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Q9JLQ0

- CD2AP_MOUSE

UniProt

Q9JLQ0 - CD2AP_MOUSE

Protein

CD2-associated protein

Gene

Cd2ap

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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: MGI

    GO - Biological processi

    1. cell migration Source: Ensembl
    2. mitotic nuclear division Source: UniProtKB-KW
    3. negative regulation of transforming growth factor beta1 production Source: MGI
    4. positive regulation of protein localization to nucleus Source: MGI
    5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    6. regulation of actin cytoskeleton reorganization Source: MGI
    7. regulation of receptor-mediated endocytosis Source: Ensembl
    8. single organismal cell-cell adhesion Source: Ensembl
    9. vesicle organization Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CD2-associated protein
    Alternative name(s):
    Mesenchyme-to-epithelium transition protein with SH3 domains 1
    Short name:
    METS-1
    Gene namesi
    Name:Cd2ap
    Synonyms:Mets1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1330281. Cd2ap.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionruffle
    Note: During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase By similarity. Located at podocyte slit diaphragm between podocyte foot processes.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cell cortex Source: MGI
    3. cytoplasm Source: MGI
    4. cytosol Source: Reactome
    5. endocytic vesicle Source: Ensembl
    6. filamentous actin Source: Ensembl
    7. nucleolus Source: Ensembl
    8. perinuclear region of cytoplasm Source: Ensembl
    9. plasma membrane Source: MGI
    10. ruffle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Disruption phenotypei

    Death at 6 to 7 weeks of age from renal failure. Mice show defects in epithelial foot processes, accompanied by mesangial cell hyperplasia and extracellular matrix deposition.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 637637CD2-associated proteinPRO_0000089436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei224 – 2241PhosphoserineBy similarity
    Modified residuei458 – 4581Phosphoserine1 Publication
    Modified residuei510 – 5101PhosphoserineBy similarity
    Modified residuei514 – 5141PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9JLQ0.
    PaxDbiQ9JLQ0.
    PRIDEiQ9JLQ0.

    PTM databases

    PhosphoSiteiQ9JLQ0.

    Expressioni

    Tissue specificityi

    Expressed in podocytes (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9JLQ0.
    CleanExiMM_CD2AP.
    GenevestigatoriQ9JLQ0.

    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

    Protein-protein interaction databases

    BioGridi198584. 19 interactions.
    IntActiQ9JLQ0. 20 interactions.
    MINTiMINT-255809.
    STRINGi10090.ENSMUSP00000024709.

    Structurei

    Secondary structure

    1
    637
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Beta strandi8 – 103
    Beta strandi14 – 174
    Beta strandi25 – 317
    Beta strandi37 – 426
    Beta strandi45 – 506
    Helixi51 – 533
    Beta strandi54 – 563
    Beta strandi113 – 1153
    Beta strandi134 – 1429
    Beta strandi145 – 1506
    Beta strandi153 – 1586
    Turni159 – 1613
    Beta strandi270 – 2789
    Beta strandi283 – 2875
    Beta strandi295 – 3017
    Beta strandi303 – 31311
    Beta strandi316 – 3216
    Helixi322 – 3243
    Beta strandi325 – 3295

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JTENMR-A270-329[»]
    2KRMNMR-A2-58[»]
    2KRNNMR-A111-166[»]
    2KRONMR-A270-329[»]
    2LZ6NMR-B270-329[»]
    2MCNNMR-A2-58[»]
    ProteinModelPortaliQ9JLQ0.
    SMRiQ9JLQ0. Positions 2-329, 475-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9JLQ0.

    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 midbodyBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili578 – 63659Sequence 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

    Potential homodimerization is mediated by the coiled coil domain.By similarity

    Sequence similaritiesi

    Contains 3 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3 domain, SH3-binding

    Phylogenomic databases

    eggNOGiNOG319250.
    GeneTreeiENSGT00530000063594.
    HOGENOMiHOG000231405.
    HOVERGENiHBG057824.
    InParanoidiQ9JLQ0.
    KOiK13738.
    OMAiVHDDELT.
    OrthoDBiEOG7W41BC.
    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.

