MRCKB_MOUSE - dbPTM
MRCKB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRCKB_MOUSE
UniProt AC Q7TT50
Protein Name Serine/threonine-protein kinase MRCK beta
Gene Name Cdc42bpb {ECO:0000312|EMBL:AAP34402.1, ECO:0000312|MGI:MGI:2136459}
Organism Mus musculus (Mouse).
Sequence Length 1713
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cell junction. Cell projection, lamellipodium . Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cel
Protein 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). 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. [PubMed: 25107909]
Protein Sequence MSAKVRLKKLEQLLLDGPWRNDSALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAKPFTQLVKDMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFDVDDDMLRNIEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSMTQSNTLTKDEDVQRDLENSLQIEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSTRALGNSNRDKEIKRLNEELERMKSKMADSNRLERQLEDTVTLRQEHEDSTHRLKGLEKQYRLARQEKEELHKQLVEASERLKSQTKELKDAHQQRKRALQEFSELNERMSELRSLKQKVSRQLRDKEEEMEVAMQKIDSMRQDLRKSEKSRKELEARLEDAAAEASKERKLREHSESFCKQMERELEALKVKQGGRGPGAASEHQQEISKIRSELEKKVLFYEEELVRREASHVLEVKNVKKEVHDSESHQLALQKEVLMLKDKLEKSKRERHSEMEEAIGTVKDKYERERAMLFDENKKLTAENEKLCSFVDKLTAQNRQLEDELQDLASKKESVAHWEAQIAEIIQWVSDEKDARGYLQALASKMTEELETLRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVQEELRKVKDSSLAFESKLKESEAKNRELLEEMQSLRKRMEEKFRADTGLKLPDFQDSIFEYFNTAPLAHDLTFRTSSASDQETQASKMDLSPSVSVATSTEQQEDMARPQQRPSPVPLPSTQALAMAGPKPKAHQFSIKSFPSPTQCSHCTSLMVGLIRQGYACEVCAFSCHVSCKDSAPQVCPIPPEQSKRPLGVDVQRGIGTAYKGYVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVVASQVLDLRDEEFAVSSVLASDVIHATRRDIPCIFRVTASLLGSPSKTSSLLILTENENEKRKWVGILEGLQAILHKNRLKSQVVHVAQEAYDSSLPLIKAVLAAAIVDGDRIAVGLEEGLYVIELTRDVIVRAADCKKVYQIELAPKEKIAILLCGRNHHVHLYPWSSFDGAEASNFDIKLPETKGCQLIATGTLRKSSSTCLFVAVKRLILCYEIQRTKPFHRKFSELVAPGHVQWMAVFKDRLCVGYPSGFSLLSIQGDGPPLDLVNPTDPSLAFLSQQSFDALCAVELKSEEYLLCFSHMGLYVDPQGRRSRMQELMWPAAPVACSCSPTHVTVYSEYGVDVFDVRTMEWVQTIGLRRIRPLNSDGSLNLLGCEPPRLIYFKNKFSGTILNVPDTSDNSKKQMLRTRSKRRFVFKVPEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAAPTVQEEKQGPTPAGLPRQPPSRSKPYVSWPSSGGSEPGVPVPLRSMSDPDQDFDKEPDSDSTKHSTPSNSSNPSGPPSPNSPHRSQLPMEGLDQPSCDA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
221PhosphorylationIRLADFGSCLKMNDD
EEECCCCCCEEECCC
19.10-
233PhosphorylationNDDGTVQSSVAVGTP
CCCCCEEECEECCCC
23.57-
239PhosphorylationQSSVAVGTPDYISPE
EECEECCCCCCCCHH
13.34-
314UbiquitinationTDVSEEAKDLIQRLI
CCCCHHHHHHHHHHH
57.24-
357PhosphorylationIRNLEAPYIPDVSSP
HHCCCCCCCCCCCCC
31.9429472430
362PhosphorylationAPYIPDVSSPSDTSN
CCCCCCCCCCCCCCC
43.8629472430
363PhosphorylationPYIPDVSSPSDTSNF
CCCCCCCCCCCCCCC
28.4222817900
365PhosphorylationIPDVSSPSDTSNFDV
CCCCCCCCCCCCCCC
56.3123649490
367PhosphorylationDVSSPSDTSNFDVDD
CCCCCCCCCCCCCCH
29.8829472430
368PhosphorylationVSSPSDTSNFDVDDD
CCCCCCCCCCCCCHH
40.2529472430
414PhosphorylationSCFSDRGSLKSMTQS
HHCCCCCCCCCHHCC
33.25-
416UbiquitinationFSDRGSLKSMTQSNT
CCCCCCCCCHHCCCC
39.6227667366
421PhosphorylationSLKSMTQSNTLTKDE
CCCCHHCCCCCCCCH
23.7122817900
423PhosphorylationKSMTQSNTLTKDEDV
CCHHCCCCCCCCHHH
40.8423140645
425PhosphorylationMTQSNTLTKDEDVQR
HHCCCCCCCCHHHHH
34.1223140645
426UbiquitinationTQSNTLTKDEDVQRD
HCCCCCCCCHHHHHH
63.3327667366
464PhosphorylationLSRKLQESTQTVQSL
HHHHHHHHHHHHHHH
16.9223984901
465PhosphorylationSRKLQESTQTVQSLH
HHHHHHHHHHHHHHH
27.7523984901
467PhosphorylationKLQESTQTVQSLHGS
HHHHHHHHHHHHHHH
22.1723984901
470PhosphorylationESTQTVQSLHGSTRA
HHHHHHHHHHHHHHH
20.2823984901
474PhosphorylationTVQSLHGSTRALGNS
HHHHHHHHHHHCCCC
12.1730352176
475PhosphorylationVQSLHGSTRALGNSN
HHHHHHHHHHCCCCC
25.2623984901
481PhosphorylationSTRALGNSNRDKEIK
HHHHCCCCCHHHHHH
31.2926824392
500AcetylationELERMKSKMADSNRL
HHHHHHHHHHHCHHH
32.3715616773
533MalonylationHRLKGLEKQYRLARQ
HHHHHHHHHHHHHHH
58.6426320211
614PhosphorylationVAMQKIDSMRQDLRK
HHHHHHHHHHHHHHH
21.2424719451
652PhosphorylationKLREHSESFCKQMER
HHHHHHHHHHHHHHH
38.6726824392
671MethylationLKVKQGGRGPGAASE
HCCCCCCCCCCHHHH
55.76-
677PhosphorylationGRGPGAASEHQQEIS
CCCCCHHHHHHHHHH
34.7726239621
684PhosphorylationSEHQQEISKIRSELE
HHHHHHHHHHHHHHH
22.6826239621
707PhosphorylationELVRREASHVLEVKN
HHHHHHHHHHEEEEC
14.91-
749PhosphorylationKSKRERHSEMEEAIG
HHHHHHHHHHHHHHH
44.8821149613
757PhosphorylationEMEEAIGTVKDKYER
HHHHHHHHHHHHHHH
20.4721149613
789UbiquitinationKLCSFVDKLTAQNRQ
HHHHHHHHHHHHHHH
42.30-
840PhosphorylationGYLQALASKMTEELE
HHHHHHHHHHHHHHH
24.66-
843PhosphorylationQALASKMTEELETLR
HHHHHHHHHHHHHHH
30.0029899451
852PhosphorylationELETLRSSSLGSRTL
HHHHHHHCCCCCCCC
24.1320139300
856PhosphorylationLRSSSLGSRTLDPLW
HHHCCCCCCCCCHHH
27.6429899451
858PhosphorylationSSSLGSRTLDPLWKV
HCCCCCCCCCHHHHH
36.8925521595
864UbiquitinationRTLDPLWKVRRSQKL
CCCCHHHHHHHHCCC
33.28-
868PhosphorylationPLWKVRRSQKLDMSA
HHHHHHHHCCCCHHH
22.5429514104
901MethylationQEELRKVKDSSLAFE
HHHHHHHCCCHHHHH
55.73-
910UbiquitinationSSLAFESKLKESEAK
CHHHHHHHHHHHHHH
57.2827667366
927PhosphorylationELLEEMQSLRKRMEE
HHHHHHHHHHHHHHH
28.9122817900
954PhosphorylationFQDSIFEYFNTAPLA
HHHHHHHHHHCCCCC
7.4422817900
957PhosphorylationSIFEYFNTAPLAHDL
HHHHHHHCCCCCCCC
21.5426643407
965PhosphorylationAPLAHDLTFRTSSAS
CCCCCCCEECCCCCC
19.6826643407
968PhosphorylationAHDLTFRTSSASDQE
CCCCEECCCCCCHHH
23.8927087446
969PhosphorylationHDLTFRTSSASDQET
CCCEECCCCCCHHHH
21.4629550500
970PhosphorylationDLTFRTSSASDQETQ
CCEECCCCCCHHHHH
31.0430352176
972PhosphorylationTFRTSSASDQETQAS
EECCCCCCHHHHHHH
41.6025521595
976PhosphorylationSSASDQETQASKMDL
CCCCHHHHHHHHCCC
24.6526643407
979PhosphorylationSDQETQASKMDLSPS
CHHHHHHHHCCCCCC
20.7826643407
984PhosphorylationQASKMDLSPSVSVAT
HHHHCCCCCCEEECC
15.7428066266
986PhosphorylationSKMDLSPSVSVATST
HHCCCCCCEEECCCH
24.5328066266
988PhosphorylationMDLSPSVSVATSTEQ
CCCCCCEEECCCHHH
15.4626060331
991PhosphorylationSPSVSVATSTEQQED
CCCEEECCCHHHHHH
33.7426060331
992PhosphorylationPSVSVATSTEQQEDM
CCEEECCCHHHHHHH
21.8726060331
993PhosphorylationSVSVATSTEQQEDMA
CEEECCCHHHHHHHC
33.2026060331
1007PhosphorylationARPQQRPSPVPLPST
CCCCCCCCCCCCCCH
40.4926060331
1013PhosphorylationPSPVPLPSTQALAMA
CCCCCCCCHHHHHHC
40.6126060331
1014PhosphorylationSPVPLPSTQALAMAG
CCCCCCCHHHHHHCC
18.8726060331
1030PhosphorylationKPKAHQFSIKSFPSP
CCCCEECCCCCCCCC
23.6525338131
1182PhosphorylationCIFRVTASLLGSPSK
EEEEEEHHHHCCCCC
18.1128066266
1186PhosphorylationVTASLLGSPSKTSSL
EEHHHHCCCCCCCEE
26.4326824392
1188PhosphorylationASLLGSPSKTSSLLI
HHHHCCCCCCCEEEE
50.7128066266
1190PhosphorylationLLGSPSKTSSLLILT
HHCCCCCCCEEEEEE
28.0821454597
1192PhosphorylationGSPSKTSSLLILTEN
CCCCCCCEEEEEECC
32.2125338131
1197PhosphorylationTSSLLILTENENEKR
CCEEEEEECCCCCCC
29.7521454597
1530UbiquitinationRLIYFKNKFSGTILN
EEEEEECCCCCEEEC
41.31-
1532PhosphorylationIYFKNKFSGTILNVP
EEEECCCCCEEECCC
36.3122871156
1534PhosphorylationFKNKFSGTILNVPDT
EECCCCCEEECCCCC
22.5422871156
1542PhosphorylationILNVPDTSDNSKKQM
EECCCCCCCCHHHHH
42.0222871156
1635PhosphorylationGLPRQPPSRSKPYVS
CCCCCCCCCCCCCEE
56.7329514104
1637PhosphorylationPRQPPSRSKPYVSWP
CCCCCCCCCCCEECC
42.1726239621
1640PhosphorylationPPSRSKPYVSWPSSG
CCCCCCCCEECCCCC
15.7326239621
1642PhosphorylationSRSKPYVSWPSSGGS
CCCCCCEECCCCCCC
27.6826239621
1645PhosphorylationKPYVSWPSSGGSEPG
CCCEECCCCCCCCCC
35.0426060331
1646PhosphorylationPYVSWPSSGGSEPGV
CCEECCCCCCCCCCC
42.9922817900
1649PhosphorylationSWPSSGGSEPGVPVP
ECCCCCCCCCCCCCC
44.1126239621
1659PhosphorylationGVPVPLRSMSDPDQD
CCCCCCCCCCCCCCC
30.2623684622
1661PhosphorylationPVPLRSMSDPDQDFD
CCCCCCCCCCCCCCC
47.4330635358
1673PhosphorylationDFDKEPDSDSTKHST
CCCCCCCCCCCCCCC
44.1429472430
1675PhosphorylationDKEPDSDSTKHSTPS
CCCCCCCCCCCCCCC
43.2229472430
1676PhosphorylationKEPDSDSTKHSTPSN
CCCCCCCCCCCCCCC
37.4523684622
1679PhosphorylationDSDSTKHSTPSNSSN
CCCCCCCCCCCCCCC
43.5025619855
1680PhosphorylationSDSTKHSTPSNSSNP
CCCCCCCCCCCCCCC
30.3825619855
1682PhosphorylationSTKHSTPSNSSNPSG
CCCCCCCCCCCCCCC
49.8125619855
1684PhosphorylationKHSTPSNSSNPSGPP
CCCCCCCCCCCCCCC
35.5125619855
1685PhosphorylationHSTPSNSSNPSGPPS
CCCCCCCCCCCCCCC
57.9425619855
1688PhosphorylationPSNSSNPSGPPSPNS
CCCCCCCCCCCCCCC
69.0827087446
1692PhosphorylationSNPSGPPSPNSPHRS
CCCCCCCCCCCCCHH
39.5927087446
1695PhosphorylationSGPPSPNSPHRSQLP
CCCCCCCCCCHHCCC
26.0127087446
1699PhosphorylationSPNSPHRSQLPMEGL
CCCCCCHHCCCCCCC
32.7923984901
1710PhosphorylationMEGLDQPSCDA----
CCCCCCCCCCC----
20.9923984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1692SPhosphorylationKinaseMTORQ9JLN9
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRCKB_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MRCKB_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNE1_HUMANCPNE1physical
12522145
CPNE4_HUMANCPNE4physical
12522145

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MRCKB_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692 AND SER-1695, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-954, AND MASSSPECTROMETRY.

TOP