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Q9Y5S2

- MRCKB_HUMAN

UniProt

Q9Y5S2 - MRCKB_HUMAN

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Protein

Serine/threonine-protein kinase MRCK beta

Gene
CDC42BPB, KIAA1124
Organism
Homo sapiens (Human)
Status
Reviewed - 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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity1 Publication

Cofactori

Magnesium By similarity.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 By similarity. Inhibited by chelerythrine chloride.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051ATP By similarityBy similarity
Active sitei200 – 2001Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATP By similarityBy similarity
Zinc fingeri1025 – 107551Phorbol-ester/DAG-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein kinase activity Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB
  5. small GTPase regulator activity Source: InterPro

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. actomyosin structure organization Source: UniProtKB
  3. cell migration Source: UniProtKB
  4. cytoskeleton organization Source: ProtInc
  5. establishment or maintenance of cell polarity Source: ProtInc
  6. intracellular signal transduction Source: InterPro
  7. protein phosphorylation Source: UniProtKB
  8. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9Y5S2.

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
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 namesi
Synonyms:KIAA1124
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:1738. CDC42BPB.

Subcellular locationi

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 CDC42.1 Publication

GO - Cellular componenti

  1. actomyosin Source: UniProtKB
  2. cell-cell junction Source: UniProtKB
  3. cell leading edge Source: UniProtKB
  4. cytoplasm Source: UniProtKB-SubCell
  5. cytoskeleton Source: ProtInc
  6. extracellular vesicular exosome Source: UniProt
  7. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26268.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17111711Serine/threonine-protein kinase MRCK betaPRO_0000086394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei221 – 2211Phosphoserine; by autocatalysis By similarityBy similarity
Modified residuei233 – 2331Phosphoserine; by autocatalysis By similarityBy similarity
Modified residuei239 – 2391Phosphothreonine; by autocatalysis By similarityBy similarity
Modified residuei954 – 9541Phosphotyrosine By similarity
Modified residuei1690 – 16901Phosphoserine4 Publications
Modified residuei1693 – 16931Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5S2.
PaxDbiQ9Y5S2.
PRIDEiQ9Y5S2.

PTM databases

PhosphoSiteiQ9Y5S2.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9Y5S2.
BgeeiQ9Y5S2.
CleanExiHS_CDC42BPB.
GenevestigatoriQ9Y5S2.

Organism-specific databases

HPAiHPA022821.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi114947. 10 interactions.
IntActiQ9Y5S2. 9 interactions.
MINTiMINT-5005780.
STRINGi9606.ENSP00000372449.

Structurei

Secondary structure

1
1711
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Turni18 – 203
Beta strandi21 – 233
Helixi27 – 4014
Helixi45 – 484
Helixi50 – 6920
Helixi73 – 753
Beta strandi76 – 849
Beta strandi86 – 9510
Beta strandi101 – 1088
Helixi109 – 1146
Turni115 – 1184
Helixi121 – 13010
Turni133 – 1353
Beta strandi139 – 1446
Beta strandi146 – 1538
Helixi161 – 1677
Turni168 – 1703
Helixi174 – 19320
Helixi203 – 2053
Beta strandi206 – 2083
Beta strandi214 – 2163
Beta strandi227 – 2293
Beta strandi231 – 2355
Helixi240 – 2423
Helixi245 – 2528
Beta strandi255 – 2584
Helixi261 – 27616
Helixi286 – 2949
Helixi296 – 2994
Helixi311 – 3188
Helixi324 – 3263
Turni328 – 3336
Helixi334 – 3374
Helixi340 – 3423
Turni347 – 3493
Helixi350 – 3523
Helixi396 – 3983
Beta strandi403 – 4064
Beta strandi408 – 4125

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QFVX-ray2.65A/B1-415[»]
3TKUX-ray2.15A/B2-417[»]
ProteinModelPortaliQ9Y5S2.
SMRiQ9Y5S2. Positions 2-415, 1026-1075.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 342267Protein kinaseBy similarityAdd
BLAST
Domaini343 – 41371AGC-kinase C-terminalAdd
BLAST
Domaini1095 – 1214120PHAdd
BLAST
Domaini1240 – 1513274CNHAdd
BLAST
Domaini1583 – 159614CRIBAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili431 – 815385 Reviewed predictionAdd
BLAST
Coiled coili878 – 93962 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Contains 1 CNH domain.
Contains 1 CRIB domain.
Contains 1 PH domain.

