ARP5_HUMAN
ID ARP5_HUMAN Reviewed; 607 AA.
AC Q9H9F9; Q86WF7; Q8IUY5; Q8N724; Q9BRN0; Q9BVB7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Actin-related protein 5;
DE Short=hARP5;
DE AltName: Full=Sarcoma antigen NY-SAR-16;
GN Name=ACTR5; Synonyms=ARP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-298 AND VAL-483.
RC TISSUE=Brain, Cervix, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-348.
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
RN [5]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE INO80 COMPLEX.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [7]
RP INTERACTION WITH ACTR8, AND SUBCELLULAR LOCATION.
RX PubMed=18163988; DOI=10.1016/j.yexcr.2007.11.020;
RA Aoyama N., Oka A., Kitayama K., Kurumizaka H., Harata M.;
RT "The actin-related protein hArp8 accumulates on the mitotic chromosomes and
RT functions in chromosome alignment.";
RL Exp. Cell Res. 314:859-868(2008).
RN [8]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19014934; DOI=10.1016/j.yexcr.2008.10.028;
RA Kitayama K., Kamo M., Oma Y., Matsuda R., Uchida T., Ikura T., Tashiro S.,
RA Ohyama T., Winsor B., Harata M.;
RT "The human actin-related protein hArp5: nucleo-cytoplasmic shuttling and
RT involvement in DNA repair.";
RL Exp. Cell Res. 315:206-217(2009).
RN [10]
RP FUNCTION IN DNA REPAIR, INTERACTION WITH DDB1, AND FUNCTION OF THE INO80
RP COMPLEX.
RX PubMed=20855601; DOI=10.1073/pnas.1008388107;
RA Jiang Y., Wang X., Bao S., Guo R., Johnson D.G., Shen X., Li L.;
RT "INO80 chromatin remodeling complex promotes the removal of UV lesions by
RT the nucleotide excision repair pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17274-17279(2010).
RN [11]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. Involved in DNA double-strand
CC break repair and UV-damage excision repair.
CC {ECO:0000269|PubMed:19014934, ECO:0000269|PubMed:20855601}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the helicase ATP-
CC binding and the helicase C-terminal domain of INO80. Interacts with
CC DDB1. Interacts with ACTR8; the interaction is observed in asynchronous
CC (interphase) cells but not in metaphase-arrested cells indicative for a
CC possible dissociation of the INO80 complex in mitotic cells.
CC {ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:18163988,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:20855601,
CC ECO:0000269|PubMed:21303910}.
CC -!- INTERACTION:
CC Q9H9F9; Q9H981: ACTR8; NbExp=3; IntAct=EBI-769418, EBI-769597;
CC Q9H9F9; Q16531: DDB1; NbExp=4; IntAct=EBI-769418, EBI-350322;
CC Q9H9F9; Q9ULG1: INO80; NbExp=8; IntAct=EBI-769418, EBI-769345;
CC Q9H9F9; O60437: PPL; NbExp=3; IntAct=EBI-769418, EBI-368321;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18026119,
CC ECO:0000269|PubMed:18163988, ECO:0000269|PubMed:19014934}. Cytoplasm
CC {ECO:0000269|PubMed:19014934}. Note=Predominantly nuclear but undergoes
CC nucleo-cytoplasmic shuttling (PubMed:19014934). Localized to interphase
CC nuclei, but not nucleoli; excluded from chromosomes as mitosis
CC progresses (PubMed:18163988).
CC -!- SIMILARITY: Belongs to the actin family. ARP5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO65164.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK022847; BAB14270.1; -; mRNA.
DR EMBL; AL133519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001324; AAH01324.1; -; mRNA.
DR EMBL; BC006162; AAH06162.1; -; mRNA.
DR EMBL; BC038402; AAH38402.1; -; mRNA.
DR EMBL; AY211911; AAO65164.1; ALT_FRAME; mRNA.
DR CCDS; CCDS13308.1; -.
DR RefSeq; NP_079131.3; NM_024855.3.
DR PDB; 6HTS; EM; 4.80 A; H=1-607.
DR PDBsum; 6HTS; -.
DR AlphaFoldDB; Q9H9F9; -.
DR SMR; Q9H9F9; -.
DR BioGRID; 122993; 75.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q9H9F9; -.
DR DIP; DIP-34297N; -.
DR IntAct; Q9H9F9; 55.
DR MINT; Q9H9F9; -.
DR STRING; 9606.ENSP00000243903; -.
DR iPTMnet; Q9H9F9; -.
DR PhosphoSitePlus; Q9H9F9; -.
DR BioMuta; ACTR5; -.
DR DMDM; 110832751; -.
DR EPD; Q9H9F9; -.