    Q9JLQ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP    50
    DNFVKEIKRE TEPKDDNLPI KRERQGNVAS LVQRISTYGL PAGGIQPHPQ 100
    TKAIKKKTKK RQCKVLFDYS PQNEDELELI VGDVIDVIEE VEEGWWSGTL 150
    NNKLGLFPSN FVKELESTED GETHNAQEES EVPLTGPTSP LPSPGNGSEP 200
    APGSVAQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK TEKPLILQPL 250
    GSRTQNVEVT KPDVDGKIKA KEYCRTLFPY TGTNEDELTF REGEIIHLIS 300
    KETGEAGWWK GELNGKEGVF PDNFAVQISE LDKDFPKPKK PPPPAKGPAP 350
    KPDLSAAEKK AFPLKAEEKD EKSLLEQKPS KPAAPQVPPK KPTAPTKASN 400
    LLRSPGAVYP KRPEKPVPPP PPAAKINGEV SIISSKIDTE PVSKPKLDPE 450
    QLPVRPKSVD LDAFVARNSK ETDDVNFDDI ASSENLLHLT ANRPKMPGRR 500
    LPGRFNGGHS PTQSPEKTLK LPKEDDSGNL KPLEFKKDAS YSSKSSLSTP 550
    SSASKVNTAA FLTPLELKAK AEADDGKRNS VDELRAQIIE LLCIVDALKK 600
    DHGKELEKLR KELEEEKAMR SNLEVEIAKL KKAVLLS 637
    Length:637
    Mass (Da):70,450
    Last modified:July 27, 2011 - v3
    Checksum:i0B618FE82AF12332
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781V → E in AAF73150. (PubMed:10913159)Curated
    Sequence conflicti107 – 1071Missing in AAC36099. (PubMed:9741631)Curated
    Sequence conflicti110 – 1101K → Q in AAC36099. (PubMed:9741631)Curated
    Sequence conflicti244 – 2441P → R in AAC36099. (PubMed:9741631)Curated
    Sequence conflicti295 – 2973IIH → LS in AAC36099. (PubMed:9741631)Curated
    Sequence conflicti392 – 3921P → PTAPTKA in AAC36099. (PubMed:9741631)Curated
    Sequence conflicti545 – 5451S → P in AAF73150. (PubMed:10913159)Curated
    Sequence conflicti545 – 5451S → P in CAD30510. 1 PublicationCurated
    Sequence conflicti545 – 5451S → P in AAH19744. (PubMed:15489334)Curated
    Sequence conflicti578 – 5781R → K in AAF73150. (PubMed:10913159)Curated
    Sequence conflicti578 – 5781R → K in CAD30510. 1 PublicationCurated
    Sequence conflicti578 – 5781R → K in AAH19744. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077003 mRNA. Translation: AAC36099.1.
    AF149092 mRNA. Translation: AAF73150.1.
    AJ459109 mRNA. Translation: CAD30510.1.
    AC111082 Genomic DNA. No translation available.
    BC019744 mRNA. Translation: AAH19744.1.
    CCDSiCCDS50114.1.
    RefSeqiNP_033977.3. NM_009847.3.
    UniGeneiMm.218637.

