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Reviewed, UniProtKB/Swiss-Prot Q9BPX5 (ARP5L_HUMAN)

Last modified December 15, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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

Cytoplasmcytoskeleton By similarity.

Sequence similarities

Belongs to the ARPC5 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processregulation of actin filament polymerization

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTR3BQ9P1U11EBI-711189,EBI-1047175

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 153152Actin-related protein 2/3 complex subunit 5-like protein
PRO_0000279480

Amino acid modifications

Modified residue641Phosphoserine Ref.5

Experimental info

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

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

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]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-49; 90-110 AND 115-145, MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[5]"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.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

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.
IPIIPI00414554.
RefSeqNP_112240.1.
UniGeneHs.132499

3D structure databases

SMRQ9BPX5. Positions 8-152.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BPX5. 3 interactions.
STRINGQ9BPX5.

Proteomic databases

PeptideAtlasQ9BPX5.
PRIDEQ9BPX5.

Genome annotation databases

EnsemblENST00000259477; ENSP00000259477; ENSG00000136950; Homo sapiens. [Genome view]
ENST00000353214; ENSP00000345361; ENSG00000136950; Homo sapiens. [Genome view]
GeneID81873.
KEGGhsa:81873.
UCSCuc004bpa.2. human.

Organism-specific databases

CTD81873.
GeneCardsGC09P126664.
HGNCHGNC:23366. ARPC5L.
HPAHPA022013.
PharmGKBPA134991012.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG377673.
HOVERGENQ9BPX5.
InParanoidQ9BPX5.
OMARNSPINT.
OrthoDBEOG9MPM8R.

Gene expression databases

ArrayExpressQ9BPX5.
BgeeQ9BPX5.
CleanExHS_ARPC5L.
GenevestigatorQ9BPX5.

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]
ProtoNetSearch...

Other Resources

NextBio72214.

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: December 15, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 9

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

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