| 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 |
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| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 166 | Phosphorylation | GDLLTLLSKFEDKLP HHHHHHHHHHHHCCC | 38.11 | 24719451 | |
| 221 | Phosphorylation | IRLADFGSCLKMNDD EEECCCCCCEEECCC | 19.10 | - | |
| 233 | Phosphorylation | NDDGTVQSSVAVGTP CCCCCEEECEECCCC | 23.57 | - | |
| 239 | Phosphorylation | QSSVAVGTPDYISPE EECEECCCCCCCCHH | 13.34 | 11283256 | |
| 244 | Phosphorylation | VGTPDYISPEILQAM CCCCCCCCHHHHHHH | 15.39 | - | |
| 304 | Phosphorylation | EERFQFPSHVTDVSE HHHCCCCCCCCCCCH | 31.70 | - | |
| 307 | Phosphorylation | FQFPSHVTDVSEEAK CCCCCCCCCCCHHHH | 25.84 | - | |
| 310 | Phosphorylation | PSHVTDVSEEAKDLI CCCCCCCCHHHHHHH | 32.31 | - | |
| 314 | Ubiquitination | TDVSEEAKDLIQRLI CCCCHHHHHHHHHHH | 57.24 | 21890473 | |
| 337 | Ubiquitination | QNGIEDFKKHAFFEG CCCHHHHHHHHHCCC | 56.84 | 21890473 | |
| 357 | Phosphorylation | IRNLEAPYIPDVSSP HHCCCCCCCCCCCCC | 31.94 | 30624053 | |
| 362 | Phosphorylation | APYIPDVSSPSDTSN CCCCCCCCCCCCCCC | 43.86 | 26657352 | |
| 363 | Phosphorylation | PYIPDVSSPSDTSNF CCCCCCCCCCCCCCC | 28.42 | 21082442 | |
| 365 | Phosphorylation | IPDVSSPSDTSNFDV CCCCCCCCCCCCCCC | 56.31 | 30624053 | |
| 367 | Phosphorylation | DVSSPSDTSNFDVDD CCCCCCCCCCCCCCC | 29.88 | 27732954 | |
| 368 | Phosphorylation | VSSPSDTSNFDVDDD CCCCCCCCCCCCCCH | 40.25 | 27732954 | |
| 417 | Phosphorylation | SDRGSLKSIMQSNTL CCCCCHHHHHHHCCC | 28.69 | - | |
| 421 | Phosphorylation | SLKSIMQSNTLTKDE CHHHHHHHCCCCCCH | 17.88 | 28857561 | |
| 423 | Phosphorylation | KSIMQSNTLTKDEDV HHHHHHCCCCCCHHH | 40.84 | 26657352 | |
| 426 | Ubiquitination | MQSNTLTKDEDVQRD HHHCCCCCCHHHHHH | 63.33 | 21890473 | |
| 454 | Ubiquitination | IRRLEQEKLELSRKL HHHHHHHHHHHHHHH | 47.13 | - | |
| 460 | Ubiquitination | EKLELSRKLQESTQT HHHHHHHHHHHHHHH | 51.66 | - | |
| 464 | Phosphorylation | LSRKLQESTQTVQSL HHHHHHHHHHHHHHH | 16.92 | 24275569 | |
| 465 | Phosphorylation | SRKLQESTQTVQSLH HHHHHHHHHHHHHHH | 27.75 | 23312004 | |
| 467 | Phosphorylation | KLQESTQTVQSLHGS HHHHHHHHHHHHHHH | 22.17 | 23312004 | |
| 470 | Phosphorylation | ESTQTVQSLHGSSRA HHHHHHHHHHHHHHH | 20.28 | 24275569 | |
| 474 | Phosphorylation | TVQSLHGSSRALSNS HHHHHHHHHHHHHCC | 13.10 | 24275569 | |
| 475 | Phosphorylation | VQSLHGSSRALSNSN HHHHHHHHHHHHCCC | 26.60 | 28857561 | |
| 479 | Phosphorylation | HGSSRALSNSNRDKE HHHHHHHHCCCHHHH | 36.91 | 26699800 | |
| 481 | Phosphorylation | SSRALSNSNRDKEIK HHHHHHCCCHHHHHH | 29.84 | 27422710 | |
| 489 | Acetylation | NRDKEIKKLNEEIER CHHHHHHHHHHHHHH | 63.31 | 20167786 | |
| 524 | Phosphorylation | LRQEREDSTQRLRGL HHHHCHHHHHHHHHH | 22.99 | - | |
| 571 | Malonylation | KDAHQQRKLALQEFS HHHHHHHHHHHHHHH | 33.50 | 26320211 | |
| 571 | Ubiquitination | KDAHQQRKLALQEFS HHHHHHHHHHHHHHH | 33.50 | - | |
| 605 | Sulfoxidation | LRDKEEEMEVATQKV HHCHHHHHHHHHHHH | 5.93 | 30846556 | |
| 641 | Phosphorylation | DDAVAEASKERKLRE HHHHHHHHHHHHHHH | 26.93 | - | |
| 642 | Ubiquitination | DAVAEASKERKLREH HHHHHHHHHHHHHHH | 69.46 | - | |
| 659 | Phosphorylation | NFCKQMESELEALKV HHHHHHHHHHHHHHC | 41.98 | - | |
| 665 | Ubiquitination | ESELEALKVKQGGRG HHHHHHHHCCCCCCC | 55.20 | - | |
| 671 | Methylation | LKVKQGGRGAGATLE HHCCCCCCCCCCCHH | 38.32 | 24129315 | |
| 676 | Phosphorylation | GGRGAGATLEHQQEI CCCCCCCCHHHHHHH | 31.59 | 25159151 | |
| 697 | Phosphorylation | LEKKVLFYEEELVRR HHHHHHHCHHHHHHH | 20.47 | 27642862 | |
| 707 | Phosphorylation | ELVRREASHVLEVKN HHHHHHHHHHEEEEC | 14.91 | - | |
| 757 | Phosphorylation | EMEEAVGTIKDKYER HHHHHHHHHHHHHHH | 20.46 | 28060719 | |
| 789 | Ubiquitination | KLCSFVDKLTAQNRQ HHHHHHHHHHHHHHH | 42.30 | - | |
| 807 | Ubiquitination | ELQDLAAKKESVAHW HHHHHHHHHHHHHHH | 52.01 | - | |
| 834 | Phosphorylation | DEKDARGYLQALASK CCCCHHHHHHHHHHH | 7.06 | 27174698 | |
| 840 | Phosphorylation | GYLQALASKMTEELE HHHHHHHHHHHHHHH | 24.66 | 27174698 | |
| 843 | Phosphorylation | QALASKMTEELEALR HHHHHHHHHHHHHHH | 30.00 | 19664994 | |
| 851 | Phosphorylation | EELEALRSSSLGSRT HHHHHHHHCCCCCCC | 25.73 | 20068231 | |
| 852 | Phosphorylation | ELEALRSSSLGSRTL HHHHHHHCCCCCCCC | 24.13 | 20068231 | |
| 853 | Phosphorylation | LEALRSSSLGSRTLD HHHHHHCCCCCCCCC | 37.69 | 22210691 | |
| 856 | Phosphorylation | LRSSSLGSRTLDPLW HHHCCCCCCCCCHHH | 27.64 | 23898821 | |
| 858 | Phosphorylation | SSSLGSRTLDPLWKV HCCCCCCCCCHHHHH | 36.89 | 23403867 | |
| 864 | Ubiquitination | RTLDPLWKVRRSQKL CCCCHHHHHHHHCCC | 33.28 | 21890473 | |
| 864 | Ubiquitination | RTLDPLWKVRRSQKL CCCCHHHHHHHHCCC | 33.28 | 21890473 | |
| 868 | Phosphorylation | PLWKVRRSQKLDMSA HHHHHHHHCCCCHHH | 22.54 | 24719451 | |
| 870 | Ubiquitination | WKVRRSQKLDMSARL HHHHHHCCCCHHHHH | 47.93 | - | |
| 881 | Phosphorylation | SARLELQSALEAEIR HHHHHHHHHHHHHHH | 47.66 | - | |
| 890 | Ubiquitination | LEAEIRAKQLVQEEL HHHHHHHHHHHHHHH | 34.02 | - | |
| 910 | Ubiquitination | ANLTLESKLKDSEAK CCCCHHHHCCCCHHH | 50.62 | - | |
| 914 | Phosphorylation | LESKLKDSEAKNREL HHHHCCCCHHHHHHH | 37.56 | 22496350 | |
| 929 | Ubiquitination | LEEMEILKKKMEEKF HHHHHHHHHHHHHHH | 56.88 | - | |
| 954 | Phosphorylation | FQDSIFEYFNTAPLA HHHHHHHHHHCCCCC | 7.44 | 22817900 | |
| 968 | Phosphorylation | AHDLTFRTSSASEQE CCCCEEECCCCCCCC | 23.89 | 23911959 | |
| 969 | Phosphorylation | HDLTFRTSSASEQET CCCEEECCCCCCCCC | 21.46 | 29116813 | |
| 970 | Phosphorylation | DLTFRTSSASEQETQ CCEEECCCCCCCCCC | 34.89 | 25627689 | |
| 984 | Phosphorylation | QAPKPEASPSMSVAA CCCCCCCCCCCCCHH | 18.82 | 25627689 | |
| 986 | Phosphorylation | PKPEASPSMSVAASE CCCCCCCCCCCHHHH | 22.61 | 25627689 | |
| 1029 | Phosphorylation | KPKAHQFSIKSFSSP CCCCEECEEECCCCC | 23.65 | 20873877 | |
| 1083 | Ubiquitination | PIPPEQSKRPLGVDV CCCHHHCCCCCCCCC | 58.70 | - | |
| 1099 | Ubiquitination | RGIGTAYKGHVKVPK CCCCCEECCCCCCCC | 39.82 | - | |
| 1118 | Phosphorylation | KKGWQRAYAVVCDCK CCCHHHEEEEEECCE | 11.34 | 28152594 | |
| 1135 | Ubiquitination | LYDLPEGKSTQPGVI EEECCCCCCCCCCEE | 48.98 | - | |
| 1179 | Phosphorylation | IPCIFRVTASLLGAP CCEEEEEHHHHHCCC | 13.28 | 28857561 | |
| 1181 | Phosphorylation | CIFRVTASLLGAPSK EEEEEHHHHHCCCCC | 18.11 | 28857561 | |
| 1188 | Ubiquitination | SLLGAPSKTSSLLIL HHHCCCCCCCEEEEE | 51.90 | - | |
| 1189 | Phosphorylation | LLGAPSKTSSLLILT HHCCCCCCCEEEEEE | 28.08 | 23403867 | |
| 1190 | Phosphorylation | LGAPSKTSSLLILTE HCCCCCCCEEEEEEC | 23.79 | 21406692 | |
| 1191 | Phosphorylation | GAPSKTSSLLILTEN CCCCCCCEEEEEECC | 32.21 | 23403867 | |
| 1196 | Phosphorylation | TSSLLILTENENEKR CCEEEEEECCCCCCC | 29.75 | 21406692 | |
| 1202 | Ubiquitination | LTENENEKRKWVGIL EECCCCCCCHHHHHH | 71.50 | - | |
| 1280 | Ubiquitination | VRAADCKKVHQIELA EHHHHCCEEEEEEEC | 51.81 | - | |
| 1337 | Methylation | LMATATLKRNSGTCL EEEEEEECCCCCCEE | 45.22 | 115973247 | |
| 1337 | Ubiquitination | LMATATLKRNSGTCL EEEEEEECCCCCCEE | 45.22 | - | |
| 1355 | Phosphorylation | VKRLILCYEIQRTKP EHHHHHHHHHHCCCC | 16.78 | - | |
| 1524 | Phosphorylation | CEPPRLIYFKSKFSG CCCCEEEEEEECCCC | 15.00 | 25599653 | |
| 1526 | Methylation | PPRLIYFKSKFSGAV CCEEEEEEECCCCCE | 35.45 | 115973255 | |
| 1527 | Phosphorylation | PRLIYFKSKFSGAVL CEEEEEEECCCCCEE | 29.09 | 25599653 | |
| 1528 | Methylation | RLIYFKSKFSGAVLN EEEEEEECCCCCEEC | 44.11 | 54395553 | |
| 1528 | Ubiquitination | RLIYFKSKFSGAVLN EEEEEEECCCCCEEC | 44.11 | - | |
