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Q9Y5K6 (CD2AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD2-associated protein
Alternative name(s):
Adapter protein CMS
Cas ligand with multiple SH3 domains
Gene names
Name:CD2AP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. 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. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis. Ref.9

Subunit structure

Self-associates. Homodimer Potential. 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. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.22

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell projectionruffle By similarity. Note: Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles. 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. Ref.9

Tissue specificity

Widely expressed in fetal and adult tissues.

Domain

The Pro-rich domain may mediate binding to SH3 domains.

Potential homodimerization is mediated by the coiled coil domain.

Post-translational modification

Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src. Ref.1 Ref.7 Ref.9

Involvement in 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.8

Sequence similarities

Contains 3 SH3 domains.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
SH3 domain
SH3-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein complex assembly

Traceable author statement Ref.1. Source: ProtInc

regulation of receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement Ref.1. Source: ProtInc

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

substrate-dependent cell migration, cell extension

Traceable author statement Ref.1. Source: ProtInc

vesicle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Traceable author statement Ref.1. Source: ProtInc

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

filamentous actin

Inferred from direct assay Ref.1. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from physical interaction Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

structural constituent of cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639CD2-associated protein
PRO_0000089435

Regions

Domain1 – 5959SH3 1; truncated
Domain108 – 16760SH3 2
Domain269 – 33062SH3 3
Region1 – 175175Interaction with ANLN and localization to the midbody
Coiled coil577 – 63862 Potential
Motif336 – 35217SH3-binding Potential
Motif378 – 39720SH3-binding Potential
Motif410 – 42213SH3-binding Potential
Compositional bias336 – 42287Pro-rich

Amino acid modifications

Modified residue2241Phosphoserine Ref.20
Modified residue4581Phosphoserine Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20
Modified residue5101Phosphoserine Ref.18 Ref.20
Modified residue5141Phosphoserine Ref.20

Natural variations

Natural variant5811N → K.
Corresponds to variant rs34069459 [ dbSNP | Ensembl ].
VAR_033672

Secondary structure

......................... 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5K6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 7576509C7ED5B343

FASTA63971,451
        10         20         30         40         50         60 
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP DNFVKEIKRE 

        70         80         90        100        110        120 
TEFKDDSLPI KRERHGNVAS LVQRISTYGL PAGGIQPHPQ TKNIKKKTKK RQCKVLFEYI 

       130        140        150        160        170        180 
PQNEDELELK VGDIIDINEE VEEGWWSGTL NNKLGLFPSN FVKELEVTDD GETHEAQDDS 

       190        200        210        220        230        240 
ETVLAGPTSP IPSLGNVSET ASGSVTQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK 

       250        260        270        280        290        300 
PEKPLILQSL GPKTQSVEIT KTDTEGKIKA KEYCRTLFAY EGTNEDELTF KEGEIIHLIS 

       310        320        330        340        350        360 
KETGEAGWWR GELNGKEGVF PDNFAVQINE LDKDFPKPKK PPPPAKAPAP KPELIAAEKK 

       370        380        390        400        410        420 
YFSLKPEEKD EKSTLEQKPS KPAAPQVPPK KPTPPTKASN LLRSSGTVYP KRPEKPVPPP 

       430        440        450        460        470        480 
PPIAKINGEV SSISSKFETE PVSKLKLDSE QLPLRPKSVD FDSLTVRTSK ETDVVNFDDI 

       490        500        510        520        530        540 
ASSENLLHLT ANRPKMPGRR LPGRFNGGHS PTHSPEKILK LPKEEDSANL KPSELKKDTC 

       550        560        570        580        590        600 
YSPKPSVYLS TPSSASKANT TAFLTPLEIK AKVETDDVKK NSLDELRAQI IELLCIVEAL 

       610        620        630 
KKDHGKELEK LRKDLEEEKT MRSNLEMEIE KLKKAVLSS 

« Hide

References

« Hide 'large scale' references
[1]"CMS: an adapter molecule involved in cytoskeletal rearrangements."
Kirsch K.H., Georgescu M.M., Ishimaru S., Hanafusa H.
Proc. Natl. Acad. Sci. U.S.A. 96:6211-6216(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, INTERACTION WITH BCAR1.
[2]"Human homolog of CD2AP."
Ora A., Toppinen M., Lehtonen E.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 548-639.
Tissue: Uterus.
[7]"The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction."
Kirsch K.H., Georgescu M.M., Shishido T., Langdon W.Y., Birge R.B., Hanafusa H.
J. Biol. Chem. 276:4957-4963(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH CBL, HOMODIMERIZATION.
[8]"CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility."
Kim J.M., Wu H., Green G., Winkler C.A., Kopp J.B., Miner J.H., Unanue E.R., Shaw A.S.
Science 300:1298-1300(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLOMERULAR DISEASE SUSCEPTIBILITY.
[9]"Clues to CD2-associated protein involvement in cytokinesis."
Monzo P., Gauthier N.C., Keslair F., Loubat A., Field C.M., Le Marchand-Brustel Y., Cormont M.
Mol. Biol. Cell 16:2891-2902(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ANLN, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[10]"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
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.
Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP17.
[11]"CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP."
Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E., Taniguchi H.
J. Biol. Chem. 281:28919-28931(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MVB12A.
[12]"Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6IP AND TSG101.
[13]"CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation of ret signal transduction."
Tsui C.C., Pierchala B.A.
J. Neurosci. 28:8789-8800(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RET.
[14]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-510, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-458; SER-510 AND SER-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain."
Moncalian G., Cardenes N., Deribe Y.L., Spinola-Amilibia M., Dikic I., Bravo J.
J. Biol. Chem. 281:38845-38853(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-62 IN COMPLEXES WITH CD2 AND CBLB, SUBUNIT.
[23]"Solution structure of the second SH3 domain of human CMS and a newly identified binding site at the C-terminus of c-Cbl."
Yao B., Zhang J., Dai H., Sun J., Jiao Y., Tang Y., Wu J., Shi Y.
Biochim. Biophys. Acta 1774:35-43(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 111-166, IDENTIFICATION BY MASS SPECTROMETRY.
[24]"Atomic resolution crystal structure of the 2nd SH3 domain from human CD2AP (CMS) in complex with a proline-rich peptide from human RIN3."
Structural genomics consortium (SGC)
Submitted (DEC-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 109-168 IN COMPLEX WITH RIN3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF146277 mRNA. Translation: AAD34595.1.
AF164377 mRNA. Translation: AAF80495.1.
AL355353, AL358178 Genomic DNA. Translation: CAH73238.1.
AL358178, AL355353 Genomic DNA. Translation: CAI16839.1.
CH471081 Genomic DNA. Translation: EAX04319.1.
BC069444 mRNA. Translation: AAH69444.1.
AL050105 mRNA. Translation: CAB43274.1.
CCDSCCDS34472.1.
PIRT13151.
RefSeqNP_036252.1. NM_012120.2.
UniGeneHs.485518.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FEINMR-A111-166[»]
2J6FX-ray1.70A1-62[»]
2J6KX-ray2.78A/B/C/D/E/F/G/H/I/J/K/L1-62[»]
2J6OX-ray2.22A1-62[»]
2J7IX-ray2.90A/B1-62[»]
3AA6X-ray1.90C485-507[»]
3LK4X-ray1.990/3/6/9/C/F/I/L/O/R/U/X475-503[»]
3U23X-ray1.11A109-168[»]
ProteinModelPortalQ9Y5K6.
SMRQ9Y5K6. Positions 2-329, 475-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117140. 66 interactions.
DIPDIP-31807N.
IntActQ9Y5K6. 30 interactions.
MINTMINT-93491.
STRING9606.ENSP00000352264.

PTM databases

PhosphoSiteQ9Y5K6.

Polymorphism databases

DMDM30172980.

Proteomic databases

MaxQBQ9Y5K6.
PaxDbQ9Y5K6.
PRIDEQ9Y5K6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359314; ENSP00000352264; ENSG00000198087.
GeneID23607.
KEGGhsa:23607.
UCSCuc003oyw.3. human.

Organism-specific databases

CTD23607.
GeneCardsGC06P047445.
HGNCHGNC:14258. CD2AP.
HPACAB004352.
HPA003267.
HPA003326.
MIM604241. gene.
607832. phenotype.
neXtProtNX_Q9Y5K6.
Orphanet93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBPA26208.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319250.
HOGENOMHOG000231405.
HOVERGENHBG057824.
InParanoidQ9Y5K6.
KOK13738.
OMAVHDDELT.
OrthoDBEOG7W41BC.
PhylomeDBQ9Y5K6.
TreeFamTF350191.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkQ9Y5K6.

Gene expression databases

BgeeQ9Y5K6.
CleanExHS_CD2AP.
GenevestigatorQ9Y5K6.

Family and domain databases

InterProIPR028445. CD2AP.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR14167:SF23. PTHR14167:SF23. 1 hit.
PfamPF00018. SH3_1. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
PROSITEPS50002. SH3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD2AP. human.
EvolutionaryTraceQ9Y5K6.
GeneWikiCD2AP.
GenomeRNAi23607.
NextBio46304.
PROQ9Y5K6.
SOURCESearch...

Entry information

Entry nameCD2AP_HUMAN
AccessionPrimary (citable) accession number: Q9Y5K6
Secondary accession number(s): A6NL34, Q5VYA3, Q9UG97
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM