ARP5L_HUMAN
ID ARP5L_HUMAN Reviewed; 153 AA.
AC Q9BPX5; Q7Z523;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Actin-related protein 2/3 complex subunit 5-like protein;
DE AltName: Full=Arp2/3 complex 16 kDa subunit 2;
DE Short=ARC16-2;
GN Name=ARPC5L;
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 [MRNA].
RA Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.;
RT "Cloning of a novel human cDNA homologous to human Arp2/3 complex 16kDa
RT subunit (ARC16) mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 PROTEIN SEQUENCE OF 12-49; 90-110 AND 115-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May function as component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with an
CC activating nucleation-promoting factor (NPF) mediates the formation of
CC branched actin networks.
CC -!- SUBUNIT: May be a component of the Arp2/3 complex in which it may
CC replace ARPC5.
CC -!- INTERACTION:
CC Q9BPX5; P59998: ARPC4; NbExp=7; IntAct=EBI-711189, EBI-351872;
CC Q9BPX5; O95257: GADD45G; NbExp=4; IntAct=EBI-711189, EBI-448202;
CC Q9BPX5; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-711189, EBI-12028784;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ARPC5 family. {ECO:0000305}.
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DR EMBL; AF087842; AAP97155.1; -; mRNA.
DR EMBL; AL354928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000018; AAH00018.1; -; mRNA.
DR EMBL; BC000798; AAH00798.1; -; mRNA.
DR EMBL; BC002418; AAH02418.1; -; mRNA.
DR CCDS; CCDS6859.1; -.
DR RefSeq; NP_112240.1; NM_030978.2.
DR PDB; 6YW6; EM; 4.20 A; G=1-153.
DR PDBsum; 6YW6; -.
DR AlphaFoldDB; Q9BPX5; -.
DR SMR; Q9BPX5; -.
DR BioGRID; 123617; 75.
DR DIP; DIP-50399N; -.
DR IntAct; Q9BPX5; 55.
DR MINT; Q9BPX5; -.
DR STRING; 9606.ENSP00000345361; -.
DR GlyGen; Q9BPX5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BPX5; -.
DR PhosphoSitePlus; Q9BPX5; -.
DR BioMuta; ARPC5L; -.
DR DMDM; 74752229; -.
DR EPD; Q9BPX5; -.
DR jPOST; Q9BPX5; -.
DR MassIVE; Q9BPX5; -.
DR MaxQB; Q9BPX5; -.
DR PaxDb; Q9BPX5; -.
DR PeptideAtlas; Q9BPX5; -.
DR PRIDE; Q9BPX5; -.
DR ProteomicsDB; 78587; -.
DR TopDownProteomics; Q9BPX5; -.
DR Antibodypedia; 16361; 66 antibodies from 19 providers.
DR DNASU; 81873; -.
DR Ensembl; ENST00000259477.6; ENSP00000259477.6; ENSG00000136950.13.
DR Ensembl; ENST00000353214.6; ENSP00000345361.2; ENSG00000136950.13.
DR GeneID; 81873; -.
DR KEGG; hsa:81873; -.
DR MANE-Select; ENST00000353214.6; ENSP00000345361.2; NM_030978.3; NP_112240.1.
DR UCSC; uc004boz.2; human.
DR CTD; 81873; -.
DR DisGeNET; 81873; -.
DR GeneCards; ARPC5L; -.
DR HGNC; HGNC:23366; ARPC5L.
DR HPA; ENSG00000136950; Low tissue specificity.
DR neXtProt; NX_Q9BPX5; -.
DR OpenTargets; ENSG00000136950; -.
DR PharmGKB; PA134991012; -.
DR VEuPathDB; HostDB:ENSG00000136950; -.
DR eggNOG; KOG3380; Eukaryota.
DR GeneTree; ENSGT00940000158501; -.
DR HOGENOM; CLU_101888_1_1_1; -.
DR InParanoid; Q9BPX5; -.
DR OMA; SQIQGRN; -.
DR OrthoDB; 1565115at2759; -.
DR PhylomeDB; Q9BPX5; -.
DR TreeFam; TF319716; -.
DR PathwayCommons; Q9BPX5; -.
DR SignaLink; Q9BPX5; -.
DR BioGRID-ORCS; 81873; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; ARPC5L; human.
DR GenomeRNAi; 81873; -.
DR Pharos; Q9BPX5; Tdark.
DR PRO; PR:Q9BPX5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BPX5; protein.
DR Bgee; ENSG00000136950; Expressed in secondary oocyte and 204 other tissues.
DR ExpressionAtlas; Q9BPX5; baseline and differential.
DR Genevisible; Q9BPX5; HS.
DR GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARPC5.
DR InterPro; IPR036743; ARPC5_sf.
DR InterPro; IPR030075; ARPC5L.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR PANTHER; PTHR12644:SF2; PTHR12644:SF2; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR PIRSF; PIRSF039096; p16-ARC; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..153
FT /note="Actin-related protein 2/3 complex subunit 5-like
FT protein"
FT /id="PRO_0000279480"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CONFLICT 30
FT /note="Missing (in Ref. 1; AAP97155)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..37
FT /note="EP -> RT (in Ref. 1; AAP97155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 16941 MW; D8E4772404300560 CRC64;
MARNTLSSRF RRVDIDEFDE NKFVDEQEEA AAAAAEPGPD PSEVDGLLRQ GDMLRAFHAA
LRNSPVNTKN QAVKERAQGV VLKVLTNFKS SEIEQAVQSL DRNGVDLLMK YIYKGFEKPT
ENSSAVLLQW HEKALAVGGL GSIIRVLTAR KTV
