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Protein

Serine/threonine-protein kinase MRCK beta

Gene

CDC42BPB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei105ATPPROSITE-ProRule annotationBy similarity1
Active sitei200Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi82 – 90ATPPROSITE-ProRule annotationBy similarity9
Zinc fingeri1025 – 1075Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • actomyosin structure organization Source: UniProtKB
  • cell migration Source: UniProtKB
  • cytoskeleton organization Source: ProtInc
  • establishment or maintenance of cell polarity Source: ProtInc
  • intracellular signal transduction Source: InterPro
  • protein phosphorylation Source: UniProtKB
  • 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

BioCyciZFISH:HS02132-MONOMER.
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
Proteomesi
  • UP000005640 Componenti: 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

  • actomyosin Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell leading edge Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • cytoskeleton Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi9578.
OpenTargetsiENSG00000198752.
PharmGKBiPA26268.

Chemistry databases

ChEMBLiCHEMBL5052.
GuidetoPHARMACOLOGYi1508.

Polymorphism and mutation databases

BioMutaiCDC42BPB.
DMDMi92090617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000863941 – 1711Serine/threonine-protein kinase MRCK betaAdd BLAST1711

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221Phosphoserine; by autocatalysisBy similarity1
Modified residuei233Phosphoserine; by autocatalysisBy similarity1
Modified residuei239Phosphothreonine; by autocatalysisBy similarity1
Modified residuei423PhosphothreonineCombined sources1
Modified residuei671Omega-N-methylarginineCombined sources1
Modified residuei954PhosphotyrosineBy similarity1
Modified residuei1680PhosphoserineCombined sources1
Modified residuei1682PhosphoserineCombined sources1
Modified residuei1686PhosphoserineCombined sources1
Modified residuei1690PhosphoserineCombined sources1
Modified residuei1693PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ9Y5S2.
MaxQBiQ9Y5S2.
PaxDbiQ9Y5S2.
PeptideAtlasiQ9Y5S2.
PRIDEiQ9Y5S2.

PTM databases

iPTMnetiQ9Y5S2.
PhosphoSitePlusiQ9Y5S2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000198752.
CleanExiHS_CDC42BPB.
ExpressionAtlasiQ9Y5S2. baseline and differential.
GenevisibleiQ9Y5S2. HS.

Organism-specific databases

HPAiHPA022821.

Interactioni

Subunit structurei

Homodimer and homotetramer via the coiled coil regions (PubMed:21949762). 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 (PubMed:18854160). Interacts with STRIP1, STRN3 and SIKE1 (PubMed:25743393). Interacts with CPNE4 (via VWFA domain) (By similarity).By similarity3 Publications

Protein-protein interaction databases

BioGridi114947. 20 interactors.
IntActiQ9Y5S2. 12 interactors.
MINTiMINT-5005780.
STRINGi9606.ENSP00000355237.

Chemistry databases

BindingDBiQ9Y5S2.

Structurei

Secondary structure

11711
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 20Combined sources18
Beta strandi21 – 23Combined sources3
Helixi27 – 41Combined sources15
Helixi44 – 47Combined sources4
Helixi50 – 69Combined sources20
Helixi73 – 75Combined sources3
Beta strandi76 – 83Combined sources8
Beta strandi86 – 95Combined sources10
Beta strandi101 – 108Combined sources8
Helixi109 – 114Combined sources6
Turni115 – 118Combined sources4
Helixi121 – 130Combined sources10
Turni133 – 135Combined sources3
Beta strandi139 – 144Combined sources6
Beta strandi146 – 153Combined sources8
Helixi161 – 167Combined sources7
Turni168 – 170Combined sources3
Helixi174 – 193Combined sources20
Helixi203 – 205Combined sources3
Beta strandi206 – 208Combined sources3
Beta strandi214 – 216Combined sources3
Beta strandi227 – 229Combined sources3
Beta strandi231 – 235Combined sources5
Helixi240 – 242Combined sources3
Helixi245 – 253Combined sources9
Beta strandi255 – 258Combined sources4
Helixi261 – 276Combined sources16
Helixi286 – 294Combined sources9
Helixi296 – 299Combined sources4
Helixi311 – 318Combined sources8
Helixi324 – 326Combined sources3
Beta strandi330 – 333Combined sources4
Helixi334 – 337Combined sources4
Helixi340 – 342Combined sources3
Turni347 – 349Combined sources3
Helixi350 – 352Combined sources3
Beta strandi362 – 365Combined sources4
Helixi396 – 398Combined sources3
Beta strandi403 – 406Combined sources4
Beta strandi408 – 412Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QFVX-ray2.65A/B1-415[»]
3TKUX-ray2.15A/B2-417[»]
4UAKX-ray1.73A2-417[»]
4UALX-ray1.71A2-417[»]
ProteinModelPortaliQ9Y5S2.
SMRiQ9Y5S2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 342Protein kinasePROSITE-ProRule annotationBy similarityAdd BLAST267
Domaini343 – 413AGC-kinase C-terminalAdd BLAST71
Domaini1095 – 1214PHPROSITE-ProRule annotationAdd BLAST120
Domaini1240 – 1513CNHPROSITE-ProRule annotationAdd BLAST274
Domaini1583 – 1596CRIBPROSITE-ProRule annotationAdd BLAST14

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili431 – 815Sequence analysisAdd BLAST385
Coiled coili878 – 939Sequence analysisAdd BLAST62

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)DescriptionActionsGraphical viewLength
Zinc fingeri1025 – 1075Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IT51. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ9Y5S2.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG091G09EX.
PhylomeDBiQ9Y5S2.
TreeFamiTF313551.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR031597. KELK.
IPR011009. Kinase-like_dom.
IPR033232. MRCK_beta.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF34. PTHR22988:SF34. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. 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 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA86438 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1017A → V in AAD37506 (PubMed:10198171).Curated1
Sequence conflicti1123D → E in AAD37506 (PubMed:10198171).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040834500K → E in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040835555R → Q.1 PublicationCorresponds to variant rs36001612dbSNPEnsembl.1
Natural variantiVAR_040836671R → Q.1 PublicationCorresponds to variant rs55948035dbSNPEnsembl.1
Natural variantiVAR_040837876R → W in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0258471077I → V.1 PublicationCorresponds to variant rs34822377dbSNPEnsembl.1
Natural variantiVAR_0708861203R → K.2 PublicationsCorresponds to variant rs146298297dbSNPEnsembl.1
Natural variantiVAR_0408381315E → K in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0408391633S → Y.1 PublicationCorresponds to variant rs56412851dbSNPEnsembl.1

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.2. human.

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.
CCDSiCCDS9978.1.
RefSeqiNP_006026.3. NM_006035.3.
UniGeneiHs.654634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QFVX-ray2.65A/B1-415[»]
3TKUX-ray2.15A/B2-417[»]
4UAKX-ray1.73A2-417[»]
4UALX-ray1.71A2-417[»]
ProteinModelPortaliQ9Y5S2.
SMRiQ9Y5S2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114947. 20 interactors.
IntActiQ9Y5S2. 12 interactors.
MINTiMINT-5005780.
STRINGi9606.ENSP00000355237.

Chemistry databases

BindingDBiQ9Y5S2.
ChEMBLiCHEMBL5052.
GuidetoPHARMACOLOGYi1508.

PTM databases

iPTMnetiQ9Y5S2.
PhosphoSitePlusiQ9Y5S2.

Polymorphism and mutation databases

BioMutaiCDC42BPB.
DMDMi92090617.

Proteomic databases

EPDiQ9Y5S2.
MaxQBiQ9Y5S2.
PaxDbiQ9Y5S2.
PeptideAtlasiQ9Y5S2.
PRIDEiQ9Y5S2.

Protocols and materials databases

DNASUi9578.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361246; ENSP00000355237; ENSG00000198752.
GeneIDi9578.
KEGGihsa:9578.
UCSCiuc001ymi.2. human.

Organism-specific databases

CTDi9578.
DisGeNETi9578.
GeneCardsiCDC42BPB.
H-InvDBHIX0011995.
HIX0011996.
HGNCiHGNC:1738. CDC42BPB.
HPAiHPA022821.
MIMi614062. gene.
neXtProtiNX_Q9Y5S2.
OpenTargetsiENSG00000198752.
PharmGKBiPA26268.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IT51. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118994.
HOGENOMiHOG000294133.
HOVERGENiHBG055933.
InParanoidiQ9Y5S2.
KOiK16307.
OMAiSCFSDRG.
OrthoDBiEOG091G09EX.
PhylomeDBiQ9Y5S2.
TreeFamiTF313551.

Enzyme and pathway databases

BioCyciZFISH:HS02132-MONOMER.
SignaLinkiQ9Y5S2.

Miscellaneous databases

ChiTaRSiCDC42BPB. human.
GenomeRNAii9578.
PROiQ9Y5S2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198752.
CleanExiHS_CDC42BPB.
ExpressionAtlasiQ9Y5S2. baseline and differential.
GenevisibleiQ9Y5S2. HS.

Family and domain databases

CDDicd00029. C1. 1 hit.
Gene3Di2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR020454. DAG/PE-bd.
IPR031597. KELK.
IPR011009. Kinase-like_dom.
IPR033232. MRCK_beta.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR22988:SF34. PTHR22988:SF34. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF08826. DMPK_coil. 1 hit.
PF15796. KELK. 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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF56112. 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]
ProtoNetiSearch...

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 30, 2016
This is version 155 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.