Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y5S2 (MRCKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
Short name=CDC42BP-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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1711 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. Ref.7 Ref.14 Ref.16

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.16 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 By similarity. Inhibited by chelerythrine chloride. Ref.14 UniProtKB Q5VT25

Subunit structure

Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42. Interacts with TJP1, when in the presence of catalytically active CDC42 By similarity. 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. Ref.7 Ref.16

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. 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 cells. Localization at the leading edge of migrating cells requires interaction with catalytically active CDC42. Ref.13

Tissue specificity

Expressed in all tissues examined, with high levels in heart, brain, placenta and lung. Ref.1

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 caution

The sequence AAH47871.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA86438.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

actomyosin structure organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cytoskeleton organization

Traceable author statement PubMed 9418861. Source: ProtInc

establishment or maintenance of cell polarity

Traceable author statement PubMed 9418861. Source: ProtInc

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

protein phosphorylation

Inferred from direct assay Ref.16. Source: UniProtKB

signal transduction

Traceable author statement PubMed 9418861. Source: ProtInc

   Cellular_componentactomyosin

Inferred from direct assay Ref.7. Source: UniProtKB

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

cytoskeleton

Traceable author statement PubMed 9418861. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

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 kinase activity

Inferred from direct assay Ref.16. 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 – 17111711Serine/threonine-protein kinase MRCK beta
PRO_0000086394

Regions

Domain76 – 342267Protein kinase UniProtKB Q5VT25
Domain343 – 41371AGC-kinase C-terminal
Domain1095 – 1214120PH
Domain1240 – 1513274CNH
Domain1583 – 159614CRIB
Nucleotide binding82 – 909ATP By similarity UniProtKB P54265
Zinc finger1025 – 107551Phorbol-ester/DAG-type
Coiled coil431 – 815385 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 By similarity
Modified residue16901Phosphoserine Ref.6 Ref.8 Ref.11 Ref.15
Modified residue16931Phosphoserine Ref.15

Natural variations

Natural variant5001K → E in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.17
VAR_040834
Natural variant5551R → Q. Ref.17
Corresponds to variant rs36001612 [ dbSNP | Ensembl ].
VAR_040835
Natural variant6711R → Q. Ref.17
Corresponds to variant rs55948035 [ dbSNP | Ensembl ].
VAR_040836
Natural variant8761R → W in a colorectal adenocarcinoma sample; somatic mutation. Ref.17
VAR_040837
Natural variant10771I → V. Ref.4
Corresponds to variant rs34822377 [ dbSNP | Ensembl ].
VAR_025847
Natural variant13151E → K in a lung large cell carcinoma sample; somatic mutation. Ref.17
VAR_040838
Natural variant16331S → Y. Ref.17
Corresponds to variant rs56412851 [ dbSNP | Ensembl ].
VAR_040839

Experimental info

Sequence conflict10171A → V in AAD37506. Ref.1
Sequence conflict11231D → E in AAD37506. Ref.1
Sequence conflict12031R → K in BAA86438. Ref.2

Secondary structure

......................................................................... 1711
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5S2 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 041A009E0273ABE0

FASTA1,711194,315
        10         20         30         40         50         60 
MSAKVRLKKL EQLLLDGPWR NESALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK 

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

       130        140        150        160        170        180 
FREERDVLVN GDCQWITALH YAFQDENHLY 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 DVDDDVLRNT EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSIMQ 

       430        440        450        460        470        480 
SNTLTKDEDV QRDLEHSLQM EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSSRALSN 

       490        500        510        520        530        540 
SNRDKEIKKL NEEIERLKNK IADSNRLERQ LEDTVALRQE REDSTQRLRG LEKQHRVVRQ 

       550        560        570        580        590        600 
EKEELHKQLV EASERLKSQA KELKDAHQQR KLALQEFSEL NERMAELRAQ KQKVSRQLRD 

       610        620        630        640        650        660 
KEEEMEVATQ KVDAMRQEMR RAEKLRKELE AQLDDAVAEA SKERKLREHS ENFCKQMESE 

       670        680        690        700        710        720 
LEALKVKQGG RGAGATLEHQ QEISKIKSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH 

       730        740        750        760        770        780 
DSESHQLALQ KEILMLKDKL EKSKRERHNE MEEAVGTIKD KYERERAMLF DENKKLTAEN 

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

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

       910        920        930        940        950        960 
KDANLTLESK LKDSEAKNRE LLEEMEILKK KMEEKFRADT GLKLPDFQDS IFEYFNTAPL 

       970        980        990       1000       1010       1020 
AHDLTFRTSS ASEQETQAPK PEASPSMSVA ASEQQEDMAR PPQRPSAVPL PTTQALALAG 

      1030       1040       1050       1060       1070       1080 
PKPKAHQFSI KSFSSPTQCS HCTSLMVGLI RQGYACEVCS FACHVSCKDG APQVCPIPPE 

      1090       1100       1110       1120       1130       1140 
QSKRPLGVDV QRGIGTAYKG HVKVPKPTGV KKGWQRAYAV VCDCKLFLYD LPEGKSTQPG 

      1150       1160       1170       1180       1190       1200 
VIASQVLDLR DDEFSVSSVL ASDVIHATRR DIPCIFRVTA SLLGAPSKTS SLLILTENEN 

