MRCKB_HUMAN - dbPTM
MRCKB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRCKB_HUMAN
UniProt AC Q9Y5S2
Protein Name Serine/threonine-protein kinase MRCK beta
Gene Name CDC42BPB {ECO:0000312|EMBL:AAD37506.1}
Organism Homo sapiens (Human).
Sequence Length 1711
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
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. [PubMed: 21457715]
Protein Sequence MSAKVRLKKLEQLLLDGPWRNESALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAKPFTQLVKEMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENHLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFDVDDDVLRNTEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSIMQSNTLTKDEDVQRDLEHSLQMEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSSRALSNSNRDKEIKKLNEEIERLKNKIADSNRLERQLEDTVALRQEREDSTQRLRGLEKQHRVVRQEKEELHKQLVEASERLKSQAKELKDAHQQRKLALQEFSELNERMAELRAQKQKVSRQLRDKEEEMEVATQKVDAMRQEMRRAEKLRKELEAQLDDAVAEASKERKLREHSENFCKQMESELEALKVKQGGRGAGATLEHQQEISKIKSELEKKVLFYEEELVRREASHVLEVKNVKKEVHDSESHQLALQKEILMLKDKLEKSKRERHNEMEEAVGTIKDKYERERAMLFDENKKLTAENEKLCSFVDKLTAQNRQLEDELQDLAAKKESVAHWEAQIAEIIQWVSDEKDARGYLQALASKMTEELEALRSSSLGSRTLDPLWKVRRSQKLDMSARLELQSALEAEIRAKQLVQEELRKVKDANLTLESKLKDSEAKNRELLEEMEILKKKMEEKFRADTGLKLPDFQDSIFEYFNTAPLAHDLTFRTSSASEQETQAPKPEASPSMSVAASEQQEDMARPPQRPSAVPLPTTQALALAGPKPKAHQFSIKSFSSPTQCSHCTSLMVGLIRQGYACEVCSFACHVSCKDGAPQVCPIPPEQSKRPLGVDVQRGIGTAYKGHVKVPKPTGVKKGWQRAYAVVCDCKLFLYDLPEGKSTQPGVIASQVLDLRDDEFSVSSVLASDVIHATRRDIPCIFRVTASLLGAPSKTSSLLILTENENEKRKWVGILEGLQSILHKNRLRNQVVHVPLEAYDSSLPLIKAILTAAIVDADRIAVGLEEGLYVIEVTRDVIVRAADCKKVHQIELAPREKIVILLCGRNHHVHLYPWSSLDGAEGSFDIKLPETKGCQLMATATLKRNSGTCLFVAVKRLILCYEIQRTKPFHRKFNEIVAPGSVQCLAVLRDRLCVGYPSGFCLLSIQGDGQPLNLVNPNDPSLAFLSQQSFDALCAVELESEEYLLCFSHMGLYVDPQGRRARAQELMWPAAPVACSCSPTHVTVYSEYGVDVFDVRTMEWVQTIGLRRIRPLNSEGTLNLLNCEPPRLIYFKSKFSGAVLNVPDTSDNSKKQMLRTRSKRRFVFKVPEEERLQQRREMLRDPELRSKMISNPTNFNHVAHMGPGDGMQVLMDLPLSAVPPSQEERPGPAPTNLARQPPSRNKPYISWPSSGGSEPSVTVPLRSMSDPDQDFDKEPDSDSTKHSTPSNSSNPSGPPSPNSPHRSQLPLEGLEQPACDT
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
166PhosphorylationGDLLTLLSKFEDKLP
HHHHHHHHHHHHCCC
38.1124719451
221PhosphorylationIRLADFGSCLKMNDD
EEECCCCCCEEECCC
19.10-
233PhosphorylationNDDGTVQSSVAVGTP
CCCCCEEECEECCCC
23.57-
239PhosphorylationQSSVAVGTPDYISPE
EECEECCCCCCCCHH
13.3411283256
244PhosphorylationVGTPDYISPEILQAM
CCCCCCCCHHHHHHH
15.39-
304PhosphorylationEERFQFPSHVTDVSE
HHHCCCCCCCCCCCH
31.70-
307PhosphorylationFQFPSHVTDVSEEAK
CCCCCCCCCCCHHHH
25.84-
310PhosphorylationPSHVTDVSEEAKDLI
