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RuvB-like protein 1 (RUVBL1) (EC 3.6.4.12) (TIP49-homology protein 1) (TIP49a homolog)

 RUVB1_YEAST             Reviewed;         463 AA.
Q03940; D6VSH3;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=RuvB-like protein 1;
Short=RUVBL1;
EC=3.6.4.12;
AltName: Full=TIP49-homology protein 1;
AltName: Full=TIP49a homolog;
Name=RVB1; Synonyms=TIH1, TIP49A; OrderedLocusNames=YDR190C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
INTERACTION WITH RVB2.
PubMed=10787406; DOI=10.1074/jbc.M001031200;
Lim C.R., Kimata Y., Ohdate H., Kokubo T., Kikuchi N., Horigome T.,
Kohno K.;
"The Saccharomyces cerevisiae RuvB-like protein, Tih2p, is required
for cell cycle progression and RNA polymerase II-directed
transcription.";
J. Biol. Chem. 275:22409-22417(2000).
[4]
IDENTIFICATION IN THE INO80 COMPLEX, FUNCTION OF THE INO80 COMPLEX,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10952318; DOI=10.1038/35020123;
Shen X., Mizuguchi G., Hamiche A., Wu C.;
"A chromatin remodelling complex involved in transcription and DNA
processing.";
Nature 406:541-544(2000).
[5]
FUNCTION, INTERACTION WITH RVB2, IDENTIFICATION IN A COMPLEX WITH
RBV2; ACT1 AND ARP4, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF LYS-85 AND GLU-312.
PubMed=11278922; DOI=10.1074/jbc.M011523200;
Jonsson Z.O., Dhar S.K., Narlikar G.J., Auty R., Wagle N., Pellman D.,
Pratt R.E., Kingston R., Dutta A.;
"Rvb1p and Rvb2p are essential components of a chromatin remodeling
complex that regulates transcription of over 5% of yeast genes.";
J. Biol. Chem. 276:16279-16288(2001).
[6]
INTERACTION WITH SPT15.
PubMed=12576485; DOI=10.1074/jbc.M213220200;
Ohdate H., Lim C.R., Kokubo T., Matsubara K., Kimata Y., Kohno K.;
"Impairment of the DNA binding activity of the TATA-binding protein
renders the transcriptional function of Rvb2p/Tih2p, the yeast RuvB-
like protein, essential for cell growth.";
J. Biol. Chem. 278:14647-14656(2003).
[7]
IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14690608; DOI=10.1016/S1097-2765(03)00497-0;
Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H.,
Haw R.A., Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X.,
Emili A., Hughes T.R., Buratowski S., Greenblatt J.F.;
"A Snf2 family ATPase complex required for recruitment of the histone
H2A variant Htz1.";
Mol. Cell 12:1565-1576(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=15525518; DOI=10.1016/j.molcel.2004.09.033;
Jonsson Z.O., Jha S., Wohlschlegel J.A., Dutta A.;
"Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin
remodeling complex.";
Mol. Cell 16:465-477(2004).
[11]
FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
Jennings J.L., Link A.J., Madhani H.D., Rine J.;
"A protein complex containing the conserved Swi2/Snf2-related ATPase
Swr1p deposits histone variant H2A.Z into euchromatin.";
PLoS Biol. 2:587-599(2004).
[12]
IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14645854; DOI=10.1126/science.1090701;
Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
"ATP-driven exchange of histone H2AZ variant catalyzed by SWR1
chromatin remodeling complex.";
Science 303:343-348(2004).
[13]
INTERACTION WITH HSP90, IDENTIFICATION IN THE R2PT COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15766533; DOI=10.1016/j.cell.2004.12.024;
Zhao R., Davey M.G., Hsu Y.-C., Kaplanek P., Tong A., Parsons A.B.,
Krogan N.J., Cagney G., Mai D., Greenblatt J.F., Boone C., Emili A.,
Houry W.A.;
"Navigating the chaperone network: an integrative map of physical and
genetic interactions mediated by the hsp90 chaperone.";
Cell 120:715-727(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: DNA helicase which participates in several chromatin
remodeling complexes, including the SWR1 and the INO80 complexes.
