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Protein

Actin-related protein 5

Gene

ACTR5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Biological processi

  • DNA recombination Source: UniProtKB-KW
  • double-strand break repair Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • UV-damage excision repair Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.
SignaLinkiQ9H9F9.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 5
Short name:
hARP5
Alternative name(s):
Sarcoma antigen NY-SAR-16
Gene namesi
Name:ACTR5
Synonyms:ARP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:14671. ACTR5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • Ino80 complex Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24490.

Polymorphism and mutation databases

BioMutaiACTR5.
DMDMi110832751.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Actin-related protein 5PRO_0000247842Add
BLAST

Proteomic databases

EPDiQ9H9F9.
MaxQBiQ9H9F9.
PaxDbiQ9H9F9.
PRIDEiQ9H9F9.

PTM databases

iPTMnetiQ9H9F9.
PhosphoSiteiQ9H9F9.

Expressioni

Gene expression databases

BgeeiQ9H9F9.
CleanExiHS_ACTR5.
GenevisibleiQ9H9F9. HS.

Organism-specific databases

HPAiHPA042676.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR8Q9H9813EBI-769418,EBI-769597
DDB1Q165313EBI-769418,EBI-350322
INO80Q9ULG17EBI-769418,EBI-769345

Protein-protein interaction databases

BioGridi122993. 40 interactions.
DIPiDIP-34297N.
IntActiQ9H9F9. 40 interactions.
MINTiMINT-3036790.
STRINGi9606.ENSP00000243903.

Structurei

3D structure databases

ProteinModelPortaliQ9H9F9.
SMRiQ9H9F9. Positions 33-260, 416-561.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili288 – 32740Sequence analysisAdd
BLAST
Coiled coili355 – 38430Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the actin family. ARP5 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0681. Eukaryota.
ENOG410XQ7K. LUCA.
GeneTreeiENSGT00720000108866.
HOGENOMiHOG000171615.
HOVERGENiHBG059801.
InParanoidiQ9H9F9.
KOiK11672.
OMAiCQFIGYD.
OrthoDBiEOG7PCJGD.
PhylomeDBiQ9H9F9.
TreeFamiTF324227.

Family and domain databases

InterProiIPR004000. Actin.
IPR004001. Actin_CS.
IPR027664. Arp5.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 2 hits.
PTHR11937:SF16. PTHR11937:SF16. 2 hits.
PfamiPF00022. Actin. 2 hits.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00432. ACTINS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H9F9-1 [UniParc]FASTAAdd to basket

« Hide

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

GGAGEQA
Length:607
Mass (Da):68,297
Last modified:July 25, 2006 - v2
Checksum:iDA3E50AE37BCC363
GO

Sequence cautioni

The sequence AAO65164.1 differs from that shown. Reason: Frameshift at positions 319, 343 and 347. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 702RG → AR in AAO65164 (PubMed:12601173).Curated
Sequence conflicti481 – 4811K → E in BAB14270 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti298 – 2981R → L.1 Publication
Corresponds to variant rs17853829 [ dbSNP | Ensembl ].
VAR_027158
Natural varianti461 – 4611I → L.
Corresponds to variant rs35805905 [ dbSNP | Ensembl ].
VAR_048189
Natural varianti483 – 4831I → V.1 Publication
Corresponds to variant rs2245231 [ dbSNP | Ensembl ].
VAR_027159
Natural varianti580 – 5801P → L.
Corresponds to variant rs3752289 [ dbSNP | Ensembl ].
VAR_027160

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13308.1.
RefSeqiNP_079131.3. NM_024855.3.
UniGeneiHs.371585.

Genome annotation databases

EnsembliENST00000243903; ENSP00000243903; ENSG00000101442.
GeneIDi79913.
KEGGihsa:79913.
UCSCiuc002xjd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13308.1.
RefSeqiNP_079131.3. NM_024855.3.
UniGeneiHs.371585.

3D structure databases

ProteinModelPortaliQ9H9F9.
SMRiQ9H9F9. Positions 33-260, 416-561.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122993. 40 interactions.
DIPiDIP-34297N.
IntActiQ9H9F9. 40 interactions.
MINTiMINT-3036790.
STRINGi9606.ENSP00000243903.

PTM databases

iPTMnetiQ9H9F9.
PhosphoSiteiQ9H9F9.

Polymorphism and mutation databases

BioMutaiACTR5.
DMDMi110832751.

Proteomic databases

EPDiQ9H9F9.
MaxQBiQ9H9F9.
PaxDbiQ9H9F9.
PRIDEiQ9H9F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000243903; ENSP00000243903; ENSG00000101442.
GeneIDi79913.
KEGGihsa:79913.
UCSCiuc002xjd.3. human.

Organism-specific databases

CTDi79913.
GeneCardsiACTR5.
H-InvDBHIX0015810.
HGNCiHGNC:14671. ACTR5.
HPAiHPA042676.
neXtProtiNX_Q9H9F9.
PharmGKBiPA24490.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0681. Eukaryota.
ENOG410XQ7K. LUCA.
GeneTreeiENSGT00720000108866.
HOGENOMiHOG000171615.
HOVERGENiHBG059801.
InParanoidiQ9H9F9.
KOiK11672.
OMAiCQFIGYD.
OrthoDBiEOG7PCJGD.
PhylomeDBiQ9H9F9.
TreeFamiTF324227.

Enzyme and pathway databases

ReactomeiR-HSA-5696394. DNA Damage Recognition in GG-NER.
SignaLinkiQ9H9F9.

Miscellaneous databases

GenomeRNAii79913.
PROiQ9H9F9.

Gene expression databases

BgeeiQ9H9F9.
CleanExiHS_ACTR5.
GenevisibleiQ9H9F9. HS.

Family and domain databases

InterProiIPR004000. Actin.
IPR004001. Actin_CS.
IPR027664. Arp5.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 2 hits.
PTHR11937:SF16. PTHR11937:SF16. 2 hits.
PfamiPF00022. Actin. 2 hits.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00432. ACTINS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-298 AND VAL-483.
    Tissue: Brain, Cervix and Ovary.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-348.
  5. Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX.

Entry informationi

Entry nameiARP5_HUMAN
AccessioniPrimary (citable) accession number: Q9H9F9
Secondary accession number(s): Q86WF7
, Q8IUY5, Q8N724, Q9BRN0, Q9BVB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: June 8, 2016
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 20
    Human chromosome 20: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.