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Protein

CD2-associated protein

Gene

CD2AP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • SH3 domain binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_23832. Nephrin interactions.
SignaLinkiQ9Y5K6.

Names & Taxonomyi

Protein namesi
Recommended name:
CD2-associated protein
Alternative name(s):
Adapter protein CMS
Cas ligand with multiple SH3 domains
Gene namesi
Name:CD2AP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14258. CD2AP.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • cell-cell junction Source: Ensembl
  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • filamentous actin Source: UniProtKB
  • nucleolus Source: HPA
  • plasma membrane Source: HPA
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Focal segmental glomerulosclerosis 3 (FSGS3)

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:607832

Organism-specific databases

MIMi607832. phenotype.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA26208.

Polymorphism and mutation databases

BioMutaiCD2AP.
DMDMi30172980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 639639CD2-associated proteinPRO_0000089435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei224 – 2241Phosphoserine1 Publication
Modified residuei458 – 4581Phosphoserine7 Publications
Modified residuei463 – 4631Phosphoserine1 Publication
Modified residuei510 – 5101Phosphoserine2 Publications
Modified residuei514 – 5141Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5K6.
PaxDbiQ9Y5K6.
PRIDEiQ9Y5K6.

PTM databases

PhosphoSiteiQ9Y5K6.

Expressioni

Tissue specificityi

Widely expressed in fetal and adult tissues.

Gene expression databases

BgeeiQ9Y5K6.
CleanExiHS_CD2AP.
GenevestigatoriQ9Y5K6.

Organism-specific databases

HPAiCAB004352.
HPA003267.
HPA003326.

Interactioni

Subunit structurei

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.Curated9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLNKQ8WV282EBI-298152,EBI-2623522
CBLP226814EBI-298152,EBI-518228
CBLBQ1319111EBI-298152,EBI-744027
CD2P067294EBI-298152,EBI-3912464
GRB2P629933EBI-298152,EBI-401755
IQGAP1P469404EBI-298152,EBI-297509
PDCD6IPQ8WUM42EBI-298152,EBI-310624
TSG101Q998162EBI-298152,EBI-346882

Protein-protein interaction databases

BioGridi117140. 71 interactions.
DIPiDIP-31807N.
IntActiQ9Y5K6. 30 interactions.
MINTiMINT-93491.
STRINGi9606.ENSP00000352264.

Structurei

Secondary structure

1
639
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi25 – 317Combined sources
Beta strandi37 – 426Combined sources
Beta strandi45 – 506Combined sources
Helixi51 – 533Combined sources
Beta strandi54 – 563Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi134 – 1429Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi153 – 1586Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1643Combined sources
Helixi489 – 4924Combined sources
Helixi503 – 5053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9Y5K6.
SMRiQ9Y5K6. Positions 2-329, 475-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5K6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5959SH3 1; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini108 – 16760SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini269 – 33062SH3 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 175175Interaction with ANLN and localization to the midbodyAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili577 – 63862Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi336 – 35217SH3-bindingSequence AnalysisAdd
BLAST
Motifi378 – 39720SH3-bindingSequence AnalysisAdd
BLAST
Motifi410 – 42213SH3-bindingSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi336 – 42287Pro-richAdd
BLAST

Domaini

The Pro-rich domain may mediate binding to SH3 domains.
Potential homodimerization is mediated by the coiled coil domain.

Sequence similaritiesi

Contains 3 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG319250.
GeneTreeiENSGT00530000063594.
HOGENOMiHOG000231405.
HOVERGENiHBG057824.
InParanoidiQ9Y5K6.
KOiK13738.
OMAiVHDDELT.
OrthoDBiEOG7W41BC.
PhylomeDBiQ9Y5K6.
TreeFamiTF350191.

Family and domain databases

InterProiIPR028445. CD2AP.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR14167:SF23. PTHR14167:SF23. 1 hit.
PfamiPF00018. SH3_1. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y5K6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP
60 70 80 90 100
DNFVKEIKRE TEFKDDSLPI KRERHGNVAS LVQRISTYGL PAGGIQPHPQ
110 120 130 140 150
TKNIKKKTKK RQCKVLFEYI PQNEDELELK VGDIIDINEE VEEGWWSGTL
160 170 180 190 200
NNKLGLFPSN FVKELEVTDD GETHEAQDDS ETVLAGPTSP IPSLGNVSET
210 220 230 240 250
ASGSVTQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK PEKPLILQSL
260 270 280 290 300
GPKTQSVEIT KTDTEGKIKA KEYCRTLFAY EGTNEDELTF KEGEIIHLIS
310 320 330 340 350
KETGEAGWWR GELNGKEGVF PDNFAVQINE LDKDFPKPKK PPPPAKAPAP
360 370 380 390 400
KPELIAAEKK YFSLKPEEKD EKSTLEQKPS KPAAPQVPPK KPTPPTKASN
410 420 430 440 450
LLRSSGTVYP KRPEKPVPPP PPIAKINGEV SSISSKFETE PVSKLKLDSE
460 470 480 490 500
QLPLRPKSVD FDSLTVRTSK ETDVVNFDDI ASSENLLHLT ANRPKMPGRR
510 520 530 540 550
LPGRFNGGHS PTHSPEKILK LPKEEDSANL KPSELKKDTC YSPKPSVYLS
560 570 580 590 600
TPSSASKANT TAFLTPLEIK AKVETDDVKK NSLDELRAQI IELLCIVEAL
610 620 630
KKDHGKELEK LRKDLEEEKT MRSNLEMEIE KLKKAVLSS
Length:639
Mass (Da):71,451
Last modified:November 1, 1999 - v1
Checksum:i7576509C7ED5B343
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti581 – 5811N → K.
Corresponds to variant rs34069459 [ dbSNP | Ensembl ].
VAR_033672

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34472.1.
PIRiT13151.
RefSeqiNP_036252.1. NM_012120.2.
UniGeneiHs.485518.

Genome annotation databases

EnsembliENST00000359314; ENSP00000352264; ENSG00000198087.
GeneIDi23607.
KEGGihsa:23607.
UCSCiuc003oyw.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34472.1.
PIRiT13151.
RefSeqiNP_036252.1. NM_012120.2.
UniGeneiHs.485518.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9Y5K6.
SMRiQ9Y5K6. Positions 2-329, 475-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117140. 71 interactions.
DIPiDIP-31807N.
IntActiQ9Y5K6. 30 interactions.
MINTiMINT-93491.
STRINGi9606.ENSP00000352264.

PTM databases

PhosphoSiteiQ9Y5K6.

Polymorphism and mutation databases

BioMutaiCD2AP.
DMDMi30172980.

Proteomic databases

MaxQBiQ9Y5K6.
PaxDbiQ9Y5K6.
PRIDEiQ9Y5K6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359314; ENSP00000352264; ENSG00000198087.
GeneIDi23607.
KEGGihsa:23607.
UCSCiuc003oyw.3. human.

Organism-specific databases

CTDi23607.
GeneCardsiGC06P047445.
HGNCiHGNC:14258. CD2AP.
HPAiCAB004352.
HPA003267.
HPA003326.
MIMi604241. gene.
607832. phenotype.
neXtProtiNX_Q9Y5K6.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA26208.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG319250.
GeneTreeiENSGT00530000063594.
HOGENOMiHOG000231405.
HOVERGENiHBG057824.
InParanoidiQ9Y5K6.
KOiK13738.
OMAiVHDDELT.
OrthoDBiEOG7W41BC.
PhylomeDBiQ9Y5K6.
TreeFamiTF350191.

Enzyme and pathway databases

ReactomeiREACT_23832. Nephrin interactions.
SignaLinkiQ9Y5K6.

Miscellaneous databases

ChiTaRSiCD2AP. human.
EvolutionaryTraceiQ9Y5K6.
GeneWikiiCD2AP.
GenomeRNAii23607.
NextBioi46304.
PROiQ9Y5K6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5K6.
CleanExiHS_CD2AP.
GenevestigatoriQ9Y5K6.

Family and domain databases

InterProiIPR028445. CD2AP.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR14167:SF23. PTHR14167:SF23. 1 hit.
PfamiPF00018. SH3_1. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "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.
  24. "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.
  25. "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.

Entry informationi

Entry nameiCD2AP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5K6
Secondary accession number(s): A6NL34, Q5VYA3, Q9UG97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 1, 1999
Last modified: May 27, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.