Q80UW5 · MRCKG_MOUSE
- ProteinSerine/threonine-protein kinase MRCK gamma
- GeneCdc42bpg
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1551 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation (By similarity).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
Maintained in an inactive, closed conformation by an interaction between the kinase domain and the negative autoregulatory C-terminal coiled-coil region. Agonist binding to the phorbol ester binding site disrupts this, releasing the kinase domain to allow N-terminus-mediated dimerization and kinase activation by transautophosphorylation (By similarity).
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell leading edge | |
Cellular Component | centriolar satellite | |
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | actin cytoskeleton organization | |
Biological Process | actomyosin structure organization | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase MRCK gamma
- EC number
- Alternative names
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 accessionQ80UW5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Concentrates at the leading edge of cells.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086398 | 1-1551 | Serine/threonine-protein kinase MRCK gamma | |||
Sequence: MEQRLRALEQLVRGEAGGSPGLDGLLDLLLGVHQELSSAPLRRERNVAQFLSWASPFVTKVKELRLQRDDFEILKVIGRGAFGEVAVVRQRGSGQIFAMKMLHKWEMLKRAETACFREERDVLVKGDSRWVTALHYAFQDEEYLYLVMDYYAGGDLLTLLSRFEDRLPPELAQFYLAEMVLAIHSLHQLGYVHRDVKPDNILLDMNGHIRLADFGSCLRLNNNGMVDSSVAVGTPDYISPEILQAMEEGKGHYGPQCDWWSLGVCAYELLFGETPFYAESLVETYGKIMNHEDHLQFPADVTDVPASAQDLIRQLLCRQEERLGRGGLDDFRKHPFFEGVDWERLATSTAPYIPELRGPMDTSNFDVDDDTLNRPETLPPSSHGAFSGHHLPFVGFTYTSGSPFDVQSSELMAAPEGTPHCVEQVKVELSHKCQEPLHGPLQPQELVRLQKEVQVLQEKLAETLRDSKASLSQTDGLHARSPAPNIQLQQEKDRLQQELTEAQAALRVQDAELCQAQNRQEEFLQRLWEAQEREAAAASQIQALNSQLEEAWVVRRELEGQVTTLSQEVTRLQGQCKQESSQAKTVHAAPETNGIGSPEGQSQEAQLRKEVAALREQLEHACSQGISVGKEEVLCRLQEENQRLSREQERLAGELELELQSKQRLEGERRETESNWEAQIADILSWVNDEKVSRGYLQALATKMAEELESLRNVGTQTLPTRPLDHQWKARRLQKMEASARLELQSALEAEIRAKQSLQEQLTQVQEAQRQAERRLQEAEKQSQALQQEVAELREELQARGPGDARPSTSLIPLLSFWNTEKDSAKDPGNSGEGPRSGAEAELRPEGRRSLRMGSVFPRVPAATTTPAEGPPAKPGSHTLRPRSFPSPTKCLRCTSLMLGLGRQGLGCDTCGYFCHSACASQAPPCPVPPELLRTALGVHPETGTGTAYEGFLSVPRPSGVRRGWQRVYAALSDSRLLLFDAPDPRGSLASGVLLQALDLRDPQFSATPVLAPDVIHAQSKDLPRIFRVTASQLTVPPTTCTVLLLAENEGERERWLQVLGELQRLLLDARPRPRPVYTLKEAYDNGLPLLPHALCAAVIDQERLALGTEEGLFVIHLHSNDIFQVGDCRRVQRLAVSSAAGLLAVLCGRGPSVRLFALDELESAEVAGAKIPESRGCQALVAGRILQARTPVLCVAVKRQVLCYQLGPGPGPWQRRIRELQAPAPVQSLGLLGDRLCVGAAGTFALYPLLNEAAPLALGTGLVAEELPASRGGLGEALGAVELSLSELLLLFATAGVYVDSAGRKSRSHELLWPAAPTGWGYTAPYLTVFSENALDVFDVRRAEWVQTVPLKKVRPLNPEGSLFLYGTEKVRLTYLRNPLAEKDEFDIPDLTDNSRRQLFRTKSKRRFFFRVSDELRQQQRREMLKDPFVRSKFISPPTNFNHLVHVGPTEGRPNTRDGTRAQEQKSRGARSSGPQRPHSFSEAFRRPVSTGSDGLPGETDPLVKRKPWTSLSSESVSCPQGSLSPAASLIQVSERPRSLPPDPESESSP | ||||||
