P22612 · KAPCG_HUMAN
- ProteincAMP-dependent protein kinase catalytic subunit gamma
- GenePRKACG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids351 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by cAMP.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cAMP-dependent protein kinase complex | |
Cellular Component | ciliary base | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | AMP-activated protein kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | cAMP-dependent protein kinase activity | |
Molecular Function | protein kinase A regulatory subunit binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | high-density lipoprotein particle assembly | |
Biological Process | male gonad development | |
Biological Process | protein kinase A signaling | |
Biological Process | renal water homeostasis | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namecAMP-dependent protein kinase catalytic subunit gamma
- EC number
- Short namesPKA C-gamma
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP22612
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Bleeding disorder, platelet-type, 19 (BDPLT19)
- Note
- DescriptionA disorder characterized by increased bleeding tendency due to platelet dysfunction. Clinical features include epistaxis, hematomas, bleeding after tooth extraction, and menorrhagia.
- See alsoMIM:616176
Natural variants in BDPLT19
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072672 | 74 | I>M | in BDPLT19; patient platelets show impaired activation; dbSNP:rs724159972 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_072672 | 74 | in BDPLT19; patient platelets show impaired activation; dbSNP:rs724159972 | |||
Sequence: I → M | ||||||
Natural variant | VAR_040595 | 251 | in dbSNP:rs56287972 | |||
Sequence: I → N | ||||||
Natural variant | VAR_033902 | 268 | in dbSNP:rs3730386 | |||
Sequence: H → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 471 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000086064 | 2-351 | UniProt | cAMP-dependent protein kinase catalytic subunit gamma | |||
Sequence: GNAPAKKDTEQEESVNEFLAKARGDFLYRWGNPAQNTASSDQFERLRTLGMGSFGRVMLVRHQETGGHYAMKILNKQKVVKMKQVEHILNEKRILQAIDFPFLVKLQFSFKDNSYLYLVMEYVPGGEMFSRLQRVGRFSEPHACFYAAQVVLAVQYLHSLDLIHRDLKPENLLIDQQGYLQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAVGFPPFYADQPIQIYEKIVSGRVRFPSKLSSDLKHLLRSLLQVDLTKRFGNLRNGVGDIKNHKWFATTSWIAIYEKKVEAPFIPKYTGPGDASNFDDYEEEELRISINEKCAKEFSEF | |||||||
Modified residue (large scale data) | 196 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 198 | UniProt | Phosphothreonine; by autocatalysis | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 339 | UniProt | Phosphoserine; by autocatalysis | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P22612 | APP P05067 | 3 | EBI-3907086, EBI-77613 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 44-298 | Protein kinase | ||||
Sequence: FERLRTLGMGSFGRVMLVRHQETGGHYAMKILNKQKVVKMKQVEHILNEKRILQAIDFPFLVKLQFSFKDNSYLYLVMEYVPGGEMFSRLQRVGRFSEPHACFYAAQVVLAVQYLHSLDLIHRDLKPENLLIDQQGYLQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAVGFPPFYADQPIQIYEKIVSGRVRFPSKLSSDLKHLLRSLLQVDLTKRFGNLRNGVGDIKNHKWF | ||||||
Domain | 299-351 | AGC-kinase C-terminal | ||||
Sequence: ATTSWIAIYEKKVEAPFIPKYTGPGDASNFDDYEEEELRISINEKCAKEFSEF |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length351
- Mass (Da)40,434
- Last updated2007-01-23 v3
- ChecksumE66BB4BFB8AF9B50
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 345 | in Ref. 5; AAH39888 | ||||
Sequence: A → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M34182 EMBL· GenBank· DDBJ | AAC41690.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AJ001597 EMBL· GenBank· DDBJ | CAA04863.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ667175 EMBL· GenBank· DDBJ | ABG25920.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL162730 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC039888 EMBL· GenBank· DDBJ | AAH39888.1 EMBL· GenBank· DDBJ | mRNA |