The SWR1 complex mediates the ATP-dependent exchange of histone
H2A for the H2A variant HZT1 leading to transcriptional regulation
of selected genes by chromatin remodeling. The INO80 complex
remodels chromatin by shifting nucleosomes. Its ability to induce
transcription of some phosphate-responsive genes is modulated by
inositol polyphosphates. The INO80 complex is involved in DNA
repair by associating to 'Ser-129' phosphorylated H2A histones as
a response to DNA damage. RVB1 recruits ARP5 to the INO80 complex.
During transcription may recruit SPT15/TBP to the TATA-boxes of
involved genes. Required for box C/D and box H/ACA snoRNA
accumulation and involved in pre-rRNA processing.
{ECO:0000269|PubMed:10952318, ECO:0000269|PubMed:11278922,
ECO:0000269|PubMed:14645854, ECO:0000269|PubMed:14690608,
ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15525518}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Probably forms a homohexamer. Interacts with RVB2 and may
form heterododecamers with RVB2. Component of the SWR1 chromatin
remodeling complex composed of at least ACT1, ARP4, RVB1, RVB2,
ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5, SWC7 and SWR1, and
perhaps BDF1. Component of the chromatin-remodeling INO80 complex,
at least composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10,
IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80. Component of
the R2TP complex composed of at least RVB1, RVB2, TAH1 and PIH1.
Interacts with SPT15/TBP and HSP90. {ECO:0000269|PubMed:10787406,
ECO:0000269|PubMed:10952318, ECO:0000269|PubMed:11278922,
ECO:0000269|PubMed:12576485, ECO:0000269|PubMed:14645854,
ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029,
ECO:0000269|PubMed:15525518, ECO:0000269|PubMed:15766533}.
-!- INTERACTION:
P38768:PIH1; NbExp=10; IntAct=EBI-30712, EBI-24499;
Q12464:RVB2; NbExp=21; IntAct=EBI-30712, EBI-31814;
P13393:SPT15; NbExp=3; IntAct=EBI-30712, EBI-19129;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 11600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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EMBL; Z48784; CAA88704.1; -; Genomic_DNA.
EMBL; BK006938; DAA12033.1; -; Genomic_DNA.
PIR; S52698; S52698.
RefSeq; NP_010476.1; NM_001180498.1.
ProteinModelPortal; Q03940; -.
SMR; Q03940; -.
BioGrid; 32243; 569.
DIP; DIP-4896N; -.
IntAct; Q03940; 157.
MINT; MINT-523823; -.
STRING; 4932.YDR190C; -.
iPTMnet; Q03940; -.
MaxQB; Q03940; -.
PRIDE; Q03940; -.
EnsemblFungi; YDR190C; YDR190C; YDR190C.
GeneID; 851771; -.
KEGG; sce:YDR190C; -.
EuPathDB; FungiDB:YDR190C; -.
SGD; S000002598; RVB1.
GeneTree; ENSGT00890000139499; -.
HOGENOM; HOG000190885; -.
InParanoid; Q03940; -.
KO; K04499; -.
OMA; DVHKRKE; -.
OrthoDB; EOG092C2Z17; -.
BioCyc; YEAST:G3O-29778-MONOMER; -.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
PRO; PR:Q03940; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0031011; C:Ino80 complex; IPI:SGD.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0097255; C:R2TP complex; IDA:SGD.
GO; GO:0000812; C:Swr1 complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IDA:SGD.
GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
GO; GO:0006338; P:chromatin remodeling; IPI:SGD.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
GO; GO:0043486; P:histone exchange; IPI:SGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR027238; RuvB-like.
InterPro; IPR010339; TIP49_C.
PANTHER; PTHR11093; PTHR11093; 1.
Pfam; PF06068; TIP49; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Acetylation; Activator; ATP-binding; Chromatin regulator;
Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:15525518}.
CHAIN 2 463 RuvB-like protein 1.
/FTId=PRO_0000165661.
NP_BIND 79 86 ATP. {ECO:0000250}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000269|PubMed:15525518}.
MUTAGEN 85 85 K->E: Lethal.
{ECO:0000269|PubMed:11278922}.
MUTAGEN 312 312 E->G: Lethal.
{ECO:0000269|PubMed:11278922}.
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


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