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Protein

Ino eighty subunit 2

Gene

IES2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33221-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ino eighty subunit 2
Gene namesi
Name:IES2
Ordered Locus Names:YNL215W
ORF Names:N1315
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL215w.
EuPathDBiFungiDB:YNL215W.
SGDiS000005159. IES2.

Subcellular locationi

GO - Cellular componenti

  • Ino80 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Ino eighty subunit 2PRO_0000084154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine1 Publication
Modified residuei129 – 1291Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40154.
PaxDbiP40154.

Interactioni

Subunit structurei

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 INO80.1 Publication

Protein-protein interaction databases

BioGridi35621. 240 interactions.
DIPiDIP-5062N.
IntActiP40154. 6 interactions.
MINTiMINT-560359.

Structurei

3D structure databases

ProteinModelPortaliP40154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IES2 family.Curated

Phylogenomic databases

eggNOGiNOG75630.
InParanoidiP40154.
KOiK11676.
OrthoDBiEOG769ZW5.

Family and domain databases

InterProiIPR029523. INO80B/Ies2.
IPR006880. INO80B_C.
[Graphical view]
PANTHERiPTHR21561:SF12. PTHR21561:SF12. 1 hit.
PfamiPF04795. PAPA-1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSEASDIEA ELSDSVSAGG EEYIDDDDYT EDIDDQIVTA KSSRRTARRS
60 70 80 90 100
VPKGVRTSKR IRDKELSVEV DEDYDEEEDV LSPSKKRHLH TRSMDKRQVA
110 120 130 140 150
ATASEKSDIG DSKGNDGEIE DGILEEEESL EKELNRGGGK EVEKSEESYY
160 170 180 190 200
AQNDVGQKGE EEQDGESGGY EDNEPSISKE SDELVSVVNG NGNEEDDEVE
210 220 230 240 250
ATKENTTDST RSTTTRSKML LDLLEDGGSK KKLTDEEIQL RRAENARKRK
260 270 280 290 300
NLSEKRLEEE KQDTINKLLK KRAGKSRSHL PNDDEKNDGS SSFVKPRRPY
310 320
NSEGMTRILR RYEEDLFCTF
Length:320
Mass (Da):36,154
Last modified:February 1, 1995 - v1
Checksum:i6F0AA04387A3B3E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78898 Genomic DNA. Translation: CAA55493.1.
Z71491 Genomic DNA. Translation: CAA96117.1.
BK006947 Genomic DNA. Translation: DAA10341.1.
PIRiS50716.
RefSeqiNP_014184.1. NM_001183053.1.

Genome annotation databases

EnsemblFungiiYNL215W; YNL215W; YNL215W.
GeneIDi855506.
KEGGisce:YNL215W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78898 Genomic DNA. Translation: CAA55493.1.
Z71491 Genomic DNA. Translation: CAA96117.1.
BK006947 Genomic DNA. Translation: DAA10341.1.
PIRiS50716.
RefSeqiNP_014184.1. NM_001183053.1.

3D structure databases

ProteinModelPortaliP40154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35621. 240 interactions.
DIPiDIP-5062N.
IntActiP40154. 6 interactions.
MINTiMINT-560359.

Proteomic databases

MaxQBiP40154.
PaxDbiP40154.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL215W; YNL215W; YNL215W.
GeneIDi855506.
KEGGisce:YNL215W.

Organism-specific databases

CYGDiYNL215w.
EuPathDBiFungiDB:YNL215W.
SGDiS000005159. IES2.

Phylogenomic databases

eggNOGiNOG75630.
InParanoidiP40154.
KOiK11676.
OrthoDBiEOG769ZW5.

Enzyme and pathway databases

BioCyciYEAST:G3O-33221-MONOMER.

Miscellaneous databases

NextBioi979514.
PROiP40154.

Family and domain databases

InterProiIPR029523. INO80B/Ies2.
IPR006880. INO80B_C.
[Graphical view]
PANTHERiPTHR21561:SF12. PTHR21561:SF12. 1 hit.
PfamiPF04795. PAPA-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 13.5 kb DNA segment from the left arm of yeast chromosome XIV reveals MER1; RAP1; a new putative member of the DNA replication complex and a new putative serine/threonine phosphatase gene."
    Coster F., van Dyck L., Jonniaux J.-L., Purnelle B., Goffeau A.
    Yeast 11:85-91(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Involvement of actin-related proteins in ATP-dependent chromatin remodeling."
    Shen X., Ranallo R., Choi E., Wu C.
    Mol. Cell 12:147-155(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIES2_YEAST
AccessioniPrimary (citable) accession number: P40154
Secondary accession number(s): D6W0X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 103 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 1470 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

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 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.