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ9Y5S2.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG7F511X.
PhylomeDBiQ9Y5S2.
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.
IPR001849. PH_domain.
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.
[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.

Q9Y5S2-1 [UniParc]FASTAAdd to Basket

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MSAKVRLKKL EQLLLDGPWR NESALSVETL LDVLVCLYTE CSHSALRRDK     50
YVAEFLEWAK PFTQLVKEMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER 100
IYAMKILNKW EMLKRAETAC FREERDVLVN GDCQWITALH YAFQDENHLY 150
LVMDYYVGGD LLTLLSKFED KLPEDMARFY IGEMVLAIDS IHQLHYVHRD 200
IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP DYISPEILQA 250
MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF 300
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI 350
RNLEAPYIPD VSSPSDTSNF DVDDDVLRNT EILPPGSHTG FSGLHLPFIG 400
FTFTTESCFS DRGSLKSIMQ SNTLTKDEDV QRDLEHSLQM EAYERRIRRL 450
EQEKLELSRK LQESTQTVQS LHGSSRALSN SNRDKEIKKL NEEIERLKNK 500
IADSNRLERQ LEDTVALRQE REDSTQRLRG LEKQHRVVRQ EKEELHKQLV 550
EASERLKSQA KELKDAHQQR KLALQEFSEL NERMAELRAQ KQKVSRQLRD 600
KEEEMEVATQ KVDAMRQEMR RAEKLRKELE AQLDDAVAEA SKERKLREHS 650
ENFCKQMESE LEALKVKQGG RGAGATLEHQ QEISKIKSEL EKKVLFYEEE 700
LVRREASHVL EVKNVKKEVH DSESHQLALQ KEILMLKDKL EKSKRERHNE 750
MEEAVGTIKD KYERERAMLF DENKKLTAEN EKLCSFVDKL TAQNRQLEDE 800
LQDLAAKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS KMTEELEALR 850
SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV 900
KDANLTLESK LKDSEAKNRE LLEEMEILKK KMEEKFRADT GLKLPDFQDS 950
IFEYFNTAPL AHDLTFRTSS ASEQETQAPK PEASPSMSVA ASEQQEDMAR 1000
PPQRPSAVPL PTTQALALAG PKPKAHQFSI KSFSSPTQCS HCTSLMVGLI 1050
RQGYACEVCS FACHVSCKDG APQVCPIPPE QSKRPLGVDV QRGIGTAYKG 1100
HVKVPKPTGV KKGWQRAYAV VCDCKLFLYD LPEGKSTQPG VIASQVLDLR 1150
DDEFSVSSVL ASDVIHATRR DIPCIFRVTA SLLGAPSKTS SLLILTENEN 1200
EKRKWVGILE GLQSILHKNR LRNQVVHVPL EAYDSSLPLI KAILTAAIVD 1250
ADRIAVGLEE GLYVIEVTRD VIVRAADCKK VHQIELAPRE KIVILLCGRN 1300
HHVHLYPWSS LDGAEGSFDI KLPETKGCQL MATATLKRNS GTCLFVAVKR 1350
LILCYEIQRT KPFHRKFNEI VAPGSVQCLA VLRDRLCVGY PSGFCLLSIQ 1400
GDGQPLNLVN PNDPSLAFLS QQSFDALCAV ELESEEYLLC FSHMGLYVDP 1450
QGRRARAQEL MWPAAPVACS CSPTHVTVYS EYGVDVFDVR TMEWVQTIGL 1500
RRIRPLNSEG TLNLLNCEPP RLIYFKSKFS GAVLNVPDTS DNSKKQMLRT 1550
RSKRRFVFKV PEEERLQQRR EMLRDPELRS KMISNPTNFN HVAHMGPGDG 1600
MQVLMDLPLS AVPPSQEERP GPAPTNLARQ PPSRNKPYIS WPSSGGSEPS 1650
VTVPLRSMSD PDQDFDKEPD SDSTKHSTPS NSSNPSGPPS PNSPHRSQLP 1700
LEGLEQPACD T 1711
Length:1,711
Mass (Da):194,315
Last modified:April 4, 2006 - v2
Checksum:i041A009E0273ABE0
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti500 – 5001K → E in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_040834
Natural varianti555 – 5551R → Q.1 Publication
Corresponds to variant rs36001612 [ dbSNP | Ensembl ].
VAR_040835
Natural varianti671 – 6711R → Q.1 Publication
Corresponds to variant rs55948035 [ dbSNP | Ensembl ].
VAR_040836
Natural varianti876 – 8761R → W in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040837
Natural varianti1077 – 10771I → V.1 Publication
Corresponds to variant rs34822377 [ dbSNP | Ensembl ].
VAR_025847
Natural varianti1203 – 12031R → K.2 Publications
Corresponds to variant rs146298297 [ dbSNP | Ensembl ].
VAR_070886
Natural varianti1315 – 13151E → K in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_040838
Natural varianti1633 – 16331S → Y.1 Publication
Corresponds to variant rs56412851 [ dbSNP | Ensembl ].
VAR_040839