      1210       1220       1230       1240       1250       1260 
EKRKWVGILE GLQSILHKNR LRNQVVHVPL EAYDSSLPLI KAILTAAIVD ADRIAVGLEE 

      1270       1280       1290       1300       1310       1320 
GLYVIEVTRD VIVRAADCKK VHQIELAPRE KIVILLCGRN HHVHLYPWSS LDGAEGSFDI 

      1330       1340       1350       1360       1370       1380 
KLPETKGCQL MATATLKRNS GTCLFVAVKR LILCYEIQRT KPFHRKFNEI VAPGSVQCLA 

      1390       1400       1410       1420       1430       1440 
VLRDRLCVGY PSGFCLLSIQ GDGQPLNLVN PNDPSLAFLS QQSFDALCAV ELESEEYLLC 

      1450       1460       1470       1480       1490       1500 
FSHMGLYVDP QGRRARAQEL MWPAAPVACS CSPTHVTVYS EYGVDVFDVR TMEWVQTIGL 

      1510       1520       1530       1540       1550       1560 
RRIRPLNSEG TLNLLNCEPP RLIYFKSKFS GAVLNVPDTS DNSKKQMLRT RSKRRFVFKV 

      1570       1580       1590       1600       1610       1620 
PEEERLQQRR EMLRDPELRS KMISNPTNFN HVAHMGPGDG MQVLMDLPLS AVPPSQEERP 

      1630       1640       1650       1660       1670       1680 
GPAPTNLARQ PPSRNKPYIS WPSSGGSEPS VTVPLRSMSD PDQDFDKEPD SDSTKHSTPS 

      1690       1700       1710 
NSSNPSGPPS PNSPHRSQLP LEGLEQPACD T 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosomal localization of human Cdc42-binding protein kinase beta."
Moncrieff C.L., Bailey M.E., Morrison N., Johnson K.J.
Genomics 57:297-300(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]NIEHS SNPs program
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-1077.
[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 1-931.
Tissue: PNS.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow."
Tan I., Yong J., Dong J.M., Lim L., Leung T.
Cell 135:123-136(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH LURAP1 AND MYO18A.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration."
Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.
EMBO J. 30:665-678(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
Tan I., Lai J., Yong J., Li S.F., Leung T.
FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A AND MYL9/MLC2, ENZYME REGULATION.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690 AND SER-1693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Co-crystal structures of inhibitors with MRCKbeta, a key regulator of tumor cell invasion."
Heikkila T., Wheatley E., Crighton D., Schroder E., Boakes A., Kaye S.J., Mezna M., Pang L., Rushbrooke M., Turnbull A., Olson M.F.
PLoS ONE 6:E24825-E24825(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-417 IN COMPLEXES WITH FASUDIL AND TPCA-1, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.
[17]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-500; GLN-555; GLN-671; TRP-876; LYS-1315 AND TYR-1633.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF128625 mRNA. Translation: AAD37506.1.
AB032950 mRNA. Translation: BAA86438.2. Different initiation.
DQ355971 Genomic DNA. Translation: ABC67469.1.
BC047871 mRNA. Translation: AAH47871.1. Sequence problems.
RefSeqNP_006026.3. NM_006035.3.
UniGeneHs.654634.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QFVX-ray2.65A/B1-415[»]
3TKUX-ray2.15A/B2-417[»]
ProteinModelPortalQ9Y5S2.
SMRQ9Y5S2. Positions 2-415, 1026-1075.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114947. 9 interactions.
IntActQ9Y5S2. 9 interactions.
MINTMINT-5005780.
STRING9606.ENSP00000372449.

Chemistry

BindingDBQ9Y5S2.
ChEMBLCHEMBL5052.
GuidetoPHARMACOLOGY1508.

PTM databases

PhosphoSiteQ9Y5S2.

Polymorphism databases

DMDM92090617.

Proteomic databases

PaxDbQ9Y5S2.
PRIDEQ9Y5S2.

Protocols and materials databases

DNASU9578.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361246; ENSP00000355237; ENSG00000198752.
GeneID9578.
KEGGhsa:9578.
UCSCuc001ymi.1. human.

Organism-specific databases

CTD9578.
GeneCardsGC14M103398.
H-InvDBHIX0011995.
HIX0011996.
HGNCHGNC:1738. CDC42BPB.
HPAHPA022821.
MIM614062. gene.
neXtProtNX_Q9Y5S2.
PharmGKBPA26268.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000294133.
HOVERGENHBG055933.
InParanoidQ9Y5S2.
KOK16307.
OMASCFSDRG.
OrthoDBEOG7F511X.
PhylomeDBQ9Y5S2.
TreeFamTF313551.

Enzyme and pathway databases

SignaLinkQ9Y5S2.

Gene expression databases

ArrayExpressQ9Y5S2.
BgeeQ9Y5S2.
CleanExHS_CDC42BPB.
GenevestigatorQ9Y5S2.

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

ChiTaRSCDC42BPB. human.
GenomeRNAi9578.
NextBio35929.
PROQ9Y5S2.
SOURCESearch...

Entry information

Entry nameMRCKB_HUMAN
AccessionPrimary (citable) accession number: Q9Y5S2
Secondary accession number(s): Q2L7A5, Q86TJ1, Q9ULU5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM