Cdc42bpb
entrez
217866
canonical
uniprot
Q7TT50
canonical
ensembl
ENSMUSG00000021279
resolver
ensp
ENSMUSP00000042565
resolver
enst
ENSMUST00000041965
resolver
genesymbol
Cdc42bpb
resolver
genesymbol_syn
Kiaa1124
resolver
uniprot
E9QK15
resolver
uniprot
Q69ZR5
resolver
uniprot
Q80W33
resolver
uniprot_entry
MRCKB_MOUSE
resolver
uniprot_sec
E9QK15
resolver
uniprot_sec
Q69ZR5
resolver
uniprot_sec
Q80W33
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. Inhibited by chelerythrine chloride (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MSAKVRLKKLEQLLLDGPWRNDSALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAKPFTQLVKDMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFDVDDDMLRNIEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSMTQSNTLTKDEDVQRDLENSLQIEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSTRALGNSNRDKEIKRLNEELERMKSKMADSNRLERQLEDTVTLRQEHEDSTHRLKGLEKQYRLARQEKEELHKQLVEASERLKSQTKELKDAHQQRKRALQEFSELNERMSELRSLKQKVSRQLRDKEEEMEVAMQKIDSMRQDLRKSEKSRKELEARLEDAAAEASKERKLREHSESFCKQMERELEALKVKQGGRGPGAASEHQQEISKIRSELEKKVLFYEEELVRREASHVLEVKNVKKEVHDSESHQLALQKEVLMLKDKLEKSKRERHSEMEEAIGTVKDKYERERAMLFDENKKLTAENEKLCSFVDKLTAQNRQLEDELQDLASKKESVAHWEAQIAEIIQWVSDEKDARGYLQALASKMTEELETLRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVQEELRKVKDSSLAFESKLKESEAKNRELLEEMQSLRKRMEEKFRADTGLKLPDFQDSIFEYFNTAPLAHDLTFRTSSASDQETQASKMDLSPSVSVATSTEQQEDMARPQQRPSPVPLPSTQALAMAGPKPKAHQFSIKSFPSPTQCSHCTSLMVGLIRQGYACEVCAFSCHVSCKDSAPQVCPIPPEQSKRPLGVDVQRGIGTAYKGYVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVVASQVLDLRDEEFAVSSVLASDVIHATRRDIPCIFRVTASLLGSPSKTSSLLILTENENEKRKWVGILEGLQAILHKNRLKSQVVHVAQEAYDSSLPLIKAVLAAAIVDGDRIAVGLEEGLYVIELTRDVIVRAADCKKVYQIELAPKEKIAILLCGRNHHVHLYPWSSFDGAEASNFDIKLPETKGCQLIATGTLRKSSSTCLFVAVKRLILCYEIQRTKPFHRKFSELVAPGHVQWMAVFKDRLCVGYPSGFSLLSIQGDGPPLDLVNPTDPSLAFLSQQSFDALCAVELKSEEYLLCFSHMGLYVDPQGRRSRMQELMWPAAPVACSCSPTHVTVYSEYGVDVFDVRTMEWVQTIGLRRIRPLNSDGSLNLLGCEPPRLIYFKNKFSGTILNVPDTSDNSKKQMLRTRSKRRFVFKVPEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAAPTVQEEKQGPTPAGLPRQPPSRSKPYVSWPSSGGSEPGVPVPLRSMSDPDQDFDKEPDSDSTKHSTPSNSSNPSGPPSPNSPHRSQLPMEGLDQPSCDA
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. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates PPP1R12A (By similarity). 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 (PubMed:25107909). {ECO:0000250|UniProtKB:Q7TT49, ECO:0000269|PubMed:25107909}.
uniprot
proteins
mass_dalton
194753
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
12522145
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25107909
uniprot
proteins
sequence_length
1713
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction {ECO:0000250}. 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. Detected at the leading edge of migrating and wounded cells; this localization requires the presence of catalytically active CDC42. Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:O54874, ECO:0000250|UniProtKB:Q3UU96, ECO:0000250|UniProtKB:Q7TT49}.
uniprot
proteins