CDC42BPB
entrez
9578
canonical
uniprot
Q9Y5S2
canonical
ensembl
ENSG00000198752
resolver
ensp
ENSP00000355237
resolver
ensp
ENSP00000453384
resolver
ensp
ENSP00000571250
resolver
enst
ENST00000361246
resolver
enst
ENST00000559043
resolver
genesymbol
CDC42BPB
resolver
genesymbol_syn
KIAA1124
resolver
hgnc
HGNC:1738
resolver
uniprot
A9JR72
resolver
uniprot
H0YLY0
resolver
uniprot
Q2L7A5
resolver
uniprot
Q86TJ1
resolver
uniprot
Q86XZ8
resolver
uniprot
Q9ULU5
resolver
uniprot_entry
H0YLY0_HUMAN
resolver
uniprot_entry
MRCKB_HUMAN
resolver
uniprot_entry
Q86XZ8_HUMAN
resolver
uniprot_sec
A9JR72
resolver
uniprot_sec
Q2L7A5
resolver
uniprot_sec
Q86TJ1
resolver
uniprot_sec
Q9ULU5
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
MSAKVRLKKLEQLLLDGPWRNESALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAKPFTQLVKEMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENHLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFDVDDDVLRNTEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSIMQSNTLTKDEDVQRDLEHSLQMEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSSRALSNSNRDKEIKKLNEEIERLKNKIADSNRLERQLEDTVALRQEREDSTQRLRGLEKQHRVVRQEKEELHKQLVEASERLKSQAKELKDAHQQRKLALQEFSELNERMAELRAQKQKVSRQLRDKEEEMEVATQKVDAMRQEMRRAEKLRKELEAQLDDAVAEASKERKLREHSENFCKQMESELEALKVKQGGRGAGATLEHQQEISKIKSELEKKVLFYEEELVRREASHVLEVKNVKKEVHDSESHQLALQKEILMLKDKLEKSKRERHNEMEEAVGTIKDKYERERAMLFDENKKLTAENEKLCSFVDKLTAQNRQLEDELQDLAAKKESVAHWEAQIAEIIQWVSDEKDARGYLQALASKMTEELEALRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVQEELRKVKDANLTLESKLKDSEAKNRELLEEMEILKKKMEEKFRADTGLKLPDFQDSIFEYFNTAPLAHDLTFRTSSASEQETQAPKPEASPSMSVAASEQQEDMARPPQRPSAVPLPTTQALALAGPKPKAHQFSIKSFSSPTQCSHCTSLMVGLIRQGYACEVCSFACHVSCKDGAPQVCPIPPEQSKRPLGVDVQRGIGTAYKGHVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVIASQVLDLRDDEFSVSSVLASDVIHATRRDIPCIFRVTASLLGAPSKTSSLLILTENENEKRKWVGILEGLQSILHKNRLRNQVVHVPLEAYDSSLPLIKAILTAAIVDADRIAVGLEEGLYVIEVTRDVIVRAADCKKVHQIELAPREKIVILLCGRNHHVHLYPWSSLDGAEGSFDIKLPETKGCQLMATATLKRNSGTCLFVAVKRLILCYEIQRTKPFHRKFNEIVAPGSVQCLAVLRDRLCVGYPSGFCLLSIQGDGQPLNLVNPNDPSLAFLSQQSFDALCAVELESEEYLLCFSHMGLYVDPQGRRARAQELMWPAAPVACSCSPTHVTVYSEYGVDVFDVRTMEWVQTIGLRRIRPLNSEGTLNLLNCEPPRLIYFKSKFSGAVLNVPDTSDNSKKQMLRTRSKRRFVFKVPEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAVPPSQEERPGPAPTNLARQPPSRNKPYISWPSSGGSEPSVTVPLRSMSDPDQDFDKEPDSDSTKHSTPSNSSNPSGPPSPNSPHRSQLPLEGLEQPACDT
uniprot
proteins
disease_involvement
DISEASE: Chilton-Okur-Chung neurodevelopmental syndrome (CHOCNS) [MIM:619841]: A disorder characterized by developmental delay, intellectual disability, hypotonia, and structural brain abnormalities including cerebellar vermis hypoplasia and agenesis or hypoplasia of the corpus callosum. Most patients have behavioral abnormalities, including autism spectrum disorder, attention deficit and hyperactivity disorder, and aggression. About half of patients have dysmorphic facial features. Rare involvement of other organ systems may be present. {ECO:0000269|PubMed:32031333}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:21457715, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). 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:21457715, ECO:0000269|PubMed:21949762}.
uniprot
proteins
mass_dalton
194315
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspases upon apoptosis induction. {ECO:0000269|PubMed:29162624}.
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
10198171
uniprot
proteins
pubmed
10574461
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18854160
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21240187
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
21949762
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25743393
uniprot
proteins
pubmed
29162624
uniprot
proteins
pubmed
32031333
uniprot
proteins
sequence_length
1711
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 cells. Localization at the leading edge of migrating cells requires interaction with 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