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1017 – 10171A → V in AAD37506. 1 Publication
Sequence conflicti1123 – 11231D → E in AAD37506. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BC155541 mRNA. Translation: AAI55542.1.
CCDSiCCDS9978.1.
RefSeqiNP_006026.3. NM_006035.3.
UniGeneiHs.654634.

Genome annotation databases

EnsembliENST00000361246; ENSP00000355237; ENSG00000198752.
GeneIDi9578.
KEGGihsa:9578.
UCSCiuc001ymi.1. human.

Polymorphism databases

DMDMi92090617.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BC155541 mRNA. Translation: AAI55542.1 .
CCDSi CCDS9978.1.
RefSeqi NP_006026.3. NM_006035.3.
UniGenei Hs.654634.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QFV X-ray 2.65 A/B 1-415 [» ]
3TKU X-ray 2.15 A/B 2-417 [» ]
ProteinModelPortali Q9Y5S2.
SMRi Q9Y5S2. Positions 2-415, 1026-1075.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114947. 10 interactions.
IntActi Q9Y5S2. 9 interactions.
MINTi MINT-5005780.
STRINGi 9606.ENSP00000372449.

Chemistry

BindingDBi Q9Y5S2.
ChEMBLi CHEMBL5052.
GuidetoPHARMACOLOGYi 1508.

PTM databases

PhosphoSitei Q9Y5S2.

Polymorphism databases

DMDMi 92090617.

Proteomic databases

MaxQBi Q9Y5S2.
PaxDbi Q9Y5S2.
PRIDEi Q9Y5S2.

Protocols and materials databases

DNASUi 9578.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361246 ; ENSP00000355237 ; ENSG00000198752 .
GeneIDi 9578.
KEGGi hsa:9578.
UCSCi uc001ymi.1. human.

Organism-specific databases

CTDi 9578.
GeneCardsi GC14M103398.
H-InvDB HIX0011995.
HIX0011996.
HGNCi HGNC:1738. CDC42BPB.
HPAi HPA022821.
MIMi 614062. gene.
neXtProti NX_Q9Y5S2.
PharmGKBi PA26268.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000294133.
HOVERGENi HBG055933.
InParanoidi Q9Y5S2.
KOi K16307.
OMAi SCFSDRG.
OrthoDBi EOG7F511X.
PhylomeDBi Q9Y5S2.
TreeFami TF313551.

Enzyme and pathway databases

SignaLinki Q9Y5S2.

Miscellaneous databases

ChiTaRSi CDC42BPB. human.
GenomeRNAii 9578.
NextBioi 35465240.
PROi Q9Y5S2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5S2.
Bgeei Q9Y5S2.
CleanExi HS_CDC42BPB.
Genevestigatori Q9Y5S2.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR001180. Citron.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR001849. PH_domain.
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.
[Graphical view ]
Pfami PF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR00008. DAGPEDOMAIN.
ProDomi PD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00109. 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 ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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], VARIANT LYS-1203.
    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], VARIANT LYS-1203.
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. 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. 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.
    , 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.

Entry informationi

Entry nameiMRCKB_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5S2
Secondary accession number(s): A9JR72
, Q2L7A5, Q86TJ1, Q9ULU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: April 4, 2006
Last modified: September 3, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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