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Q9Y5K6

- CD2AP_HUMAN

UniProt

Q9Y5K6 - CD2AP_HUMAN

Protein

CD2-associated protein

Gene

CD2AP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    1. protein binding Source: UniProtKB
    2. SH3 domain binding Source: UniProtKB
    3. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    3. protein complex assembly Source: ProtInc
    4. regulation of receptor-mediated endocytosis Source: Ensembl
    5. signal transduction Source: ProtInc
    6. single organismal cell-cell adhesion Source: Ensembl
    7. substrate-dependent cell migration, cell extension Source: ProtInc
    8. vesicle organization Source: Ensembl

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14258. CD2AP.

    Subcellular locationi

    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.By similarity1 Publication

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cytoplasm Source: ProtInc
    3. endocytic vesicle Source: Ensembl
    4. extracellular vesicular exosome Source: UniProt
    5. filamentous actin Source: UniProtKB
    6. perinuclear region of cytoplasm Source: Ensembl
    7. plasma membrane Source: Ensembl
    8. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Organism-specific databases

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

    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 – 4581Phosphoserine6 Publications
    Modified residuei510 – 5101Phosphoserine2 Publications
    Modified residuei514 – 5141Phosphoserine1 Publication

    Post-translational modificationi

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

    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. 66 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 – 63
    Beta strandi25 – 317
    Beta strandi37 – 426
    Beta strandi45 – 506
    Helixi51 – 533
    Beta strandi54 – 563
    Beta strandi112 – 1154
    Beta strandi134 – 1429
    Beta strandi145 – 1506
    Beta strandi153 – 1586
    Helixi159 – 1613
    Beta strandi162 – 1643
    Helixi489 – 4924
    Helixi503 – 5053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP    50
    DNFVKEIKRE TEFKDDSLPI KRERHGNVAS LVQRISTYGL PAGGIQPHPQ 100
    TKNIKKKTKK RQCKVLFEYI PQNEDELELK VGDIIDINEE VEEGWWSGTL 150
    NNKLGLFPSN FVKELEVTDD GETHEAQDDS ETVLAGPTSP IPSLGNVSET 200
    ASGSVTQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK PEKPLILQSL 250
    GPKTQSVEIT KTDTEGKIKA KEYCRTLFAY EGTNEDELTF KEGEIIHLIS 300
    KETGEAGWWR GELNGKEGVF PDNFAVQINE LDKDFPKPKK PPPPAKAPAP 350
    KPELIAAEKK YFSLKPEEKD EKSTLEQKPS KPAAPQVPPK KPTPPTKASN 400
    LLRSSGTVYP KRPEKPVPPP PPIAKINGEV SSISSKFETE PVSKLKLDSE 450
    QLPLRPKSVD FDSLTVRTSK ETDVVNFDDI ASSENLLHLT ANRPKMPGRR 500
    LPGRFNGGHS PTHSPEKILK LPKEEDSANL KPSELKKDTC YSPKPSVYLS 550
    TPSSASKANT TAFLTPLEIK AKVETDDVKK NSLDELRAQI IELLCIVEAL 600
    KKDHGKELEK LRKDLEEEKT MRSNLEMEIE KLKKAVLSS 639
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi30172980.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS34472.1.
    PIRi T13151.
    RefSeqi NP_036252.1. NM_012120.2.
    UniGenei Hs.485518.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q9Y5K6.
    SMRi Q9Y5K6. Positions 2-329, 475-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117140. 66 interactions.
    DIPi DIP-31807N.
    IntActi Q9Y5K6. 30 interactions.
    MINTi MINT-93491.
    STRINGi 9606.ENSP00000352264.

    PTM databases

    PhosphoSitei Q9Y5K6.

    Polymorphism databases

    DMDMi 30172980.

    Proteomic databases

    MaxQBi Q9Y5K6.
    PaxDbi Q9Y5K6.
    PRIDEi Q9Y5K6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359314 ; ENSP00000352264 ; ENSG00000198087 .
    GeneIDi 23607.
    KEGGi hsa:23607.
    UCSCi uc003oyw.3. human.

    Organism-specific databases

    CTDi 23607.
    GeneCardsi GC06P047445.
    HGNCi HGNC:14258. CD2AP.
    HPAi CAB004352.
    HPA003267.
    HPA003326.
    MIMi 604241. gene.
    607832. phenotype.
    neXtProti NX_Q9Y5K6.
    Orphaneti 93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
    PharmGKBi PA26208.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319250.
    HOGENOMi HOG000231405.
    HOVERGENi HBG057824.
    InParanoidi Q9Y5K6.
    KOi K13738.
    OMAi VHDDELT.
    OrthoDBi EOG7W41BC.
    PhylomeDBi Q9Y5K6.
    TreeFami TF350191.

    Enzyme and pathway databases

    Reactomei REACT_23832. Nephrin interactions.
    SignaLinki Q9Y5K6.

    Miscellaneous databases

    ChiTaRSi CD2AP. human.
    EvolutionaryTracei Q9Y5K6.
    GeneWikii CD2AP.
    GenomeRNAii 23607.
    NextBioi 46304.
    PROi Q9Y5K6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y5K6.
    CleanExi HS_CD2AP.
    Genevestigatori Q9Y5K6.

    Family and domain databases

    InterProi IPR028445. CD2AP.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR14167:SF23. PTHR14167:SF23. 1 hit.
    Pfami PF00018. SH3_1. 1 hit.
    PF14604. SH3_9. 2 hits.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 3 hits.
    PROSITEi PS50002. SH3. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.

    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: October 1, 2014
    This is version 135 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