CCCCCCCCHHHHHHH
32.31-
314UbiquitinationTDVSEEAKDLIQRLI
CCCCHHHHHHHHHHH
57.2421890473
337UbiquitinationQNGIEDFKKHAFFEG
CCCHHHHHHHHHCCC
56.8421890473
357PhosphorylationIRNLEAPYIPDVSSP
HHCCCCCCCCCCCCC
31.9430624053
362PhosphorylationAPYIPDVSSPSDTSN
CCCCCCCCCCCCCCC
43.8626657352
363PhosphorylationPYIPDVSSPSDTSNF
CCCCCCCCCCCCCCC
28.4221082442
365PhosphorylationIPDVSSPSDTSNFDV
CCCCCCCCCCCCCCC
56.3130624053
367PhosphorylationDVSSPSDTSNFDVDD
CCCCCCCCCCCCCCC
29.8827732954
368PhosphorylationVSSPSDTSNFDVDDD
CCCCCCCCCCCCCCH
40.2527732954
417PhosphorylationSDRGSLKSIMQSNTL
CCCCCHHHHHHHCCC
28.69-
421PhosphorylationSLKSIMQSNTLTKDE
CHHHHHHHCCCCCCH
17.8828857561
423PhosphorylationKSIMQSNTLTKDEDV
HHHHHHCCCCCCHHH
40.8426657352
426UbiquitinationMQSNTLTKDEDVQRD
HHHCCCCCCHHHHHH
63.3321890473
454UbiquitinationIRRLEQEKLELSRKL
HHHHHHHHHHHHHHH
47.13-
460UbiquitinationEKLELSRKLQESTQT
HHHHHHHHHHHHHHH
51.66-
464PhosphorylationLSRKLQESTQTVQSL
HHHHHHHHHHHHHHH
16.9224275569
465PhosphorylationSRKLQESTQTVQSLH
HHHHHHHHHHHHHHH
27.7523312004
467PhosphorylationKLQESTQTVQSLHGS
HHHHHHHHHHHHHHH
22.1723312004
470PhosphorylationESTQTVQSLHGSSRA
HHHHHHHHHHHHHHH
20.2824275569
474PhosphorylationTVQSLHGSSRALSNS
HHHHHHHHHHHHHCC
13.1024275569
475PhosphorylationVQSLHGSSRALSNSN
HHHHHHHHHHHHCCC
26.6028857561
479PhosphorylationHGSSRALSNSNRDKE
HHHHHHHHCCCHHHH
36.9126699800
481PhosphorylationSSRALSNSNRDKEIK
HHHHHHCCCHHHHHH
29.8427422710
489AcetylationNRDKEIKKLNEEIER
CHHHHHHHHHHHHHH
63.3120167786
524PhosphorylationLRQEREDSTQRLRGL
HHHHCHHHHHHHHHH
22.99-
571MalonylationKDAHQQRKLALQEFS
HHHHHHHHHHHHHHH
33.5026320211
571UbiquitinationKDAHQQRKLALQEFS
HHHHHHHHHHHHHHH
33.50-
605SulfoxidationLRDKEEEMEVATQKV
HHCHHHHHHHHHHHH
5.9330846556
641PhosphorylationDDAVAEASKERKLRE
HHHHHHHHHHHHHHH
26.93-
642UbiquitinationDAVAEASKERKLREH
HHHHHHHHHHHHHHH
69.46-
659PhosphorylationNFCKQMESELEALKV
HHHHHHHHHHHHHHC
41.98-
665UbiquitinationESELEALKVKQGGRG
HHHHHHHHCCCCCCC
55.20-
671MethylationLKVKQGGRGAGATLE
HHCCCCCCCCCCCHH
38.3224129315
676PhosphorylationGGRGAGATLEHQQEI
CCCCCCCCHHHHHHH
31.5925159151
697PhosphorylationLEKKVLFYEEELVRR
HHHHHHHCHHHHHHH
20.4727642862
707PhosphorylationELVRREASHVLEVKN
HHHHHHHHHHEEEEC
14.91-
757PhosphorylationEMEEAVGTIKDKYER
HHHHHHHHHHHHHHH
20.4628060719
789UbiquitinationKLCSFVDKLTAQNRQ
HHHHHHHHHHHHHHH
42.30-
807UbiquitinationELQDLAAKKESVAHW
HHHHHHHHHHHHHHH
52.01-
834PhosphorylationDEKDARGYLQALASK
CCCCHHHHHHHHHHH
7.0627174698
840PhosphorylationGYLQALASKMTEELE
HHHHHHHHHHHHHHH
24.6627174698
843PhosphorylationQALASKMTEELEALR
HHHHHHHHHHHHHHH
30.0019664994
851PhosphorylationEELEALRSSSLGSRT
HHHHHHHHCCCCCCC
25.7320068231
852PhosphorylationELEALRSSSLGSRTL
HHHHHHHCCCCCCCC
24.1320068231
853PhosphorylationLEALRSSSLGSRTLD
HHHHHHCCCCCCCCC
37.6922210691
856PhosphorylationLRSSSLGSRTLDPLW
HHHCCCCCCCCCHHH
27.6423898821
858PhosphorylationSSSLGSRTLDPLWKV
HCCCCCCCCCHHHHH
36.8923403867
864UbiquitinationRTLDPLWKVRRSQKL
CCCCHHHHHHHHCCC
33.2821890473
864UbiquitinationRTLDPLWKVRRSQKL
CCCCHHHHHHHHCCC
33.2821890473
868PhosphorylationPLWKVRRSQKLDMSA
HHHHHHHHCCCCHHH
22.5424719451
870UbiquitinationWKVRRSQKLDMSARL
HHHHHHCCCCHHHHH
47.93-
881PhosphorylationSARLELQSALEAEIR
HHHHHHHHHHHHHHH
47.66-
890UbiquitinationLEAEIRAKQLVQEEL
HHHHHHHHHHHHHHH
34.02-
910UbiquitinationANLTLESKLKDSEAK
CCCCHHHHCCCCHHH
50.62-
914PhosphorylationLESKLKDSEAKNREL
HHHHCCCCHHHHHHH
37.5622496350
929UbiquitinationLEEMEILKKKMEEKF
HHHHHHHHHHHHHHH
56.88-
954PhosphorylationFQDSIFEYFNTAPLA
HHHHHHHHHHCCCCC
7.4422817900
968PhosphorylationAHDLTFRTSSASEQE
CCCCEEECCCCCCCC
23.8923911959
969PhosphorylationHDLTFRTSSASEQET
CCCEEECCCCCCCCC
21.4629116813
970PhosphorylationDLTFRTSSASEQETQ
CCEEECCCCCCCCCC
34.8925627689
984PhosphorylationQAPKPEASPSMSVAA
CCCCCCCCCCCCCHH
18.8225627689
986PhosphorylationPKPEASPSMSVAASE
CCCCCCCCCCCHHHH
22.6125627689
1029PhosphorylationKPKAHQFSIKSFSSP
CCCCEECEEECCCCC
23.6520873877
1083UbiquitinationPIPPEQSKRPLGVDV
CCCHHHCCCCCCCCC
58.70-
1099UbiquitinationRGIGTAYKGHVKVPK
CCCCCEECCCCCCCC
39.82-
1118PhosphorylationKKGWQRAYAVVCDCK
CCCHHHEEEEEECCE
11.3428152594
1135UbiquitinationLYDLPEGKSTQPGVI
EEECCCCCCCCCCEE
48.98-
1179PhosphorylationIPCIFRVTASLLGAP
CCEEEEEHHHHHCCC
13.2828857561
1181PhosphorylationCIFRVTASLLGAPSK
EEEEEHHHHHCCCCC
18.1128857561
1188UbiquitinationSLLGAPSKTSSLLIL
HHHCCCCCCCEEEEE
51.90-
1189PhosphorylationLLGAPSKTSSLLILT
HHCCCCCCCEEEEEE
28.0823403867
1190PhosphorylationLGAPSKTSSLLILTE
HCCCCCCCEEEEEEC
23.7921406692
1191PhosphorylationGAPSKTSSLLILTEN
CCCCCCCEEEEEECC
32.2123403867
1196PhosphorylationTSSLLILTENENEKR
CCEEEEEECCCCCCC
29.7521406692
1202UbiquitinationLTENENEKRKWVGIL
EECCCCCCCHHHHHH
71.50-
1280UbiquitinationVRAADCKKVHQIELA
EHHHHCCEEEEEEEC
51.81-
1337MethylationLMATATLKRNSGTCL
EEEEEEECCCCCCEE
45.22115973247
1337UbiquitinationLMATATLKRNSGTCL
EEEEEEECCCCCCEE
45.22-
1355PhosphorylationVKRLILCYEIQRTKP
EHHHHHHHHHHCCCC
16.78-
1524PhosphorylationCEPPRLIYFKSKFSG
CCCCEEEEEEECCCC
15.0025599653
1526MethylationPPRLIYFKSKFSGAV
CCEEEEEEECCCCCE
35.45115973255
1527PhosphorylationPRLIYFKSKFSGAVL
