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Q9Y5S2

- MRCKB_HUMAN

UniProt

Q9Y5S2 - MRCKB_HUMAN

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Protein

Serine/threonine-protein kinase MRCK beta

Gene

CDC42BPB

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

Mg2+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 – 1051ATPBy similarityPROSITE-ProRule annotation
Active sitei200 – 2001Proton acceptorBy similarityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 909ATPBy similarityPROSITE-ProRule annotation
Zinc fingeri1025 – 107551Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
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
Name:CDC42BPBImported
Synonyms:KIAA1124Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:1738. CDC42BPB.

Subcellular locationi

Cytoplasm By similarity. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell junction 1 Publication
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.By similarity

GO - Cellular componenti

  1. actomyosin Source: UniProtKB
  2. cell-cell junction Source: UniProtKB
  3. cell leading edge Source: UniProtKB
  4. cytoplasm Source: UniProtKB-KW
  5. cytoskeleton Source: ProtInc
  6. extracellular vesicular exosome Source: UniProt
  7. plasma membrane Source: UniProtKB-KW
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 autocatalysisBy similarity
Modified residuei233 – 2331Phosphoserine; by autocatalysisBy similarity
Modified residuei239 – 2391Phosphothreonine; by autocatalysisBy similarity
Modified residuei954 – 9541PhosphotyrosineBy 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

BgeeiQ9Y5S2.
CleanExiHS_CDC42BPB.
ExpressionAtlasiQ9Y5S2. baseline and differential.
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.By similarity2 Publications

Protein-protein interaction databases

BioGridi114947. 13 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 – 1614Combined sources
Turni18 – 203Combined sources
Beta strandi21 – 233Combined sources
Helixi27 – 4014Combined sources
Helixi45 – 484Combined sources
Helixi50 – 6920Combined sources
Helixi73 – 753Combined sources
Beta strandi76 – 849Combined sources
Beta strandi86 – 9510Combined sources
Beta strandi101 – 1088Combined sources
Helixi109 – 1146Combined sources
Turni115 – 1184Combined sources
Helixi121 – 13010Combined sources
Turni133 – 1353Combined sources
Beta strandi139 – 1446Combined sources
Beta strandi146 – 1538Combined sources
Helixi161 – 1677Combined sources
Turni168 – 1703Combined sources
Helixi174 – 19320Combined sources
Helixi203 – 2053Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi231 – 2355Combined sources
Helixi240 – 2423Combined sources
Helixi245 – 2528Combined sources
Beta strandi255 – 2584Combined sources
Helixi261 – 27616Combined sources
Helixi286 – 2949Combined sources
Helixi296 – 2994Combined sources
Helixi311 – 3188Combined sources
Helixi324 – 3263Combined sources
Turni328 – 3336Combined sources
Helixi334 – 3374Combined sources
Helixi340 – 3423Combined sources
Turni347 – 3493Combined sources
Helixi350 – 3523Combined sources
Helixi396 – 3983Combined sources
Beta strandi403 – 4064Combined sources
Beta strandi408 – 4125Combined sources

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 342267Protein kinaseBy similarityPROSITE-ProRule annotationAdd
BLAST
Domaini343 – 41371AGC-kinase C-terminalAdd
BLAST
Domaini1095 – 1214120PHPROSITE-ProRule annotationAdd
BLAST
Domaini1240 – 1513274CNHPROSITE-ProRule annotationAdd
BLAST
Domaini1583 – 159614CRIBPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili431 – 815385Sequence AnalysisAdd
BLAST
Coiled coili878 – 93962Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 CNH domain.PROSITE-ProRule annotation
Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1025 – 107551Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118994.
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.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide

