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Reviewed, UniProtKB/Swiss-Prot Q7TT50 (MRCKB_MOUSE)

Last modified July 22, 2008. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Myotonic dystrophy kinase-related CDC42-binding kinase beta
      Short name(s)=Myotonic dystrophy protein kinase-like beta, MRCK beta
    DMPK-like beta
Gene names
Name: Cdc42bpb
Synonyms: Kiaa1124
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1713 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May act as a downstream effector of CDC42 in cytoskeletal reorganization. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

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 By similarity.

Subunit structure

Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42 By similarity.

Subcellular location

CytoplasmBy 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 17131713Serine/threonine-protein kinase MRCK beta

Regions

Domain76 – 342267Protein kinase
Domain343 – 41371AGC-kinase C-terminal
Domain1096 – 1215120PH
Domain1242 – 1515274CNH
Domain1585 – 159814CRIB
Nucleotide binding82 – 909ATP By similarity
Zinc finger1026 – 107651Phorbol-ester/DAG-type
Coiled coil434 – 649216 Potential
Coiled coil681 – 815135 Potential
Coiled coil878 – 93962 Potential

Sites

Active site2001Proton acceptor By similarity
Binding site1051ATP By similarity

Amino acid modifications

Modified residue2211Phosphoserine; by autocatalysis By similarity
Modified residue2331Phosphoserine; by autocatalysis By similarity
Modified residue2391Phosphothreonine; by autocatalysis By similarity
Modified residue9141Phosphoserine By similarity
Modified residue9541Phosphotyrosine
Modified residue11971Phosphothreonine By similarity
Modified residue16921Phosphoserine
Modified residue16951Phosphoserine

Sequences

Sequence LengthMass (Da)Tools
Q7TT50-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0D63976EAC61DDE1

FASTA1,713194,781
        10         20         30         40         50         60 
MSAKVRLKKL EQLLLDGPWR NDSALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK 

        70         80         90        100        110        120 
PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMRNTER 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]"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: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-1713.
Tissue: Fetal brain.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1139-1713.
Strain: FVB/N.
Tissue: Kidney.
[4]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-954, MASS SPECTROMETRY.
[5]"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: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692 AND SER-1695, MASS SPECTROMETRY.
Tissue: Liver.

Cross-references

Sequence databases

AY277589 mRNA. Translation: AAP34402.1.
AK173103 mRNA. Translation: BAD32381.1.
BC049921 mRNA. Translation: AAH49921.1.
RefSeqNP_898837.1.
UniGeneMm.27397

3D structure databases

HSSPHSSP built from PDB template 1MRY based on UniProtKB P31751.
ModBaseSearch...

Protein-protein interaction databases

IntActQ7TT50.

PTM databases

PhosphoSiteQ7TT50.

Genome annotation databases

EnsemblENSMUSG00000021279. Mus musculus. [Contig view]
GeneID217866.
KEGGmmu:217866.

Organism-specific databases

MGIMGI:2136459. Cdc42bpb.
RougeSearch...

Phylogenomic databases

HOGENOMQ7TT50.
HOVERGENQ7TT50.

Gene expression databases

ArrayExpressQ7TT50.
CleanExMM_CDC42BPB.
GermOnlineENSMUSG00000021279. Mus musculus.

Family and domain databases

InterProIPR001180. Citron.
IPR002219. DAG_PE_bd.
IPR014930. DMPK_coil.
IPR000095. PAK_box_Rho_bd.
IPR001849. PH.
IPR000961. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF00786. PBD. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
ProDomPD000001. Prot_kinase. 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]
PROSITEPS51285. AGC_KINASE_CTER. 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]
BLOCKSSearch...

Other Resources

SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameMRCKB_MOUSE
AccessionPrimary (citable) accession number: Q7TT50
Secondary accession number(s): Q69ZR5, Q80W33
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2003
Last modified: July 22, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents