed of
CC the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as
CC well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Associates with alpha and gamma tubulins, particularly during
CC metaphase and early anaphase. Interacts with NPAT. Component of the
CC chromatin-remodeling INO80 complex; specifically part of a complex
CC module associated with the helicase ATP-binding and the helicase C-
CC terminal domain of INO80. Interacts with IGHMBP2. Interacts with OFD1.
CC Interacts with HINT1. Component of a complex with USP49 and PSMC5.
CC 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 PIH1D1. Interacts with ITFG1. 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 (By
CC similarity). The RUVBL1/RUVBL2 complex interacts with ZNHIT1 (via HIT-
CC type zinc finger), ZNHIT3 (via HIT-type zinc finger), ZNHIT6 (via HIT-
CC type zinc finger) and DDX59/ZNHIT5 (via HIT-type zinc finger) in the
CC presence of ADP (By similarity). Interacts with NOPCHAP1; the
CC interaction is direct and disrupted upon ATP binding (By similarity).
CC Interacts with SMG1 (By similarity). {ECO:0000250|UniProtKB:Q9Y265}.
CC -!- INTERACTION:
CC P60122; Q9WTM5: Ruvbl2; NbExp=3; IntAct=EBI-1634999, EBI-2549911;
CC P60122; Q9UHK0: NUFIP1; Xeno; NbExp=2; IntAct=EBI-1634999, EBI-2563549;
CC P60122; Q9NWS0: PIH1D1; Xeno; NbExp=2; IntAct=EBI-1634999, EBI-357318;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q9Y265}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y265}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y265}. Membrane
CC {ECO:0000250|UniProtKB:Q9Y265}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y265}. Dynein
CC axonemal particle {ECO:0000250|UniProtKB:Q9DE26}. Note=Mainly localized
CC in the nucleus, associated with nuclear matrix or in the nuclear
CC cytosol, although it is also present in the cytoplasm and associated
CC with the cell membranes. In prophase and prometaphase it is located at
CC the centrosome and the branching microtubule spindles. After mitotic
CC nuclear membrane disintigration it accumulates at the centrosome and
CC sites of tubulin polymerization. As cells pass through metaphase and
CC into telophase it is located close to the centrosome at the early phase
CC of tubulin polymerization. In anaphase it accumulates at the zone of
CC tubule interdigitation. In telophase it is found at polar tubule
CC overlap, and it reappears at the site of chromosomal decondensation in
CC the daughter cells. {ECO:0000250|UniProtKB:Q9Y265}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR EMBL; AF100694; AAD02877.1; -; mRNA.
DR EMBL; BC004718; AAH04718.1; -; mRNA.
DR CCDS; CCDS20336.1; -.
DR RefSeq; NP_062659.1; NM_019685.3.
DR AlphaFoldDB; P60122; -.
DR SMR; P60122; -.
DR BioGRID; 208024; 106.
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; P60122; 179.
DR MINT; P60122; -.
DR STRING; 10090.ENSMUSP00000032165; -.
DR iPTMnet; P60122; -.
DR PhosphoSitePlus; P60122; -.
DR SwissPalm; P60122; -.
DR EPD; P60122; -.
DR jPOST; P60122; -.
DR PaxDb; P60122; -.
DR PeptideAtlas; P60122; -.
DR PRIDE; P60122; -.
DR ProteomicsDB; 256662; -.
DR Antibodypedia; 17283; 387 antibodies from 34 providers.
DR DNASU; 56505; -.
DR Ensembl; ENSMUST00000032165; ENSMUSP00000032165; ENSMUSG00000030079.
DR GeneID; 56505; -.
DR KEGG; mmu:56505; -.
DR UCSC; uc009cvh.1; mouse.
DR CTD; 8607; -.
DR MGI; MGI:1928760; Ruvbl1.
DR VEuPathDB; HostDB:ENSMUSG00000030079; -.
DR eggNOG; KOG1942; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; P60122; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; P60122; -.
DR TreeFam; TF300457; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR BioGRID-ORCS; 56505; 46 hits in 111 CRISPR screens.
DR ChiTaRS; Ruvbl1; mouse.
DR PRO; PR:P60122; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P60122; protein.
DR Bgee; ENSMUSG00000030079; Expressed in epiblast (generic) and 79 other tissues.
DR ExpressionAtlas; P60122; baseline and differential.
DR Genevisible; P60122; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; 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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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:0043138; F:3'-5' DNA helicase activity; ISO:MGI.
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:0003678; F:DNA helicase activity; 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:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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: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:0090263; P:positive 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:0010756; P:positive regulation of plasminogen activation; ISO:MGI.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
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:2000269; P:regulation of fibroblast apoptotic process; ISO:MGI.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; IPR037938; RUVBL1.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF6; PTHR11093:SF6; 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; Cell cycle; Cell division;
KW Chromatin regulator; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW DNA damage; DNA recombination; DNA repair; Growth regulation; Helicase;
KW Hydrolase; Isopeptide bond; Membrane; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..456
FT /note="RuvB-like 1"
FT /id="PRO_0000165640"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 453
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y265"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y265"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y265"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y265"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y265"
SQ SEQUENCE 456 AA; 50214 MW; 9AE73EFFBA194BA1 CRC64;
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG VAELVPGVLF
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK
