Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase MRCK beta

Gene

Cdc42bpb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Mg2+By similarity

Enzyme regulationi

Maintained in an inactive, closed conformation by an interaction between the kinase domain and the negative autoregulatory C-terminal coiled-coil region. Agonist binding to the phorbol ester binding site disrupts this, releasing the kinase domain to allow N-terminus-mediated dimerization and kinase activation by transautophosphorylation. Inhibited by chelerythrine chloride (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei105ATPPROSITE-ProRule annotationBy similarity1
Active sitei200Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi82 – 90ATPPROSITE-ProRule annotationBy similarity9
Zinc fingeri1026 – 1076Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase MRCK beta (EC:2.7.11.1)
Alternative name(s):
CDC42-binding protein kinase beta
DMPK-like beta
Myotonic dystrophy kinase-related CDC42-binding kinase beta
Short name:
MRCK beta
Short name:
Myotonic dystrophy protein kinase-like beta
Gene namesi
Name:Cdc42bpbImported
Synonyms:Kiaa1124Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2136459. Cdc42bpb.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000863951 – 1713Serine/threonine-protein kinase MRCK betaAdd BLAST1713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221Phosphoserine; by autocatalysisBy similarity1
Modified residuei233Phosphoserine; by autocatalysisBy similarity1
Modified residuei239Phosphothreonine; by autocatalysisBy similarity1
Modified residuei423PhosphothreonineBy similarity1
Modified residuei671Omega-N-methylarginineBy similarity1
Modified residuei927PhosphoserineCombined sources1
Modified residuei954PhosphotyrosineCombined sources1
Modified residuei1682PhosphoserineBy similarity1
Modified residuei1684PhosphoserineBy similarity1
Modified residuei1688PhosphoserineCombined sources1
Modified residuei1692PhosphoserineCombined sources1
Modified residuei1695PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ7TT50.
PaxDbiQ7TT50.
PRIDEiQ7TT50.

PTM databases

iPTMnetiQ7TT50.
PhosphoSitePlusiQ7TT50.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021279.
CleanExiMM_CDC42BPB.
GenevisibleiQ7TT50. MM.

Interactioni

Subunit structurei

Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42. Interacts with TJP1; this interaction requires the presence of catalytically active CDC42. Forms a tripartite complex with MYO18A and LURAP1 with the latter acting as an adapter connecting CDC42BPB and MYO18A. LURAP1 binding results in activation of CDC42BPB by abolition of its negative autoregulation. Interacts with STRIP1, STRN3 and SIKE1 (By similarity). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with LURAP1 (By similarity). Interacts (via AGC-kinase C-terminal domain) with FAM89B/LRAP25 (via LRR repeat)(PubMed:25107909). Forms a tripartite complex with FAM89B/LRAP25 and LIMK1 (PubMed:25107909).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229972. 3 interactors.
IntActiQ7TT50. 1 interactor.
STRINGi10090.ENSMUSP00000042565.

Structurei

3D structure databases

ProteinModelPortaliQ7TT50.
SMRiQ7TT50.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 342Protein kinasePROSITE-ProRule annotationBy similarityAdd BLAST267
Domaini343 – 413AGC-kinase C-terminalAdd BLAST71
Domaini1096 – 1215PHPROSITE-ProRule annotationAdd BLAST120
Domaini1241 – 1515CNHPROSITE-ProRule annotationAdd BLAST275
Domaini1585 – 1598CRIBPROSITE-ProRule annotationAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili434 – 649Sequence analysisAdd BLAST216
Coiled coili681 – 815Sequence analysisAdd BLAST135
Coiled coili878 – 939Sequence analysisAdd BLAST62

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1026 – 1076Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IT51. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ7TT50.
KOiK16307.
OMAiDSAPQVC.
OrthoDBiEOG091G09EX.
TreeFamiTF313551.

