Overview
| Uniprot ID | A0A287AY04 |
| Protein Name | Serine/threonine-protein kinase MRCK beta |
| Gene Name | CDC42BPB |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 1198 |
VRVADYKKVYQIELA |
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. In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Phosphorylates PPP1R12A. 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
Protein Sequence
10
MSAKVRLKKL
20
EQLLLDGPWR
30
NESALSVETL
40
LDVLVCLYTE
50
CSHSALRRDK
60
YVAEFLEWAK
70
PFTQLVKEMQ
80
LHREDFEIIK
90
VIGRGAFGEV
100
AVVRMKSTER
110
IYAMKILNKW
120
EMLKRAETAC
130
FREERDVLVN
140
GDSQWLTTLH
150
YAFQDENYLY
160
LVMDYYVGGD
170
LLTLLSKFED
180
RLPEDMARFY
190
IGEMVLAIDS
200
IHQLHYVHRD
210
IKPDNVLLDV
220
NGHIRLADFG
230
SCLKMNDDGT
240
VQSSVAVGTP
250
DYISPEILQA
260
MEDGMGRYGP
270
ECDWWSLGVC
280
MYEMLYGETP
290
FYAESLVETY
300
GKIMNHEEIL
310
PPASHTGFSG
320
LHLPFIGFTF
330
TTESCFSDRG
340
SLKSIMQSST
350
LTKDEGLQRD
360
LENSLQVEAY
370
ERRIRRLEQE
380
RLELSRKLQE
390
ATQTVQSFHG
400
AARTLGSAAR
410
DKEIKKLNEE
420
IERLKNKIAE
430
SNKLERQLED
440
TVTLRQEQED
450
STHRLKGLEK
460
QYRAVRQEKE
470
DFHKQLIEAS
480
ERLKSQAREL
490
KDAHQQRKLA
500
LQEFSELNER
510
MAELRSQKQK
520
VSRQLRDREE
530
EVEAALQKID
540
ALRQEVRRAD
550
KCRKELEAQL
560
EDAVAEASKE
570
RKLREHSENF
580
SKQIESELEA
590
LKMKQGGRGP
600
GAALEHQQEI
610
SRIKSELEKK
620
VLFYEEELVR
630
REASHVLELK
640
TVKKEVHDSE
650
GHQLALQKEV
660
LVLKDKLEKS
670
KRERHSELEE
680
AVGTVKDKYE
690
RERAVLSEEN
700
KKLTAENEKL
710
CAFVDKLTAQ
720
NRQLEDELQD
730
LAAKKESVAH
740
WEAQIAEIIQ
750
WVSDEKDARG
760
YLQALASKMT
770
EELEALRSSS
780
LGSRTLDPLW
790
KVRRSQKLDM
800
SARLELQSAL
810
EAEIRAKQLV
820
QEELRKVKDM
830
NLSFESKLKD
840
SEAKNRELLE
850
EMEILKKKME
860
EKFRTDAGLK
870
LPDFQDSIFE
880
YFNTAPLAHD
890
LTFRASSASE
900
QETQAAKPEA
910
MPPSSVAAST
920
EQQEDVARAP
930
QRPPTVPLPS
940
TQALALAGPK
950
PKAHQFSIKS
960
FSSPTQCSHC
970
TSLMVGLIRQ
980
GYACDVCSFA
990
CHVSCRDSAP
1000
QVCPIPPEQS
1010
KRPLGVDVQR
1020
GIGTAYKGYV
1030
KVPKPTGVKK
1040
GWQRAYAVVC
1050
DCKLFLYDLP
1060
EGKSTQPGVV
1070
ASQVLDLRDE
1080
EFSVSSVLAS
1090
DVIHASRRDI
1100
PCIFRVTASL
1110
LGTPSKTSSL
1120
LILTENENEK
1130
RKWVGILEGL
1140
QSILQKNRLR
1150
SQVVHSPQEA
1160
YDSSLPLIKA
1170
VLAAAILDAD
1180
RIAVGLEEGL
1190
YVVEVTRDVI
1200
VRVADYKKVY
1210
QIELAPKEKV
1220
AALLCGRNHH
1230
VHLCPWSSFD
1240
GAEGTVDIKL
1250
PETKGCQLIA
1260
TGAPKKSSPT
1270
CLFVAVKRLV
1280
LCYEMQRTKP
1290
FHRKLSELAA
1300
PGPVQWMAVL
1310
KDKLCVGYPS
1320
GFSLLSPQGE
1330
GQALNLVNPN
1340
DPSLTFLSQQ
1350
SFDALCAVEL
1360
QSEEYLLCFS
1370
HMGLYVDPQG
1380
RRSRMQELMW
1390
PAAPVACSCS
1400
PSHVTVYSDY
1410
GVDVFDARSM
1420
EWVQTIGLRR
1430
IRPLNSEGSL
1440
NLLNCEPPRL
1450
IYFKSKFAGP
1460
ALNVPDTSDN
1470
SKKQMLRTRS
1480
KRRFVFKVPE
1490
EERLQQRREM
1500
LRDPELRSRM
1510
ISNPTNFNHV
1520
AHMGPGDGMQ
1530
VLMDLPLSAV
1540
PPSQEERPGP
1550
APASLSRQPP
1560
PRNKPYVSWP
1570
SSGGSEPGVA
1580
VPLRSMSDPD
1590
QDFDKEPDSD
1600
STKHSTPSNS
1610
SNPSGPPSPN
1620
SPHRSQLPLE
GLEQPSYDA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0042641 |
actomyosin |
| Cellular Component |
GO:0070161 |
anchoring junction |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0030027 |
lamellipodium |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0004674 |
protein serine/threonine kinase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0031032 |
actomyosin structure organization |
| Biological Process |
GO:0016477 |
cell migration |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.