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Protein

RuvB-like protein 2

Gene

RVB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.9 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 828ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent 3'-5' DNA helicase activity Source: SGD
  • ATP-dependent 5'-3' DNA helicase activity Source: SGD

GO - Biological processi

  • box C/D snoRNP assembly Source: SGD
  • chromatin remodeling Source: SGD
  • DNA duplex unwinding Source: GOC
  • DNA repair Source: UniProtKB-KW
  • histone exchange Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • rRNA processing Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34122-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RuvB-like protein 2 (EC:3.6.4.12)
Short name:
RUVBL2
Alternative name(s):
TIP49-homology protein 2
TIP49b homolog
Gene namesi
Name:RVB2
Synonyms:TIH2, TIP49B
Ordered Locus Names:YPL235W
ORF Names:P1060
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL235W.
SGDiS000006156. RVB2.

Subcellular locationi

GO - Cellular componenti

  • Ino80 complex Source: SGD
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: SGD
  • R2TP complex Source: SGD
  • Swr1 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi75 – 751G → A: Lethal. 1 Publication
Mutagenesisi80 – 801G → A: Growth defect at 37 degrees Celsius. 1 Publication
Mutagenesisi81 – 811K → A: Defect in snoRNA accumulation. Growth defect at 37 degrees Celsius. 3 Publications
Mutagenesisi81 – 811K → E: Lethal. 3 Publications
Mutagenesisi81 – 811K → R: Growth defect at 37 degrees Celsius. 3 Publications
Mutagenesisi296 – 2961D → N: Lethal. 1 Publication
Mutagenesisi297 – 2971E → G: Lethal. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471RuvB-like protein 2PRO_0000165675Add
BLAST

Proteomic databases

MaxQBiQ12464.
PeptideAtlasiQ12464.

PTM databases

iPTMnetiQ12464.

Interactioni

Subunit structurei

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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RVB1Q0394010EBI-31814,EBI-30712
SPT15P133933EBI-31814,EBI-19129
SWC4P532013EBI-31814,EBI-23061

Protein-protein interaction databases

BioGridi35927. 196 interactions.
DIPiDIP-5207N.
IntActiQ12464. 164 interactions.
MINTiMINT-523843.

Structurei

3D structure databases

ProteinModelPortaliQ12464.
SMRiQ12464. Positions 10-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvB family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075034.
HOGENOMiHOG000190885.
InParanoidiQ12464.
KOiK11338.
OMAiYDAMGAQ.
OrthoDBiEOG7FBRT0.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12464-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIQTSDPNE TSDLKSLSLI AAHSHITGLG LDENLQPRPT SEGMVGQLQA
60 70 80 90 100
RRAAGVILKM VQNGTIAGRA VLVAGPPSTG KTALAMGVSQ SLGKDVPFTA
110 120 130 140 150
IAGSEIFSLE LSKTEALTQA FRKSIGIKIK EETELIEGEV VEIQIDRSIT
160 170 180 190 200
GGHKQGKLTI KTTDMETIYE LGNKMIDGLT KEKVLAGDVI SIDKASGKIT
210 220 230 240 250
KLGRSFARSR DYDAMGADTR FVQCPEGELQ KRKTVVHTVS LHEIDVINSR
260 270 280 290 300
TQGFLALFTG DTGEIRSEVR DQINTKVAEW KEEGKAEIVP GVLFIDEVHM
310 320 330 340 350
LDIECFSFIN RALEDEFAPI VMMATNRGVS KTRGTNYKSP HGLPLDLLDR
360 370 380 390 400
SIIITTKSYN EQEIKTILSI RAQEEEVELS SDALDLLTKT GVETSLRYSS
410 420 430 440 450
NLISVAQQIA MKRKNNTVEV EDVKRAYLLF LDSARSVKYV QENESQYIDD
460 470
QGNVQISIAK SADPDAMDTT E
Length:471
Mass (Da):51,612
Last modified:November 1, 1996 - v1
Checksum:i0D8EFBA7EC711AB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67751 Genomic DNA. Translation: CAA91609.1.
X94561 Genomic DNA. Translation: CAA64252.1.
Z73591 Genomic DNA. Translation: CAA97952.1.
BK006949 Genomic DNA. Translation: DAA11201.1.
PIRiS61029.
RefSeqiNP_015089.1. NM_001184049.1.

Genome annotation databases

EnsemblFungiiYPL235W; YPL235W; YPL235W.
GeneIDi855841.
KEGGisce:YPL235W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z67751 Genomic DNA. Translation: CAA91609.1.
X94561 Genomic DNA. Translation: CAA64252.1.
Z73591 Genomic DNA. Translation: CAA97952.1.
BK006949 Genomic DNA. Translation: DAA11201.1.
PIRiS61029.
RefSeqiNP_015089.1. NM_001184049.1.

3D structure databases

ProteinModelPortaliQ12464.
SMRiQ12464. Positions 10-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35927. 196 interactions.
DIPiDIP-5207N.
IntActiQ12464. 164 interactions.
MINTiMINT-523843.

PTM databases

iPTMnetiQ12464.

Proteomic databases

MaxQBiQ12464.
PeptideAtlasiQ12464.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL235W; YPL235W; YPL235W.
GeneIDi855841.
KEGGisce:YPL235W.

Organism-specific databases

EuPathDBiFungiDB:YPL235W.
SGDiS000006156. RVB2.

Phylogenomic databases

GeneTreeiENSGT00550000075034.
HOGENOMiHOG000190885.
InParanoidiQ12464.
KOiK11338.
OMAiYDAMGAQ.
OrthoDBiEOG7FBRT0.

Enzyme and pathway databases

BioCyciYEAST:G3O-34122-MONOMER.

Miscellaneous databases

PROiQ12464.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    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.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The Saccharomyces cerevisiae RuvB-like protein, Tih2p, is required for cell cycle progression and RNA polymerase II-directed transcription."
    Lim C.R., Kimata Y., Ohdate H., Kokubo T., Kikuchi N., Horigome T., Kohno K.
    J. Biol. Chem. 275:22409-22417(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-81, INTERACTION WITH RVB1.
  4. "A chromatin remodelling complex involved in transcription and DNA processing."
    Shen X., Mizuguchi G., Hamiche A., Wu C.
    Nature 406:541-544(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX, FUNCTION OF THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes."
    Jonsson Z.O., Dhar S.K., Narlikar G.J., Auty R., Wagle N., Pellman D., Pratt R.E., Kingston R., Dutta A.
    J. Biol. Chem. 276:16279-16288(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RVB1, IDENTIFICATION IN A COMPLEX WITH RBV1; ACT1 AND ARP4, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-81 AND GLU-297.
  6. "A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins."
    King T.H., Decatur W.A., Bertrand E., Maxwell E.S., Fournier M.J.
    Mol. Cell. Biol. 21:7731-7746(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNORNA SYNTHESIS, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-75; GLY-80; LYS-81 AND ASP-296.
  7. "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."
    Ohdate H., Lim C.R., Kokubo T., Matsubara K., Kimata Y., Kohno K.
    J. Biol. Chem. 278:14647-14656(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SPT15.
  8. Cited for: IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex."
    Jonsson Z.O., Jha S., Wohlschlegel J.A., Dutta A.
    Mol. Cell 16:465-477(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
    Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.
    PLoS Biol. 2:587-599(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex."
    Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.
    Science 303:343-348(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone."
    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.
    Cell 120:715-727(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE R2PT COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRUVB2_YEAST
AccessioniPrimary (citable) accession number: Q12464
Secondary accession number(s): D6W3D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3030 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.