Family and domain databases

CDDicd00029. C1. 1 hit.
cd00132. CRIB. 1 hit.
Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiView protein in InterPro
IPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR036936. CRIB_dom_sf.
IPR020454. DAG/PE-bd.
IPR031597. KELK.
IPR011009. Kinase-like_dom_sf.
IPR033232. MRCK_beta.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH-like_dom_sf.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PANTHERiPTHR22988:SF34. PTHR22988:SF34. 1 hit.
PfamiView protein in Pfam
PF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 1 hit.
PF00069. Pkinase. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
SMARTiView protein in SMART
SM00109. C1. 1 hit.
SM00036. CNH. 1 hit.
SM00285. PBD. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS51285. AGC_KINASE_CTER. 1 hit.
PS50219. CNH. 1 hit.
PS50108. CRIB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7TT50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKVRLKKL EQLLLDGPWR NDSALSVETL LDVLVCLYTE CSHSALRRDK
60 70 80 90 100
YVAEFLEWAK PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER
110 120 130 140 150
IYAMKILNKW EMLKRAETAC FREERDVLVN GDCQWITALH YAFQDENYLY
160 170 180 190 200
LVMDYYVGGD LLTLLSKFED KLPEDMARFY IGEMVLAIDS IHQLHYVHRD
210 220 230 240 250
IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP DYISPEILQA
260 270 280 290 300
MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
310 320 330 340 350
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI
360 370 380 390 400
RNLEAPYIPD VSSPSDTSNF DVDDDMLRNI EILPPGSHTG FSGLHLPFIG
410 420 430 440 450
FTFTTESCFS DRGSLKSMTQ SNTLTKDEDV QRDLENSLQI EAYERRIRRL
460 470 480 490 500
EQEKLELSRK LQESTQTVQS LHGSTRALGN SNRDKEIKRL NEELERMKSK
510 520 530 540 550
MADSNRLERQ LEDTVTLRQE HEDSTHRLKG LEKQYRLARQ EKEELHKQLV
560 570 580 590 600
EASERLKSQT KELKDAHQQR KRALQEFSEL NERMSELRSL KQKVSRQLRD
610 620 630 640 650
KEEEMEVAMQ KIDSMRQDLR KSEKSRKELE ARLEDAAAEA SKERKLREHS
660 670 680 690 700
ESFCKQMERE LEALKVKQGG RGPGAASEHQ QEISKIRSEL EKKVLFYEEE
710 720 730 740 750
LVRREASHVL EVKNVKKEVH DSESHQLALQ KEVLMLKDKL EKSKRERHSE
760 770 780 790 800
MEEAIGTVKD KYERERAMLF DENKKLTAEN EKLCSFVDKL TAQNRQLEDE
810 820 830 840 850
LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS KMTEELETLR
860 870 880 890 900
SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV
910 920 930 940 950
KDSSLAFESK LKESEAKNRE LLEEMQSLRK RMEEKFRADT GLKLPDFQDS
960 970 980 990 1000
IFEYFNTAPL AHDLTFRTSS ASDQETQASK MDLSPSVSVA TSTEQQEDMA
1010 1020 1030 1040 1050
RPQQRPSPVP LPSTQALAMA GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL
1060 1070 1080 1090 1100
IRQGYACEVC AFSCHVSCKD SAPQVCPIPP EQSKRPLGVD VQRGIGTAYK
1110 1120 1130 1140 1150
GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP GVVASQVLDL
1160 1170 1180 1190 1200
RDEEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
1210 1220 1230 1240 1250
NEKRKWVGIL EGLQAILHKN RLKSQVVHVA QEAYDSSLPL IKAVLAAAIV
1260 1270 1280 1290 1300
DGDRIAVGLE EGLYVIELTR DVIVRAADCK KVYQIELAPK EKIAILLCGR
1310 1320 1330 1340 1350
NHHVHLYPWS SFDGAEASNF DIKLPETKGC QLIATGTLRK SSSTCLFVAV
1360 1370 1380 1390 1400
KRLILCYEIQ RTKPFHRKFS ELVAPGHVQW MAVFKDRLCV GYPSGFSLLS
1410 1420 1430 1440 1450
IQGDGPPLDL VNPTDPSLAF LSQQSFDALC AVELKSEEYL LCFSHMGLYV
1460 1470 1480 1490 1500
DPQGRRSRMQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI
1510 1520 1530 1540 1550
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTILNVPD TSDNSKKQML
1560 1570 1580 1590 1600
RTRSKRRFVF KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG
1610 1620 1630 1640 1650
DGMQVLMDLP LSAAPTVQEE KQGPTPAGLP RQPPSRSKPY VSWPSSGGSE
1660 1670 1680 1690 1700
PGVPVPLRSM SDPDQDFDKE PDSDSTKHST PSNSSNPSGP PSPNSPHRSQ
1710
LPMEGLDQPS CDA
Length:1,713
Mass (Da):194,753
Last modified:July 27, 2011 - v2
Checksum:iCD809A3743986A4D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96K → R in AAP34402 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY277589 mRNA. Translation: AAP34402.1.
AC127580 Genomic DNA. No translation available.
AK173103 mRNA. Translation: BAD32381.1.
BC049921 mRNA. Translation: AAH49921.1.
CCDSiCCDS26176.1.
RefSeqiNP_898837.2. NM_183016.2.
UniGeneiMm.27397.

Genome annotation databases

EnsembliENSMUST00000041965; ENSMUSP00000042565; ENSMUSG00000021279.
GeneIDi217866.
KEGGimmu:217866.
UCSCiuc007pct.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiMRCKB_MOUSE
AccessioniPrimary (citable) accession number: Q7TT50
Secondary accession number(s): E9QK15, Q69ZR5, Q80W33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 27, 2011
Last modified: November 22, 2017
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families