    Genome annotation databases

    EnsembliENSMUST00000024709; ENSMUSP00000024709; ENSMUSG00000061665.
    GeneIDi12488.
    KEGGimmu:12488.
    UCSCiuc008cot.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077003 mRNA. Translation: AAC36099.1 .
    AF149092 mRNA. Translation: AAF73150.1 .
    AJ459109 mRNA. Translation: CAD30510.1 .
    AC111082 Genomic DNA. No translation available.
    BC019744 mRNA. Translation: AAH19744.1 .
    CCDSi CCDS50114.1.
    RefSeqi NP_033977.3. NM_009847.3.
    UniGenei Mm.218637.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JTE NMR - A 270-329 [» ]
    2KRM NMR - A 2-58 [» ]
    2KRN NMR - A 111-166 [» ]
    2KRO NMR - A 270-329 [» ]
    2LZ6 NMR - B 270-329 [» ]
    2MCN NMR - A 2-58 [» ]
    ProteinModelPortali Q9JLQ0.
    SMRi Q9JLQ0. Positions 2-329, 475-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198584. 19 interactions.
    IntActi Q9JLQ0. 20 interactions.
    MINTi MINT-255809.
    STRINGi 10090.ENSMUSP00000024709.

    PTM databases

    PhosphoSitei Q9JLQ0.

    Proteomic databases

    MaxQBi Q9JLQ0.
    PaxDbi Q9JLQ0.
    PRIDEi Q9JLQ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024709 ; ENSMUSP00000024709 ; ENSMUSG00000061665 .
    GeneIDi 12488.
    KEGGi mmu:12488.
    UCSCi uc008cot.1. mouse.

    Organism-specific databases

    CTDi 23607.
    MGIi MGI:1330281. Cd2ap.

    Phylogenomic databases

    eggNOGi NOG319250.
    GeneTreei ENSGT00530000063594.
    HOGENOMi HOG000231405.
    HOVERGENi HBG057824.
    InParanoidi Q9JLQ0.
    KOi K13738.
    OMAi VHDDELT.
    OrthoDBi EOG7W41BC.
    TreeFami TF350191.

    Miscellaneous databases

    ChiTaRSi CD2AP. mouse.
    EvolutionaryTracei Q9JLQ0.
    NextBioi 281400.
    PROi Q9JLQ0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JLQ0.
    CleanExi MM_CD2AP.
    Genevestigatori Q9JLQ0.

    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. "A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts."
      Dustin M.L., Olszowy M.W., Holdorf A.D., Li J., Bromley S., Desai N., Widder P., Rosenberger F., van der Merwe P.A., Allen P.M., Shaw A.S.
      Cell 94:667-677(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CD2.
    2. "In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2."
      Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S., Lehtonen E.
      J. Biol. Chem. 275:32888-32893(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PKD2.
    3. "Role of the interaction between CD2AP and c-Cbl."
      Meton I., Le Marchand-Brustel Y., Cormont M.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 394-637.
      Tissue: Mammary tumor.
    6. "Congenital nephrotic syndrome in mice lacking CD2-associated protein."
      Shih N.Y., Li J., Karpitskii V., Nguyen A., Dustin M.L., Kanagawa O., Miner J.H., Shaw A.S.
      Science 286:312-315(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPHS1, DISRUPTION PHENOTYPE.
    7. "CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain."
      Shih N.Y., Li J., Cotran R., Mundel P., Miner J.H., Shaw A.S.
      Am. J. Pathol. 159:2303-2308(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NPHS1.
    8. "Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin."
      Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W., Shaw A.S., Holzman L.B., Mundel P.
      J. Clin. Invest. 108:1621-1629(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NPHS1 AND NPHS2.
    9. "CD2-associated protein directly interacts with the actin cytoskeleton."
      Lehtonen S., Zhao F., Lehtonen E.
      Am. J. Physiol. 283:F734-F743(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH F-ACTIN.
    10. Cited for: INTERACTION WITH WTIP.
    11. "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin promotes apoptosis of podocytes."
      Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.
      Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDN.
    12. "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, TISSUE SPECIFICITY.
    13. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: STRUCTURE BY NMR OF 270-329.

    Entry informationi

    Entry nameiCD2AP_MOUSE
    AccessioniPrimary (citable) accession number: Q9JLQ0
    Secondary accession number(s): E9QL86
    , O88903, Q8K4Z1, Q8VCI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3