Modified residue | 216 | Phosphoserine; by autocatalysis | ||||
Sequence: S | ||||||
Modified residue | 228 | Phosphoserine; by autocatalysis | ||||
Sequence: S | ||||||
Modified residue | 234 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 1481 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 71-337 | Protein kinase | ||||
Sequence: FEILKVIGRGAFGEVAVVRQRGSGQIFAMKMLHKWEMLKRAETACFREERDVLVKGDSRWVTALHYAFQDEEYLYLVMDYYAGGDLLTLLSRFEDRLPPELAQFYLAEMVLAIHSLHQLGYVHRDVKPDNILLDMNGHIRLADFGSCLRLNNNGMVDSSVAVGTPDYISPEILQAMEEGKGHYGPQCDWWSLGVCAYELLFGETPFYAESLVETYGKIMNHEDHLQFPADVTDVPASAQDLIRQLLCRQEERLGRGGLDDFRKHPFF | ||||||
Domain | 338-408 | AGC-kinase C-terminal | ||||
Sequence: EGVDWERLATSTAPYIPELRGPMDTSNFDVDDDTLNRPETLPPSSHGAFSGHHLPFVGFTYTSGSPFDVQS | ||||||
Coiled coil | 442-675 | |||||
Sequence: QPQELVRLQKEVQVLQEKLAETLRDSKASLSQTDGLHARSPAPNIQLQQEKDRLQQELTEAQAALRVQDAELCQAQNRQEEFLQRLWEAQEREAAAASQIQALNSQLEEAWVVRRELEGQVTTLSQEVTRLQGQCKQESSQAKTVHAAPETNGIGSPEGQSQEAQLRKEVAALREQLEHACSQGISVGKEEVLCRLQEENQRLSREQERLAGELELELQSKQRLEGERRETESN | ||||||
Region | 578-605 | Disordered | ||||
Sequence: QESSQAKTVHAAPETNGIGSPEGQSQEA | ||||||
Coiled coil | 729-801 | |||||
Sequence: KARRLQKMEASARLELQSALEAEIRAKQSLQEQLTQVQEAQRQAERRLQEAEKQSQALQQEVAELREELQARG | ||||||
Region | 820-886 | Disordered | ||||
Sequence: TEKDSAKDPGNSGEGPRSGAEAELRPEGRRSLRMGSVFPRVPAATTTPAEGPPAKPGSHTLRPRSFP | ||||||
Zinc finger | 877-926 | Phorbol-ester/DAG-type | ||||
Sequence: SHTLRPRSFPSPTKCLRCTSLMLGLGRQGLGCDTCGYFCHSACASQAPPC | ||||||
Domain | 946-1065 | PH | ||||
Sequence: GTAYEGFLSVPRPSGVRRGWQRVYAALSDSRLLLFDAPDPRGSLASGVLLQALDLRDPQFSATPVLAPDVIHAQSKDLPRIFRVTASQLTVPPTTCTVLLLAENEGERERWLQVLGELQR | ||||||
Domain | 1091-1365 | CNH | ||||
Sequence: LPHALCAAVIDQERLALGTEEGLFVIHLHSNDIFQVGDCRRVQRLAVSSAAGLLAVLCGRGPSVRLFALDELESAEVAGAKIPESRGCQALVAGRILQARTPVLCVAVKRQVLCYQLGPGPGPWQRRIRELQAPAPVQSLGLLGDRLCVGAAGTFALYPLLNEAAPLALGTGLVAEELPASRGGLGEALGAVELSLSELLLLFATAGVYVDSAGRKSRSHELLWPAAPTGWGYTAPYLTVFSENALDVFDVRRAEWVQTVPLKKVRPLNPEGSLF | ||||||
Domain | 1436-1449 | CRIB | ||||
Sequence: ISPPTNFNHLVHVG | ||||||
Region | 1441-1551 | Disordered | ||||
Sequence: NFNHLVHVGPTEGRPNTRDGTRAQEQKSRGARSSGPQRPHSFSEAFRRPVSTGSDGLPGETDPLVKRKPWTSLSSESVSCPQGSLSPAASLIQVSERPRSLPPDPESESSP | ||||||
Compositional bias | 1508-1533 | Polar residues | ||||
Sequence: KPWTSLSSESVSCPQGSLSPAASLIQ |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,551
- Mass (Da)172,147
- Last updated2005-11-08 v2
- Checksum74458CA5FEF6F8A7
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1065 | in Ref. 2; AAH46418 | ||||
Sequence: R → Q | ||||||
Compositional bias | 1508-1533 | Polar residues | ||||
Sequence: KPWTSLSSESVSCPQGSLSPAASLIQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC127556 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC046418 EMBL· GenBank· DDBJ | AAH46418.1 EMBL· GenBank· DDBJ | mRNA |