CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023929
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase MRCK beta 
Protein Synonyms/Alias
 CDC42-binding protein kinase beta; CDC42BP-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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
314TDVSEEAKDLIQRLIubiquitination[1, 2]
337QNGIEDFKKHAFFEGubiquitination[1, 2]
426MQSNTLTKDEDVQRDubiquitination[1]
489NRDKEIKKLNEEIERacetylation[3]
864RTLDPLWKVRRSQKLubiquitination[4, 5]
1188SLLGAPSKTSSLLILubiquitination[2]
1337LMATATLKRNSGTCLubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
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 1095 1214 PH.
 DOMAIN 1240 1513 CNH.
 DOMAIN 1583 1596 CRIB.
 NP_BIND 82 90 ATP (By similarity).
 ZN_FING 1025 1075 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 1690 1690 Phosphoserine.
 MOD_RES 1693 1693 Phosphoserine.  
Keyword
 3D-structure; ATP-binding; Cell junction; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1711 AA 
Protein Sequence
MSAKVRLKKL EQLLLDGPWR NESALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK 60
PFTQLVKEMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC 120
FREERDVLVN GDCQWITALH YAFQDENHLY 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 DVDDDVLRNT EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSIMQ 420
SNTLTKDEDV QRDLEHSLQM EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSSRALSN 480
SNRDKEIKKL NEEIERLKNK IADSNRLERQ LEDTVALRQE REDSTQRLRG LEKQHRVVRQ 540
EKEELHKQLV EASERLKSQA KELKDAHQQR KLALQEFSEL NERMAELRAQ KQKVSRQLRD 600
KEEEMEVATQ KVDAMRQEMR RAEKLRKELE AQLDDAVAEA SKERKLREHS ENFCKQMESE 660
LEALKVKQGG RGAGATLEHQ QEISKIKSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH 720
DSESHQLALQ KEILMLKDKL EKSKRERHNE MEEAVGTIKD KYERERAMLF DENKKLTAEN 780
EKLCSFVDKL TAQNRQLEDE LQDLAAKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS 840
KMTEELEALR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV 900
KDANLTLESK LKDSEAKNRE LLEEMEILKK KMEEKFRADT GLKLPDFQDS IFEYFNTAPL 960
AHDLTFRTSS ASEQETQAPK PEASPSMSVA ASEQQEDMAR PPQRPSAVPL PTTQALALAG 1020
PKPKAHQFSI KSFSSPTQCS HCTSLMVGLI RQGYACEVCS FACHVSCKDG APQVCPIPPE 1080
QSKRPLGVDV QRGIGTAYKG HVKVPKPTGV KKGWQRAYAV VCDCKLFLYD LPEGKSTQPG 1140
VIASQVLDLR DDEFSVSSVL ASDVIHATRR DIPCIFRVTA SLLGAPSKTS SLLILTENEN 1200
EKRKWVGILE GLQSILHKNR LRNQVVHVPL EAYDSSLPLI KAILTAAIVD ADRIAVGLEE 1260
GLYVIEVTRD VIVRAADCKK VHQIELAPRE KIVILLCGRN HHVHLYPWSS LDGAEGSFDI 1320
KLPETKGCQL MATATLKRNS GTCLFVAVKR LILCYEIQRT KPFHRKFNEI VAPGSVQCLA 1380
VLRDRLCVGY PSGFCLLSIQ GDGQPLNLVN PNDPSLAFLS QQSFDALCAV ELESEEYLLC 1440
FSHMGLYVDP QGRRARAQEL MWPAAPVACS CSPTHVTVYS EYGVDVFDVR TMEWVQTIGL 1500
RRIRPLNSEG TLNLLNCEPP RLIYFKSKFS GAVLNVPDTS DNSKKQMLRT RSKRRFVFKV 1560
PEEERLQQRR EMLRDPELRS KMISNPTNFN HVAHMGPGDG MQVLMDLPLS AVPPSQEERP 1620
GPAPTNLARQ PPSRNKPYIS WPSSGGSEPS VTVPLRSMSD PDQDFDKEPD SDSTKHSTPS 1680
NSSNPSGPPS PNSPHRSQLP LEGLEQPACD T 1711 
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: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:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
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.