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Q7TT50 (MRCKB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cdc42bpb
Synonyms:Kiaa1124
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1713 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. UniProtKB Q5VT25

Cofactor

Magnesium By similarity. UniProtKB Q5VT25

Enzyme regulation

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. UniProtKB Q5VT25

Subunit structure

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.

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein; 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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. DMPK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 CNH domain.

Contains 1 CRIB domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

actomyosin structure organization

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactomyosin

Inferred from electronic annotation. Source: Ensembl

cell leading edge

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17131713Serine/threonine-protein kinase MRCK beta
PRO_0000086395

Regions

Domain76 – 342267Protein kinase UniProtKB Q5VT25
Domain343 – 41371AGC-kinase C-terminal
Domain1096 – 1215120PH
Domain1241 – 1515275CNH
Domain1585 – 159814CRIB
Nucleotide binding82 – 909ATP By similarity UniProtKB P54265
Zinc finger1026 – 107651Phorbol-ester/DAG-type
Coiled coil434 – 649216 Potential
Coiled coil681 – 815135 Potential
Coiled coil878 – 93962 Potential

Sites

Active site2001Proton acceptor By similarity UniProtKB P54265
Binding site1051ATP By similarity UniProtKB Q5VT25

Amino acid modifications

Modified residue2211Phosphoserine; by autocatalysis By similarity UniProtKB Q5VT25
Modified residue2331Phosphoserine; by autocatalysis By similarity UniProtKB Q5VT25
Modified residue2391Phosphothreonine; by autocatalysis By similarity UniProtKB Q5VT25
Modified residue9541Phosphotyrosine Ref.6
Modified residue16921Phosphoserine Ref.7 Ref.8
Modified residue16951Phosphoserine Ref.7

Experimental info

Sequence conflict961K → R in AAP34402. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7TT50 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: CD809A3743986A4D

FASTA1,713194,753
        10         20         30         40         50         60 
MSAKVRLKKL EQLLLDGPWR NDSALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK 

        70         80         90        100        110        120 
PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC 

       130        140        150        160        170        180 
FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY 

       190        200        210        220        230        240 
IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP 

       250        260        270        280        290        300 
DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF 

       310        320        330        340        350        360 
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD 

       370        380        390        400        410        420 
VSSPSDTSNF DVDDDMLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMTQ 

       430        440        450        460        470        480 
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN 

       490        500        510        520        530        540 
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTHRLKG LEKQYRLARQ 

       550        560        570        580        590        600 
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMSELRSL KQKVSRQLRD 

       610        620        630        640        650        660 
KEEEMEVAMQ KIDSMRQDLR KSEKSRKELE ARLEDAAAEA SKERKLREHS ESFCKQMERE 

       670        680        690        700        710        720 
LEALKVKQGG RGPGAASEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH 

       730        740        750        760        770        780 
DSESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGTVKD KYERERAMLF DENKKLTAEN 

       790        800        810        820        830        840 
EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS 

       850        860        870        880        890        900 
KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV 

       910        920        930        940        950        960 
KDSSLAFESK LKESEAKNRE LLEEMQSLRK RMEEKFRADT GLKLPDFQDS IFEYFNTAPL 

       970        980        990       1000       1010       1020 
AHDLTFRTSS ASDQETQASK MDLSPSVSVA TSTEQQEDMA RPQQRPSPVP LPSTQALAMA 

      1030       1040       1050       1060       1070       1080 
GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP 

      1090       1100       1110       1120       1130       1140 
EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP 

      1150       1160       1170       1180       1190       1200 
GVVASQVLDL RDEEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE 

      1210       1220       1230       1240       1250       1260 
NEKRKWVGIL EGLQAILHKN RLKSQVVHVA QEAYDSSLPL IKAVLAAAIV DGDRIAVGLE 

      1270       1280       1290       1300       1310       1320 
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKIAILLCGR NHHVHLYPWS SFDGAEASNF 

      1330       1340       1350       1360       1370       1380 
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLILCYEIQ RTKPFHRKFS ELVAPGHVQW 

      1390       1400       1410       1420       1430       1440 
MAVFKDRLCV GYPSGFSLLS IQGDGPPLDL VNPTDPSLAF LSQQSFDALC AVELKSEEYL 

      1450       1460       1470       1480       1490       1500 
LCFSHMGLYV DPQGRRSRMQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI 

      1510       1520       1530       1540       1550       1560 
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTILNVPD TSDNSKKQML RTRSKRRFVF 

      1570       1580       1590       1600       1610       1620 
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTVQEE 

      1630       1640       1650       1660       1670       1680 
KQGPTPAGLP RQPPSRSKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST 

      1690       1700       1710 
PSNSSNPSGP PSPNSPHRSQ LPMEGLDQPS CDA 

« Hide

References

« Hide 'large scale' references
[1]Huang C.Q., Wu S.L., Cheng Z.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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 brain.
[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/N.
Tissue: Kidney.
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY277589 mRNA. Translation: AAP34402.1.
AC127580 Genomic DNA. No translation available.
AK173103 mRNA. Translation: BAD32381.1.
BC049921 mRNA. Translation: AAH49921.1.
RefSeqNP_898837.2. NM_183016.2.
UniGeneMm.27397.

3D structure databases

ProteinModelPortalQ7TT50.
SMRQ7TT50. Positions 2-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229972. 2 interactions.
IntActQ7TT50. 1 interaction.
STRING10090.ENSMUSP00000042565.

PTM databases

PhosphoSiteQ7TT50.

Proteomic databases

PaxDbQ7TT50.
PRIDEQ7TT50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041965; ENSMUSP00000042565; ENSMUSG00000021279.
GeneID217866.
KEGGmmu:217866.
UCSCuc007pct.2. mouse.

Organism-specific databases

CTD9578.
MGIMGI:2136459. Cdc42bpb.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117511.
HOGENOMHOG000294133.
HOVERGENHBG055933.
InParanoidQ7TT50.
KOK16307.
OMASCFSDRG.
OrthoDBEOG7F511X.
TreeFamTF313551.

Gene expression databases

BgeeQ7TT50.
CleanExMM_CDC42BPB.
GenevestigatorQ7TT50.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR001180. Citron.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR026611. Ser/Thr_kinase_MRCK.
[Graphical view]
PANTHERPTHR22988:SF2. PTHR22988:SF2. 1 hit.
PfamPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
ProDomPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00109. 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]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

NextBio376071.
PROQ7TT50.
SOURCESearch...

Entry information

Entry nameMRCKB_MOUSE
AccessionPrimary (citable) accession number: Q7TT50
Secondary accession number(s): E9QK15, Q69ZR5, Q80W33
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot