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Reviewed, UniProtKB/Swiss-Prot Q80UW5 (MRCKG_MOUSE)

Last modified July 22, 2008. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase MRCK gamma
    EC=2.7.11.1
Alternative name(s):
    CDC42-binding protein kinase gamma
    Myotonic dystrophy kinase-related CDC42-binding kinase gamma
      Short name(s)=MRCK gamma
    Myotonic dystrophy protein kinase-like alpha
    DMPK-like gamma
Gene names
Name: Cdc42bpg
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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= Concentrates at the leading edge of cells 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 2 CNH domains.

Contains 1 CRIB domain.

Contains 1 PH domain.

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

Contains 1 protein kinase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 15511551Serine/threonine-protein kinase MRCK gamma

Regions

Domain71 – 337267Protein kinase
Domain338 – 40871AGC-kinase C-terminal
Domain394 – 667274CNH 1
Domain946 – 1065120PH
Domain1092 – 1365274CNH 2
Domain1436 – 144914CRIB
Nucleotide binding77 – 859ATP By similarity
Zinc finger877 – 92650Phorbol-ester/DAG-type
Coiled coil442 – 675234 Potential
Coiled coil729 – 80173 Potential
Compositional bias1289 – 12924Poly-Leu

Sites

Active site1951Proton acceptor By similarity
Binding site1001ATP By similarity

Amino acid modifications

Modified residue2161Phosphoserine; by autocatalysis By similarity
Modified residue2281Phosphoserine; by autocatalysis By similarity
Modified residue2341Phosphothreonine; by autocatalysis By similarity

Experimental info

Sequence conflict10651R → Q in AAH46418. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q80UW5-1 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: 74458CA5FEF6F8A7

FASTA1,551172,147
        10         20         30         40         50         60 
MEQRLRALEQ LVRGEAGGSP GLDGLLDLLL GVHQELSSAP LRRERNVAQF LSWASPFVTK 

        70         80         90        100        110        120 
VKELRLQRDD FEILKVIGRG AFGEVAVVRQ RGSGQIFAMK MLHKWEMLKR AETACFREER 

       130        140        150        160        170        180 
DVLVKGDSRW VTALHYAFQD EEYLYLVMDY YAGGDLLTLL SRFEDRLPPE LAQFYLAEMV 

       190        200        210        220        230        240 
LAIHSLHQLG YVHRDVKPDN ILLDMNGHIR LADFGSCLRL NNNGMVDSSV AVGTPDYISP 

       250        260        270        280        290        300 
EILQAMEEGK GHYGPQCDWW SLGVCAYELL FGETPFYAES LVETYGKIMN HEDHLQFPAD 

       310        320        330        340        350        360 
VTDVPASAQD LIRQLLCRQE ERLGRGGLDD FRKHPFFEGV DWERLATSTA PYIPELRGPM 

       370        380        390        400        410        420 
DTSNFDVDDD TLNRPETLPP SSHGAFSGHH LPFVGFTYTS GSPFDVQSSE LMAAPEGTPH 

       430        440        450        460        470        480 
CVEQVKVELS HKCQEPLHGP LQPQELVRLQ KEVQVLQEKL AETLRDSKAS LSQTDGLHAR 

       490        500        510        520        530        540 
SPAPNIQLQQ EKDRLQQELT EAQAALRVQD AELCQAQNRQ EEFLQRLWEA QEREAAAASQ 

       550        560        570        580        590        600 
IQALNSQLEE AWVVRRELEG QVTTLSQEVT RLQGQCKQES SQAKTVHAAP ETNGIGSPEG 

       610        620        630        640        650        660 
QSQEAQLRKE VAALREQLEH ACSQGISVGK EEVLCRLQEE NQRLSREQER LAGELELELQ 

       670        680        690        700        710        720 
SKQRLEGERR ETESNWEAQI ADILSWVNDE KVSRGYLQAL ATKMAEELES LRNVGTQTLP 

       730        740        750        760        770        780 
TRPLDHQWKA RRLQKMEASA RLELQSALEA EIRAKQSLQE QLTQVQEAQR QAERRLQEAE 

       790        800        810        820        830        840 
KQSQALQQEV AELREELQAR GPGDARPSTS LIPLLSFWNT EKDSAKDPGN SGEGPRSGAE 

       850        860        870        880        890        900 
AELRPEGRRS LRMGSVFPRV PAATTTPAEG PPAKPGSHTL RPRSFPSPTK CLRCTSLMLG 

       910        920        930        940        950        960 
LGRQGLGCDT CGYFCHSACA SQAPPCPVPP ELLRTALGVH PETGTGTAYE GFLSVPRPSG 

       970        980        990       1000       1010       1020 
VRRGWQRVYA ALSDSRLLLF DAPDPRGSLA SGVLLQALDL RDPQFSATPV LAPDVIHAQS 

      1030       1040       1050       1060       1070       1080 
KDLPRIFRVT ASQLTVPPTT CTVLLLAENE GERERWLQVL GELQRLLLDA RPRPRPVYTL 

      1090       1100       1110       1120       1130       1140 
KEAYDNGLPL LPHALCAAVI DQERLALGTE EGLFVIHLHS NDIFQVGDCR RVQRLAVSSA 

      1150       1160       1170       1180       1190       1200 
AGLLAVLCGR GPSVRLFALD ELESAEVAGA KIPESRGCQA LVAGRILQAR TPVLCVAVKR 

      1210       1220       1230       1240       1250       1260 
QVLCYQLGPG PGPWQRRIRE LQAPAPVQSL GLLGDRLCVG AAGTFALYPL LNEAAPLALG 

      1270       1280       1290       1300       1310       1320 
TGLVAEELPA SRGGLGEALG AVELSLSELL LLFATAGVYV DSAGRKSRSH ELLWPAAPTG 

      1330       1340       1350       1360       1370       1380 
WGYTAPYLTV FSENALDVFD VRRAEWVQTV PLKKVRPLNP EGSLFLYGTE KVRLTYLRNP 

      1390       1400       1410       1420       1430       1440 
LAEKDEFDIP DLTDNSRRQL FRTKSKRRFF FRVSDELRQQ QRREMLKDPF VRSKFISPPT 

      1450       1460       1470       1480       1490       1500 
NFNHLVHVGP TEGRPNTRDG TRAQEQKSRG ARSSGPQRPH SFSEAFRRPV STGSDGLPGE 

      1510       1520       1530       1540       1550 
TDPLVKRKPW TSLSSESVSC PQGSLSPAAS LIQVSERPRS LPPDPESESS P

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References

[1]The mouse genome sequencing consortium
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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 699-1551.
Strain: FVB/N.
Tissue: Mammary gland.

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Cross-references

Sequence databases

AC127556 Genomic DNA. No translation available.
BC046418 mRNA. Translation: AAH46418.1.
UniGeneMm.329622

3D structure databases

HSSPHSSP built from PDB template 1TBN based on UniProtKB P05697.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000024769. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:2652845. Cdc42bpg.

Phylogenomic databases

HOGENOMQ80UW5.
HOVERGENQ80UW5.

Gene expression databases

ArrayExpressQ80UW5.
CleanExMM_CDC42BPG.
GermOnlineENSMUSG00000024769. 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.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00109. C1. 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...

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Entry information

Entry nameMRCKG_MOUSE
AccessionPrimary (citable) accession number: Q80UW5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: July 22, 2008
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

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