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Reviewed, UniProtKB/Swiss-Prot Q9BPX5 (ARP5L_HUMAN)

Last modified July 22, 2008. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Actin-related protein 2/3 complex subunit 5-like protein
Alternative name(s):
    Arp2/3 complex 16 kDa subunit 2
      Short name=ARC16-2
Gene names
Name: ARPC5L
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May function 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.

Subunit structure

May be a component of the Arp2/3 complex in which it may replace ARPC5.

Subcellular location

Cytoplasm › cytoskeletonBy similarity.

Sequence similarities

Belongs to the ARPC5 family.

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Ontologies

Keywords

   Cellular componentCytoplasm
Cytoskeleton
   LigandActin-binding
   PTMPhosphoprotein

Gene Ontology (GO)

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARP3betaQ9P1U11EBI-711189,EBI-1047175

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 153152Actin-related protein 2/3 complex subunit 5-like protein

Amino acid modifications

Modified residue641Phosphoserine

Experimental info

Sequence conflict301Missing in AAP97155. Ref.1
Sequence conflict36 – 372EP → RT in AAP97155. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9BPX5-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D8E4772404300560

FASTA15316,941
        10         20         30         40         50         60 
MARNTLSSRF RRVDIDEFDE NKFVDEQEEA AAAAAEPGPD PSEVDGLLRQ GDMLRAFHAA 

        70         80         90        100        110        120 
LRNSPVNTKN QAVKERAQGV VLKVLTNFKS SEIEQAVQSL DRNGVDLLMK YIYKGFEKPT 

       130        140        150 
ENSSAVLLQW HEKALAVGGL GSIIRVLTAR KTV

« Hide

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References

« Hide 'large scale' references
[1]"Cloning of a novel human cDNA homologous to human Arp2/3 complex 16kDa subunit (ARC16) mRNA."
Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [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].
Tissue: Brain and Placenta.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
Tissue: Epithelium.

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Cross-references

Sequence databases

AF087842 mRNA. Translation: AAP97155.1.
AL354928 Genomic DNA. Translation: CAI39641.1.
BC000018 mRNA. Translation: AAH00018.1.
BC000798 mRNA. Translation: AAH00798.1.
BC002418 mRNA. Translation: AAH02418.1.
RefSeqNP_112240.1.
UniGeneHs.132499

3D structure databases

SMRQ9BPX5. Positions 8-152.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BPX5.

Proteomic databases

PeptideAtlasQ9BPX5.

Genome annotation databases

EnsemblENSG00000136950. Homo sapiens. [Contig view]
GeneID81873.
KEGGhsa:81873.

Organism-specific databases

HGNCHGNC:23366. ARPC5L.
PharmGKBPA134991012.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ9BPX5.

Gene expression databases

ArrayExpressQ9BPX5.
CleanExHS_ARPC5L.

Family and domain databases

InterProIPR006789. ARP2/3_p16_Arc.
[Graphical view]
Gene3DG3DSA:1.25.40.190. p16_Arc. 1 hit.
PANTHERPTHR12644. p16_Arc. 1 hit.
PfamPF04699. P16-Arc. 1 hit.
[Graphical view]
ProDomQ9BPX5.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameARP5L_HUMAN
AccessionPrimary (citable) accession number: Q9BPX5
Secondary accession number(s): Q7Z523
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: June 1, 2001
Last modified: July 22, 2008
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents