Q9ULG1 (INO80_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1556 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle Cell division DNA damage DNA recombination DNA repair Mitosis
Cellular component	Microtubule Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Actin-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UV-damage excision repair Inferred from mutant phenotype Ref.16. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW 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 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 DNA replication involved in S phase Inferred from mutant phenotype Ref.15. Source: UniProtKB positive regulation of cell growth 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_component	Ino80 complex Inferred from direct assay Ref.8Ref.17. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTR5	Q9H9F9	6	EBI-769345,EBI-769418
DDB1	Q16531	4	EBI-769345,EBI-350322
YY1	P25490	5	EBI-769345,EBI-765538

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1556	1556	DNA helicase INO80		PRO_0000248829
Regions
	Domain	280 – 405	126	DBINO
	Domain	530 – 701	172	Helicase ATP-binding
	Domain	1105 – 1260	156	Helicase C-terminal
	Nucleotide binding	543 – 550	8	ATP By similarity
	Region	1 – 266	266	Assembles INO80 complex module with putative regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1 and IN80D
	Region	212 – 526	315	Assembles INO80 complex module consisting of conserved components ACTR8, ACTL6A and YY1
	Region	521 – 1556	1036	Assembles INO80 complex module consisting of conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2
Amino acid modifications
	Modified residue	118	1	N6-acetyllysine Ref.12
	Modified residue	1512	1	Phosphoserine Ref.10
Natural variations
	Natural variant	882	1	I → V. Corresponds to variant rs34153025 [ dbSNP | Ensembl ].		VAR_049500
	Natural variant	1108	1	V → G. Corresponds to variant rs34178030 [ dbSNP | Ensembl ].		VAR_061233
Experimental info
	Mutagenesis	653	1	E → Q: Abolishes DNA-dependent ATPase and nucleosome remodeling activities. Ref.17

Sequences

	Sequence		Length	Mass (Da)
	Q9ULG1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: 712A1EEA26D6A720	FASTA	1,556	176,753
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
IPI	IPI00008091.
PIR	T46350.
RefSeq	NP_060023.1. NM_017553.1.
UniGene	Hs.292949.
3D structure databases
HSSP	HSSP built from PDB template 1Z63 based on UniProtKB Q97XQ5.
ProteinModelPortal	Q9ULG1.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34296N.
IntAct	Q9ULG1. 14 interactions.
STRING	9606.ENSP00000355205.
PTM databases
PhosphoSite	Q9ULG1.
Polymorphism databases
DMDM	114149322.
Proteomic databases
PaxDb	Q9ULG1.
PRIDE	Q9ULG1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361937; ENSP00000355205; ENSG00000128908. ENST00000401393; ENSP00000384686; ENSG00000128908.
GeneID	54617.
KEGG	hsa:54617.
UCSC	uc001zni.3. human.
Organism-specific databases
CTD	54617.
GeneCards	GC15M041271.
HGNC	HGNC:26956. INO80.
MIM	610169. gene.
neXtProt	NX_Q9ULG1.
PharmGKB	PA162392040.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0553.
HOGENOM	HOG000231795.
HOVERGEN	HBG057875.
InParanoid	Q9ULG1.
KO	K11665.
OMA	KVIRKFW.
OrthoDB	EOG4ZKJKF.
Gene expression databases
ArrayExpress	Q9ULG1.
Bgee	Q9ULG1.
CleanEx	HS_INO80.
Genevestigator	Q9ULG1.
GermOnline	ENSG00000128908. Homo sapiens.
Family and domain databases
InterPro	IPR020838. DBINO. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. [Graphical view]
Pfam	PF13892. DBINO. 1 hit. PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS51413. DBINO. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	INO80. human.
GenomeRNAi	54617.
NextBio	57137.
SOURCE	Search...

Entry information

Entry name

INO80_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.