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Protein

Actin-related protein 2/3 complex subunit 5

Gene

ARPC5

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

Functioni

Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks.

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • Arp2/3 complex-mediated actin nucleation Source: FlyBase
  • cell migration Source: CACAO
  • ephrin receptor signaling pathway Source: Reactome
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • movement of cell or subcellular component Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 5
Alternative name(s):
Arp2/3 complex 16 kDa subunit
Short name:
p16-ARC
Gene namesi
Name:ARPC5
Synonyms:ARC16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:708. ARPC5.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • Arp2/3 protein complex Source: FlyBase
  • cell projection Source: UniProtKB-SubCell
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25003.

Polymorphism and mutation databases

BioMutaiARPC5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 151150Actin-related protein 2/3 complex subunit 5PRO_0000124054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Post-translational modificationi

Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiO15511.
MaxQBiO15511.
PaxDbiO15511.
PeptideAtlasiO15511.
PRIDEiO15511.
TopDownProteomicsiO15511-1. [O15511-1]
O15511-2. [O15511-2]

2D gel databases

OGPiO15511.
SWISS-2DPAGEO15511.

PTM databases

iPTMnetiO15511.
PhosphoSiteiO15511.

Expressioni

Gene expression databases

BgeeiO15511.
CleanExiHS_ARPC5.
ExpressionAtlasiO15511. baseline and differential.
GenevisibleiO15511. HS.

Organism-specific databases

HPAiHPA022013.

Interactioni

Subunit structurei

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC.

Protein-protein interaction databases

BioGridi115399. 56 interactions.
DIPiDIP-33144N.
IntActiO15511. 21 interactions.
MINTiMINT-2999073.
STRINGi9606.ENSP00000352918.

Structurei

3D structure databases

ProteinModelPortaliO15511.
SMRiO15511. Positions 9-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC5 family.Curated

Phylogenomic databases

eggNOGiKOG3380. Eukaryota.
ENOG4111FGV. LUCA.
GeneTreeiENSGT00390000014806.
HOGENOMiHOG000197215.
HOVERGENiHBG050583.
InParanoidiO15511.
KOiK05754.
OMAiGHGAIMR.
PhylomeDBiO15511.
TreeFamiTF319716.

Family and domain databases

Gene3Di1.25.40.190. 1 hit.
InterProiIPR006789. ARPC5.
[Graphical view]
PANTHERiPTHR12644. PTHR12644. 1 hit.
PfamiPF04699. P16-Arc. 1 hit.
[Graphical view]
PIRSFiPIRSF039096. p16-ARC. 1 hit.
SUPFAMiSSF69103. SSF69103. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15511-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN
60 70 80 90 100
MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK
110 120 130 140 150
NGVDLLMKYI YKGFESPSDN SSAMLLQWHE KALAAGGVGS IVRVLTARKT

V
Length:151
Mass (Da):16,320
Last modified:January 23, 2007 - v3
Checksum:iF050B11774EA6E66
GO
Isoform 2 (identifier: O15511-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-48: Q → HSIT

Note: No experimental confirmation available.
Show »
Length:154
Mass (Da):16,631
Checksum:i0FF22E5126BDC54A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei48 – 481Q → HSIT in isoform 2. 1 PublicationVSP_024028

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006088 mRNA. Translation: AAB64193.1.
AF017807 mRNA. Translation: AAB70561.1.
AL137800 Genomic DNA. Translation: CAC19687.1.
AL137800 Genomic DNA. Translation: CAI19482.1.
CH471067 Genomic DNA. Translation: EAW91163.1.
BC057237 mRNA. Translation: AAH57237.1.
CCDSiCCDS1357.1. [O15511-1]
CCDS58050.1. [O15511-2]
RefSeqiNP_001257368.1. NM_001270439.1. [O15511-2]
NP_005708.1. NM_005717.3. [O15511-1]
UniGeneiHs.518609.

Genome annotation databases

EnsembliENST00000294742; ENSP00000294742; ENSG00000162704. [O15511-2]
ENST00000359856; ENSP00000352918; ENSG00000162704. [O15511-1]
GeneIDi10092.
KEGGihsa:10092.
UCSCiuc021pgb.3. human. [O15511-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006088 mRNA. Translation: AAB64193.1.
AF017807 mRNA. Translation: AAB70561.1.
AL137800 Genomic DNA. Translation: CAC19687.1.
AL137800 Genomic DNA. Translation: CAI19482.1.
CH471067 Genomic DNA. Translation: EAW91163.1.
BC057237 mRNA. Translation: AAH57237.1.
CCDSiCCDS1357.1. [O15511-1]
CCDS58050.1. [O15511-2]
RefSeqiNP_001257368.1. NM_001270439.1. [O15511-2]
NP_005708.1. NM_005717.3. [O15511-1]
UniGeneiHs.518609.

3D structure databases

ProteinModelPortaliO15511.
SMRiO15511. Positions 9-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115399. 56 interactions.
DIPiDIP-33144N.
IntActiO15511. 21 interactions.
MINTiMINT-2999073.
STRINGi9606.ENSP00000352918.

PTM databases

iPTMnetiO15511.
PhosphoSiteiO15511.

Polymorphism and mutation databases

BioMutaiARPC5.

2D gel databases

OGPiO15511.
SWISS-2DPAGEO15511.

Proteomic databases

EPDiO15511.
MaxQBiO15511.
PaxDbiO15511.
PeptideAtlasiO15511.
PRIDEiO15511.
TopDownProteomicsiO15511-1. [O15511-1]
O15511-2. [O15511-2]

Protocols and materials databases

DNASUi10092.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294742; ENSP00000294742; ENSG00000162704. [O15511-2]
ENST00000359856; ENSP00000352918; ENSG00000162704. [O15511-1]
GeneIDi10092.
KEGGihsa:10092.
UCSCiuc021pgb.3. human. [O15511-1]

Organism-specific databases

CTDi10092.
GeneCardsiARPC5.
HGNCiHGNC:708. ARPC5.
HPAiHPA022013.
MIMi604227. gene.
neXtProtiNX_O15511.
PharmGKBiPA25003.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3380. Eukaryota.
ENOG4111FGV. LUCA.
GeneTreeiENSGT00390000014806.
HOGENOMiHOG000197215.
HOVERGENiHBG050583.
InParanoidiO15511.
KOiK05754.
OMAiGHGAIMR.
PhylomeDBiO15511.
TreeFamiTF319716.

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

ChiTaRSiARPC5. human.
GeneWikiiARPC5.
GenomeRNAii10092.
PROiO15511.
SOURCEiSearch...

Gene expression databases

BgeeiO15511.
CleanExiHS_ARPC5.
ExpressionAtlasiO15511. baseline and differential.
GenevisibleiO15511. HS.

Family and domain databases

Gene3Di1.25.40.190. 1 hit.
InterProiIPR006789. ARPC5.
[Graphical view]
PANTHERiPTHR12644. PTHR12644. 1 hit.
PfamiPF04699. P16-Arc. 1 hit.
[Graphical view]
PIRSFiPIRSF039096. p16-ARC. 1 hit.
SUPFAMiSSF69103. SSF69103. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly."
    Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.
    J. Cell Biol. 138:375-384(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins."
    Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A., Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W.
    Biochem. J. 328:105-112(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Skin.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10.
    Tissue: Platelet.
  7. "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity."
    Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.
    Mol. Cell 8:1041-1052(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE ARP2/3 COMPLEX.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal reorganization through ubiquitination and degradation of Arp2/3 subunit 5 and coronin 1A."
    Ichikawa D., Mizuno M., Yamamura T., Miyake S.
    J. Biol. Chem. 286:43465-43474(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY RNF128.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARPC5_HUMAN
AccessioniPrimary (citable) accession number: O15511
Secondary accession number(s): A6NEC4, Q6PG42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 139 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.