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Protein

Serine/threonine-protein kinase mrck-1

Gene

mrck-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation (PubMed:19675126). Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation (PubMed:25743393).1 Publication1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121ATPPROSITE-ProRule annotation
Active sitei207 – 2071Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi89 – 979ATPPROSITE-ProRule annotation
Zinc fingeri957 – 100751Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • embryo development ending in birth or egg hatching Source: WormBase
  • embryonic body morphogenesis Source: WormBase
  • embryonic morphogenesis Source: WormBase
  • intracellular signal transduction Source: InterPro
  • nematode larval development Source: WormBase
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

SignaLinkiO01583.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase mrck-1Curated (EC:2.7.11.1By similarity)
Alternative name(s):
Myotonic dystrophy kinase-related CDC42-binding kinase homologImported
Gene namesi
Name:mrck-1Imported
ORF Names:K08B12.5Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiK08B12.5; CE30818; WBGene00006437; mrck-1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Normal adult development, but progeny arrest at either the L1 stage or during embryogenesis (PubMed:19675126). RNAi-mediated knockdown causes excretory canal truncation, abnormal lumen and cyst formation. In addition, causes a reduced distribution of Golgi and ER components along the excretory canal length and a decrease in cdc-42 activation (PubMed:25743393).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15921592Serine/threonine-protein kinase mrck-1PRO_0000432383Add
BLAST

Proteomic databases

EPDiO01583.
PaxDbiO01583.

Expressioni

Tissue specificityi

Expressed in embryonic and L4 larval seam cells and in embryonic dorsal and ventral epidermal cells. Also expressed in the pharynx throughout development and in sublateral nerve cords in the L4 larva.1 Publication

Gene expression databases

ExpressionAtlasiO01583. baseline.

Interactioni

Protein-protein interaction databases

DIPiDIP-25790N.
MINTiMINT-1104226.
STRINGi6239.K08B12.5.2.

Structurei

3D structure databases

ProteinModelPortaliO01583.
SMRiO01583. Positions 9-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 351269Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini352 – 42675AGC-kinase C-terminalSequence analysisAdd
BLAST
Domaini1026 – 1154129PHPROSITE-ProRule annotationAdd
BLAST
Domaini1181 – 1479299CNHPROSITE-ProRule annotationAdd
BLAST
Domaini1544 – 155714CRIBPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili444 – 782339Sequence analysisAdd
BLAST
Coiled coili811 – 87161Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi516 – 5194Poly-GlnSequence analysis

Sequence similaritiesi

Contains 1 CNH domain.PROSITE-ProRule annotation
Contains 1 CRIB domain.PROSITE-ProRule annotation
Contains 1 PH domain.
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri957 – 100751Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0612. Eukaryota.
ENOG410XR1Q. LUCA.
HOGENOMiHOG000294133.
InParanoidiO01583.
OMAiSNNKCSI.
PhylomeDBiO01583.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
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]
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
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.

