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CD2-associated protein (Adapter protein CMS) (Cas ligand with multiple SH3 domains)

 CD2AP_HUMAN             Reviewed;         639 AA.
Q9Y5K6; A6NL34; Q5VYA3; Q9UG97;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=CD2-associated protein;
AltName: Full=Adapter protein CMS;
AltName: Full=Cas ligand with multiple SH3 domains;
Name=CD2AP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMODIMERIZATION, INTERACTION
WITH BCAR1, SUBCELLULAR LOCATION, DOMAIN, AND PHOSPHORYLATION.
PubMed=10339567; DOI=10.1073/pnas.96.11.6211;
Kirsch K.H., Georgescu M.M., Ishimaru S., Hanafusa H.;
"CMS: an adapter molecule involved in cytoskeletal rearrangements.";
Proc. Natl. Acad. Sci. U.S.A. 96:6211-6216(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Ora A., Toppinen M., Lehtonen E.;
"Human homolog of CD2AP.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 548-639.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION, INTERACTION WITH CBL, AND HOMODIMERIZATION.
PubMed=11067845; DOI=10.1074/jbc.M005784200;
Kirsch K.H., Georgescu M.M., Shishido T., Langdon W.Y., Birge R.B.,
Hanafusa H.;
"The adapter type protein CMS/CD2AP binds to the proto-oncogenic
protein c-Cbl through a tyrosine phosphorylation-regulated Src
homology 3 domain interaction.";
J. Biol. Chem. 276:4957-4963(2001).
[8]
INVOLVEMENT IN SUSCEPTIBILITY TO FSGS3.
PubMed=12764198; DOI=10.1126/science.1081068;
Kim J.M., Wu H., Green G., Winkler C.A., Kopp J.B., Miner J.H.,
Unanue E.R., Shaw A.S.;
"CD2-associated protein haploinsufficiency is linked to glomerular
disease susceptibility.";
Science 300:1298-1300(2003).
[9]
FUNCTION, INTERACTION WITH ANLN, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION.
PubMed=15800069; DOI=10.1091/mbc.E04-09-0773;
Monzo P., Gauthier N.C., Keslair F., Loubat A., Field C.M.,
Le Marchand-Brustel Y., Cormont M.;
"Clues to CD2-associated protein involvement in cytokinesis.";
Mol. Biol. Cell 16:2891-2902(2005).
[10]
INTERACTION WITH ARHGAP17.
PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
Starostine A., Metalnikov P., Pawson T.;
"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
proteins in epithelial cells.";
Cell 125:535-548(2006).
[11]
INTERACTION WITH MVB12A.
PubMed=16895919; DOI=10.1074/jbc.M605693200;
Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E.,
Taniguchi H.;
"CFBP is a novel tyrosine-phosphorylated protein that might function
as a regulator of CIN85/CD2AP.";
J. Biol. Chem. 281:28919-28931(2006).
[12]
INTERACTION WITH PDCD6IP AND TSG101.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[13]
INTERACTION WITH RET.
PubMed=18753381; DOI=10.1523/JNEUROSCI.2738-08.2008;
Tsui C.C., Pierchala B.A.;
"CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the
regulation of ret signal transduction.";
J. Neurosci. 28:8789-8800(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-510, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-458; SER-510
AND SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
FUNCTION, INTERACTION WITH CAPZA1; CGNL1 AND SH3BP1, AND SUBCELLULAR
LOCATION.
PubMed=22891260; DOI=10.1083/jcb.201202094;
Elbediwy A., Zihni C., Terry S.J., Clark P., Matter K., Balda M.S.;
"Epithelial junction formation requires confinement of Cdc42 activity
by a novel SH3BP1 complex.";
J. Cell Biol. 198:677-693(2012).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-80; SER-86;
SER-224; SER-458; SER-463; SER-510; SER-514; THR-565 AND SER-582, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-463, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-523, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-62 IN COMPLEXES WITH CD2
AND CBLB, AND SUBUNIT.
PubMed=17020880; DOI=10.1074/jbc.M606411200;
Moncalian G., Cardenes N., Deribe Y.L., Spinola-Amilibia M., Dikic I.,
Bravo J.;
"Atypical polyproline recognition by the CMS N-terminal Src homology 3
domain.";
J. Biol. Chem. 281:38845-38853(2006).
[28]
STRUCTURE BY NMR OF 111-166, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17188587; DOI=10.1016/j.bbapap.2006.09.018;
Yao B., Zhang J., Dai H., Sun J., Jiao Y., Tang Y., Wu J., Shi Y.;
"Solution structure of the second SH3 domain of human CMS and a newly
identified binding site at the C-terminus of c-Cbl.";
Biochim. Biophys. Acta 1774:35-43(2007).
[29]
X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 109-168 IN COMPLEX WITH
RIN3.
Structural genomics consortium (SGC);
"Atomic resolution crystal structure of the 2nd SH3 domain from human
CD2AP (CMS) in complex with a proline-rich peptide from human RIN3.";
Submitted (DEC-2011) to the PDB data bank.
-!- FUNCTION: Seems to act as an adapter protein between membrane
proteins and the actin cytoskeleton (PubMed:10339567). In
collaboration with CBLC, modulates the rate of RET turnover and
may act as regulatory checkpoint that limits the potency of GDNF
on neuronal survival. Controls CBLC function, converting it from
an inhibitor to a promoter of RET degradation (By similarity). May
play a role in receptor clustering and cytoskeletal polarity in
the junction between T-cell and antigen-presenting cell (By
similarity). May anchor the podocyte slit diaphragm to the actin
cytoskeleton in renal glomerolus. Also required for cytokinesis
(PubMed:15800069). Plays a role in epithelial cell junctions
formation (PubMed:22891260). {ECO:0000250|UniProtKB:F1LRS8,
ECO:0000250|UniProtKB:Q9JLQ0, ECO:0000269|PubMed:10339567,
ECO:0000269|PubMed:15800069, ECO:0000269|PubMed:22891260}.
-!- SUBUNIT: Homodimer. Interacts with F-actin, PKD2, NPHS1 and NPHS2.
Interacts with WTIP. Interacts with DDN; interaction is direct.
Interacts (via SH3 2 domain) with CBL (via phosphorylated C-
terminus). Interacts with BCAR1/p130Cas (via SH3 domain).
Interacts with MVB12A and ARHGAP17. Interacts with ANLN, CD2 and
CBLB. Interacts with PDCD6IP and TSG101. Interacts with RIN3.
Interacts directly with RET (inactive) and CBLC; upon RET
activation by GDNF suggested to dissociate from RET as CBLC:CD2AP
complex (Probable) (PubMed:10339567, PubMed:11067845,
PubMed:15800069, PubMed:16678097, PubMed:16895919,
PubMed:17020880, PubMed:17853893, PubMed:18753381, Ref.29).
Interacts with CGNL1 and SH3BP1; probably part of a complex at
cell junctions (PubMed:22891260). Interacts with CAPZA1
(PubMed:22891260). {ECO:0000269|PubMed:10339567,
ECO:0000269|PubMed:11067845, ECO:0000269|PubMed:15800069,
ECO:0000269|PubMed:16678097, ECO:0000269|PubMed:16895919,
ECO:0000269|PubMed:17020880, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:22891260,
ECO:0000269|Ref.29, ECO:0000305}.
-!- INTERACTION:
Q8WV28:BLNK; NbExp=2; IntAct=EBI-298152, EBI-2623522;
P22681:CBL; NbExp=4; IntAct=EBI-298152, EBI-518228;
Q13191:CBLB; NbExp=11; IntAct=EBI-298152, EBI-744027;
P06729:CD2; NbExp=4; IntAct=EBI-298152, EBI-3912464;
P62993:GRB2; NbExp=3; IntAct=EBI-298152, EBI-401755;
P46940:IQGAP1; NbExp=4; IntAct=EBI-298152, EBI-297509;
Q8WUM4:PDCD6IP; NbExp=2; IntAct=EBI-298152, EBI-310624;
Q99816:TSG101; NbExp=2; IntAct=EBI-298152, EBI-346882;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15800069}. Cell projection, ruffle
{ECO:0000269|PubMed:10339567}. Cell junction
{ECO:0000269|PubMed:22891260}. Note=Colocalizes with F-actin and
BCAR1/p130Cas in membrane ruffles (PubMed:10339567). Located at
podocyte slit diaphragm between podocyte foot processes (By
similarity). During late anaphase and telophase, concentrates in
the vicinity of the midzone microtubules and in the midbody in
late telophase (PubMed:15800069). {ECO:0000250|UniProtKB:Q9JLQ0,
ECO:0000269|PubMed:10339567, ECO:0000269|PubMed:15800069}.
-!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues.
-!- DOMAIN: The Pro-rich domain may mediate binding to SH3 domains.
-!- DOMAIN: Potential homodimerization is mediated by the coiled coil
domain. {ECO:0000269|PubMed:10339567}.
-!- PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn
and c-Src. {ECO:0000269|PubMed:10339567,
ECO:0000269|PubMed:11067845, ECO:0000269|PubMed:15800069}.
-!- DISEASE: Focal segmental glomerulosclerosis 3 (FSGS3)
[MIM:607832]: A renal pathology defined by the presence of
segmental sclerosis in glomeruli and resulting in proteinuria,
reduced glomerular filtration rate and progressive decline in
renal function. Renal insufficiency often progresses to end-stage
renal disease, a highly morbid state requiring either dialysis
therapy or kidney transplantation. {ECO:0000269|PubMed:12764198}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
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EMBL; AF146277; AAD34595.1; -; mRNA.
EMBL; AF164377; AAF80495.1; -; mRNA.
EMBL; AL355353; CAH73238.1; -; Genomic_DNA.
EMBL; AL358178; CAH73238.1; JOINED; Genomic_DNA.
EMBL; AL358178; CAI16839.1; -; Genomic_DNA.
EMBL; AL355353; CAI16839.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX04319.1; -; Genomic_DNA.
EMBL; BC069444; AAH69444.1; -; mRNA.
EMBL; AL050105; CAB43274.1; -; mRNA.
CCDS; CCDS34472.1; -.
PIR; T13151; T13151.
RefSeq; NP_036252.1; NM_012120.2.
UniGene; Hs.485518; -.
PDB; 2FEI; NMR; -; A=111-166.
PDB; 2J6F; X-ray; 1.70 A; A=1-62.
PDB; 2J6K; X-ray; 2.78 A; A/B/C/D/E/F/G/H/I/J/K/L=1-62.
PDB; 2J6O; X-ray; 2.22 A; A=1-62.
PDB; 2J7I; X-ray; 2.90 A; A/B=1-62.
PDB; 3AA6; X-ray; 1.90 A; C=485-507.
PDB; 3LK4; X-ray; 1.99 A; 0/3/6/9/C/F/I/L/O/R/U/X=475-503.
PDB; 3U23; X-ray; 1.11 A; A=109-168.
PDB; 4WCI; X-ray; 1.65 A; A/C/E=1-60.
PDB; 4X1V; X-ray; 1.58 A; A=109-168.
PDBsum; 2FEI; -.
PDBsum; 2J6F; -.
PDBsum; 2J6K; -.
PDBsum; 2J6O; -.
PDBsum; 2J7I; -.
PDBsum; 3AA6; -.
PDBsum; 3LK4; -.
PDBsum; 3U23; -.
PDBsum; 4WCI; -.
PDBsum; 4X1V; -.
ProteinModelPortal; Q9Y5K6; -.
SMR; Q9Y5K6; -.
BioGrid; 117140; 110.
CORUM; Q9Y5K6; -.
DIP; DIP-31807N; -.
IntAct; Q9Y5K6; 44.
MINT; MINT-93491; -.
STRING; 9606.ENSP00000352264; -.
iPTMnet; Q9Y5K6; -.
PhosphoSitePlus; Q9Y5K6; -.
BioMuta; CD2AP; -.
DMDM; 30172980; -.
EPD; Q9Y5K6; -.
MaxQB; Q9Y5K6; -.
PaxDb; Q9Y5K6; -.
PeptideAtlas; Q9Y5K6; -.
PRIDE; Q9Y5K6; -.
Ensembl; ENST00000359314; ENSP00000352264; ENSG00000198087.
GeneID; 23607; -.
KEGG; hsa:23607; -.
UCSC; uc003oyw.4; human.
CTD; 23607; -.
DisGeNET; 23607; -.
EuPathDB; HostDB:ENSG00000198087.7; -.
GeneCards; CD2AP; -.
HGNC; HGNC:14258; CD2AP.
HPA; CAB004352; -.
HPA; HPA003267; -.
HPA; HPA003326; -.
MalaCards; CD2AP; -.
MIM; 604241; gene.
MIM; 607832; phenotype.
neXtProt; NX_Q9Y5K6; -.
OpenTargets; ENSG00000198087; -.
Orphanet; 93213; Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKB; PA26208; -.
eggNOG; KOG4348; Eukaryota.
eggNOG; ENOG410XQBY; LUCA.
GeneTree; ENSGT00530000063594; -.
HOGENOM; HOG000231405; -.
HOVERGEN; HBG057824; -.
InParanoid; Q9Y5K6; -.
KO; K13738; -.
OMA; YDAVHDD; -.
OrthoDB; EOG091G041Q; -.
PhylomeDB; Q9Y5K6; -.
