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Protein

Putative DNA helicase INO80

Gene

INO80

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

Putative DNA helicase component of the INO80 complex which 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.5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi731 – 7388ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • helicase activity Source: UniProtKB-KW

GO - Biological processi

  • chromatin remodeling Source: SGD
  • chromatin silencing at telomere Source: SGD
  • DNA duplex unwinding Source: GOC
  • DNA repair Source: SGD
  • histone exchange Source: SGD
  • nucleosome mobilization Source: SGD
  • nucleosome positioning Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of chromosome segregation Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  • telomere maintenance via recombination Source: SGD
  • transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30642-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative DNA helicase INO80 (EC:3.6.4.12)
Alternative name(s):
Inositol-requiring protein 80
Gene namesi
Name:INO80
Ordered Locus Names:YGL150C
ORF Names:G1880
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL150C.
SGDiS000003118. INO80.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • Ino80 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi737 – 7371K → A: Reduced ATPase activity of the INO80 complex. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14891489Putative DNA helicase INO80PRO_0000074329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651PhosphoserineCombined sources
Modified residuei115 – 1151PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei610 – 6101PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53115.

PTM databases

iPTMnetiP53115.

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 INO80.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NHP10Q0343511EBI-24019,EBI-12010

Protein-protein interaction databases

BioGridi33103. 118 interactions.
DIPiDIP-1386N.
IntActiP53115. 46 interactions.
MINTiMINT-388693.

Structurei

3D structure databases

ProteinModelPortaliP53115.
SMRiP53115. Positions 651-1021, 1294-1439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini476 – 601126DBINOPROSITE-ProRule annotationAdd
BLAST
Domaini718 – 890173Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1303 – 1467165Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi841 – 8444DEAQ box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi188 – 1936Poly-Ala
Compositional biasi259 – 26810Poly-Glu
Compositional biasi300 – 3067Poly-Ser
Compositional biasi568 – 5736Poly-Glu
Compositional biasi675 – 6828Poly-Glu

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 DBINO domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00740000115601.
HOGENOMiHOG000048482.
InParanoidiP53115.
KOiK11665.
OMAiANAHEEE.
OrthoDBiEOG77T1D0.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR031047. Ino80.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF665. PTHR10799:SF665. 7 hits.
PfamiPF13892. DBINO. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51413. DBINO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53115-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLAVLLNKE DKDISDFSKT TAGKSAKKNS RERVADVAPT RVLDKKQAYL
60 70 80 90 100
SQLNSEFNRI KRRDSIEQLY QDWKFINLQE FELISEWNQQ SKDWQFDNTN
110 120 130 140 150
DSQDLHFKKL YRDMSMINKE WAEYQSFKNA NLSDIINEKD ADEDEEDDED
160 170 180 190 200
ELEDGEEDME EDEASTGRHT NGKSMRGNGI QKSRKKDAAA AAAIGKAIKD
210 220 230 240 250
DQTHADTVVT VNGDENEDGN NGEDEDNDND NENNNDNDND NENENDNDSD
260 270 280 290 300
NDDEEENGEE DEEEEEIEDL DEEDFAAFEE QDDNDDEDFN PDVEKRRKRS
310 320 330 340 350
SSSSSSTKLS MNSLSLITSK KINKNITINS DRPKIVRELI KMCNKNKHQK
360 370 380 390 400
IKKRRFTNCI VTDYNPIDSK LNIKITLKQY HVKRLKKLIN DAKREREREE
410 420 430 440 450
ALKNNVGLDG NDLDNDEDGS ESHKRRKLNN NTANGADDAN KRKFNTRHGL
460 470 480 490 500
PTYGMKMNAK EARAIQRHYD NTYTTIWKDM ARKDSTKMSR LVQQIQSIRS
510 520 530 540 550
TNFRKTSSLC AREAKKWQSK NFKQIKDFQT RARRGIREMS NFWKKNEREE
560 570 580 590 600
RDLKKKIEKE AMEQAKKEEE EKESKRQAKK LNFLLTQTEL YSHFIGRKIK
610 620 630 640 650
TNELEGNNVS SNDSESQKNI DISALAPNKN DFHAIDFDNE NDEQLRLRAA
660 670 680 690 700
ENASNALAET RAKAKQFDDH ANAHEEEEEE DELNFQNPTS LGEITIEQPK
710 720 730 740 750
ILACTLKEYQ LKGLNWLANL YDQGINGILA DEMGLGKTVQ SISVLAHLAE
760 770 780 790 800
NHNIWGPFLV VTPASTLHNW VNEISKFLPQ FKILPYWGNA NDRKVLRKFW
810 820 830 840 850
DRKNLRYNKN APFHVMVTSY QMVVTDANYL QKMKWQYMIL DEAQAIKSSQ
860 870 880 890 900
SSRWKNLLSF HCRNRLLLTG TPIQNSMQEL WALLHFIMPS LFDSHDEFNE
910 920 930 940 950
WFSKDIESHA EANTKLNQQQ LRRLHMILKP FMLRRVKKNV QSELGDKIEI
960 970 980 990 1000
DVLCDLTQRQ AKLYQVLKSQ ISTNYDAIEN AATNDSTSNS ASNSGSDQNL
1010 1020 1030 1040 1050
INAVMQFRKV CNHPDLFERA DVDSPFSFTT FGKTTSMLTA SVANNNSSVI
1060 1070 1080 1090 1100
SNSNMNLSSM SSNNISNGKF TDLIYSSRNP IKYSLPRLIY EDLILPNYNN
1110 1120 1130 1140 1150
DVDIANKLKN VKFNIFNPST NYELCLFLSK LTGEPSLNEF FRVSTTPLLK
1160 1170 1180 1190 1200
RVIERTNGPK NTDSLSFKTI TQELLEVTRN APSEGVMASL LNVEKHAYER
1210 1220 1230 1240 1250
EYLNCIQRGY HPNVSAPPVT IEVLGSSHVT NSINNELFDP LISQALSDIP
1260 1270 1280 1290 1300
AITQYNMHVK KGIPVEDFPK TGLFPEPLNK NFSSNISMPS MDRFITESAK
1310 1320 1330 1340 1350
LRKLDELLVK LKSEGHRVLI YFQMTKMMDL MEEYLTYRQY NHIRLDGSSK
1360 1370 1380 1390 1400
LEDRRDLVHD WQTNPEIFVF LLSTRAGGLG INLTAADTVI FYDSDWNPTI
1410 1420 1430 1440 1450
DSQAMDRAHR LGQTRQVTVY RLLVRGTIEE RMRDRAKQKE QVQQVVMEGK
1460 1470 1480
TQEKNIKTIE VGENDSEVTR EGSKSISQDG IKEAASALA
Length:1,489
Mass (Da):171,455
Last modified:October 1, 1996 - v1
Checksum:i017053C5A245337E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48618 Genomic DNA. Translation: CAA88537.1.
X99960 Genomic DNA. Translation: CAA68224.1.
Z72672 Genomic DNA. Translation: CAA96861.1.
BK006941 Genomic DNA. Translation: DAA07961.1.
PIRiS60416.
RefSeqiNP_011365.1. NM_001181015.1.