| 1530 | Phosphorylation | IYFKSKFSGAVLNVP EEEEECCCCCEECCC | 29.58 | 23911959 | |
| 1544 | Ubiquitination | PDTSDNSKKQMLRTR CCCCCCHHHHHHHHH | 53.96 | - | |
| 1550 | Phosphorylation | SKKQMLRTRSKRRFV HHHHHHHHHHCCCCE | 35.02 | 29514088 | |
| 1552 | Phosphorylation | KQMLRTRSKRRFVFK HHHHHHHHCCCCEEE | 29.87 | 29514088 | |
| 1559 | Ubiquitination | SKRRFVFKVPEEERL HCCCCEEECCHHHHH | 52.13 | - | |
| 1638 | Phosphorylation | PPSRNKPYISWPSSG CCCCCCCCEECCCCC | 14.81 | 21945579 | |
| 1640 | Phosphorylation | SRNKPYISWPSSGGS CCCCCCEECCCCCCC | 27.39 | 21945579 | |
| 1643 | Phosphorylation | KPYISWPSSGGSEPS CCCEECCCCCCCCCC | 35.04 | 21945579 | |
| 1644 | Phosphorylation | PYISWPSSGGSEPSV CCEECCCCCCCCCCE | 42.99 | 21945579 | |
| 1647 | Phosphorylation | SWPSSGGSEPSVTVP ECCCCCCCCCCEEEE | 50.27 | 21945579 | |
| 1650 | Phosphorylation | SSGGSEPSVTVPLRS CCCCCCCCEEEECCC | 26.77 | 21945579 | |
| 1652 | Phosphorylation | GGSEPSVTVPLRSMS CCCCCCEEEECCCCC | 22.27 | 21945579 | |
| 1657 | Phosphorylation | SVTVPLRSMSDPDQD CEEEECCCCCCCCCC | 30.26 | 23403867 | |
| 1659 | Phosphorylation | TVPLRSMSDPDQDFD EEECCCCCCCCCCCC | 47.43 | 25159151 | |
| 1671 | Phosphorylation | DFDKEPDSDSTKHST CCCCCCCCCCCCCCC | 44.14 | 23403867 | |
| 1673 | Phosphorylation | DKEPDSDSTKHSTPS CCCCCCCCCCCCCCC | 43.22 | 23403867 | |
| 1674 | Phosphorylation | KEPDSDSTKHSTPSN CCCCCCCCCCCCCCC | 37.45 | 23403867 | |
| 1677 | Phosphorylation | DSDSTKHSTPSNSSN CCCCCCCCCCCCCCC | 43.50 | 23927012 | |
| 1678 | Phosphorylation | SDSTKHSTPSNSSNP CCCCCCCCCCCCCCC | 30.38 | 23927012 | |
| 1680 | Phosphorylation | STKHSTPSNSSNPSG CCCCCCCCCCCCCCC | 49.81 | 23927012 | |
| 1682 | Phosphorylation | KHSTPSNSSNPSGPP CCCCCCCCCCCCCCC | 35.51 | 23927012 | |
| 1683 | Phosphorylation | HSTPSNSSNPSGPPS CCCCCCCCCCCCCCC | 57.94 | 22167270 | |
| 1686 | Phosphorylation | PSNSSNPSGPPSPNS CCCCCCCCCCCCCCC | 69.08 | 22167270 | |
| 1690 | Phosphorylation | SNPSGPPSPNSPHRS CCCCCCCCCCCCCCC | 39.59 | 22167270 | |
| 1693 | Phosphorylation | SGPPSPNSPHRSQLP CCCCCCCCCCCCCCC | 26.01 | 22167270 | |
| 1697 | Phosphorylation | SPNSPHRSQLPLEGL CCCCCCCCCCCCCCC | 32.79 | 25159151 | |
| 1711 | Phosphorylation | LEQPACDT------- CCCCCCCC------- | 40.15 | 29514088 |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MRCKB_HUMAN !! | ||||||
* 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 !! | ||||||
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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. | |