RUVB1_YEAST
ID RUVB1_YEAST Reviewed; 463 AA.
AC Q03940; D6VSH3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=RuvB-like protein 1;
DE Short=RUVBL1;
DE EC=3.6.4.12;
DE AltName: Full=TIP49-homology protein 1;
DE AltName: Full=TIP49a homolog;
GN Name=RVB1; Synonyms=TIH1, TIP49A; OrderedLocusNames=YDR190C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH RVB2.
RX PubMed=10787406; DOI=10.1074/jbc.m001031200;
RA Lim C.R., Kimata Y., Ohdate H., Kokubo T., Kikuchi N., Horigome T.,
RA Kohno K.;
RT "The Saccharomyces cerevisiae RuvB-like protein, Tih2p, is required for
RT cell cycle progression and RNA polymerase II-directed transcription.";
RL J. Biol. Chem. 275:22409-22417(2000).
RN [4]
RP IDENTIFICATION IN THE INO80 COMPLEX, FUNCTION OF THE INO80 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10952318; DOI=10.1038/35020123;
RA Shen X., Mizuguchi G., Hamiche A., Wu C.;
RT "A chromatin remodelling complex involved in transcription and DNA
RT processing.";
RL Nature 406:541-544(2000).
RN [5]
RP FUNCTION, INTERACTION WITH RVB2, IDENTIFICATION IN A COMPLEX WITH RBV2;
RP ACT1 AND ARP4, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP LYS-85 AND GLU-312.
RX PubMed=11278922; DOI=10.1074/jbc.m011523200;
RA Jonsson Z.O., Dhar S.K., Narlikar G.J., Auty R., Wagle N., Pellman D.,
RA Pratt R.E., Kingston R., Dutta A.;
RT "Rvb1p and Rvb2p are essential components of a chromatin remodeling complex
RT that regulates transcription of over 5% of yeast genes.";
RL J. Biol. Chem. 276:16279-16288(2001).
RN [6]
RP INTERACTION WITH SPT15.
RX PubMed=12576485; DOI=10.1074/jbc.m213220200;
RA Ohdate H., Lim C.R., Kokubo T., Matsubara K., Kimata Y., Kohno K.;
RT "Impairment of the DNA binding activity of the TATA-binding protein renders
RT the transcriptional function of Rvb2p/Tih2p, the yeast RuvB-like protein,
RT essential for cell growth.";
RL J. Biol. Chem. 278:14647-14656(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [8]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP PROTEIN SEQUENCE OF 2-17, ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15525518; DOI=10.1016/j.molcel.2004.09.033;
RA Jonsson Z.O., Jha S., Wohlschlegel J.A., Dutta A.;
RT "Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin
RT remodeling complex.";
RL Mol. Cell 16:465-477(2004).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [13]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645854; DOI=10.1126/science.1090701;
RA Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT remodeling complex.";
RL Science 303:343-348(2004).
RN [14]
RP INTERACTION WITH HSP90, IDENTIFICATION IN THE R2PT COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15766533; DOI=10.1016/j.cell.2004.12.024;
RA Zhao R., Davey M.G., Hsu Y.-C., Kaplanek P., Tong A., Parsons A.B.,
RA Krogan N.J., Cagney G., Mai D., Greenblatt J.F., Boone C., Emili A.,
RA Houry W.A.;
RT "Navigating the chaperone network: an integrative map of physical and
RT genetic interactions mediated by the hsp90 chaperone.";
RL Cell 120:715-727(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: DNA helicase which participates in several chromatin
CC remodeling complexes, including the SWR1 and the INO80 complexes. The
CC SWR1 complex mediates the ATP-dependent exchange of histone H2A for the
CC H2A variant HZT1 leading to transcriptional regulation of selected
CC genes by chromatin remodeling. The INO80 complex remodels chromatin by
CC shifting nucleosomes. Its ability to induce transcription of some
CC phosphate-responsive genes is modulated by inositol polyphosphates. The
CC INO80 complex is involved in DNA repair by associating to 'Ser-129'
CC phosphorylated H2A histones as a response to DNA damage. RVB1 recruits
CC ARP5 to the INO80 complex. During transcription may recruit SPT15/TBP
CC to the TATA-boxes of involved genes. Required for box C/D and box H/ACA
CC snoRNA accumulation and involved in pre-rRNA processing.
CC {ECO:0000269|PubMed:10952318, ECO:0000269|PubMed:11278922,
CC ECO:0000269|PubMed:14645854, ECO:0000269|PubMed:14690608,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15525518}.
