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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).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051ATPPROSITE-ProRule annotationBy similarity
Active sitei200 – 2001Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATPPROSITE-ProRule annotationBy similarity
Zinc fingeri1026 – 107651Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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
Synonyms:Kiaa1124Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2136459. Cdc42bpb.

Subcellular locationi

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

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17131713Serine/threonine-protein kinase MRCK betaPRO_0000086395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei221 – 2211Phosphoserine; by autocatalysisBy similarity
Modified residuei233 – 2331Phosphoserine; by autocatalysisBy similarity
Modified residuei239 – 2391Phosphothreonine; by autocatalysisBy similarity
Modified residuei423 – 4231PhosphothreonineBy similarity
Modified residuei954 – 9541Phosphotyrosine1 Publication
Modified residuei1682 – 16821PhosphoserineBy similarity
Modified residuei1684 – 16841PhosphoserineBy similarity
Modified residuei1688 – 16881PhosphoserineBy similarity
Modified residuei1692 – 16921Phosphoserine2 Publications
Modified residuei1695 – 16951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7TT50.
PaxDbiQ7TT50.
PRIDEiQ7TT50.

PTM databases

PhosphoSiteiQ7TT50.

Expressioni

Gene expression databases

BgeeiQ7TT50.
CleanExiMM_CDC42BPB.
GenevestigatoriQ7TT50.

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. 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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi229972. 3 interactions.
IntActiQ7TT50. 1 interaction.
STRINGi10090.ENSMUSP00000042565.

Structurei

3D structure databases

ProteinModelPortaliQ7TT50.
SMRiQ7TT50. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 342267Protein kinasePROSITE-ProRule annotationBy similarityAdd
BLAST
Domaini343 – 41371AGC-kinase C-terminalAdd
BLAST
Domaini1096 – 1215120PHPROSITE-ProRule annotationAdd
BLAST
Domaini1241 – 1515275CNHPROSITE-ProRule annotationAdd
BLAST
Domaini1585 – 159814CRIBPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili434 – 649216Sequence AnalysisAdd
BLAST
Coiled coili681 – 815135Sequence AnalysisAdd
BLAST
Coiled coili878 – 93962Sequence AnalysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1026 – 107651Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ7TT50.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG7F511X.
TreeFamiTF313551.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR001180. Citron.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 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]
SUPFAMiSSF56112. 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961K → R in AAP34402 (Ref. 1) Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ7TT50.
SMRiQ7TT50. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229972. 3 interactions.
IntActiQ7TT50. 1 interaction.
STRINGi10090.ENSMUSP00000042565.

PTM databases

PhosphoSiteiQ7TT50.

Proteomic databases

MaxQBiQ7TT50.
PaxDbiQ7TT50.
PRIDEiQ7TT50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9578.
MGIiMGI:2136459. Cdc42bpb.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ7TT50.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG7F511X.
TreeFamiTF313551.

Miscellaneous databases

NextBioi376071.
PROiQ7TT50.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TT50.
CleanExiMM_CDC42BPB.
GenevestigatoriQ7TT50.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR001180. Citron.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 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]
SUPFAMiSSF56112. 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...

Publicationsi

« Hide 'large scale' publications
  1. Huang C.Q., Wu S.L., Cheng Z.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-1713.
    Tissue: Fetal brainImported.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 633-642, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1139-1713.
    Strain: FVB/NImported.
    Tissue: KidneyImported.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-954, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692 AND SER-1695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMRCKB_MOUSE
AccessioniPrimary (citable) accession number: Q7TT50
Secondary accession number(s): E9QK15, Q69ZR5, Q80W33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 121 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

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 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.