Cdc42bpa
entrez
114116
canonical
uniprot
O54874
canonical
ensembl
ENSRNOG00000002841
resolver
ensp
ENSRNOP00000003837
resolver
ensp
ENSRNOP00000077481
resolver
ensp
ENSRNOP00000081450
resolver
ensp
ENSRNOP00000086891
resolver
ensp
ENSRNOP00000093143
resolver
ensp
ENSRNOP00000099199
resolver
ensp
ENSRNOP00000103002
resolver
enst
ENSRNOT00000003837
resolver
enst
ENSRNOT00000102712
resolver
enst
ENSRNOT00000116713
resolver
enst
ENSRNOT00000151394
resolver
enst
ENSRNOT00000151561
resolver
genesymbol
Cdc42bpa
resolver
genesymbol_syn
Pk428
resolver
uniprot
A0A8I5Y183
resolver
uniprot
A0A8I6AWL9
resolver
uniprot
A0ABK0LGA0
resolver
uniprot
A0ABK0LPG6
resolver
uniprot
G3V6C9
resolver
uniprot_entry
A0A8I5Y183_RAT
resolver
uniprot_entry
A0A8I6AWL9_RAT
resolver
uniprot_entry
A0ABK0LGA0_RAT
resolver
uniprot_entry
A0ABK0LPG6_RAT
resolver
uniprot_entry
G3V6C9_RAT
resolver
uniprot_entry
MRCKA_RAT
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
MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEEMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPTQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELTRKLQESTQTVQALQYSTVDGPLTASKDLEIKSLKEEIEKLRKQVAEVNHLEQQLEEANSVRRELDDAFRQIKAFEKQIKTLQQEREELNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKAESLRQELRRAERAKKELEVHTEALIAEASKDRKLREQSRHYSKQLENELEGLKQKQISYSPGICSIEHQQEITKLKTDLEKKSIFYEEEISKREGIHASEIKNLKKELHDSEGQQLALNKEIMVLKDKLEKTRRESQSEREEFENEFKQQYEREKVLLTEENKKLTSELDKLTSLYESLSLRNQHLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGVEHRDSQHSFLAFLNTPTDALDQFERSPSCTPAGKGRRIADSAPLPVHTPTLRKKGCPASAGFPPKRKTHQFFVKSFTAPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKGVGTAYEGHVRIPKPAGVKKGWQRALAVVCDFKLFLYDIAEGKASQPSSVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSAPSDKCSILMLADSETERSKWVGVLSELHKVLKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERVALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPSDQLVAVISGRNRHVRLFPMSALDGRETDFYKLAETKGCQTIAAGKVRHGALSCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPCNVQWMAIFSEHLCVGFQSGFLRYPLNGEGSPCNMLHSNDHTLAFITHQPMDAICAVEISNKEYLLCFSSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSIYSENAVDIFDVNSMEWIQTLPLKKVRPLNTEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYNTKRQPMPSPSEGSLSSGGVDQGSDAPVRDYDGEDSDSPRHSTASNSSNLSSPPSPVSPRKTKSLSLESTDRGSWDP
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 (PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12A and MYL9/MLC2 (PubMed:21457715). 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: PPP1R12C, LIMK1 and LIMK2. May play a role in TFRC-mediated iron uptake. 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). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (By similarity). {ECO:0000250|UniProtKB:Q3UU96, ECO:0000250|UniProtKB:Q5VT25, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:9418861}.
uniprot
proteins
mass_dalton
197064
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="K->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:9418861
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
11283256
uniprot
proteins
pubmed
12568720
uniprot
proteins
pubmed
16641100
uniprot
proteins
pubmed
18854160
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
25107909
uniprot
proteins
pubmed
9418861
uniprot
proteins
sequence_length
1732
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9418861}. 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 (PubMed:9418861). Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q3UU96, ECO:0000269|PubMed:9418861}.
uniprot
proteins