Genome annotation databases

EnsemblFungiiYGL150C; YGL150C; YGL150C.
GeneIDi852728.
KEGGisce:YGL150C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48618 Genomic DNA. Translation: CAA88537.1.
X99960 Genomic DNA. Translation: CAA68224.1.
Z72672 Genomic DNA. Translation: CAA96861.1.
BK006941 Genomic DNA. Translation: DAA07961.1.
PIRiS60416.
RefSeqiNP_011365.1. NM_001181015.1.

3D structure databases

ProteinModelPortaliP53115.
SMRiP53115. Positions 651-1021, 1294-1439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33103. 118 interactions.
DIPiDIP-1386N.
IntActiP53115. 46 interactions.
MINTiMINT-388693.

PTM databases

iPTMnetiP53115.

Proteomic databases

MaxQBiP53115.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL150C; YGL150C; YGL150C.
GeneIDi852728.
KEGGisce:YGL150C.

Organism-specific databases

EuPathDBiFungiDB:YGL150C.
SGDiS000003118. INO80.

Phylogenomic databases

GeneTreeiENSGT00740000115601.
HOGENOMiHOG000048482.
InParanoidiP53115.
KOiK11665.
OMAiANAHEEE.
OrthoDBiEOG77T1D0.

Enzyme and pathway databases

BioCyciYEAST:G3O-30642-MONOMER.

Miscellaneous databases

PROiP53115.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR031047. Ino80.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF665. PTHR10799:SF665. 7 hits.
PfamiPF13892. DBINO. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51413. DBINO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43."
    James C.M., Indge K.J., Oliver S.G.
    Yeast 11:1413-1419(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a nearly unclonable 22.8 kb segment on the left arm chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1, MRF1 genes and six new open reading frames."
    Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.
    Yeast 13:177-182(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE INO80 COMPLEX, FUNCTION, MUTAGENESIS OF LYS-737.
  6. "The product of the SNF2/SWI2 paralogue INO80 of Saccharomyces cerevisiae required for efficient expression of various yeast structural genes is part of a high-molecular-weight protein complex."
    Ebbert R., Birkmann A., Schueller H.-J.
    Mol. Microbiol. 32:741-751(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A HIGH MOLECULAR WEIGHT COMPLEX.
  7. "Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis."
    Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.
    Yeast 15:219-253(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A PUTATIVE HELICASE.
  8. "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: FUNCTION OF THE INO80 COMPLEX.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Regulation of chromatin remodeling by inositol polyphosphates."
    Steger D.J., Haswell E.S., Miller A.L., Wente S.R., O'Shea E.K.
    Science 299:114-116(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION OF THE INO80 COMPLEX BY INOSITOL POLYPHOSPHATES.
  12. "INO80 and gamma-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair."
    Morrison A.J., Highland J., Krogan N.J., Arbel-Eden A., Greenblatt J.F., Haber J.E., Shen X.
    Cell 119:767-775(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE INO80 COMPLEX.
  13. "Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair."
    van Attikum H., Fritsch O., Hohn B., Gasser S.M.
    Cell 119:777-788(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE INO80 COMPLEX.
  14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  15. "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-65; SER-115 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-65; SER-133 AND SER-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiINO80_YEAST
AccessioniPrimary (citable) accession number: P53115
Secondary accession number(s): D6VU00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 142 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 1110 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.