Q60598 · SRC8_MOUSE
- ProteinSrc substrate cortactin
- GeneCttn
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids546 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:17403031).
Plays a role in the formation of lamellipodia and in cell migration (By similarity).
Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity).
Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (PubMed:22262902).
Plays a role in focal adhesion assembly and turnover (By similarity).
In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity).
Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782).
Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity).
Required for stabilization of KCNH1 channels at the cell membrane (By similarity).
Plays a role in the formation of lamellipodia and in cell migration (By similarity).
Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity).
Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (PubMed:22262902).
Plays a role in focal adhesion assembly and turnover (By similarity).
In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity).
Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (PubMed:17959782).
Plays a role in receptor-mediated endocytosis via clathrin-coated pits (By similarity).
Required for stabilization of KCNH1 channels at the cell membrane (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 nameSrc substrate cortactin
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60598
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity).
Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft. Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity).
Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft. Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 22 | Abolishes cortactin-mediated endocytosis of KCNA2. | ||||
Sequence: W → A | ||||||
Mutagenesis | 421 | No effect on interaction with KCNA2. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 466 | No effect on interaction with KCNA2, but decreases KCNA2 levels at the cell membrane. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 482 | No effect on interaction with KCNA2, but decreases KCNA2 levels at the cell membrane. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000072190 | 1-546 | Src substrate cortactin | |||
Sequence: MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQTPPASPSPQPIEDRPPSSPIYEDAAPFKAEPSYRGSEPEPEYSIEAAGIPEAGSQQGLTYTSEPVYETTEAPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ | ||||||
Modified residue | 87 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 107 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 113 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 119 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 124 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 144 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 144 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 144 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 150 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 152 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 161 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 171 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 181 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 181 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 181 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 193 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 198 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 218 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | ||||||
Modified residue | 235 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 261 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 272 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 295 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 295 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 304 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 309 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 314 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 346 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 401 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 405 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 407 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 417 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 418 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 421 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 442 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 443 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 466 | Phosphotyrosine; by FAK1 | ||||
Sequence: Y | ||||||
Modified residue | 482 | Phosphotyrosine; by SRC | ||||
Sequence: Y | ||||||
Modified residue | 485 | Phosphotyrosine; by SRC | ||||
Sequence: Y |
Post-translational modification
Acetylated.
Phosphorylated by FER. Phosphorylated in response to FGR activation (PubMed:7693700).
Phosphorylation by SRC promotes MYLK binding (By similarity).
Phosphorylated on tyrosine residues in response to CHRM1 activation (By similarity).
Phosphorylated by PTK2/FAK1 in response to cell adhesion (By similarity).
Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated by PKN2 at both serine and threonine residues in a GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence down-regulated CTTN ability to associate with filamentous actin
Phosphorylation by SRC promotes MYLK binding (By similarity).
Phosphorylated on tyrosine residues in response to CHRM1 activation (By similarity).
Phosphorylated by PTK2/FAK1 in response to cell adhesion (By similarity).
Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated by PKN2 at both serine and threonine residues in a GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence down-regulated CTTN ability to associate with filamentous actin
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Part of a complex composed of NEDD9, AURKA and CTTN; within the complex NEDD9 acts as a scaffold protein and is required for complex formation (By similarity).
Interacts (via N-terminus) with NEDD9 (PubMed:24574519).
Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Forms a complex with ABL1 and MYLK (By similarity).
Interacts with SHANK2 and SHANK3 (via its SH3 domain). Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts (via SH3 domain) with DNM2. Interacts with ACTN1 (By similarity).
Interacts with FER. Interacts with KCNA2 (via non-phosphorylated C-terminus). Interacts with FGD1. Interacts with ABL2 (PubMed:22297987).
Interacts with CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts with CTTNBP2; this interaction may target CTTN at the cell cortex or dendritic spines. Interacts with KCNH1 (By similarity).
Interacts (via SH3 domain) with DIP2A (via N-terminus); the interaction enhances CTTN acetylation and is required for proper synaptic transmission (PubMed:31600191).
Interacts with XIRP1 (via N-terminus); the interaction promotes CTTN localization to intercalated disks in cardiomyocytes (PubMed:23296090).
Interacts (via N-terminus) with NEDD9 (PubMed:24574519).
Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Forms a complex with ABL1 and MYLK (By similarity).
Interacts with SHANK2 and SHANK3 (via its SH3 domain). Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts (via SH3 domain) with DNM2. Interacts with ACTN1 (By similarity).
Interacts with FER. Interacts with KCNA2 (via non-phosphorylated C-terminus). Interacts with FGD1. Interacts with ABL2 (PubMed:22297987).
Interacts with CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts with CTTNBP2; this interaction may target CTTN at the cell cortex or dendritic spines. Interacts with KCNH1 (By similarity).
Interacts (via SH3 domain) with DIP2A (via N-terminus); the interaction enhances CTTN acetylation and is required for proper synaptic transmission (PubMed:31600191).
Interacts with XIRP1 (via N-terminus); the interaction promotes CTTN localization to intercalated disks in cardiomyocytes (PubMed:23296090).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, coiled coil, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Disordered | ||||
Sequence: MWKASAGHAVSITQDDGGADDWETDPDF | ||||||
Repeat | 80-116 | Cortactin 1 | ||||
Sequence: ASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVD | ||||||
Repeat | 117-153 | Cortactin 2 | ||||
Sequence: SVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKD | ||||||
Repeat | 154-190 | Cortactin 3 | ||||
Sequence: YSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKD | ||||||
Repeat | 191-227 | Cortactin 4 | ||||
Sequence: YSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKD | ||||||
Repeat | 228-264 | Cortactin 5 | ||||
Sequence: YVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKD | ||||||
Repeat | 265-301 | Cortactin 6 | ||||
Sequence: YKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQD | ||||||
Repeat | 302-324 | Cortactin 7; truncated | ||||
Sequence: YAKGFGGKYGVQKDRMDKNASTF | ||||||
Coiled coil | 348-401 | |||||
Sequence: SNIRANFENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQT | ||||||
Compositional bias | 355-397 | Basic and acidic residues | ||||
Sequence: ENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARA | ||||||
Region | 355-424 | Disordered | ||||
Sequence: ENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQTPPASPSPQPIEDRPPSSPIYEDA | ||||||
Domain | 488-546 | SH3 | ||||
Sequence: DLGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ |
Domain
The SH3 motif may mediate binding to the cytoskeleton.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length546
- Mass (Da)61,250
- Last updated2011-07-27 v2
- Checksum8F5CA026ACCD6D4F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q921L6 | Q921L6_MOUSE | Cttn | 509 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 9 | in Ref. 2; AA sequence | ||||
Sequence: A → R | ||||||
Sequence conflict | 298 | in Ref. 1; AAA19689 | ||||
Sequence: S → P | ||||||
Compositional bias | 355-397 | Basic and acidic residues | ||||
Sequence: ENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U03184 EMBL· GenBank· DDBJ | AAA19689.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146856 EMBL· GenBank· DDBJ | BAE27485.1 EMBL· GenBank· DDBJ | mRNA | ||
AK148010 EMBL· GenBank· DDBJ | BAE28287.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168699 EMBL· GenBank· DDBJ | BAE40543.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466531 EMBL· GenBank· DDBJ | EDL18251.1 EMBL· GenBank· DDBJ | Genomic DNA |