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Protein

Serine/threonine-protein kinase MRCK beta

Gene

Cdc42bpb

Organism
Rattus norvegicus (Rat)
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.3 Publications

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 (By similarity). Inhibited by chelerythrine chloride.By similarity1 Publication

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

  • actin cytoskeleton organization Source: RGD
  • actin cytoskeleton reorganization Source: UniProtKB
  • actomyosin structure organization Source: UniProtKB
  • cell migration Source: UniProtKB
  • intracellular signal transduction Source: InterPro
  • protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621753. Cdc42bpb.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
  • Cell junction 1 Publication

  • Note: Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity). Detected at the leading edge of migrating and wounded cells; this localization requires the presence of catalytically active CDC42.By similarity

GO - Cellular componenti

  • actomyosin Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell leading edge Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: Ensembl
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi952F → Q: Abolishes interaction with TJP1; when associated with Q-954. 1 Publication1
Mutagenesisi954Y → Q: Abolishes interaction with TJP1; when associated with Q-952. 1 Publication1
Mutagenesisi964L → Q: Abolishes interaction with TJP1; when associated with Q-966. 1 Publication1
Mutagenesisi966F → Q: Abolishes interaction with TJP1; when associated with Q-964. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000863961 – 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 residuei927PhosphoserineBy similarity1
Modified residuei954PhosphotyrosineBy similarity1
Modified residuei1682PhosphoserineBy similarity1
Modified residuei1684PhosphoserineBy similarity1
Modified residuei1688PhosphoserineCombined sources1
Modified residuei1692PhosphoserineCombined sources1
Modified residuei1695PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ7TT49.
PRIDEiQ7TT49.

PTM databases

iPTMnetiQ7TT49.
PhosphoSitePlusiQ7TT49.

Expressioni

Tissue specificityi

Expressed in all tissues examined with highest levels in lung and kidney.1 Publication

Gene expression databases

BgeeiENSRNOG00000009675.
ExpressionAtlasiQ7TT49. baseline and differential.
GenevisibleiQ7TT49. RN.

Interactioni

Subunit structurei

Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42 (By similarity). Interacts with TJP1; this interaction requires the presence of catalytically active CDC42 (PubMed:21240187). 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 (PubMed:18854160). Interacts with STRIP1, STRN3 and SIKE1 (By similarity). Interacts with CPNE4 (via VWFA domain) (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lurap1D4A8G34EBI-692673,EBI-2015467

GO - Molecular functioni

  • Rho GTPase binding Source: RGD

Protein-protein interaction databases

IntActiQ7TT49. 6 interactors.
STRINGi10116.ENSRNOP00000036487.

Structurei

3D structure databases

ProteinModelPortaliQ7TT49.
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 coili882 – 939Sequence analysisAdd BLAST58

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 CNH domain.PROSITE-ProRule annotation
Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

