Full text data of ARPC5L
ARPC5L
[Confidence: low (only semi-automatic identification from reviews)]
Actin-related protein 2/3 complex subunit 5-like protein (Arp2/3 complex 16 kDa subunit 2; ARC16-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Actin-related protein 2/3 complex subunit 5-like protein (Arp2/3 complex 16 kDa subunit 2; ARC16-2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BPX5
ID ARP5L_HUMAN Reviewed; 153 AA.
AC Q9BPX5; Q7Z523;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 94.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 16kDa 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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
RT project: 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 MASS 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May function as component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with
CC an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks.
CC -!- SUBUNIT: May be a component of the Arp2/3 complex in which it may
CC replace ARPC5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- SIMILARITY: Belongs to the ARPC5 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF087842; AAP97155.1; -; mRNA.
DR EMBL; AL354928; CAI39641.1; -; Genomic_DNA.
DR EMBL; BC000018; AAH00018.1; -; mRNA.
DR EMBL; BC000798; AAH00798.1; -; mRNA.
DR EMBL; BC002418; AAH02418.1; -; mRNA.
DR RefSeq; NP_112240.1; NM_030978.1.
DR RefSeq; XP_005252307.1; XM_005252250.1.
DR UniGene; Hs.132499; -.
DR ProteinModelPortal; Q9BPX5; -.
DR SMR; Q9BPX5; 8-152.
DR IntAct; Q9BPX5; 3.
DR MINT; MINT-5001923; -.
DR STRING; 9606.ENSP00000259477; -.
DR PhosphoSite; Q9BPX5; -.
DR DMDM; 74752229; -.
DR PaxDb; Q9BPX5; -.
DR PeptideAtlas; Q9BPX5; -.
DR PRIDE; Q9BPX5; -.
DR DNASU; 81873; -.
DR Ensembl; ENST00000259477; ENSP00000259477; ENSG00000136950.
DR Ensembl; ENST00000353214; ENSP00000345361; ENSG00000136950.
DR GeneID; 81873; -.
DR KEGG; hsa:81873; -.
DR UCSC; uc004bpa.4; human.
DR CTD; 81873; -.
DR GeneCards; GC09P127624; -.
DR H-InvDB; HIX0008377; -.
DR HGNC; HGNC:23366; ARPC5L.
DR HPA; HPA022013; -.
DR neXtProt; NX_Q9BPX5; -.
DR PharmGKB; PA134991012; -.
DR eggNOG; NOG303792; -.
DR HOGENOM; HOG000197215; -.
DR HOVERGEN; HBG050583; -.
DR InParanoid; Q9BPX5; -.
DR KO; K05754; -.
DR OMA; VLLTWHE; -.
DR OrthoDB; EOG79PJQP; -.
DR ChiTaRS; ARPC5L; human.
DR GenomeRNAi; 81873; -.
DR NextBio; 72214; -.
DR PRO; PR:Q9BPX5; -.
DR Bgee; Q9BPX5; -.
DR CleanEx; HS_ARPC5L; -.
DR Genevestigator; Q9BPX5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARP2/3_p16_Arc.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1 153 Actin-related protein 2/3 complex subunit
FT 5-like protein.
FT /FTId=PRO_0000279480.
FT MOD_RES 64 64 Phosphoserine.
FT CONFLICT 30 30 Missing (in Ref. 1; AAP97155).
FT CONFLICT 36 37 EP -> RT (in Ref. 1; AAP97155).
SQ SEQUENCE 153 AA; 16941 MW; D8E4772404300560 CRC64;
MARNTLSSRF RRVDIDEFDE NKFVDEQEEA AAAAAEPGPD PSEVDGLLRQ GDMLRAFHAA
LRNSPVNTKN QAVKERAQGV VLKVLTNFKS SEIEQAVQSL DRNGVDLLMK YIYKGFEKPT
ENSSAVLLQW HEKALAVGGL GSIIRVLTAR KTV
//
ID ARP5L_HUMAN Reviewed; 153 AA.
AC Q9BPX5; Q7Z523;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 94.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 16kDa 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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
RT project: 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 MASS 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May function as component of the Arp2/3 complex which is
CC involved in regulation of actin polymerization and together with
CC an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks.
CC -!- SUBUNIT: May be a component of the Arp2/3 complex in which it may
CC replace ARPC5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- SIMILARITY: Belongs to the ARPC5 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF087842; AAP97155.1; -; mRNA.
DR EMBL; AL354928; CAI39641.1; -; Genomic_DNA.
DR EMBL; BC000018; AAH00018.1; -; mRNA.
DR EMBL; BC000798; AAH00798.1; -; mRNA.
DR EMBL; BC002418; AAH02418.1; -; mRNA.
DR RefSeq; NP_112240.1; NM_030978.1.
DR RefSeq; XP_005252307.1; XM_005252250.1.
DR UniGene; Hs.132499; -.
DR ProteinModelPortal; Q9BPX5; -.
DR SMR; Q9BPX5; 8-152.
DR IntAct; Q9BPX5; 3.
DR MINT; MINT-5001923; -.
DR STRING; 9606.ENSP00000259477; -.
DR PhosphoSite; Q9BPX5; -.
DR DMDM; 74752229; -.
DR PaxDb; Q9BPX5; -.
DR PeptideAtlas; Q9BPX5; -.
DR PRIDE; Q9BPX5; -.
DR DNASU; 81873; -.
DR Ensembl; ENST00000259477; ENSP00000259477; ENSG00000136950.
DR Ensembl; ENST00000353214; ENSP00000345361; ENSG00000136950.
DR GeneID; 81873; -.
DR KEGG; hsa:81873; -.
DR UCSC; uc004bpa.4; human.
DR CTD; 81873; -.
DR GeneCards; GC09P127624; -.
DR H-InvDB; HIX0008377; -.
DR HGNC; HGNC:23366; ARPC5L.
DR HPA; HPA022013; -.
DR neXtProt; NX_Q9BPX5; -.
DR PharmGKB; PA134991012; -.
DR eggNOG; NOG303792; -.
DR HOGENOM; HOG000197215; -.
DR HOVERGEN; HBG050583; -.
DR InParanoid; Q9BPX5; -.
DR KO; K05754; -.
DR OMA; VLLTWHE; -.
DR OrthoDB; EOG79PJQP; -.
DR ChiTaRS; ARPC5L; human.
DR GenomeRNAi; 81873; -.
DR NextBio; 72214; -.
DR PRO; PR:Q9BPX5; -.
DR Bgee; Q9BPX5; -.
DR CleanEx; HS_ARPC5L; -.
DR Genevestigator; Q9BPX5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 1.25.40.190; -; 1.
DR InterPro; IPR006789; ARP2/3_p16_Arc.
DR PANTHER; PTHR12644; PTHR12644; 1.
DR Pfam; PF04699; P16-Arc; 1.
DR SUPFAM; SSF69103; SSF69103; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1 153 Actin-related protein 2/3 complex subunit
FT 5-like protein.
FT /FTId=PRO_0000279480.
FT MOD_RES 64 64 Phosphoserine.
FT CONFLICT 30 30 Missing (in Ref. 1; AAP97155).
FT CONFLICT 36 37 EP -> RT (in Ref. 1; AAP97155).
SQ SEQUENCE 153 AA; 16941 MW; D8E4772404300560 CRC64;
MARNTLSSRF RRVDIDEFDE NKFVDEQEEA AAAAAEPGPD PSEVDGLLRQ GDMLRAFHAA
LRNSPVNTKN QAVKERAQGV VLKVLTNFKS SEIEQAVQSL DRNGVDLLMK YIYKGFEKPT
ENSSAVLLQW HEKALAVGGL GSIIRVLTAR KTV
//