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 -!- SUBUNIT: Probably forms a homohexamer. Interacts with RVB2 and may form
CC heterododecamers with RVB2. Component of the SWR1 chromatin remodeling
CC complex composed of at least ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71,
CC VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and perhaps BDF1. Component of
CC the chromatin-remodeling INO80 complex, at least composed of ARP4,
CC ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1,
CC IES2, IES5 and INO80. Component of the R2TP complex composed of at
CC least RVB1, RVB2, TAH1 and PIH1. Interacts with SPT15/TBP and HSP90.
CC {ECO:0000269|PubMed:10787406, ECO:0000269|PubMed:10952318,
CC ECO:0000269|PubMed:11278922, ECO:0000269|PubMed:12576485,
CC ECO:0000269|PubMed:14645854, ECO:0000269|PubMed:14690608,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15525518,
CC ECO:0000269|PubMed:15766533}.
CC -!- INTERACTION:
CC Q03940; P38768: PIH1; NbExp=10; IntAct=EBI-30712, EBI-24499;
CC Q03940; Q12464: RVB2; NbExp=21; IntAct=EBI-30712, EBI-31814;
CC Q03940; P13393: SPT15; NbExp=3; IntAct=EBI-30712, EBI-19129;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 11600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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; Z48784; CAA88704.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12033.1; -; Genomic_DNA.
DR PIR; S52698; S52698.
DR RefSeq; NP_010476.1; NM_001180498.1.
DR PDB; 6GEJ; EM; 3.60 A; T/V/X=1-463.
DR PDB; 6GEN; EM; 3.60 A; T/V/X=1-463.
DR PDBsum; 6GEJ; -.
DR PDBsum; 6GEN; -.
DR AlphaFoldDB; Q03940; -.
DR SMR; Q03940; -.
DR BioGRID; 32243; 626.
DR ComplexPortal; CPX-1814; R2TP co-chaperone complex.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR DIP; DIP-4896N; -.
DR IntAct; Q03940; 158.
DR MINT; Q03940; -.
DR STRING; 4932.YDR190C; -.
DR iPTMnet; Q03940; -.
DR MaxQB; Q03940; -.
DR PaxDb; Q03940; -.
DR PRIDE; Q03940; -.
DR EnsemblFungi; YDR190C_mRNA; YDR190C; YDR190C.
DR GeneID; 851771; -.
DR KEGG; sce:YDR190C; -.
DR SGD; S000002598; RVB1.
DR VEuPathDB; FungiDB:YDR190C; -.
DR eggNOG; KOG1942; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; Q03940; -.
DR OMA; VIYVEAN; -.
DR BioCyc; YEAST:G3O-29778-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR PRO; PR:Q03940; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03940; protein.
DR GO; GO:0070209; C:ASTRA complex; HDA:SGD.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0031011; C:Ino80 complex; IPI:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0097255; C:R2TP complex; IDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IPI:SGD.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC: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 3D-structure; Acetylation; Activator; ATP-binding; Chromatin regulator;
KW Direct protein sequencing; DNA damage; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15525518"
FT CHAIN 2..463
FT /note="RuvB-like protein 1"
FT /id="PRO_0000165661"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000269|PubMed:15525518"
FT MUTAGEN 85
FT /note="K->E: Lethal."
FT /evidence="ECO:0000269|PubMed:11278922"
FT MUTAGEN 312
FT /note="E->G: Lethal."
FT /evidence="ECO:0000269|PubMed:11278922"
SQ SEQUENCE 463 AA; 50453 MW; 93D6ECB7006AF0F2 CRC64;
MVAISEVKEN PGVNSSNSGA VTRTAAHTHI KGLGLDESGV AKRVEGGFVG QIEAREACGV
IVDLIKAKKM SGRAILLAGG PSTGKTALAL AISQELGPKV PFCPLVGSEL YSVEVKKTET
LMENFRRAIG LRIKETKEVY EGEVTELTPE DAENPLGGYG KTISHVIVGL KSAKGTKTLR
LDPTIYESIQ REKVSIGDVI YIEANTGAVK RVGRSDAYAT EFDLETEEYV PLPKGEVHKK
KEIVQDVTLH DLDVANARPQ GGQDVISMMG QLLKPKKTEI TEKLRQEVNK VVAKYIDQGV
AELIPGVLFI DEVNMLDIEI FTYLNKALES NIAPVVVLAS NRGMTTVRGT EDVISPHGVP
PDLIDRLLIV RTLPYDKDEI RTIIERRATV ERLQVESSAL DLLATMGTET SLRYALQLLA
PCGILAQTSN RKEIVVNDVN EAKLLFLDAK RSTKILETSA NYL
