P40123 · CAP2_HUMAN
- ProteinAdenylyl cyclase-associated protein 2
- GeneCAP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids477 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the regulation of actin polymerization.
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic density | |
Molecular Function | actin binding | |
Molecular Function | adenylate cyclase binding | |
Molecular Function | identical protein binding | |
Biological Process | actin filament organization | |
Biological Process | activation of adenylate cyclase activity | |
Biological Process | cAMP-mediated signaling | |
Biological Process | cell morphogenesis | |
Biological Process | establishment or maintenance of cell polarity | |
Biological Process | presynaptic actin cytoskeleton organization | |
Biological Process | signal transduction |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylyl cyclase-associated protein 2
- Short namesCAP 2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP40123
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cardiomyopathy, dilated, 2I (CMD2I)
- Note
- DescriptionA form of dilated cardiomyopathy, a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. CMD2I is an autosomal recessive, severe form characterized by onset in infancy or childhood.
- See alsoMIM:620462
Natural variants in CMD2I
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088860 | 316-477 | missing | in CMD2I; likely pathogenic |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_033717 | 311 | in dbSNP:rs34620829 | |||
Sequence: T → A | ||||||
Natural variant | VAR_033718 | 316 | in dbSNP:rs34206659 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_088860 | 316-477 | in CMD2I; likely pathogenic | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 502 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000205700 | 2-477 | UniProt | Adenylyl cyclase-associated protein 2 | |||
Sequence: ANMQGLVERLERAVSRLESLSAESHRPPGNCGEVNGVIAGVAPSVEAFDKLMDSMVAEFLKNSRILAGDVETHAEMVHSAFQAQRAFLLMASQYQQPHENDVAALLKPISEKIQEIQTFRERNRGSNMFNHLSAVSESIPALGWIAVSPKPGPYVKEMNDAATFYTNRVLKDYKHSDLRHVDWVKSYLNIWSELQAYIKEHHTTGLTWSKTGPVASTVSAFSVLSSGPGLPPPPPPLPPPGPPPLFENEGKKEESSPSRSALFAQLNQGEAITKGLRHVTDDQKTYKNPSLRAQGGQTQSPTKSHTPSPTSPKSYPSQKHAPVLELEGKKWRVEYQEDRNDLVISETELKQVAYIFKCEKSTIQIKGKVNSIIIDNCKKLGLVFDNVVGIVEVINSQDIQIQVMGRVPTISINKTEGCHIYLSEDALDCEIVSAKSSEMNILIPQDGDYREFPIPEQFKTAWDGSKLITEPAEIMA | |||||||
Modified residue (large scale data) | 257 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 301 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 309 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P40123 | ACTB P60709 | 9 | EBI-1051165, EBI-353944 | |
BINARY | P40123 | ACTG1 P63261 | 13 | EBI-1051165, EBI-351292 | |
BINARY | P40123 | ADO Q96SZ5 | 3 | EBI-1051165, EBI-11102284 | |
BINARY | P40123 | ALAS1 P13196 | 3 | EBI-1051165, EBI-3905054 | |
BINARY | P40123 | CAP2 P40123 | 4 | EBI-1051165, EBI-1051165 | |
BINARY | P40123 | CFL2 Q549N0 | 3 | EBI-1051165, EBI-10201319 | |
BINARY | P40123 | GRXCR1 A8MXD5 | 3 | EBI-1051165, EBI-5235612 | |
BINARY | P40123 | PS1TP5BP1 Q1KLZ0 | 3 | EBI-1051165, EBI-9978131 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 225-261 | Disordered | ||||
Sequence: LSSGPGLPPPPPPLPPPGPPPLFENEGKKEESSPSRS | ||||||
Compositional bias | 228-247 | Pro residues | ||||
Sequence: GPGLPPPPPPLPPPGPPPLF | ||||||
Region | 273-321 | Disordered | ||||
Sequence: ITKGLRHVTDDQKTYKNPSLRAQGGQTQSPTKSHTPSPTSPKSYPSQKH | ||||||
Compositional bias | 287-318 | Polar residues | ||||
Sequence: YKNPSLRAQGGQTQSPTKSHTPSPTSPKSYPS | ||||||
Domain | 317-455 | C-CAP/cofactor C-like | ||||
Sequence: PSQKHAPVLELEGKKWRVEYQEDRNDLVISETELKQVAYIFKCEKSTIQIKGKVNSIIIDNCKKLGLVFDNVVGIVEVINSQDIQIQVMGRVPTISINKTEGCHIYLSEDALDCEIVSAKSSEMNILIPQDGDYREFPI |
Sequence similarities
Belongs to the CAP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P40123-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length477
- Mass (Da)52,824
- Last updated1995-02-01 v1
- Checksum2FD3950C094F5AF7
P40123-2
- Name2
- Differences from canonical
- 149-212: Missing
P40123-3
- Name3
- Differences from canonical
- 75-334: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_055519 | 75-334 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_055520 | 149-212 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 228-247 | Pro residues | ||||
Sequence: GPGLPPPPPPLPPPGPPPLF | ||||||
Compositional bias | 287-318 | Polar residues | ||||
Sequence: YKNPSLRAQGGQTQSPTKSHTPSPTSPKSYPS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U02390 EMBL· GenBank· DDBJ | AAA20587.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457022 EMBL· GenBank· DDBJ | CAG33303.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294215 EMBL· GenBank· DDBJ | BAH11700.1 EMBL· GenBank· DDBJ | mRNA | ||
AL034372 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138824 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK293134 EMBL· GenBank· DDBJ | BAH11460.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312362 EMBL· GenBank· DDBJ | BAG35280.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471087 EMBL· GenBank· DDBJ | EAW55380.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008481 EMBL· GenBank· DDBJ | AAH08481.1 EMBL· GenBank· DDBJ | mRNA |