Q9JLQ0 · CD2AP_MOUSE
- ProteinCD2-associated protein
- GeneCd2ap
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids637 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (By similarity).
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 (By similarity).
May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (PubMed:9741631).
May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus (PubMed:10514378).
Also required for cytokinesis. Plays a role in epithelial cell junctions formation (By similarity).
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 (By similarity).
May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (PubMed:9741631).
May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus (PubMed:10514378).
Also required for cytokinesis. Plays a role in epithelial cell junctions formation (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCD2-associated protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9JLQ0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (By similarity).
Located at podocyte slit diaphragm between podocyte foot processes (PubMed:10514378, PubMed:11733379).
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 (PubMed:10514378, PubMed:11733379).
During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
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.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000089436 | 1-637 | CD2-associated protein | |||
Sequence: MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEPKDDNLPIKRERQGNVASLVQRISTYGLPAGGIQPHPQTKAIKKKTKKRQCKVLFDYSPQNEDELELIVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELESTEDGETHNAQEESEVPLTGPTSPLPSPGNGSEPAPGSVAQPKKIRGIGFGDIFKEGSVKLRTRTSSSETEEKKTEKPLILQPLGSRTQNVEVTKPDVDGKIKAKEYCRTLFPYTGTNEDELTFREGEIIHLISKETGEAGWWKGELNGKEGVFPDNFAVQISELDKDFPKPKKPPPPAKGPAPKPDLSAAEKKAFPLKAEEKDEKSLLEQKPSKPAAPQVPPKKPTAPTKASNLLRSPGAVYPKRPEKPVPPPPPAAKINGEVSIISSKIDTEPVSKPKLDPEQLPVRPKSVDLDAFVARNSKETDDVNFDDIASSENLLHLTANRPKMPGRRLPGRFNGGHSPTQSPEKTLKLPKEDDSGNLKPLEFKKDASYSSKSSLSTPSSASKVNTAAFLTPLELKAKAEADDGKRNSVDELRAQIIELLCIVDALKKDHGKELEKLRKELEEEKAMRSNLEVEIAKLKKAVLLS | ||||||
Cross-link | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 80 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 86 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 224 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 458 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 469 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 510 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 514 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 523 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 563 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 580 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in podocytes (at protein level).
Gene expression databases
Interaction
Subunit
Homodimer. 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. Interacts with CGNL1 and SH3BP1; probably part of a complex at cell junctions. Interacts with CAPZA1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9JLQ0 | Cbl P22682 | 5 | EBI-644807, EBI-640919 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-59 | SH3 1; truncated | ||||
Sequence: MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKR | ||||||
Region | 1-175 | Interaction with ANLN and localization to the midbody | ||||
Sequence: MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEPKDDNLPIKRERQGNVASLVQRISTYGLPAGGIQPHPQTKAIKKKTKKRQCKVLFDYSPQNEDELELIVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELESTEDGETHN | ||||||
Domain | 108-167 | SH3 2 | ||||
Sequence: TKKRQCKVLFDYSPQNEDELELIVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELES | ||||||
Region | 166-209 | Disordered | ||||
Sequence: ESTEDGETHNAQEESEVPLTGPTSPLPSPGNGSEPAPGSVAQPK | ||||||
Region | 226-254 | Disordered | ||||
Sequence: KLRTRTSSSETEEKKTEKPLILQPLGSRT | ||||||
Domain | 269-330 | SH3 3 | ||||
Sequence: KAKEYCRTLFPYTGTNEDELTFREGEIIHLISKETGEAGWWKGELNGKEGVFPDNFAVQISE | ||||||
Region | 333-455 | Disordered | ||||
Sequence: KDFPKPKKPPPPAKGPAPKPDLSAAEKKAFPLKAEEKDEKSLLEQKPSKPAAPQVPPKKPTAPTKASNLLRSPGAVYPKRPEKPVPPPPPAAKINGEVSIISSKIDTEPVSKPKLDPEQLPVR | ||||||
Motif | 336-352 | SH3-binding | ||||
Sequence: PKPKKPPPPAKGPAPKP | ||||||
Compositional bias | 358-377 | Basic and acidic residues | ||||
Sequence: EKKAFPLKAEEKDEKSLLEQ | ||||||
Motif | 378-397 | SH3-binding | ||||
Sequence: KPSKPAAPQVPPKKPTAPTK | ||||||
Motif | 410-422 | SH3-binding | ||||
Sequence: PKRPEKPVPPPPP | ||||||
Compositional bias | 411-425 | Pro residues | ||||
Sequence: KRPEKPVPPPPPAAK | ||||||
Compositional bias | 441-455 | Basic and acidic residues | ||||
Sequence: PVSKPKLDPEQLPVR | ||||||
Region | 488-555 | Disordered | ||||
Sequence: HLTANRPKMPGRRLPGRFNGGHSPTQSPEKTLKLPKEDDSGNLKPLEFKKDASYSSKSSLSTPSSASK | ||||||
Compositional bias | 518-533 | Basic and acidic residues | ||||
Sequence: TLKLPKEDDSGNLKPL | ||||||
Compositional bias | 539-555 | Polar residues | ||||
Sequence: ASYSSKSSLSTPSSASK | ||||||
Coiled coil | 578-636 | |||||
Sequence: RNSVDELRAQIIELLCIVDALKKDHGKELEKLRKELEEEKAMRSNLEVEIAKLKKAVLL |
Domain
Potential homodimerization is mediated by the coiled coil domain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length637
- Mass (Da)70,450
- Last updated2011-07-27 v3
- Checksum0B618FE82AF12332
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3B2W812 | A0A3B2W812_MOUSE | Cd2ap | 532 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 78 | in Ref. 2; AAF73150 | ||||
Sequence: V → E | ||||||
Sequence conflict | 107 | in Ref. 1; AAC36099 | ||||
Sequence: Missing | ||||||
Sequence conflict | 110 | in Ref. 1; AAC36099 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 244 | in Ref. 1; AAC36099 | ||||
Sequence: P → R | ||||||
Sequence conflict | 295-297 | in Ref. 1; AAC36099 | ||||
Sequence: IIH → LS | ||||||
Compositional bias | 358-377 | Basic and acidic residues | ||||
Sequence: EKKAFPLKAEEKDEKSLLEQ | ||||||
Sequence conflict | 392 | in Ref. 1; AAC36099 | ||||
Sequence: P → PTAPTKA | ||||||
Compositional bias | 411-425 | Pro residues | ||||
Sequence: KRPEKPVPPPPPAAK | ||||||
Compositional bias | 441-455 | Basic and acidic residues | ||||
Sequence: PVSKPKLDPEQLPVR | ||||||
Compositional bias | 518-533 | Basic and acidic residues | ||||
Sequence: TLKLPKEDDSGNLKPL | ||||||
Compositional bias | 539-555 | Polar residues | ||||
Sequence: ASYSSKSSLSTPSSASK | ||||||
Sequence conflict | 545 | in Ref. 2; AAF73150, 3; CAD30510 and 5; AAH19744 | ||||
Sequence: S → P | ||||||
Sequence conflict | 578 | in Ref. 2; AAF73150, 3; CAD30510 and 5; AAH19744 | ||||
Sequence: R → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF077003 EMBL· GenBank· DDBJ | AAC36099.1 EMBL· GenBank· DDBJ | mRNA | ||
AF149092 EMBL· GenBank· DDBJ | AAF73150.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ459109 EMBL· GenBank· DDBJ | CAD30510.1 EMBL· GenBank· DDBJ | mRNA | ||
AC111082 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC019744 EMBL· GenBank· DDBJ | AAH19744.1 EMBL· GenBank· DDBJ | mRNA |