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RuvB-like protein 2 (RUVBL2) (EC 3.6.4.12) (TIP49-homology protein 2) (TIP49b homolog)

 RUVB2_YEAST             Reviewed;         471 AA.
Q12464; D6W3D5;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=RuvB-like protein 2;
Short=RUVBL2;
EC=3.6.4.12;
AltName: Full=TIP49-homology protein 2;
AltName: Full=TIP49b homolog;
Name=RVB2; Synonyms=TIH2, TIP49B; OrderedLocusNames=YPL235W;
ORFNames=P1060;
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=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(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]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-81, AND INTERACTION
WITH RVB1.
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 RVB1, IDENTIFICATION IN A COMPLEX WITH
RBV1; ACT1 AND ARP4, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF LYS-81 AND GLU-297.
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]
FUNCTION IN SNORNA SYNTHESIS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-75; GLY-80; LYS-81 AND ASP-296.
PubMed=11604509; DOI=10.1128/MCB.21.22.7731-7746.2001;
King T.H., Decatur W.A., Bertrand E., Maxwell E.S., Fournier M.J.;
"A well-connected and conserved nucleoplasmic helicase is required for
production of box C/D and H/ACA snoRNAs and localization of snoRNP
proteins.";
Mol. Cell. Biol. 21:7731-7746(2001).
[7]
FUNCTION, AND 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).
[8]
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).
[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]
FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX, 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]
IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF 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]
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).
-!- 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. 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:10787406,
ECO:0000269|PubMed:10952318, ECO:0000269|PubMed:11278922,
ECO:0000269|PubMed:11604509, ECO:0000269|PubMed:12576485,
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 RVB1 and may
form heterododecamers with RVB1. 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. Belongs also
to the R2TP complex composed of at least RVB1, RVB2, TAH1 and
PIH1. Interacts with SPT15/TBP. {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=7; IntAct=EBI-31814, EBI-24499;
Q03940:RVB1; NbExp=21; IntAct=EBI-31814, EBI-30712;
P13393:SPT15; NbExp=3; IntAct=EBI-31814, EBI-19129;
P53201:SWC4; NbExp=4; IntAct=EBI-31814, EBI-23061;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:10787406, ECO:0000269|PubMed:11604509}.
-!- MISCELLANEOUS: Present with 3030 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z67751; CAA91609.1; -; Genomic_DNA.
EMBL; X94561; CAA64252.1; -; Genomic_DNA.
EMBL; Z73591; CAA97952.1; -; Genomic_DNA.
EMBL; BK006949; DAA11201.1; -; Genomic_DNA.
PIR; S61029; S61029.
RefSeq; NP_015089.1; NM_001184049.1.
ProteinModelPortal; Q12464; -.
SMR; Q12464; -.
BioGrid; 35927; 487.
DIP; DIP-5207N; -.
IntAct; Q12464; 206.
MINT; MINT-523843; -.
STRING; 4932.YPL235W; -.
iPTMnet; Q12464; -.
MaxQB; Q12464; -.
PRIDE; Q12464; -.
EnsemblFungi; YPL235W; YPL235W; YPL235W.
GeneID; 855841; -.
KEGG; sce:YPL235W; -.
EuPathDB; FungiDB:YPL235W; -.
SGD; S000006156; RVB2.
GeneTree; ENSGT00890000139527; -.
HOGENOM; HOG000190885; -.
InParanoid; Q12464; -.
KO; K11338; -.
OMA; VPFTMIA; -.
OrthoDB; EOG092C2Z17; -.
BioCyc; YEAST:G3O-34122-MONOMER; -.
PRO; PR:Q12464; -.
Proteomes; UP000002311; Chromosome XVI.
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:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IDA:SGD.
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:0006364; P:rRNA processing; 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; 1.
1: Evidence at protein level;
Activator; ATP-binding; Chromatin regulator; Complete proteome;
DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding;
Nucleus; Reference proteome; rRNA processing; Transcription;
Transcription regulation.
CHAIN 1 471 RuvB-like protein 2.
/FTId=PRO_0000165675.
NP_BIND 75 82 ATP. {ECO:0000250}.
MUTAGEN 75 75 G->A: Lethal.
{ECO:0000269|PubMed:11604509}.
MUTAGEN 80 80 G->A: Growth defect at 37 degrees
Celsius. {ECO:0000269|PubMed:11604509}.
MUTAGEN 81 81 K->A: Defect in snoRNA accumulation.
Growth defect at 37 degrees Celsius.
{ECO:0000269|PubMed:10787406,
ECO:0000269|PubMed:11278922,
ECO:0000269|PubMed:11604509}.
MUTAGEN 81 81 K->E: Lethal.
{ECO:0000269|PubMed:10787406,
ECO:0000269|PubMed:11278922,
ECO:0000269|PubMed:11604509}.
MUTAGEN 81 81 K->R: Growth defect at 37 degrees
Celsius. {ECO:0000269|PubMed:10787406,
ECO:0000269|PubMed:11278922,
ECO:0000269|PubMed:11604509}.
MUTAGEN 296 296 D->N: Lethal.
{ECO:0000269|PubMed:11604509}.
MUTAGEN 297 297 E->G: Lethal.
{ECO:0000269|PubMed:11278922}.
SEQUENCE 471 AA; 51612 MW; 0D8EFBA7EC711AB8 CRC64;
MSIQTSDPNE TSDLKSLSLI AAHSHITGLG LDENLQPRPT SEGMVGQLQA RRAAGVILKM
VQNGTIAGRA VLVAGPPSTG KTALAMGVSQ SLGKDVPFTA IAGSEIFSLE LSKTEALTQA
FRKSIGIKIK EETELIEGEV VEIQIDRSIT GGHKQGKLTI KTTDMETIYE LGNKMIDGLT
KEKVLAGDVI SIDKASGKIT KLGRSFARSR DYDAMGADTR FVQCPEGELQ KRKTVVHTVS
LHEIDVINSR TQGFLALFTG DTGEIRSEVR DQINTKVAEW KEEGKAEIVP GVLFIDEVHM
LDIECFSFIN RALEDEFAPI VMMATNRGVS KTRGTNYKSP HGLPLDLLDR SIIITTKSYN
EQEIKTILSI RAQEEEVELS SDALDLLTKT GVETSLRYSS NLISVAQQIA MKRKNNTVEV
EDVKRAYLLF LDSARSVKYV QENESQYIDD QGNVQISIAK SADPDAMDTT E


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