CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015878
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
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
542YRLARQEKEELHKQLacetylation[1]
1281VRAADCKKVYQIELAacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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. 
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 (By similarity).
 MOD_RES 1692 1692 Phosphoserine (By similarity).
 MOD_RES 1695 1695 Phosphoserine (By similarity).  
Keyword
 ATP-binding; Cell junction; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; 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 NESSLSVETL 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 DVDDDVLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMIQ 420
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN 480
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTQRLKG LEKQYRLARQ 540
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMAELRSQ KQKVSRQLRD 600
KEEEMEVAMQ KIDSMRQDIR KSEKSRKELE ARLEDAVAEA SKERKLREHS ESFSKQMERE 660
LETLKVKQGG RGPGATLEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH 720
ESESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGAMKD KYERERAMLF DENKKLTAEN 780
EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS 840
KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVHEELRKV 900
KDTSLAFESK LKESEAKNRE LLEEMQSLKK RMEEKFRADT GLKLPDFQDP IFEYFNTAPL 960
AHDLTFRTSS ASDQETQASK LDLSPSVSVA TSTEQQEDAA RSQQRPSTVP LPNTQALAMA 1020
GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP 1080
EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP 1140
GVIASQVLDL RDDEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE 1200
NEKRKWVGIL EGLQAILHKN RLRSQVVHVA QEAYDSSLPL IKTVLAAAIV DGDRIAVGLE 1260
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKLILLLCGR NHHVHLYPWT SFDGAEASNF 1320
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLVLCYEIQ RTKPFHRKFN EIVAPGHVQW 1380
MAMFKDRLCV GYPSGFSLLS IQGDGQPLDL VNPADPSLAF LSQQSFDALC AVELKSEEYL 1440
LCFSHMGLYV DPQGRRSRTQ ELMWPAAPVA CSCSSSHVTV YSEYGVDVFD VRTMEWVQTI 1500
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTVLNVPD TSDNSKKQML RTRSKRRFVF 1560
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTAQEE 1620
KQGPAPTGLP RQLPSRNKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST 1680
PSNSSNPSGP PSPNSPHRSQ LPLEGLDQPA CDA 1713 
Gene Ontology
 GO:0042641; C:actomyosin; IDA:UniProtKB.
 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:0017048; F:Rho GTPase binding; IDA:RGD.
 GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
 GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
 GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR001180; Citron.
 IPR020454; DAG/PE-bd.
 IPR011009; Kinase-like_dom.
 IPR014930; Myotonic_dystrophy_kinase_coil.
 IPR000095; PAK_box_Rho-bd.
 IPR017892; Pkinase_C.
 IPR001849; Pleckstrin_homology.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS.
 IPR026611; Ser/Thr_kinase_MRCK. 
Pfam
 PF00130; C1_1
 PF00780; CNH
 PF08826; DMPK_coil
 PF00069; Pkinase
 PF00433; Pkinase_C 
SMART
 SM00109; C1
 SM00036; CNH
 SM00285; PBD
 SM00233; PH
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS50219; CNH
 PS50108; CRIB
 PS50003; PH_DOMAIN
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS
 PR00008; DAGPEDOMAIN.