DR jPOST; Q9H9F9; -.
DR MassIVE; Q9H9F9; -.
DR MaxQB; Q9H9F9; -.
DR PaxDb; Q9H9F9; -.
DR PeptideAtlas; Q9H9F9; -.
DR PRIDE; Q9H9F9; -.
DR ProteomicsDB; 81319; -.
DR Antibodypedia; 43543; 136 antibodies from 23 providers.
DR DNASU; 79913; -.
DR Ensembl; ENST00000243903.6; ENSP00000243903.4; ENSG00000101442.10.
DR GeneID; 79913; -.
DR KEGG; hsa:79913; -.
DR MANE-Select; ENST00000243903.6; ENSP00000243903.4; NM_024855.4; NP_079131.3.
DR UCSC; uc002xjd.3; human.
DR CTD; 79913; -.
DR DisGeNET; 79913; -.
DR GeneCards; ACTR5; -.
DR HGNC; HGNC:14671; ACTR5.
DR HPA; ENSG00000101442; Low tissue specificity.
DR MIM; 619730; gene.
DR neXtProt; NX_Q9H9F9; -.
DR OpenTargets; ENSG00000101442; -.
DR PharmGKB; PA24490; -.
DR VEuPathDB; HostDB:ENSG00000101442; -.
DR eggNOG; KOG0681; Eukaryota.
DR GeneTree; ENSGT00720000108866; -.
DR HOGENOM; CLU_008246_2_0_1; -.
DR InParanoid; Q9H9F9; -.
DR OMA; TNWNHQE; -.
DR OrthoDB; 344271at2759; -.
DR PhylomeDB; Q9H9F9; -.
DR TreeFam; TF324227; -.
DR PathwayCommons; Q9H9F9; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9H9F9; -.
DR BioGRID-ORCS; 79913; 156 hits in 1093 CRISPR screens.
DR ChiTaRS; ACTR5; human.
DR GenomeRNAi; 79913; -.
DR Pharos; Q9H9F9; Tbio.
DR PRO; PR:Q9H9F9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H9F9; protein.
DR Bgee; ENSG00000101442; Expressed in hair follicle and 178 other tissues.
DR Genevisible; Q9H9F9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IMP:UniProtKB.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR027664; Arp5.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 2.
DR PANTHER; PTHR11937:SF16; PTHR11937:SF16; 2.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..607
FT /note="Actin-related protein 5"
FT /id="PRO_0000247842"
FT REGION 584..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 288..327
FT /evidence="ECO:0000255"
FT COILED 355..384
FT /evidence="ECO:0000255"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 298
FT /note="R -> L (in dbSNP:rs17853829)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027158"
FT VARIANT 461
FT /note="I -> L (in dbSNP:rs35805905)"
FT /id="VAR_048189"
FT VARIANT 483
FT /note="I -> V (in dbSNP:rs2245231)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027159"
FT VARIANT 580
FT /note="P -> L (in dbSNP:rs3752289)"
FT /id="VAR_027160"
FT CONFLICT 69..70
FT /note="RG -> AR (in Ref. 4; AAO65164)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="K -> E (in Ref. 1; BAB14270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68297 MW; DA3E50AE37BCC363 CRC64;
MAANVFPFRD ARAAPDPVLE AGPVAHGPLP VPLVLDNGSF QVRAGWACPG QDPGPEPRLQ
FRAVCARGRG GARGASGPQV GNALGSLEPL RWMLRSPFDR NVPVNLELQE LLLDYSFQHL
GVSSQGCVDH PIVLTEAVCN PLYSRQMMSE LLFECYGIPK VAYGIDSLFS FYHNKPKNSM
CSGLIISSGY QCTHVLPILE GRLDAKNCKR INLGGSQAAG YLQRLLQLKY PGHLAAITLS
RMEEILHEHS YIAEDYVEEL HKWRCPDYYE NNVHKMQLPF SSKLLGSTLT SEEKQERRQQ
QLRRLQELNA RRREEKLQLD QERLDRLLYV QELLEDGQMD QFHKALIELN MDSPEELQSY
IQKLSIAVEQ AKQKILQAEV NLEVDVVDSK PETPDLEQLE PSLEDVESMN DFDPLFSEET
PGVEKPVTTV QPVFNLAAYH QLFVGTERIR APEIIFQPSL IGEEQAGIAE TLQYILDRYP
KDIQEMLVQN VFLTGGNTMY PGMKARMEKE LLEMRPFRSS FQVQLASNPV LDAWYGARDW
ALNHLDDNEV WITRKEYEEK GGEYLKEHCA SNIYVPIRLP KQASRSSDAQ ASSKGSAAGG
GGAGEQA
