Overview
| Uniprot ID | Q9Y5S2 |
| Protein Name | Serine/threonine-protein kinase MRCK beta |
| Gene Name | CDC42BPB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 426 |
MQSNTLTKDEDVQRD |
Function
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, PubMed:21949762). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates PPP1R12A (PubMed:21457715). 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 (By similarity)
Protein Sequence
10
MSAKVRLKKL
20
EQLLLDGPWR
30
NESALSVETL
40
LDVLVCLYTE
50
CSHSALRRDK
60
YVAEFLEWAK
70
PFTQLVKEMQ
80
LHREDFEIIK
90
VIGRGAFGEV
100
AVVKMKNTER
110
IYAMKILNKW
120
EMLKRAETAC
130
FREERDVLVN
140
GDCQWITALH
150
YAFQDENHLY
160
LVMDYYVGGD
170
LLTLLSKFED
180
KLPEDMARFY
190
IGEMVLAIDS
200
IHQLHYVHRD
210
IKPDNVLLDV
220
NGHIRLADFG
230
SCLKMNDDGT
240
VQSSVAVGTP
250
DYISPEILQA
260
MEDGMGKYGP
270
ECDWWSLGVC
280
MYEMLYGETP
290
FYAESLVETY
300
GKIMNHEERF
310
QFPSHVTDVS
320
EEAKDLIQRL
330
ICSRERRLGQ
340
NGIEDFKKHA
350
FFEGLNWENI
360
RNLEAPYIPD
370
VSSPSDTSNF
380
DVDDDVLRNT
390
EILPPGSHTG
400
FSGLHLPFIG
410
FTFTTESCFS
420
DRGSLKSIMQ
430
SNTLTKDEDV
440
QRDLEHSLQM
450
EAYERRIRRL
460
EQEKLELSRK
470
LQESTQTVQS
480
LHGSSRALSN
490
SNRDKEIKKL
500
NEEIERLKNK
510
IADSNRLERQ
520
LEDTVALRQE
530
REDSTQRLRG
540
LEKQHRVVRQ
550
EKEELHKQLV
560
EASERLKSQA
570
KELKDAHQQR
580
KLALQEFSEL
590
NERMAELRAQ
600
KQKVSRQLRD
610
KEEEMEVATQ
620
KVDAMRQEMR
630
RAEKLRKELE
640
AQLDDAVAEA
650
SKERKLREHS
660
ENFCKQMESE
670
LEALKVKQGG
680
RGAGATLEHQ
690
QEISKIKSEL
700
EKKVLFYEEE
710
LVRREASHVL
720
EVKNVKKEVH
730
DSESHQLALQ
740
KEILMLKDKL
750
EKSKRERHNE
760
MEEAVGTIKD
770
KYERERAMLF
780
DENKKLTAEN
790
EKLCSFVDKL
800
TAQNRQLEDE
810
LQDLAAKKES
820
VAHWEAQIAE
830
IIQWVSDEKD
840
ARGYLQALAS
850
KMTEELEALR
860
SSSLGSRTLD
870
PLWKVRRSQK
880
LDMSARLELQ
890
SALEAEIRAK
900
QLVQEELRKV
910
KDANLTLESK
920
LKDSEAKNRE
930
LLEEMEILKK
940
KMEEKFRADT
950
GLKLPDFQDS
960
IFEYFNTAPL
970
AHDLTFRTSS
980
ASEQETQAPK
990
PEASPSMSVA
1000
ASEQQEDMAR
1010
PPQRPSAVPL
1020
PTTQALALAG
1030
PKPKAHQFSI
1040
KSFSSPTQCS
1050
HCTSLMVGLI
1060
RQGYACEVCS
1070
FACHVSCKDG
1080
APQVCPIPPE
1090
QSKRPLGVDV
1100
QRGIGTAYKG
1110
HVKVPKPTGV
1120
KKGWQRAYAV
1130
VCDCKLFLYD
1140
LPEGKSTQPG
1150
VIASQVLDLR
1160
DDEFSVSSVL
1170
ASDVIHATRR
1180
DIPCIFRVTA
1190
SLLGAPSKTS
1200
SLLILTENEN
1210
EKRKWVGILE
1220
GLQSILHKNR
1230
LRNQVVHVPL
1240
EAYDSSLPLI
1250
KAILTAAIVD
1260
ADRIAVGLEE
1270
GLYVIEVTRD
1280
VIVRAADCKK
1290
VHQIELAPRE
1300
KIVILLCGRN
1310
HHVHLYPWSS
1320
LDGAEGSFDI
1330
KLPETKGCQL
1340
MATATLKRNS
1350
GTCLFVAVKR
1360
LILCYEIQRT
1370
KPFHRKFNEI
1380
VAPGSVQCLA
1390
VLRDRLCVGY
1400
PSGFCLLSIQ
1410
GDGQPLNLVN
1420
PNDPSLAFLS
1430
QQSFDALCAV
1440
ELESEEYLLC
1450
FSHMGLYVDP
1460
QGRRARAQEL
1470
MWPAAPVACS
1480
CSPTHVTVYS
1490
EYGVDVFDVR
1500
TMEWVQTIGL
1510
RRIRPLNSEG
1520
TLNLLNCEPP
1530
RLIYFKSKFS
1540
GAVLNVPDTS
1550
DNSKKQMLRT
1560
RSKRRFVFKV
1570
PEEERLQQRR
1580
EMLRDPELRS
1590
KMISNPTNFN
1600
HVAHMGPGDG
1610
MQVLMDLPLS
1620
AVPPSQEERP
1630
GPAPTNLARQ
1640
PPSRNKPYIS
1650
WPSSGGSEPS
1660
VTVPLRSMSD
1670
PDQDFDKEPD
1680
SDSTKHSTPS
1690
NSSNPSGPPS
1700
PNSPHRSQLP
1710
LEGLEQPACD
T
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0042641 |
actomyosin |
| Cellular Component |
GO:0031252 |
cell leading edge |
| Cellular Component |
GO:0005911 |
cell-cell junction |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005856 |
cytoskeleton |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0030027 |
lamellipodium |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0000287 |
magnesium ion binding |
| Molecular Function |
GO:0004672 |
protein kinase activity |
| Molecular Function |
GO:0106310 |
protein serine kinase activity |
| Molecular Function |
GO:0004674 |
protein serine/threonine kinase activity |
| Molecular Function |
GO:0044877 |
protein-containing complex binding |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0030036 |
actin cytoskeleton organization |
| Biological Process |
GO:0031032 |
actomyosin structure organization |
| Biological Process |
GO:0016477 |
cell migration |
| Biological Process |
GO:0007010 |
cytoskeleton organization |
| Biological Process |
GO:0007163 |
establishment or maintenance of cell polarity |
| Biological Process |
GO:0006468 |
protein phosphorylation |
| Biological Process |
GO:0007165 |
signal transduction |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.