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.
InParanoidiQ7TT49.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG091G09EX.
PhylomeDBiQ7TT49.
TreeFamiTF313551.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR031597. KELK.
IPR011009. Kinase-like_dom.
IPR033232. MRCK_beta.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF34. PTHR22988:SF34. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
ProDomiPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00109. 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.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TT49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKVRLKKL EQLLLDGPWR NESSLSVETL 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 DVDDDVLRNI EILPPGSHTG FSGLHLPFIG
410 420 430 440 450
FTFTTESCFS DRGSLKSMIQ SNTLTKDEDV QRDLENSLQI EAYERRIRRL
460 470 480 490 500
EQEKLELSRK LQESTQTVQS LHGSTRALGN SNRDKEIKRL NEELERMKSK
510 520 530 540 550
MADSNRLERQ LEDTVTLRQE HEDSTQRLKG LEKQYRLARQ EKEELHKQLV
560 570 580 590 600
EASERLKSQT KELKDAHQQR KRALQEFSEL NERMAELRSQ KQKVSRQLRD
610 620 630 640 650
KEEEMEVAMQ KIDSMRQDIR KSEKSRKELE ARLEDAVAEA SKERKLREHS
660 670 680 690 700
ESFSKQMERE LETLKVKQGG RGPGATLEHQ QEISKIRSEL EKKVLFYEEE
710 720 730 740 750
LVRREASHVL EVKNVKKEVH ESESHQLALQ KEVLMLKDKL EKSKRERHSE
760 770 780 790 800
MEEAIGAMKD KYERERAMLF DENKKLTAEN EKLCSFVDKL TAQNRQLEDE
810 820 830 840 850
LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS KMTEELETLR
860 870 880 890 900
SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVHEELRKV
910 920 930 940 950
KDTSLAFESK LKESEAKNRE LLEEMQSLKK RMEEKFRADT GLKLPDFQDP
960 970 980 990 1000
IFEYFNTAPL AHDLTFRTSS ASDQETQASK LDLSPSVSVA TSTEQQEDAA
1010 1020 1030 1040 1050
RSQQRPSTVP LPNTQALAMA GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL
1060 1070 1080 1090 1100
IRQGYACEVC AFSCHVSCKD SAPQVCPIPP EQSKRPLGVD VQRGIGTAYK
1110 1120 1130 1140 1150
GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP GVIASQVLDL
1160 1170 1180 1190 1200
RDDEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
1210 1220 1230 1240 1250
NEKRKWVGIL EGLQAILHKN RLRSQVVHVA QEAYDSSLPL IKTVLAAAIV
1260 1270 1280 1290 1300
DGDRIAVGLE EGLYVIELTR DVIVRAADCK KVYQIELAPK EKLILLLCGR
1310 1320 1330 1340 1350
NHHVHLYPWT SFDGAEASNF DIKLPETKGC QLIATGTLRK SSSTCLFVAV
1360 1370 1380 1390 1400
KRLVLCYEIQ RTKPFHRKFN EIVAPGHVQW MAMFKDRLCV GYPSGFSLLS
1410 1420 1430 1440 1450
IQGDGQPLDL VNPADPSLAF LSQQSFDALC AVELKSEEYL LCFSHMGLYV
1460 1470 1480 1490 1500
DPQGRRSRTQ ELMWPAAPVA CSCSSSHVTV YSEYGVDVFD VRTMEWVQTI
1510 1520 1530 1540 1550
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTVLNVPD TSDNSKKQML
1560 1570 1580 1590 1600
RTRSKRRFVF KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG
1610 1620 1630 1640 1650
DGMQVLMDLP LSAAPTAQEE KQGPAPTGLP RQLPSRNKPY VSWPSSGGSE
1660 1670 1680 1690 1700
PGVPVPLRSM SDPDQDFDKE PDSDSTKHST PSNSSNPSGP PSPNSPHRSQ
1710
LPLEGLDQPA CDA
Length:1,713
Mass (Da):194,888
Last modified:October 1, 2003 - v1
Checksum:i80C999262C96DAA6
GO

Sequence cautioni

The sequence AAC02942 differs from that shown. Reason: Frameshift at positions 1613, 1633 and 1680.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti706A → R in AAC02942 (PubMed:9418861).Curated1
Sequence conflicti1523R → C in AAC02942 (PubMed:9418861).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021936 mRNA. Translation: AAC02942.1. Frameshift.
AY277590 mRNA. Translation: AAP34403.1.
PIRiT14050.
RefSeqiNP_446072.2. NM_053620.3.
UniGeneiRn.105815.

Genome annotation databases

EnsembliENSRNOT00000039059; ENSRNOP00000036487; ENSRNOG00000009675.
GeneIDi113960.
KEGGirno:113960.
UCSCiRGD:621753. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021936 mRNA. Translation: AAC02942.1. Frameshift.
AY277590 mRNA. Translation: AAP34403.1.
PIRiT14050.
RefSeqiNP_446072.2. NM_053620.3.
UniGeneiRn.105815.

3D structure databases

ProteinModelPortaliQ7TT49.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7TT49. 6 interactors.
STRINGi10116.ENSRNOP00000036487.

PTM databases

iPTMnetiQ7TT49.
PhosphoSitePlusiQ7TT49.

Proteomic databases

PaxDbiQ7TT49.
PRIDEiQ7TT49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000039059; ENSRNOP00000036487; ENSRNOG00000009675.
GeneIDi113960.
KEGGirno:113960.
UCSCiRGD:621753. rat.

Organism-specific databases

CTDi9578.
RGDi621753. Cdc42bpb.

Phylogenomic databases

eggNOGiENOG410IT51. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ7TT49.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG091G09EX.
PhylomeDBiQ7TT49.
TreeFamiTF313551.

Miscellaneous databases

PROiQ7TT49.

Gene expression databases

BgeeiENSRNOG00000009675.
ExpressionAtlasiQ7TT49. baseline and differential.
GenevisibleiQ7TT49. RN.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR031597. KELK.
IPR011009. Kinase-like_dom.
IPR033232. MRCK_beta.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF34. PTHR22988:SF34. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
ProDomiPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00109. 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.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMRCKB_RAT
AccessioniPrimary (citable) accession number: Q7TT49
Secondary accession number(s): O54875
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.