CEEEEEEECCCCCEE
29.0925599653
1528MethylationRLIYFKSKFSGAVLN
EEEEEEECCCCCEEC
44.1154395553
1528UbiquitinationRLIYFKSKFSGAVLN
EEEEEEECCCCCEEC
44.11-
1530PhosphorylationIYFKSKFSGAVLNVP
EEEEECCCCCEECCC
29.5823911959
1544UbiquitinationPDTSDNSKKQMLRTR
CCCCCCHHHHHHHHH
53.96-
1550PhosphorylationSKKQMLRTRSKRRFV
HHHHHHHHHHCCCCE
35.0229514088
1552PhosphorylationKQMLRTRSKRRFVFK
HHHHHHHHCCCCEEE
29.8729514088
1559UbiquitinationSKRRFVFKVPEEERL
HCCCCEEECCHHHHH
52.13-
1638PhosphorylationPPSRNKPYISWPSSG
CCCCCCCCEECCCCC
14.8121945579
1640PhosphorylationSRNKPYISWPSSGGS
CCCCCCEECCCCCCC
27.3921945579
1643PhosphorylationKPYISWPSSGGSEPS
CCCEECCCCCCCCCC
35.0421945579
1644PhosphorylationPYISWPSSGGSEPSV
CCEECCCCCCCCCCE
42.9921945579
1647PhosphorylationSWPSSGGSEPSVTVP
ECCCCCCCCCCEEEE
50.2721945579
1650PhosphorylationSSGGSEPSVTVPLRS
CCCCCCCCEEEECCC
26.7721945579
1652PhosphorylationGGSEPSVTVPLRSMS
CCCCCCEEEECCCCC
22.2721945579
1657PhosphorylationSVTVPLRSMSDPDQD
CEEEECCCCCCCCCC
30.2623403867
1659PhosphorylationTVPLRSMSDPDQDFD
EEECCCCCCCCCCCC
47.4325159151
1671PhosphorylationDFDKEPDSDSTKHST
CCCCCCCCCCCCCCC
44.1423403867
1673PhosphorylationDKEPDSDSTKHSTPS
CCCCCCCCCCCCCCC
43.2223403867
1674PhosphorylationKEPDSDSTKHSTPSN
CCCCCCCCCCCCCCC
37.4523403867
1677PhosphorylationDSDSTKHSTPSNSSN
CCCCCCCCCCCCCCC
43.5023927012
1678PhosphorylationSDSTKHSTPSNSSNP
CCCCCCCCCCCCCCC
30.3823927012
1680PhosphorylationSTKHSTPSNSSNPSG
CCCCCCCCCCCCCCC
49.8123927012
1682PhosphorylationKHSTPSNSSNPSGPP
CCCCCCCCCCCCCCC
35.5123927012
1683PhosphorylationHSTPSNSSNPSGPPS
CCCCCCCCCCCCCCC
57.9422167270
1686PhosphorylationPSNSSNPSGPPSPNS
CCCCCCCCCCCCCCC
69.0822167270
1690PhosphorylationSNPSGPPSPNSPHRS
CCCCCCCCCCCCCCC
39.5922167270
1693PhosphorylationSGPPSPNSPHRSQLP
CCCCCCCCCCCCCCC
26.0122167270
1697PhosphorylationSPNSPHRSQLPLEGL
CCCCCCCCCCCCCCC
32.7925159151
1711PhosphorylationLEQPACDT-------
CCCCCCCC-------
40.1529514088

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

Oops, there are no upstream regulatory protein records of MRCKB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL3_HUMANRPL3physical
17353931
DCD_HUMANDCDphysical
17353931
BRX1_HUMANBRIX1physical
17353931

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-363; THR-676;SER-1686; SER-1690 AND SER-1693, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-914; SER-1690 ANDSER-1693, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1196, AND MASSSPECTROMETRY.

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