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Protein

CD2-associated protein

Gene

Cd2ap

Organism
Mus musculus (Mouse)
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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-373753. Nephrin interactions.

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
Proteomesi
  • UP000000589 Componenti: 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

  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell cortex Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • endocytic vesicle Source: Ensembl
  • extracellular exosome Source: MGI
  • filamentous actin Source: MGI
  • nucleolus Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: MGI
  • ruffle Source: MGI
Complete GO annotation...

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000894361 – 637CD2-associated proteinAdd BLAST637

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei80PhosphoserineBy similarity1
Modified residuei86PhosphoserineBy similarity1
Modified residuei224PhosphoserineCombined sources1
Modified residuei458PhosphoserineCombined sources1
Modified residuei469PhosphoserineBy similarity1
Modified residuei510PhosphoserineCombined sources1
Modified residuei514PhosphoserineCombined sources1
Modified residuei563PhosphothreonineBy similarity1
Modified residuei580PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9JLQ0.
MaxQBiQ9JLQ0.
PaxDbiQ9JLQ0.
PeptideAtlasiQ9JLQ0.
PRIDEiQ9JLQ0.

PTM databases

iPTMnetiQ9JLQ0.
PhosphoSitePlusiQ9JLQ0.

Expressioni

Tissue specificityi

Expressed in podocytes (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000061665.
CleanExiMM_CD2AP.
GenevisibleiQ9JLQ0. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198584. 81 interactors.
IntActiQ9JLQ0. 82 interactors.
MINTiMINT-255809.
STRINGi10090.ENSMUSP00000024709.

Structurei

Secondary structure

1637
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi8 – 10Combined sources3
Beta strandi14 – 17Combined sources4
Beta strandi25 – 31Combined sources7
Beta strandi37 – 42Combined sources6
Beta strandi45 – 50Combined sources6
Helixi51 – 53Combined sources3
Beta strandi54 – 56Combined sources3
Beta strandi113 – 115Combined sources3
Beta strandi134 – 142Combined sources9
Beta strandi145 – 150Combined sources6
Beta strandi153 – 158Combined sources6
Turni159 – 161Combined sources3
Beta strandi270 – 278Combined sources9
Beta strandi283 – 287Combined sources5
Beta strandi295 – 301Combined sources7
Beta strandi303 – 313Combined sources11
Beta strandi316 – 321Combined sources6
Helixi322 – 324Combined sources3
Beta strandi325 – 329Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JTENMR-A270-329[»]
2KRMNMR-A2-58[»]
2KRNNMR-A111-166[»]
2KRONMR-A270-329[»]
2LZ6NMR-B270-329[»]
2MCNNMR-A2-62[»]
ProteinModelPortaliQ9JLQ0.
SMRiQ9JLQ0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLQ0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 59SH3 1; truncatedPROSITE-ProRule annotationAdd BLAST59
Domaini108 – 167SH3 2PROSITE-ProRule annotationAdd BLAST60
Domaini269 – 330SH3 3PROSITE-ProRule annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 175Interaction with ANLN and localization to the midbodyBy similarityAdd BLAST175

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili578 – 636Sequence analysisAdd BLAST59

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi336 – 352SH3-bindingSequence analysisAdd BLAST17
Motifi378 – 397SH3-bindingSequence analysisAdd BLAST20
Motifi410 – 422SH3-bindingSequence analysisAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi336 – 422Pro-richAdd BLAST87

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

eggNOGiKOG4348. Eukaryota.
ENOG410XQBY. LUCA.
GeneTreeiENSGT00530000063594.
HOGENOMiHOG000231405.
HOVERGENiHBG057824.
InParanoidiQ9JLQ0.
KOiK13738.
OMAiVHDDELT.
OrthoDBiEOG091G041Q.
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

