Q9H9F9 (ARP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-related protein 5
Short name=hARP5

Alternative name(s):
Sarcoma antigen NY-SAR-16

Gene names

Name:	ACTR5
Synonyms:	ARP5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	607 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in DNA double-strand break repair and UV-damage excision repair. Ref.9 Ref.10
Subunit structure	Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C-terminal domain of INO80. Interacts with DDB1. Interacts with ACTR8; the interaction is observed in asynchronous (interphase) cells but not in metaphase-arrested cells indicative for a possible dissociation of the INO80 complex in mitotic cells. Ref.7 Ref.10
Subcellular location	Nucleus. Cytoplasm. Note: Predominantly nuclear but undergoes nucleo-cytoplasmic shuttling. Localized to interphase nuclei, but not nucleoli; excluded from chromosomes as mitosis progresses. Ref.6 Ref.7 Ref.9
Sequence similarities	Belongs to the actin family. ARP5 subfamily.
Sequence caution	The sequence AAO65164.1 differs from that shown. Reason: Frameshift at positions 319, 343 and 347.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW UV-damage excision repair Inferred from mutant phenotype Ref.10. Source: UniProtKB double-strand break repair Inferred from mutant phenotype Ref.9. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Ino80 complex Inferred from direct assay Ref.6Ref.11. Source: UniProtKB cytoplasm Inferred from direct assay Ref.9. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.7Ref.10. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTR8	Q9H981	2	EBI-769418,EBI-769597
DDB1	Q16531	3	EBI-769418,EBI-350322
INO80	Q9ULG1	6	EBI-769418,EBI-769345

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 607	607	Actin-related protein 5		PRO_0000247842
Regions
	Coiled coil	288 – 327	40	Potential
	Coiled coil	355 – 384	30	Potential
Natural variations
	Natural variant	298	1	R → L. Ref.3 Corresponds to variant rs17853829 [ dbSNP | Ensembl ].		VAR_027158
	Natural variant	461	1	I → L. Corresponds to variant rs35805905 [ dbSNP | Ensembl ].		VAR_048189
	Natural variant	483	1	I → V. Ref.3 Corresponds to variant rs2245231 [ dbSNP | Ensembl ].		VAR_027159
	Natural variant	580	1	P → L. Corresponds to variant rs3752289 [ dbSNP | Ensembl ].		VAR_027160
Experimental info
	Sequence conflict	69 – 70	2	RG → AR in AAO65164. Ref.4
	Sequence conflict	481	1	K → E in BAB14270. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H9F9 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: DA3E50AE37BCC363	FASTA	607	68,297
	10 20 30 40 50 60 MAANVFPFRD ARAAPDPVLE AGPVAHGPLP VPLVLDNGSF QVRAGWACPG QDPGPEPRLQ 70 80 90 100 110 120 FRAVCARGRG GARGASGPQV GNALGSLEPL RWMLRSPFDR NVPVNLELQE LLLDYSFQHL 130 140 150 160 170 180 GVSSQGCVDH PIVLTEAVCN PLYSRQMMSE LLFECYGIPK VAYGIDSLFS FYHNKPKNSM 190 200 210 220 230 240 CSGLIISSGY QCTHVLPILE GRLDAKNCKR INLGGSQAAG YLQRLLQLKY PGHLAAITLS 250 260 270 280 290 300 RMEEILHEHS YIAEDYVEEL HKWRCPDYYE NNVHKMQLPF SSKLLGSTLT SEEKQERRQQ 310 320 330 340 350 360 QLRRLQELNA RRREEKLQLD QERLDRLLYV QELLEDGQMD QFHKALIELN MDSPEELQSY 370 380 390 400 410 420 IQKLSIAVEQ AKQKILQAEV NLEVDVVDSK PETPDLEQLE PSLEDVESMN DFDPLFSEET 430 440 450 460 470 480 PGVEKPVTTV QPVFNLAAYH QLFVGTERIR APEIIFQPSL IGEEQAGIAE TLQYILDRYP 490 500 510 520 530 540 KDIQEMLVQN VFLTGGNTMY PGMKARMEKE LLEMRPFRSS FQVQLASNPV LDAWYGARDW 550 560 570 580 590 600 ALNHLDDNEV WITRKEYEEK GGEYLKEHCA SNIYVPIRLP KQASRSSDAQ ASSKGSAAGG GGAGEQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-298 AND VAL-483. Tissue: Brain, Cervix and Ovary.
[4]	"Immunomic analysis of human sarcoma." Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J. Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003) [PubMed: 12601173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-348.
[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: 16230350] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE INO80 COMPLEX.
[6]	"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: 18026119] [Abstract] Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH THE INO80 COMPLEX.
[7]	"The actin-related protein hArp8 accumulates on the mitotic chromosomes and functions in chromosome alignment." Aoyama N., Oka A., Kitayama K., Kurumizaka H., Harata M. Exp. Cell Res. 314:859-868(2008) [PubMed: 18163988] [Abstract] Cited for: INTERACTION WITH ACTR8, SUBCELLULAR LOCATION.
[8]	"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: 18922472] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX, MASS SPECTROMETRY.
[9]	"The human actin-related protein hArp5: nucleo-cytoplasmic shuttling and involvement in DNA repair." Kitayama K., Kamo M., Oma Y., Matsuda R., Uchida T., Ikura T., Tashiro S., Ohyama T., Winsor B., Harata M. Exp. Cell Res. 315:206-217(2009) [PubMed: 19014934] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"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: 20855601] [Abstract] Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH DDB1, FUNCTION OF THE INO80 COMPLEX.
[11]	"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: 21303910] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK022847 mRNA. Translation: BAB14270.1. AL133519 Genomic DNA. Translation: CAD37358.1. BC001324 mRNA. Translation: AAH01324.1. BC006162 mRNA. Translation: AAH06162.1. BC038402 mRNA. Translation: AAH38402.1. AY211911 mRNA. Translation: AAO65164.1. Frameshift.
IPI	IPI00292787.
RefSeq	NP_079131.3. NM_024855.3.
UniGene	Hs.371585.
3D structure databases
ProteinModelPortal	Q9H9F9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H9F9. 14 interactions.
STRING	Q9H9F9.
Polymorphism databases
DMDM	110832751.
Proteomic databases
PRIDE	Q9H9F9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000243903; ENSP00000243903; ENSG00000101442.
GeneID	79913.
KEGG	hsa:79913.
UCSC	uc002xjd.2. human.
Organism-specific databases
CTD	79913.
GeneCards	GC20P037377.
H-InvDB	HIX0015810.
HGNC	HGNC:14671. ACTR5.
neXtProt	NX_Q9H9F9.
PharmGKB	PA24490.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16466.
GeneTree	ENSGT00550000075062.
HOGENOM	HBG315355.
HOVERGEN	HBG059801.
InParanoid	Q9H9F9.
OMA	TTVQPVF.
OrthoDB	EOG4DZ1V0.
PhylomeDB	Q9H9F9.
Gene expression databases
ArrayExpress	Q9H9F9.
Bgee	Q9H9F9.
CleanEx	HS_ACTR5.
Genevestigator	Q9H9F9.
GermOnline	ENSG00000101442. Homo sapiens.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR004001. Actin_CS. [Graphical view]
KO	K11672.
PANTHER	PTHR11937. Actin_like. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00432. ACTINS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	69786.

Entry information

Entry name

ARP5_HUMAN

Accession

Primary (citable) accession number: Q9H9F9
Secondary accession number(s): Q86WF7 , Q8IUY5, Q8N724, Q9BRN0, Q9BVB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	January 25, 2012
This is version 80 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.