TreeFam; TF350191; -.
Reactome; R-HSA-373753; Nephrin family interactions.
SignaLink; Q9Y5K6; -.
SIGNOR; Q9Y5K6; -.
ChiTaRS; CD2AP; human.
EvolutionaryTrace; Q9Y5K6; -.
GeneWiki; CD2AP; -.
GenomeRNAi; 23607; -.
PRO; PR:Q9Y5K6; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000198087; -.
CleanEx; HS_CD2AP; -.
Genevisible; Q9Y5K6; HS.
GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IEA:Ensembl.
GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IMP:UniProtKB.
GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
GO; GO:0006930; P:substrate-dependent cell migration, cell extension; TAS:ProtInc.
GO; GO:0016050; P:vesicle organization; IEA:Ensembl.
CDD; cd12053; SH3_CD2AP_1; 1.
CDD; cd12054; SH3_CD2AP_2; 1.
CDD; cd12056; SH3_CD2AP_3; 1.
InterPro; IPR028445; CD2AP.
InterPro; IPR035775; CD2AP_SH3_1.
InterPro; IPR035777; CD2AP_SH3_3.
InterPro; IPR035776; CD2AP_SH_2.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR14167:SF23; PTHR14167:SF23; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF14604; SH3_9; 2.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell junction;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Isopeptide bond; Mitosis; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3 domain; SH3-binding; Ubl conjugation.
CHAIN 1 639 CD2-associated protein.
/FTId=PRO_0000089435.
DOMAIN 1 59 SH3 1; truncated. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 108 167 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 269 330 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 1 175 Interaction with ANLN and localization to
the midbody.
{ECO:0000269|PubMed:15800069}.
COILED 577 638 {ECO:0000255}.
MOTIF 336 352 SH3-binding. {ECO:0000255}.
MOTIF 378 397 SH3-binding. {ECO:0000255}.
MOTIF 410 422 SH3-binding. {ECO:0000255}.
COMPBIAS 336 422 Pro-rich.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:F1LRS8}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 565 565 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 523 523 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 581 581 N -> K (in dbSNP:rs34069459).
/FTId=VAR_033672.
STRAND 4 6 {ECO:0000244|PDB:4WCI}.
STRAND 25 30 {ECO:0000244|PDB:4WCI}.
STRAND 37 42 {ECO:0000244|PDB:4WCI}.
STRAND 45 50 {ECO:0000244|PDB:4WCI}.
STRAND 53 56 {ECO:0000244|PDB:4WCI}.
STRAND 112 115 {ECO:0000244|PDB:3U23}.
STRAND 134 142 {ECO:0000244|PDB:3U23}.
STRAND 145 150 {ECO:0000244|PDB:3U23}.
STRAND 153 158 {ECO:0000244|PDB:3U23}.
HELIX 159 161 {ECO:0000244|PDB:3U23}.
STRAND 162 164 {ECO:0000244|PDB:3U23}.
HELIX 489 492 {ECO:0000244|PDB:3AA6}.
HELIX 503 505 {ECO:0000244|PDB:3AA6}.
SEQUENCE 639 AA; 71451 MW; 7576509C7ED5B343 CRC64;
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP DNFVKEIKRE
TEFKDDSLPI KRERHGNVAS LVQRISTYGL PAGGIQPHPQ TKNIKKKTKK RQCKVLFEYI
PQNEDELELK VGDIIDINEE VEEGWWSGTL NNKLGLFPSN FVKELEVTDD GETHEAQDDS
ETVLAGPTSP IPSLGNVSET ASGSVTQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK
PEKPLILQSL GPKTQSVEIT KTDTEGKIKA KEYCRTLFAY EGTNEDELTF KEGEIIHLIS
KETGEAGWWR GELNGKEGVF PDNFAVQINE LDKDFPKPKK PPPPAKAPAP KPELIAAEKK
YFSLKPEEKD EKSTLEQKPS KPAAPQVPPK KPTPPTKASN LLRSSGTVYP KRPEKPVPPP
PPIAKINGEV SSISSKFETE PVSKLKLDSE QLPLRPKSVD FDSLTVRTSK ETDVVNFDDI
ASSENLLHLT ANRPKMPGRR LPGRFNGGHS PTHSPEKILK LPKEEDSANL KPSELKKDTC
YSPKPSVYLS TPSSASKANT TAFLTPLEIK AKVETDDVKK NSLDELRAQI IELLCIVEAL
KKDHGKELEK LRKDLEEEKT MRSNLEMEIE KLKKAVLSS


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