Q9Y5K6 (CD2AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CD2-associated protein

Alternative name(s):
Adapter protein CMS
Cas ligand with multiple SH3 domains

Gene names

Name:

CD2AP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. 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 By similarity. Interacts with DDN; interaction is direct By similarity. 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. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.20
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cell projection › ruffle 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 process	Cell cycle Cell division Mitosis
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat SH3 domain SH3-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Traceable author statement Ref.1. Source: ProtInc signal transduction Non-traceable author statement Ref.1. Source: ProtInc substrate-dependent cell migration, cell extension Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA filamentous actin Inferred from direct assay Ref.1. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA ruffle Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	structural constituent of cytoskeleton Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	3	EBI-298152,EBI-401755

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

CD2-associated protein

PRO_0000089435

Regions

Domain

1 – 59

59

SH3 1; truncated

Domain

108 – 167

60

SH3 2

Domain

269 – 330

62

SH3 3

Region

1 – 175

175

Interaction with ANLN and localization to the midbody

Coiled coil

577 – 638

62

Potential

Motif

336 – 352

17

SH3-binding Potential

Motif

378 – 397

20

SH3-binding Potential

Motif

410 – 422

13

SH3-binding Potential

Compositional bias

336 – 422

87

Pro-rich

Amino acid modifications

Modified residue

224

1

Phosphoserine Ref.19

Modified residue

458

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Modified residue

510

1

Phosphoserine Ref.17 Ref.19

Modified residue

514

1

Phosphoserine Ref.19

Natural variations

Natural variant

581

1

N → K.
Corresponds to variant rs34069459 [ dbSNP | Ensembl ].

VAR_033672

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

639

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

25 – 31

7

Beta strand

37 – 42

6

Beta strand

45 – 50

6

Helix

51 – 53

3

Beta strand

54 – 56

3

Beta strand

112 – 115

4

Beta strand

134 – 142

9

Beta strand

145 – 150

6

Beta strand

153 – 158

6

Helix

159 – 161

3

Beta strand

162 – 164

3

Helix

489 – 492

4

Helix

503 – 505

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5K6 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7576509C7ED5B343	FASTA	639	71,451
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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, MASS SPECTROMETRY. Tissue: Platelet.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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, MASS SPECTROMETRY.
[20]	"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.
[21]	"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, MASS SPECTROMETRY.
[22]	"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.

Web resources

GeneReviews

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.

IPI

IPI00412771.

PIR

T13151.

RefSeq

NP_036252.1. NM_012120.2.

UniGene

Hs.485518.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FEI	NMR	-	A	111-166	[»]
2J6F	X-ray	1.70	A	1-62	[»]
2J6K	X-ray	2.78	A/B/C/D/E/F/G/H/I/J/K/L	1-62	[»]
2J6O	X-ray	2.22	A	1-62	[»]
2J7I	X-ray	2.90	A/B	1-62	[»]
3AA6	X-ray	1.90	C	485-507	[»]
3LK4	X-ray	1.99	0/3/6/9/C/F/I/L/O/R/U/X	475-503	[»]
3U23	X-ray	1.11	A	109-168	[»]

ProteinModelPortal

Q9Y5K6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31807N.

IntAct

Q9Y5K6. 21 interactions.

MINT

MINT-93491.

STRING

9606.ENSP00000352264.

PTM databases

PhosphoSite

Q9Y5K6.

Polymorphism databases

DMDM

30172980.

Proteomic databases

PaxDb

Q9Y5K6.

PRIDE

Q9Y5K6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359314; ENSP00000352264; ENSG00000198087.

GeneID

23607.

KEGG

hsa:23607.

UCSC

uc003oyw.3. human.

Organism-specific databases

CTD

23607.

GeneCards

GC06P047445.

HGNC

HGNC:14258. CD2AP.

HPA

CAB004352.
HPA003267.
HPA003326.

MIM

604241. gene.
607832. phenotype.

neXtProt

NX_Q9Y5K6.

Orphanet

93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.

PharmGKB

PA26208.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG319250.

HOGENOM

HOG000231405.

HOVERGEN

HBG057824.

InParanoid

Q9Y5K6.

KO

K13738.

OMA

FAVQINE.

OrthoDB

EOG4GMTWW.

PhylomeDB

Q9Y5K6.

Enzyme and pathway databases

Pathway_Interaction_DB

vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

Bgee

Q9Y5K6.

CleanEx

HS_CD2AP.

Genevestigator

Q9Y5K6.

GermOnline

ENSG00000198087. Homo sapiens.

Family and domain databases

InterPro

IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 3 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 3 hits.

PROSITE

PS50002. SH3. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CD2AP. human.

EvolutionaryTrace

Q9Y5K6.

GenomeRNAi

23607.

NextBio

46304.

SOURCE

Search...

Entry information

Entry name

CD2AP_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.