Cdc42bpb
entrez
113960
canonical
uniprot
Q7TT49
canonical
ensembl
ENSRNOG00000009675
resolver
ensembl
ENSRNOG00055029879
resolver
ensembl
ENSRNOG00060025767
resolver
ensembl
ENSRNOG00065024999
resolver
ensp
ENSRNOP00000036487
resolver
ensp
ENSRNOP00000108806
resolver
ensp
ENSRNOP00055042750
resolver
ensp
ENSRNOP00060037070
resolver
ensp
ENSRNOP00065035208
resolver
enst
ENSRNOT00000039059
resolver
enst
ENSRNOT00000157383
resolver
enst
ENSRNOT00055051813
resolver
enst
ENSRNOT00060044719
resolver
enst
ENSRNOT00065043009
resolver
genesymbol
Cdc42bpb
resolver
uniprot
A0ABK0LYP4
resolver
uniprot
O54875
resolver
uniprot_entry
A0ABK0LYP4_RAT
resolver
uniprot_entry
MRCKB_RAT
resolver
uniprot_sec
O54875
resolver
activity_regulation
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). Inhibited by chelerythrine chloride. {ECO:0000250, ECO:0000269|PubMed:21457715}.
uniprot
proteins
amino_acid_sequence
MSAKVRLKKLEQLLLDGPWRNESSLSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAKPFTQLVKDMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFDVDDDVLRNIEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSMIQSNTLTKDEDVQRDLENSLQIEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSTRALGNSNRDKEIKRLNEELERMKSKMADSNRLERQLEDTVTLRQEHEDSTQRLKGLEKQYRLARQEKEELHKQLVEASERLKSQTKELKDAHQQRKRALQEFSELNERMAELRSQKQKVSRQLRDKEEEMEVAMQKIDSMRQDIRKSEKSRKELEARLEDAVAEASKERKLREHSESFSKQMERELETLKVKQGGRGPGATLEHQQEISKIRSELEKKVLFYEEELVRREASHVLEVKNVKKEVHESESHQLALQKEVLMLKDKLEKSKRERHSEMEEAIGAMKDKYERERAMLFDENKKLTAENEKLCSFVDKLTAQNRQLEDELQDLASKKESVAHWEAQIAEIIQWVSDEKDARGYLQALASKMTEELETLRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVHEELRKVKDTSLAFESKLKESEAKNRELLEEMQSLKKRMEEKFRADTGLKLPDFQDPIFEYFNTAPLAHDLTFRTSSASDQETQASKLDLSPSVSVATSTEQQEDAARSQQRPSTVPLPNTQALAMAGPKPKAHQFSIKSFPSPTQCSHCTSLMVGLIRQGYACEVCAFSCHVSCKDSAPQVCPIPPEQSKRPLGVDVQRGIGTAYKGYVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVIASQVLDLRDDEFAVSSVLASDVIHATRRDIPCIFRVTASLLGSPSKTSSLLILTENENEKRKWVGILEGLQAILHKNRLRSQVVHVAQEAYDSSLPLIKTVLAAAIVDGDRIAVGLEEGLYVIELTRDVIVRAADCKKVYQIELAPKEKLILLLCGRNHHVHLYPWTSFDGAEASNFDIKLPETKGCQLIATGTLRKSSSTCLFVAVKRLVLCYEIQRTKPFHRKFNEIVAPGHVQWMAMFKDRLCVGYPSGFSLLSIQGDGQPLDLVNPADPSLAFLSQQSFDALCAVELKSEEYLLCFSHMGLYVDPQGRRSRTQELMWPAAPVACSCSSSHVTVYSEYGVDVFDVRTMEWVQTIGLRRIRPLNSDGSLNLLGCEPPRLIYFKNKFSGTVLNVPDTSDNSKKQMLRTRSKRRFVFKVPEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAAPTAQEEKQGPAPTGLPRQLPSRNKPYVSWPSSGGSEPGVPVPLRSMSDPDQDFDKEPDSDSTKHSTPSNSSNPSGPPSPNSPHRSQLPLEGLDQPACDA
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21240187, PubMed:21457715). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates PPP1R12A (PubMed:18854160). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). {ECO:0000250|UniProtKB:Q7TT50, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21240187, ECO:0000269|PubMed:21457715}.
uniprot
proteins
mass_dalton
194888
uniprot
proteins
mutagenesis
MUTAGEN 952; /note="F->Q: Abolishes interaction with TJP1; when associated with Q-954."; /evidence="ECO:0000269|PubMed:21240187"; MUTAGEN 954; /note="Y->Q: Abolishes interaction with TJP1; when associated with Q-952."; /evidence="ECO:0000269|PubMed:21240187"; MUTAGEN 964; /note="L->Q: Abolishes interaction with TJP1; when associated with Q-966."; /evidence="ECO:0000269|PubMed:21240187"; MUTAGEN 966; /note="F->Q: Abolishes interaction with TJP1; when associated with Q-964."; /evidence="ECO:0000269|PubMed:21240187
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspases upon apoptosis induction. {ECO:0000250|UniProtKB:Q9Y5S2}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
DMPK subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
18854160
uniprot
proteins
pubmed
21240187
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
25107909
uniprot
proteins
pubmed
9418861
uniprot
proteins
sequence_length
1713
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:21240187}; Peripheral membrane protein {ECO:0000269|PubMed:21240187}; Cytoplasmic side {ECO:0000269|PubMed:21240187}. Cell junction {ECO:0000269|PubMed:21240187}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q3UU96}. Note=Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity). Detected at the leading edge of migrating and wounded cells; this localization requires the presence of catalytically active CDC42 (PubMed:21240187). Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner (By similarity). {ECO:0000250|UniProtKB:O54874, ECO:0000250|UniProtKB:Q3UU96, ECO:0000269|PubMed:21240187}.
uniprot
proteins