        10         20         30         40         50
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP
60 70 80 90 100
DNFVKEIKRE TEPKDDNLPI KRERQGNVAS LVQRISTYGL PAGGIQPHPQ
110 120 130 140 150
TKAIKKKTKK RQCKVLFDYS PQNEDELELI VGDVIDVIEE VEEGWWSGTL
160 170 180 190 200
NNKLGLFPSN FVKELESTED GETHNAQEES EVPLTGPTSP LPSPGNGSEP
210 220 230 240 250
APGSVAQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK TEKPLILQPL
260 270 280 290 300
GSRTQNVEVT KPDVDGKIKA KEYCRTLFPY TGTNEDELTF REGEIIHLIS
310 320 330 340 350
KETGEAGWWK GELNGKEGVF PDNFAVQISE LDKDFPKPKK PPPPAKGPAP
360 370 380 390 400
KPDLSAAEKK AFPLKAEEKD EKSLLEQKPS KPAAPQVPPK KPTAPTKASN
410 420 430 440 450
LLRSPGAVYP KRPEKPVPPP PPAAKINGEV SIISSKIDTE PVSKPKLDPE
460 470 480 490 500
QLPVRPKSVD LDAFVARNSK ETDDVNFDDI ASSENLLHLT ANRPKMPGRR
510 520 530 540 550
LPGRFNGGHS PTQSPEKTLK LPKEDDSGNL KPLEFKKDAS YSSKSSLSTP
560 570 580 590 600
SSASKVNTAA FLTPLELKAK AEADDGKRNS VDELRAQIIE LLCIVDALKK
610 620 630
DHGKELEKLR KELEEEKAMR SNLEVEIAKL KKAVLLS
Length:637
Mass (Da):70,450
Last modified:July 27, 2011 - v3
Checksum:i0B618FE82AF12332
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78V → E in AAF73150 (PubMed:10913159).Curated1
Sequence conflicti107Missing in AAC36099 (PubMed:9741631).Curated1
Sequence conflicti110K → Q in AAC36099 (PubMed:9741631).Curated1
Sequence conflicti244P → R in AAC36099 (PubMed:9741631).Curated1
Sequence conflicti295 – 297IIH → LS in AAC36099 (PubMed:9741631).Curated3
Sequence conflicti392P → PTAPTKA in AAC36099 (PubMed:9741631).Curated1
Sequence conflicti545S → P in AAF73150 (PubMed:10913159).Curated1
Sequence conflicti545S → P in CAD30510 (Ref. 3) Curated1
Sequence conflicti545S → P in AAH19744 (PubMed:15489334).Curated1
Sequence conflicti578R → K in AAF73150 (PubMed:10913159).Curated1
Sequence conflicti578R → K in CAD30510 (Ref. 3) Curated1
Sequence conflicti578R → K in AAH19744 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JTENMR-A270-329[»]
2KRMNMR-A2-58[»]
2KRNNMR-A111-166[»]
2KRONMR-A270-329[»]
2LZ6NMR-B270-329[»]
2MCNNMR-A2-62[»]
ProteinModelPortaliQ9JLQ0.
SMRiQ9JLQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198584. 81 interactors.
IntActiQ9JLQ0. 82 interactors.
MINTiMINT-255809.
STRINGi10090.ENSMUSP00000024709.

PTM databases

iPTMnetiQ9JLQ0.
PhosphoSitePlusiQ9JLQ0.

Proteomic databases

EPDiQ9JLQ0.
MaxQBiQ9JLQ0.
PaxDbiQ9JLQ0.
PeptideAtlasiQ9JLQ0.
PRIDEiQ9JLQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23607.
MGIiMGI:1330281. Cd2ap.

Phylogenomic databases

eggNOGiKOG4348. Eukaryota.
ENOG410XQBY. LUCA.
GeneTreeiENSGT00530000063594.
HOGENOMiHOG000231405.
HOVERGENiHBG057824.
InParanoidiQ9JLQ0.
KOiK13738.
OMAiVHDDELT.
OrthoDBiEOG091G041Q.
TreeFamiTF350191.

Enzyme and pathway databases

ReactomeiR-MMU-373753. Nephrin interactions.

Miscellaneous databases

ChiTaRSiCd2ap. mouse.
EvolutionaryTraceiQ9JLQ0.
PROiQ9JLQ0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000061665.
CleanExiMM_CD2AP.
GenevisibleiQ9JLQ0. MM.

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...

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: November 2, 2016
This is version 141 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

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 one 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.