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Q9ULG1 (INO80_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA helicase INO80

Short name=hINO80
EC=3.6.4.12
Alternative name(s):
INO80 complex subunit A
Putative DNA helicase INO80 complex homolog 1
Gene names
Name:INO80
Synonyms:INO80A, INOC1, KIAA1259
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1556 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA helicase and probable main scaffold component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; according to Ref.14 the contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Recruited by YY1 to YY1-activated genes, where it acts as an essential coactivator. Binds DNA. In vitro, has double-stranded DNA-dependent ATPase activity. Involved in UV-damage excision repair, DNA replication and chromosome segregation during normal cell division cycle. Ref.5 Ref.6 Ref.7 Ref.14 Ref.15 Ref.16 Ref.17

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the chromatin-remodeling INO80 complex; three different complex modules assemble on different domains of INO80. Interacts with DDB1. Ref.5 Ref.7 Ref.8 Ref.9 Ref.16 Ref.17

Subcellular location

Nucleus. Note: Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damage sites in a ACTR8-dependent manner. Ref.6 Ref.8 Ref.13

Tissue specificity

According to Ref.1, widely expressed. According to Ref.6, specifically expressed in brain, liver and pancreas. Ref.1 Ref.6

Domain

The DBINO region is involved in binding to DNA.

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 DBINO domain.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAA86573.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
Mitosis
   Cellular componentMicrotubule
Nucleus
   Coding sequence diversityPolymorphism
   LigandActin-binding
ATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.6. Source: GOC

DNA duplex unwinding

Inferred from direct assay Ref.6. Source: GOC

UV-damage excision repair

Inferred from mutant phenotype Ref.16. Source: UniProtKB

cellular response to UV

Inferred from mutant phenotype Ref.8. Source: UniProtKB

cellular response to ionizing radiation

Inferred from mutant phenotype Ref.14. Source: UniProtKB

chromatin remodeling

Inferred from direct assay Ref.6. Source: UniProtKB

double-strand break repair

Inferred from mutant phenotype Ref.14. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.8. Source: UniProtKB

mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of cell growth

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of nuclear cell cycle DNA replication

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype Ref.15. Source: UniProtKB

spindle assembly

Inferred from mutant phenotype Ref.15. Source: UniProtKB

   Cellular_componentIno80 complex

Inferred from direct assay Ref.8Ref.17. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay Ref.6Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.6. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.6. Source: UniProtKB

DNA helicase activity

Inferred from direct assay Ref.6. Source: UniProtKB

alpha-tubulin binding

Inferred from mutant phenotype Ref.15. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8PubMed 19014934Ref.16. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15561556DNA helicase INO80
PRO_0000248829

Regions

Domain280 – 405126DBINO
Domain530 – 701172Helicase ATP-binding
Domain1105 – 1260156Helicase C-terminal
Nucleotide binding543 – 5508ATP By similarity
Region1 – 266266Assembles INO80 complex module with putative regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1 and IN80D
Region212 – 526315Assembles INO80 complex module consisting of conserved components ACTR8, ACTL6A and YY1
Region521 – 15561036Assembles INO80 complex module consisting of conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2

Amino acid modifications

Modified residue1181N6-acetyllysine Ref.12
Modified residue15121Phosphoserine Ref.10

Natural variations

Natural variant8821I → V.
Corresponds to variant rs34153025 [ dbSNP | Ensembl ].
VAR_049500
Natural variant11081V → G.
Corresponds to variant rs34178030 [ dbSNP | Ensembl ].
VAR_061233

Experimental info

Mutagenesis6531E → Q: Abolishes DNA-dependent ATPase and nucleosome remodeling activities. Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q9ULG1 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 712A1EEA26D6A720

FASTA1,556176,753
        10         20         30         40         50         60 
MASELGARDD GGCTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDD SEDGLDDSNP 

        70         80         90        100        110        120 
LLPQSGDPLI QVKEEPPNSL LGETSGAGSS GMLNTYSLNG VLQSESKCDK GNLYNFSKLK 

       130        140        150        160        170        180 
KSRKWLKSIL LSDESSEADS QSEDDDEEEL NLSREELHNM LRLHKYKKLH QNKYSKDKEL 

       190        200        210        220        230        240 
QQYQYYSAGL LSTYDPFYEQ QRHLLGPKKK KFKEEKKLKA KLKKVKKKRR RDEELSSEES 

       250        260        270        280        290        300 
PRRHHHQTKV FAKFSHDAPP PGTKKKHLSI EQLNARRRKV WLSIVKKELP KANKQKASAR 

       310        320        330        340        350        360 
NLFLTNSRKL AHQCMKEVRR AALQAQKNCK ETLPRARRLT KEMLLYWKKY EKVEKEHRKR 

       370        380        390        400        410        420 
AEKEALEQRK LDEEMREAKR QQRKLNFLIT QTELYAHFMS RKRDMGHDGI QEEILRKLED 

       430        440        450        460        470        480 
SSTQRQIDIG GGVVVNITQE DYDSNHFKAQ ALKNAENAYH IHQARTRSFD EDAKESRAAA 

       490        500        510        520        530        540 
LRAANKSGTG FGESYSLANP SIRAGEDIPQ PTIFNGKLKG YQLKGMNWLA NLYEQGINGI 

       550        560        570        580        590        600 
LADEMGLGKT VQSIALLAHL AERENIWGPF LIISPASTLN NWHQEFTRFV PKFKVLPYWG 

       610        620        630        640        650        660 
NPHDRKVIRR FWSQKTLYTQ DAPFHVVITS YQLVVQDVKY FQRVKWQYMV LDEAQALKSS 

       670        680        690        700        710        720 
SSVRWKILLQ FQCRNRLLLT GTPIQNTMAE LWALLHFIMP TLFDSHEEFN EWFSKDIESH 

       730        740        750        760        770        780 
AENKSAIDEN QLSRLHMILK PFMLRRIKKD VENELSDKIE ILMYCQLTSR QKLLYQALKN 

       790        800        810        820        830        840 
KISIEDLLQS SMGSTQQAQN TTSSLMNLVM QFRKVCNHPE LFERQETWSP FHISLKPYHI 

       850        860        870        880        890        900 
SKFIYRHGQI RVFNHSRDRW LRVLSPFAPD YIQRSLFHRK GINEESCFSF LRFIDISPAE 

       910        920        930        940        950        960 
MANLMLQGLL ARWLALFLSL KASYRLHQLR SWGAPEGESH QRYLRNKDFL LGVNFPLSFP 

       970        980        990       1000       1010       1020 
NLCSCPLLKS LVFSSHCKAV SGYSDQVVHQ RRSATSSLRR CLLTELPSFL CVASPRVTAV 

      1030       1040       1050       1060       1070       1080 
PLDSYCNDRS AEYERRVLKE GGSLAAKQCL LNGAPELAAD WLNRRSQFFP EPAGGLWSIR 

      1090       1100       1110       1120       1130       1140 
PQNGWSFIRI PGKESLITDS GKLYALDVLL TRLKSQGHRV LIYSQMTRMI DLLEEYMVYR 

      1150       1160       1170       1180       1190       1200 
KHTYMRLDGS SKISERRDMV ADFQNRNDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP 

      1210       1220       1230       1240       1250       1260 
TVDQQAMDRA HRLGQTKQVT VYRLICKGTI EERILQRAKE KSEIQRMVIS GGNFKPDTLK 

      1270       1280       1290       1300       1310       1320 
PKEVVSLLLD DEELEKKLRL RQEEKRQQEE TNRVKERKRK REKYAEKKKK EDELDGKRRK 

      1330       1340       1350       1360       1370       1380 
EGVNLVIPFV PSADNSNLSA DGDDSFISVD SAMPSPFSEI SISSELHTGS IPLDESSSDM 

      1390       1400       1410       1420       1430       1440 
LVIVDDPASS APQSRATNSP ASITGSVSDT VNGISIQEMP AAGRGHSARS RGRPKGSGST 

      1450       1460       1470       1480       1490       1500 
AKGAGKGRSR KSTAGSAAAM AGAKAGAAAA SAAAYAAYGY NVSKGISASS PLQTSLVRPA 

      1510       1520       1530       1540       1550 
GLADFGPSSA SSPLSSPLSK GNNVPGNPKN LHMTSSLAPD SLVRKQGKGT NPSGGR 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
Tissue: Brain.
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1302-1556.
Tissue: Testis.
[5]"A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex."
Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K., Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P., Conaway R.C., Conaway J.W.
J. Biol. Chem. 280:41207-41212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity."
Bakshi R., Mehta A.K., Sharma R., Maiti S., Pasha S., Brahmachari V.
Biochem. Biophys. Res. Commun. 339:313-320(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]"YY1 functions with INO80 to activate transcription."
Cai Y., Jin J., Yao T., Gottschalk A.J., Swanson S.K., Wu S., Shi Y., Washburn M.P., Florens L., Conaway R.C., Conaway J.W.
Nat. Struct. Mol. Biol. 14:872-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH YY1.
[8]"A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE INO80 COMPLEX.
[9]"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The mammalian INO80 complex is recruited to DNA damage sites in an ARP8 dependent manner."
Kashiwaba S., Kitahashi K., Watanabe T., Onoda F., Ohtsu M., Murakami Y.
Biochem. Biophys. Res. Commun. 402:619-625(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Human INO80 chromatin-remodelling complex contributes to DNA double-strand break repair via the expression of Rad54B and XRCC3 genes."
Park E.J., Hur S.K., Kwon J.
Biochem. J. 431:179-187(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR.
[15]"Roles of human INO80 chromatin remodeling enzyme in DNA replication and chromosome segregation suppress genome instability."
Hur S.K., Park E.J., Han J.E., Kim Y.A., Kim J.D., Kang D., Kwon J.
Cell. Mol. Life Sci. 67:2283-2296(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway."
Jiang Y., Wang X., Bao S., Guo R., Johnson D.G., Shen X., Li L.
Proc. Natl. Acad. Sci. U.S.A. 107:17274-17279(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH DDB1, FUNCTION OF THE INO80 COMPLEX.
[17]"Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX, MUTAGENESIS OF GLU-653.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB033085 mRNA. Translation: BAA86573.1. Different initiation.
CH471125 Genomic DNA. Translation: EAW92469.1.
BC146785 mRNA. Translation: AAI46786.1.
AL137280 mRNA. Translation: CAB70675.1.
CCDSCCDS10071.1.
PIRT46350.
RefSeqNP_060023.1. NM_017553.2.
UniGeneHs.292949.

3D structure databases

ProteinModelPortalQ9ULG1.
SMRQ9ULG1. Positions 518-821, 1096-1241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120076. 24 interactions.
DIPDIP-34296N.
IntActQ9ULG1. 14 interactions.
STRING9606.ENSP00000355205.

PTM databases

PhosphoSiteQ9ULG1.

Polymorphism databases

DMDM114149322.

Proteomic databases

MaxQBQ9ULG1.
PaxDbQ9ULG1.
PRIDEQ9ULG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361937; ENSP00000355205; ENSG00000128908.
ENST00000401393; ENSP00000384686; ENSG00000128908.
GeneID54617.
KEGGhsa:54617.
UCSCuc001zni.3. human.

Organism-specific databases

CTD54617.
GeneCardsGC15M041271.
HGNCHGNC:26956. INO80.
HPAHPA055495.
MIM610169. gene.
neXtProtNX_Q9ULG1.
PharmGKBPA162392040.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000231795.
HOVERGENHBG057875.
InParanoidQ9ULG1.
KOK11665.
OMASLHMTSS.
OrthoDBEOG7B05C6.
PhylomeDBQ9ULG1.
TreeFamTF324408.

Gene expression databases

ArrayExpressQ9ULG1.
BgeeQ9ULG1.
CleanExHS_INO80.
GenevestigatorQ9ULG1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF13892. DBINO. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
PROSITEPS51413. DBINO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINO80. human.
GenomeRNAi54617.
NextBio57137.
PROQ9ULG1.
SOURCESearch...

Entry information

Entry nameINO80_HUMAN
AccessionPrimary (citable) accession number: Q9ULG1
Secondary accession number(s): A6H8X4, Q9NTG6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM