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Q9ULG1

- INO80_HUMAN

UniProt

Q9ULG1 - INO80_HUMAN

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Protein
DNA helicase INO80
Gene
INO80, INO80A, INOC1, KIAA1259
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 1 Publication 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.7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi543 – 5508ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. DNA helicase activity Source: UniProtKB
  5. alpha-tubulin binding Source: UniProtKB
  6. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA duplex unwinding Source: GOC
  3. UV-damage excision repair Source: UniProtKB
  4. cellular response to UV Source: UniProtKB
  5. cellular response to ionizing radiation Source: UniProtKB
  6. chromatin remodeling Source: UniProtKB
  7. double-strand break repair Source: UniProtKB
  8. double-strand break repair via homologous recombination Source: UniProtKB
  9. mitotic sister chromatid segregation Source: UniProtKB
  10. positive regulation of cell growth Source: UniProtKB
  11. positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  12. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  13. regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  14. spindle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Mitosis

Keywords - Ligandi

Actin-binding, ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA helicase INO80 (EC:3.6.4.12)
Short name:
hINO80
Alternative name(s):
INO80 complex subunit A
Putative DNA helicase INO80 complex homolog 1
Gene namesi
Name:INO80
Synonyms:INO80A, INOC1, KIAA1259
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:26956. INO80.

Subcellular locationi

Nucleus
Note: Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damage sites in a ACTR8-dependent manner.3 Publications

GO - Cellular componenti

  1. Ino80 complex Source: UniProtKB
  2. microtubule Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi653 – 6531E → Q: Abolishes DNA-dependent ATPase and nucleosome remodeling activities. 1 Publication

Organism-specific databases

PharmGKBiPA162392040.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15561556DNA helicase INO80
PRO_0000248829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei1512 – 15121Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9ULG1.
PaxDbiQ9ULG1.
PRIDEiQ9ULG1.

PTM databases

PhosphoSiteiQ9ULG1.

Expressioni

Tissue specificityi

According to 1 Publication, widely expressed. According to 1 Publication, specifically expressed in brain, liver and pancreas.2 Publications

Gene expression databases

ArrayExpressiQ9ULG1.
BgeeiQ9ULG1.
CleanExiHS_INO80.
GenevestigatoriQ9ULG1.

Organism-specific databases

HPAiHPA055495.

Interactioni

Subunit structurei

Component of the chromatin-remodeling INO80 complex; three different complex modules assemble on different domains of INO80. Interacts with DDB1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR5Q9H9F96EBI-769345,EBI-769418
DDB1Q165314EBI-769345,EBI-350322
YY1P254905EBI-769345,EBI-765538

Protein-protein interaction databases

BioGridi120076. 24 interactions.
DIPiDIP-34296N.
IntActiQ9ULG1. 14 interactions.
STRINGi9606.ENSP00000355205.

Structurei

3D structure databases

ProteinModelPortaliQ9ULG1.
SMRiQ9ULG1. Positions 518-821, 1096-1241.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 405126DBINO
Add
BLAST
Domaini530 – 701172Helicase ATP-binding
Add
BLAST
Domaini1105 – 1260156Helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 266266Assembles INO80 complex module with putative regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1 and IN80D
Add
BLAST
Regioni212 – 526315Assembles INO80 complex module consisting of conserved components ACTR8, ACTL6A and YY1
Add
BLAST
Regioni521 – 15561036Assembles INO80 complex module consisting of conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2
Add
BLAST

Domaini

The DBINO region is involved in binding to DNA.

Sequence similaritiesi

Contains 1 DBINO domain.

Phylogenomic databases

eggNOGiCOG0553.
HOGENOMiHOG000231795.
HOVERGENiHBG057875.
InParanoidiQ9ULG1.
KOiK11665.
OMAiSLHMTSS.
OrthoDBiEOG7B05C6.
PhylomeDBiQ9ULG1.
TreeFamiTF324408.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
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.

Q9ULG1-1 [UniParc]FASTAAdd to Basket

« Hide

MASELGARDD GGCTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDD     50
SEDGLDDSNP LLPQSGDPLI QVKEEPPNSL LGETSGAGSS GMLNTYSLNG 100
VLQSESKCDK GNLYNFSKLK KSRKWLKSIL LSDESSEADS QSEDDDEEEL 150
NLSREELHNM LRLHKYKKLH QNKYSKDKEL QQYQYYSAGL LSTYDPFYEQ 200
QRHLLGPKKK KFKEEKKLKA KLKKVKKKRR RDEELSSEES PRRHHHQTKV 250
FAKFSHDAPP PGTKKKHLSI EQLNARRRKV WLSIVKKELP KANKQKASAR 300
NLFLTNSRKL AHQCMKEVRR AALQAQKNCK ETLPRARRLT KEMLLYWKKY 350
EKVEKEHRKR AEKEALEQRK LDEEMREAKR QQRKLNFLIT QTELYAHFMS 400
RKRDMGHDGI QEEILRKLED SSTQRQIDIG GGVVVNITQE DYDSNHFKAQ 450
ALKNAENAYH IHQARTRSFD EDAKESRAAA LRAANKSGTG FGESYSLANP 500
SIRAGEDIPQ PTIFNGKLKG YQLKGMNWLA NLYEQGINGI LADEMGLGKT 550
VQSIALLAHL AERENIWGPF LIISPASTLN NWHQEFTRFV PKFKVLPYWG 600
NPHDRKVIRR FWSQKTLYTQ DAPFHVVITS YQLVVQDVKY FQRVKWQYMV 650
LDEAQALKSS SSVRWKILLQ FQCRNRLLLT GTPIQNTMAE LWALLHFIMP 700
TLFDSHEEFN EWFSKDIESH AENKSAIDEN QLSRLHMILK PFMLRRIKKD 750
VENELSDKIE ILMYCQLTSR QKLLYQALKN KISIEDLLQS SMGSTQQAQN 800
TTSSLMNLVM QFRKVCNHPE LFERQETWSP FHISLKPYHI SKFIYRHGQI 850
RVFNHSRDRW LRVLSPFAPD YIQRSLFHRK GINEESCFSF LRFIDISPAE 900
MANLMLQGLL ARWLALFLSL KASYRLHQLR SWGAPEGESH QRYLRNKDFL 950
LGVNFPLSFP NLCSCPLLKS LVFSSHCKAV SGYSDQVVHQ RRSATSSLRR 1000
CLLTELPSFL CVASPRVTAV PLDSYCNDRS AEYERRVLKE GGSLAAKQCL 1050
LNGAPELAAD WLNRRSQFFP EPAGGLWSIR PQNGWSFIRI PGKESLITDS 1100
GKLYALDVLL TRLKSQGHRV LIYSQMTRMI DLLEEYMVYR KHTYMRLDGS 1150
SKISERRDMV ADFQNRNDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP 1200
TVDQQAMDRA HRLGQTKQVT VYRLICKGTI EERILQRAKE KSEIQRMVIS 1250
GGNFKPDTLK PKEVVSLLLD DEELEKKLRL RQEEKRQQEE TNRVKERKRK 1300
REKYAEKKKK EDELDGKRRK EGVNLVIPFV PSADNSNLSA DGDDSFISVD 1350
SAMPSPFSEI SISSELHTGS IPLDESSSDM LVIVDDPASS APQSRATNSP 1400
ASITGSVSDT VNGISIQEMP AAGRGHSARS RGRPKGSGST AKGAGKGRSR 1450
KSTAGSAAAM AGAKAGAAAA SAAAYAAYGY NVSKGISASS PLQTSLVRPA 1500
GLADFGPSSA SSPLSSPLSK GNNVPGNPKN LHMTSSLAPD SLVRKQGKGT 1550
NPSGGR 1556
Length:1,556
Mass (Da):176,753
Last modified:September 5, 2006 - v2
Checksum:i712A1EEA26D6A720
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti882 – 8821I → V.
Corresponds to variant rs34153025 [ dbSNP | Ensembl ].
VAR_049500
Natural varianti1108 – 11081V → G.
Corresponds to variant rs34178030 [ dbSNP | Ensembl ].
VAR_061233

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033085 mRNA. Translation: BAA86573.1. Different initiation.
CH471125 Genomic DNA. Translation: EAW92469.1.
BC146785 mRNA. Translation: AAI46786.1.
AL137280 mRNA. Translation: CAB70675.1.
CCDSiCCDS10071.1.
PIRiT46350.
RefSeqiNP_060023.1. NM_017553.2.
UniGeneiHs.292949.

Genome annotation databases

EnsembliENST00000361937; ENSP00000355205; ENSG00000128908.
ENST00000401393; ENSP00000384686; ENSG00000128908.
GeneIDi54617.
KEGGihsa:54617.
UCSCiuc001zni.3. human.

Polymorphism databases

DMDMi114149322.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033085 mRNA. Translation: BAA86573.1 . Different initiation.
CH471125 Genomic DNA. Translation: EAW92469.1 .
BC146785 mRNA. Translation: AAI46786.1 .
AL137280 mRNA. Translation: CAB70675.1 .
CCDSi CCDS10071.1.
PIRi T46350.
RefSeqi NP_060023.1. NM_017553.2.
UniGenei Hs.292949.

3D structure databases

ProteinModelPortali Q9ULG1.
SMRi Q9ULG1. Positions 518-821, 1096-1241.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120076. 24 interactions.
DIPi DIP-34296N.
IntActi Q9ULG1. 14 interactions.
STRINGi 9606.ENSP00000355205.

PTM databases

PhosphoSitei Q9ULG1.

Polymorphism databases

DMDMi 114149322.

Proteomic databases

MaxQBi Q9ULG1.
PaxDbi Q9ULG1.
PRIDEi Q9ULG1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361937 ; ENSP00000355205 ; ENSG00000128908 .
ENST00000401393 ; ENSP00000384686 ; ENSG00000128908 .
GeneIDi 54617.
KEGGi hsa:54617.
UCSCi uc001zni.3. human.

Organism-specific databases

CTDi 54617.
GeneCardsi GC15M041271.
HGNCi HGNC:26956. INO80.
HPAi HPA055495.
MIMi 610169. gene.
neXtProti NX_Q9ULG1.
PharmGKBi PA162392040.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
HOGENOMi HOG000231795.
HOVERGENi HBG057875.
InParanoidi Q9ULG1.
KOi K11665.
OMAi SLHMTSS.
OrthoDBi EOG7B05C6.
PhylomeDBi Q9ULG1.
TreeFami TF324408.

Miscellaneous databases

ChiTaRSi INO80. human.
GenomeRNAii 54617.
NextBioi 57137.
PROi Q9ULG1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULG1.
Bgeei Q9ULG1.
CleanExi HS_INO80.
Genevestigatori Q9ULG1.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR020838. DBINO.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF13892. DBINO. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
PROSITEi PS51413. DBINO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1302-1556.
    Tissue: Testis.
  5. 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. 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. 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.

Entry informationi

Entry nameiINO80_HUMAN
AccessioniPrimary (citable) accession number: Q9ULG1
Secondary accession number(s): A6H8X4, Q9NTG6
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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