O01583-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPPPDDSA PVRLKTLENI YMDGPSKKPE ALSFETLIDS LICLYDECCN
60 70 80 90 100
STLRKEKCIA EFVESVKTVI SKAKKLRLSR DDFEVLKVIG KGAFGEVAVV
110 120 130 140 150
RMRGVGEIYA MKILNKWEMV KRAETACFRE ERDVLVYGDR RWITNLHYAF
160 170 180 190 200
QDEKNLYFVM DYYIGGDMLT LLSKFVDHIP ESMAKFYIAE MVLAIDSLHR
210 220 230 240 250
LGYVHRDVKP DNVLLDMQGH IRLADFGSCL RILADGSVAS NVAVGTPDYI
260 270 280 290 300
SPEILRAMED GRGRYGKECD WWSLGICMYE MLYGTTPFYS ERLVDTYGKI
310 320 330 340 350
MSHQDMLDFP DDEIDWVVSE EAKDLIRQLI CSSDVRFGRN GLSDFQLHPF
360 370 380 390 400
FEGIDWNTIR DSNPPYVPEV SSPEDTSNFD VDVCEDDFTP CLQETQPPRV
410 420 430 440 450
LAAFTGNHLP FVGFSYTHGS LLSDARSLTD EIRAIAQRCQ GDAELMEKSV
460 470 480 490 500
DGFMVELENE KAELVQKLKE AQTIIAQHVA ENPRSEEDRN YESTIAQLKD
510 520 530 540 550
EIQILNKRLE DEALAQQQQK PKDEIVAESE KKLKELKERN KQLVMEKSEI
560 570 580 590 600
QRELDNINDH LDQVLVEKAT VVQQRDDMQA ELADVGDSLL TEKDSVKRLQ
610 620 630 640 650
DEAEKAKKQV ADFEEKLKEI ETEKIALIKK QEEVTIEARK SVETDDHLSE
660 670 680 690 700
EVVAAKNTIA SLQATNEERE TEIKKLKQRM DEERASHTAQ SEQEMKQLEA
710 720 730 740 750
HYERAQKMLQ DNVEQMNVEN RGLRDEIEKL SQQMAALPRG GLNEQQLHEI
760 770 780 790 800
FNWVSEEKAT REEMENLTRK ITGEVESLKN NSPLTTSNYI QNTPSGWGSR
810 820 830 840 850
RMNNVARKDG LDLQRQLQAE IDAKLKLKAE LKNSQEQYLT SAARLDDTEK
860 870 880 890 900
RMASLMREVA MLKQQKNIEN SSDSAFSSTM GRGDLMISMN NDYEMSNSSL
910 920 930 940 950
MRQEMISRQS TPSYENAILL HDHQVPKRVD DLRYKQKPMK TASGIFSPVS
960 970 980 990 1000
ISAMERGHNF ERMKIKTPTK CGHCTSILIG LDRQGLFCQS CQYACHVSCA
1010 1020 1030 1040 1050
ERVSQSCPVP EEERRPLGID PTRGVGTAYE GLVKTPRAGG VRKGWQTAYV
1060 1070 1080 1090 1100
VVCDFKLYLY DCTVDRQNKM QDVKNEIRLV LDMRDPDFTV CGVSEADVIH
1110 1120 1130 1140 1150
AQKGDIPKIF RVTTTQILNS SSEYSSSSKF YTLFMAETEE EKRKWVVALS
1160 1170 1180 1190 1200
ELKTLLRRSK LADRKAFLVK EVFDVTTLPS IRVAQCCAII DRSKIVIGFS
1210 1220 1230 1240 1250
DHGLYCIEIS RQLLIPVGGE KENKQRCVET VEYDEAEQLL MMIVGPAKDR
1260 1270 1280 1290 1300
HVRIVPSAAL DGRDLKWIKV NDTKGCHLLA VGTNNPGGRA GFFAVAFKKS
1310 1320 1330 1340 1350
VTIFQIDRSE KRHKKWKDLA MPGTPQSIAI FNGRLYVGFS HSFRSWSLVG
1360 1370 1380 1390 1400
VDSSPVGSGD ASGAVLQHIS LVNMEDTSLQ FLNQQTSYEA KLIVNVPGSP
1410 1420 1430 1440 1450
DEYLLVFNMI GLYVNEMGRR SRLPEVMFPT QAKYFAYHEP YLCVFSENEV
1460 1470 1480 1490 1500
DIFNVTLAEW VQTINLRSAK PLSGDGILST CLCNDSPIFV LLQNVLQDQD
1510 1520 1530 1540 1550
SIEVPVNLAS GSTDGRKVTR RKFTFRTIGK DDRSASERRS HIQISTPSDF
1560 1570 1580 1590
MHIVHMGPAP VMELQQNFID LQSNHSHTSS DKDSLNRSVN ND
Length:1,592
Mass (Da):180,744
Last modified:October 1, 2002 - v3
Checksum:iF909FA8F5C9C876C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081273 Genomic DNA. Translation: CCD70382.1.
PIRiT25808.
RefSeqiNP_504599.2. NM_072198.5.
UniGeneiCel.20082.

Genome annotation databases

EnsemblMetazoaiK08B12.5a.1; K08B12.5a.1; WBGene00006437.
K08B12.5a.2; K08B12.5a.2; WBGene00006437.
GeneIDi179013.
UCSCiK08B12.5.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081273 Genomic DNA. Translation: CCD70382.1.
PIRiT25808.
RefSeqiNP_504599.2. NM_072198.5.
UniGeneiCel.20082.

3D structure databases

ProteinModelPortaliO01583.
SMRiO01583. Positions 9-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-25790N.
MINTiMINT-1104226.
STRINGi6239.K08B12.5.2.

Proteomic databases

EPDiO01583.
PaxDbiO01583.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiK08B12.5a.1; K08B12.5a.1; WBGene00006437.
K08B12.5a.2; K08B12.5a.2; WBGene00006437.
GeneIDi179013.
UCSCiK08B12.5.1. c. elegans.

Organism-specific databases

CTDi179013.
WormBaseiK08B12.5; CE30818; WBGene00006437; mrck-1.

Phylogenomic databases

eggNOGiKOG0612. Eukaryota.
ENOG410XR1Q. LUCA.
HOGENOMiHOG000294133.
InParanoidiO01583.
OMAiSNNKCSI.
PhylomeDBiO01583.

Enzyme and pathway databases

SignaLinkiO01583.

Miscellaneous databases

PROiO01583.

Gene expression databases

ExpressionAtlasiO01583. baseline.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
InterProiIPR000961. AGC-kinase_C.
IPR001180. CNH_dom.
IPR000095. CRIB_dom.
IPR011009. Kinase-like_dom.
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]
PfamiPF00130. C1_1. 1 hit.
PF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.
  2. "Myosin II regulation during C. elegans embryonic elongation: LET-502/ROCK, MRCK-1 and PAK-1, three kinases with different roles."
    Gally C., Wissler F., Zahreddine H., Quintin S., Landmann F., Labouesse M.
    Development 136:3109-3119(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  3. "CCM-3/STRIPAK promotes seamless tube extension through endocytic recycling."
    Lant B., Yu B., Goudreault M., Holmyard D., Knight J.D., Xu P., Zhao L., Chin K., Wallace E., Zhen M., Gingras A.C., Derry W.B.
    Nat. Commun. 6:6449-6449(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMRCK_CAEEL
AccessioniPrimary (citable) accession number: O01583
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 4, 2015
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. 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.