        10         20         30         40         50
MSAKVRLKKL EQLLLDGPWR NESALSVETL LDVLVCLYTE CSHSALRRDK
60 70 80 90 100
YVAEFLEWAK PFTQLVKEMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER
110 120 130 140 150
IYAMKILNKW EMLKRAETAC FREERDVLVN GDCQWITALH YAFQDENHLY
160 170 180 190 200
LVMDYYVGGD LLTLLSKFED KLPEDMARFY IGEMVLAIDS IHQLHYVHRD
210 220 230 240 250
IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP DYISPEILQA
260 270 280 290 300
MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
310 320 330 340 350
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI
360 370 380 390 400
RNLEAPYIPD VSSPSDTSNF DVDDDVLRNT EILPPGSHTG FSGLHLPFIG
410 420 430 440 450
FTFTTESCFS DRGSLKSIMQ SNTLTKDEDV QRDLEHSLQM EAYERRIRRL
460 470 480 490 500
EQEKLELSRK LQESTQTVQS LHGSSRALSN SNRDKEIKKL NEEIERLKNK
510 520 530 540 550
IADSNRLERQ LEDTVALRQE REDSTQRLRG LEKQHRVVRQ EKEELHKQLV
560 570 580 590 600
EASERLKSQA KELKDAHQQR KLALQEFSEL NERMAELRAQ KQKVSRQLRD
610 620 630 640 650
KEEEMEVATQ KVDAMRQEMR RAEKLRKELE AQLDDAVAEA SKERKLREHS
660 670 680 690 700
ENFCKQMESE LEALKVKQGG RGAGATLEHQ QEISKIKSEL EKKVLFYEEE
710 720 730 740 750
LVRREASHVL EVKNVKKEVH DSESHQLALQ KEILMLKDKL EKSKRERHNE
760 770 780 790 800
MEEAVGTIKD KYERERAMLF DENKKLTAEN EKLCSFVDKL TAQNRQLEDE
810 820 830 840 850
LQDLAAKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS KMTEELEALR
860 870 880 890 900
SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV
910 920 930 940 950
KDANLTLESK LKDSEAKNRE LLEEMEILKK KMEEKFRADT GLKLPDFQDS
960 970 980 990 1000
IFEYFNTAPL AHDLTFRTSS ASEQETQAPK PEASPSMSVA ASEQQEDMAR
1010 1020 1030 1040 1050
PPQRPSAVPL PTTQALALAG PKPKAHQFSI KSFSSPTQCS HCTSLMVGLI
1060 1070 1080 1090 1100
RQGYACEVCS FACHVSCKDG APQVCPIPPE QSKRPLGVDV QRGIGTAYKG
1110 1120 1130 1140 1150
HVKVPKPTGV KKGWQRAYAV VCDCKLFLYD LPEGKSTQPG VIASQVLDLR
1160 1170 1180 1190 1200
DDEFSVSSVL ASDVIHATRR DIPCIFRVTA SLLGAPSKTS SLLILTENEN
1210 1220 1230 1240 1250
EKRKWVGILE GLQSILHKNR LRNQVVHVPL EAYDSSLPLI KAILTAAIVD
1260 1270 1280 1290 1300
ADRIAVGLEE GLYVIEVTRD VIVRAADCKK VHQIELAPRE KIVILLCGRN
1310 1320 1330 1340 1350
HHVHLYPWSS LDGAEGSFDI KLPETKGCQL MATATLKRNS GTCLFVAVKR
1360 1370 1380 1390 1400
LILCYEIQRT KPFHRKFNEI VAPGSVQCLA VLRDRLCVGY PSGFCLLSIQ
1410 1420 1430 1440 1450
GDGQPLNLVN PNDPSLAFLS QQSFDALCAV ELESEEYLLC FSHMGLYVDP
1460 1470 1480 1490 1500
QGRRARAQEL MWPAAPVACS CSPTHVTVYS EYGVDVFDVR TMEWVQTIGL
1510 1520 1530 1540 1550
RRIRPLNSEG TLNLLNCEPP RLIYFKSKFS GAVLNVPDTS DNSKKQMLRT
1560 1570 1580 1590 1600
RSKRRFVFKV PEEERLQQRR EMLRDPELRS KMISNPTNFN HVAHMGPGDG
1610 1620 1630 1640 1650
MQVLMDLPLS AVPPSQEERP GPAPTNLARQ PPSRNKPYIS WPSSGGSEPS
1660 1670 1680 1690 1700
VTVPLRSMSD PDQDFDKEPD SDSTKHSTPS NSSNPSGPPS PNSPHRSQLP
1710
LEGLEQPACD T
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.Curated
The sequence BAA86438.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1017 – 10171A → V in AAD37506. (PubMed:10198171)Curated
Sequence conflicti1123 – 11231D → E in AAD37506. (PubMed:10198171)Curated

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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 13 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.
GeneTreei ENSGT00760000118994.
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

Bgeei Q9Y5S2.
CleanExi HS_CDC42BPB.
ExpressionAtlasi Q9Y5S2. baseline and differential.
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.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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: BrainImported.
  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: BrainImported.
  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: PNSImported.
  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: November 26, 2014
This is version 134 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