CDC42BPA
entrez
8476
canonical
uniprot
Q5VT25
canonical
ensembl
ENSG00000143776
resolver
ensp
ENSP00000335341
resolver
ensp
ENSP00000355726
resolver
ensp
ENSP00000355728
resolver
ensp
ENSP00000355729
resolver
ensp
ENSP00000355731
resolver
ensp
ENSP00000633255
resolver
ensp
ENSP00000633256
resolver
ensp
ENSP00000633257
resolver
ensp
ENSP00000782977
resolver
enst
ENST00000366764
resolver
enst
ENST00000366766
resolver
genesymbol
CDC42BPA
resolver
genesymbol_syn
KIAA0451
resolver
hgnc
HGNC:1737
resolver
uniprot
A0A0A0MRJ0
resolver
uniprot
A0A0A0MRJ1
resolver
uniprot
O75039
resolver
uniprot
Q59GZ1
resolver
uniprot
Q5H9N9
resolver
uniprot
Q5T797
resolver
uniprot
Q5VT26
resolver
uniprot
Q5VT27
resolver
uniprot
Q86XX2
resolver
uniprot
Q86XX3
resolver
uniprot
Q99646
resolver
uniprot_entry
A0A0A0MRJ0_HUMAN
resolver
uniprot_entry
A0A0A0MRJ1_HUMAN
resolver
uniprot_entry
MRCKA_HUMAN
resolver
uniprot_sec
O75039
resolver
uniprot_sec
Q59GZ1
resolver
uniprot_sec
Q5H9N9
resolver
uniprot_sec
Q5T797
resolver
uniprot_sec
Q5VT26
resolver
uniprot_sec
Q5VT27
resolver
uniprot_sec
Q86XX2
resolver
uniprot_sec
Q86XX3
resolver
uniprot_sec
Q99646
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. {ECO:0000269|PubMed:11283256, ECO:0000269|PubMed:21457715}.
uniprot
proteins
amino_acid_sequence
MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDNKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPAQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELSRKLQESTQTVQALQYSTVDGPLTASKDLEIKNLKEEIEKLRKQVTESSHLEQQLEEANAVRQELDDAFRQIKAYEKQIKTLQQEREDLNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKVESLRQELRRTERAKKELEVHTEALAAEASKDRKLREQSEHYSKQLENELEGLKQKQISYSPGVCSIEHQQEITKLKTDLEKKSIFYEEELSKREGIHANEIKNLKKELHDSEGQQLALNKEIMILKDKLEKTRRESQSEREEFESEFKQQYEREKVLLTEENKKLTSELDKLTTLYENLSIHNQQLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGIEHQDSQHSFLAFLNTPTDALDQFERSPSCTPASKGRRTVDSTPLSVHTPTLRKKGCPGSTGFPPKRKTHQFFVKSFTTPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKGIGTAYEGHVRIPKPAGVKKGWQRALAIVCDFKLFLYDIAEGKASQPSVVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSASNNKCSILMLADTENEKNKWVGVLSELHKILKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERIALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPNDQLVAVISGRNRHVRLFPMSALDGRETDFYKLSETKGCQTVTSGKVRHGALTCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPYNVQWMAIFSEQLCVGFQSGFLRYPLNGEGNPYSMLHSNDHTLSFIAHQPMDAICAVEISSKEYLLCFNSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSVYSENAVDIFDVNSMEWIQTLPLKKVRPLNNEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYSAKRQPMPSPSEGSLSSGGMDQGSDAPARDFDGEDSDSPRHSTASNSSNLSSPPSPASPRKTKSLSLESTDRGSWDP
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:15723050, PubMed:9092543, PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C 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: PPP1R12A, LIMK1 and LIMK2 (PubMed:11340065, PubMed:11399775). May play a role in TFRC-mediated iron uptake (PubMed:20188707). 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 (PubMed:29162624). {ECO:0000250|UniProtKB:Q3UU96, ECO:0000269|PubMed:11340065, ECO:0000269|PubMed:11399775, ECO:0000269|PubMed:15723050, ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:20188707, ECO:0000269|PubMed:21457715, ECO:0000269|PubMed:29162624, ECO:0000269|PubMed:9092543, ECO:0000269|PubMed:9418861}.
uniprot
proteins
mass_dalton
197307
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="K->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:11283256"; MUTAGEN 222; /note="S->L: Increase in autophosphorylation but not kinase activity."; /evidence="ECO:0000269|PubMed:11283256"; MUTAGEN 234; /note="S->A: Loss of autophosphorylation and kinase activity."; /evidence="ECO:0000269|PubMed:11283256"; MUTAGEN 240; /note="T->A: Loss of autophosphorylation and kinase activity."; /evidence="ECO:0000269|PubMed:11283256"; MUTAGEN 403; /note="T->A: Loss of autophosphorylation and kinase activity."; /evidence="ECO:0000269|PubMed:11283256"; MUTAGEN 478; /note="D->A: Prevents cleavage by CASP3, impairs the increase of its kinase activity and impairs extrusion apical actin ring assembly."; /evidence="ECO:0000269|PubMed:29162624"; MUTAGEN 984; /note="D->A: Prevents cleavage by CASP3."; /evidence="ECO:0000269|PubMed:29162624"; MUTAGEN 1579; /note="H->A: Loss of CDC42 binding; when associated with A-1582."; /evidence="ECO:0000269|PubMed:9418861"; MUTAGEN 1582; /note="H->A: Loss of CDC42 binding; when associated with A-1579."; /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: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
11283256
uniprot
proteins
pubmed
11340065
uniprot
proteins
pubmed
11399775
uniprot
proteins
pubmed
12568720
uniprot
proteins
pubmed
15723050
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18854160
uniprot
proteins
pubmed
20188707
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21457715
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29162624
uniprot
proteins
pubmed
9092543
uniprot
proteins
pubmed
9418861
uniprot
proteins
pubmed
9455484
uniprot
proteins
sequence_length
1732
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54874}. 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. Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner. {ECO:0000250|UniProtKB:O54874, ECO:0000250|UniProtKB:Q3UU96}.
uniprot
proteins