Details for: CD2AP

Gene ID: 23607

Symbol: CD2AP

Ensembl ID: ENSG00000198087

Description: CD2 associated protein

Associated with

Other Information

Genular Protein ID: 3756096852

Symbol: CD2AP_HUMAN

Name: CD2-associated protein

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10339567

Title: CMS: an adapter molecule involved in cytoskeletal rearrangements.

PubMed ID: 10339567

DOI: 10.1073/pnas.96.11.6211

PubMed ID: 14574404

Title: The DNA sequence and analysis of human chromosome 6.

PubMed ID: 14574404

DOI: 10.1038/nature02055

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 11067845

Title: The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction.

PubMed ID: 11067845

DOI: 10.1074/jbc.m005784200

PubMed ID: 12764198

Title: CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility.

PubMed ID: 12764198

DOI: 10.1126/science.1081068

PubMed ID: 15800069

Title: Clues to CD2-associated protein involvement in cytokinesis.

PubMed ID: 15800069

DOI: 10.1091/mbc.e04-09-0773

PubMed ID: 16678097

Title: A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells.

PubMed ID: 16678097

DOI: 10.1016/j.cell.2006.02.045

PubMed ID: 16895919

Title: CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP.

PubMed ID: 16895919

DOI: 10.1074/jbc.m605693200

PubMed ID: 17853893

Title: Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis.

PubMed ID: 17853893

DOI: 10.1038/sj.emboj.7601850

PubMed ID: 18753381

Title: CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation of ret signal transduction.

PubMed ID: 18753381

DOI: 10.1523/jneurosci.2738-08.2008

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22891260

Title: Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex.

PubMed ID: 22891260

DOI: 10.1083/jcb.201202094

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 31493651

Title: Structural characterization and biological function of bivalent binding of CD2AP to intrinsically disordered domain of chikungunya virus nsP3 protein.

PubMed ID: 31493651

DOI: 10.1016/j.virol.2019.08.022

PubMed ID: 17020880

Title: Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain.

PubMed ID: 17020880

DOI: 10.1074/jbc.m606411200

PubMed ID: 17188587

Title: Solution structure of the second SH3 domain of human CMS and a newly identified binding site at the C-terminus of c-Cbl.

PubMed ID: 17188587

DOI: 10.1016/j.bbapap.2006.09.018

PubMed ID: 23595123

Title: A molecular genetic analysis of childhood nephrotic syndrome in a cohort of Saudi Arabian families.

PubMed ID: 23595123

DOI: 10.1038/jhg.2013.27

Sequence Information:

  • Length: 639
  • Mass: 71451
  • Checksum: 7576509C7ED5B343
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.