Cdc42bpa
entrez
226751
canonical
uniprot
Q3UU96
canonical
ensembl
ENSMUSG00000026490
resolver
ensp
ENSMUSP00000075980
resolver
ensp
ENSMUSP00000095059
resolver
ensp
ENSMUSP00000106746
resolver
ensp
ENSMUSP00000148469
resolver
ensp
ENSMUSP00000261772
resolver
ensp
ENSMUSP00000261773
resolver
ensp
ENSMUSP00000261775
resolver
enst
ENSMUST00000076687
resolver
enst
ENSMUST00000111117
resolver
enst
ENSMUST00000212756
resolver
genesymbol
Cdc42bpa
resolver
genesymbol_syn
Kiaa0451
resolver
uniprot
A0A1D5RLQ9
resolver
uniprot
B2RY49
resolver
uniprot
E9PVY0
resolver
uniprot
H7BX44
resolver
uniprot
Q4V9U7
resolver
uniprot
Q6ZQA9
resolver
uniprot
Q8R495
resolver
uniprot_entry
A0A1D5RLQ9_MOUSE
resolver
uniprot_entry
E9PVY0_MOUSE
resolver
uniprot_entry
H7BX44_MOUSE
resolver
uniprot_entry
MRCKA_MOUSE
resolver
uniprot_sec
B2RY49
resolver
uniprot_sec
Q4V9U7
resolver
uniprot_sec
Q6ZQA9
resolver
uniprot_sec
Q8R495
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
MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEEMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPAQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVSVQRTLDNNLATEAYERRIKRLEQEKLELTRKLQESTQTVQALQYSTVDGPLTASKDLEIKSLKEEIEKLRKQVAEVNHLEQQLEEANSVRRELDDAFRQIKASEKQIKTLQQEREELNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKAESLRQELRRAERAKKELEVHTEALIAEASKDKKLREQSEHYSKQLENELEGLKQKQISYSPGICSIEHQQEITKLKTDLEKKSIFYEEEISKREGIHASEIKNLKKELHDSEGQQLALNKEILVLKDKLEKTRRESQSEREEFENEFKQQYEREKVLLTEENKKLTSELDKLTSLYESLSLRNQHLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNILTECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGIEHQDSQHSFLAFLNTPTDALDQFEIADCAPLPAHTPTLRKKGCPASTGFPPKRKTHQFFVKSFTAPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTVCPVPPEQTKGPLGIDPQKGVGTAYEGHVRIPKPAGVKKGWQRALAVVCDFKLFLYDIAEGKASQPTSVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSAPSNKCSILMLADSENERSKWVGVLSELHKILKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERIALGNEEGLFVVHVTKDEIVRVGDNKKIHQIELIPSDQLVAVISGRNRHVRLFPMSALDGRETDFYKLAETKGCQTIAAGKVRHGALSCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPCNVQWMAIFSEHLCVGFQSGFLRYPLNGEGGPCNMLHSNDHTLSFISHQPMDALCAVEISNKEYLLCFNSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSVYSENAVDIFDVNSMEWIQTLPLKKVRPLNTEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYNTKRQPMPSPSEGSLSSGGMDQGSDAPARDYDGEDSDSPRHSTASNSSNLSSPPSPISPQKTKSLSLESTDRGSWDP
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 LRP35A, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates: PPP1R12A and LIMK2. May play a role in TFRC-mediated iron uptake (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). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (By similarity). {ECO:0000250|UniProtKB:Q5VT25, ECO:0000269|PubMed:25107909}.
uniprot
proteins
mass_dalton
195536
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspases upon apoptosis induction. The cleavage at Asp-478 by CASP3 increases its kinase activity (in vitro). {ECO:0000250|UniProtKB:Q5VT25}.
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
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25107909
uniprot
proteins
sequence_length
1719
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, lamellipodium {ECO:0000269|PubMed:25107909}. 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). Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner (PubMed:25107909). {ECO:0000250|UniProtKB:O54874, ECO:0000269|PubMed:25107909}.
uniprot
proteins