| Tag | Content |
|---|
| CPLM ID | CPLM-015879 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase MRCK beta |
Protein Synonyms/Alias | CDC42-binding protein kinase beta; DMPK-like beta; Myotonic dystrophy kinase-related CDC42-binding kinase beta; MRCK beta; Myotonic dystrophy protein kinase-like beta |
Gene Name | Cdc42bpb |
Gene Synonyms/Alias | Kiaa1124 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 314 | TDVSEEAKDLIQRLI | ubiquitination | [1] | | 416 | FSDRGSLKSMTQSNT | ubiquitination | [1] | | 426 | TQSNTLTKDEDVQRD | ubiquitination | [1] | | 789 | KLCSFVDKLTAQNRQ | ubiquitination | [1] | | 864 | RTLDPLWKVRRSQKL | ubiquitination | [1] | | 1530 | RLIYFKNKFSGTILN | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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). |
Sequence Annotation | DOMAIN 76 342 Protein kinase.
DOMAIN 343 413 AGC-kinase C-terminal.
DOMAIN 1096 1215 PH.
DOMAIN 1241 1515 CNH.
DOMAIN 1585 1598 CRIB.
NP_BIND 82 90 ATP (By similarity).
ZN_FING 1026 1076 Phorbol-ester/DAG-type.
ACT_SITE 200 200 Proton acceptor (By similarity).
BINDING 105 105 ATP (By similarity).
MOD_RES 221 221 Phosphoserine; by autocatalysis (By
MOD_RES 233 233 Phosphoserine; by autocatalysis (By
MOD_RES 239 239 Phosphothreonine; by autocatalysis (By
MOD_RES 954 954 Phosphotyrosine.
MOD_RES 1692 1692 Phosphoserine.
MOD_RES 1695 1695 Phosphoserine. |
Keyword | ATP-binding; Cell junction; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1713 AA |
Protein Sequence | MSAKVRLKKL EQLLLDGPWR NDSALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK 60
PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC 120
FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY 180
IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP 240
DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF 300
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD 360
VSSPSDTSNF DVDDDMLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMTQ 420
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN 480
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTHRLKG LEKQYRLARQ 540
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMSELRSL KQKVSRQLRD 600
KEEEMEVAMQ KIDSMRQDLR KSEKSRKELE ARLEDAAAEA SKERKLREHS ESFCKQMERE 660
LEALKVKQGG RGPGAASEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH 720
DSESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGTVKD KYERERAMLF DENKKLTAEN 780
EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS 840
KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV 900
KDSSLAFESK LKESEAKNRE LLEEMQSLRK RMEEKFRADT GLKLPDFQDS IFEYFNTAPL 960
AHDLTFRTSS ASDQETQASK MDLSPSVSVA TSTEQQEDMA RPQQRPSPVP LPSTQALAMA 1020
GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP 1080
EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP 1140
GVVASQVLDL RDEEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE 1200
NEKRKWVGIL EGLQAILHKN RLKSQVVHVA QEAYDSSLPL IKAVLAAAIV DGDRIAVGLE 1260
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKIAILLCGR NHHVHLYPWS SFDGAEASNF 1320
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLILCYEIQ RTKPFHRKFS ELVAPGHVQW 1380
MAVFKDRLCV GYPSGFSLLS IQGDGPPLDL VNPTDPSLAF LSQQSFDALC AVELKSEEYL 1440
LCFSHMGLYV DPQGRRSRMQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI 1500
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTILNVPD TSDNSKKQML RTRSKRRFVF 1560
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTVQEE 1620
KQGPTPAGLP RQPPSRSKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST 1680
PSNSSNPSGP PSPNSPHRSQ LPMEGLDQPS CDA 1713 |
Gene Ontology | GO:0042641; C:actomyosin; IEA:Compara. GO:0031252; C:cell leading edge; ISS:UniProtKB. GO:0005911; C:cell-cell junction; ISS:UniProtKB. GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; ISS:UniProtKB. GO:0000287; F:magnesium ion binding; ISS:UniProtKB. GO:0005543; F:phospholipid binding; IEA:InterPro. GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. GO:0005083; F:small GTPase regulator activity; IEA:InterPro. GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB. GO:0031032; P:actomyosin structure organization; IEA:Compara. GO:0016477; P:cell migration; IEA:Compara. GO:0035556; P:intracellular signal transduction; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |