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Protein

Maternal embryonic leucine zipper kinase

Gene

melk

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, self-renewal of stem cells, apoptosis and splicing regulation. Also plays a role in primitive hematopoiesis, possibly by affecting the expression of genes critical for hematopoiesis (By similarity). Plays a role in cytokinesis during early development.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by autophosphorylation of the T-loop at Thr-169 and Ser-173: in contrast to other members of the SNF1 subfamily, phosphorylation at Thr-169 is not mediated by STK11/LKB1 but via autophosphorylation instead.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei42 – 421ATPPROSITE-ProRule annotation
Active sitei134 – 1341Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Maternal embryonic leucine zipper kinase (EC:2.7.11.1)
Short name:
MELK
Alternative name(s):
Protein kinase Eg3
Short name:
pEg3 kinase
Gene namesi
Name:melk
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-987660. melk.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Maternal embryonic leucine zipper kinasePRO_0000413430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691Phosphothreonine; by autocatalysisBy similarity
Modified residuei173 – 1731Phosphoserine; by autocatalysisBy similarity
Modified residuei414 – 4141Phosphothreonine1 Publication
Modified residuei449 – 4491Phosphothreonine1 Publication
Modified residuei451 – 4511Phosphothreonine1 Publication
Modified residuei481 – 4811Phosphothreonine1 Publication
Modified residuei483 – 4831Phosphothreonine1 Publication
Modified residuei498 – 4981Phosphoserine1 Publication
Modified residuei505 – 5051Phosphoserine1 Publication
Modified residuei517 – 5171Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated: autophosphorylation of the T-loop at Thr-169 and Ser-173 is required for activation (By similarity). Phosphorylated by the maturation promoting factor (MPF), composed of cdk1 and a cyclin-B. Also phosphorylated by some MAPK. Phosphorylated during oocyte maturation. Dephosphorylation destabilizes the protein. There is some ambiguity for some phosphosites: Thr-481/Thr-483 and Ser-505/Ser-517.By similarity3 Publications
Degraded when cells exit mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiQ91821.

Interactioni

Protein-protein interaction databases

BioGridi99263. 1 interaction.
IntActiQ91821. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ91821.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 265253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini602 – 65150KA1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni284 – 32340UBA-likeBy similarityAdd
BLAST
Regioni328 – 651324Autoinhibitory regionBy similarityAdd
BLAST

Domaini

The KA1 domain mediates binding to phospholipids and targeting to membranes.By similarity

Sequence similaritiesi

Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG106273.
KOiK08799.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVDDYEELL KYYELHETVG TGGFAKVKLA SHLITGEKVA IKIMDKESLG
60 70 80 90 100
DDLPRVKTEI DAMKNLSHQH VCRLYHVIET PKKIFMVLEY CPGGELFDYI
110 120 130 140 150
IAKDRLTEEE ARVFFRQIVS AVAYIHSQGY AHRDLKPENL LIDEDQNLKL
160 170 180 190 200
IDFGLCAKPK GGLDYHLMTC CGSPAYAAPE LIQGKAYIGS EADIWSMGVL
210 220 230 240 250
MYALMCGYLP FDDDNVMVLY KKIMRGKYEI PKWLSPGSVL LLSQMMQVDP
260 270 280 290 300
KKRITVKHLL NHPWLMHGYS CPVEWQSKYP LGYIDEDCVT ELSVFYKYSR
310 320 330 340 350
TSTTRLISEW SYDHITASYL LLHSKKSHGK AVRLKHPLAV GDQAVTSFKE
360 370 380 390 400
LRPKSKLDFE EPNGEIAYVF GSMDFSDEEL FSEDFTYSSF EPHTPKEYVK
410 420 430 440 450
GRLEFNSVDS APATPVVQRN ARHKNEDKEN SNTAVARDEN VFLHPAPWTP
460 470 480 490 500
TPRRKQNEKK GILTTPNKNT QTKEKNQSKE TPTKKPIGTG EEFANVISPE
510 520 530 540 550
RRCRSVELDL NQAHIDSAQK KKGAKVFGSL ERGLDKMITM LTPSKRKGYT
560 570 580 590 600
REGPRKLRAH YNVTTTNIVN PEQLLNQIVR VLPSKNVDYV QKGYTLKCKT
610 620 630 640 650
QSDFGKVTMQ FELEVCQLSK SEVVGIRRQR LKGDAWVYKR LVEDILSSCK

V
Length:651
Mass (Da):74,307
Last modified:October 1, 2001 - v2
Checksum:iA21B397D0F1A9C9A
GO

Sequence cautioni

The sequence AAI00162.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z17205 mRNA. Translation: CAA78913.2.
BC106635 mRNA. Translation: AAI06636.1.
BC100161 mRNA. Translation: AAI00162.1. Sequence problems.
PIRiS52244.
RefSeqiNP_001081569.1. NM_001088100.1.
UniGeneiXl.7325.

Genome annotation databases

GeneIDi397927.
KEGGixla:397927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z17205 mRNA. Translation: CAA78913.2.
BC106635 mRNA. Translation: AAI06636.1.
BC100161 mRNA. Translation: AAI00162.1. Sequence problems.
PIRiS52244.
RefSeqiNP_001081569.1. NM_001088100.1.
UniGeneiXl.7325.

3D structure databases

ProteinModelPortaliQ91821.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi99263. 1 interaction.
IntActiQ91821. 1 interaction.

PTM databases

iPTMnetiQ91821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397927.
KEGGixla:397927.

Organism-specific databases

CTDi9833.
XenbaseiXB-GENE-987660. melk.

Phylogenomic databases

HOVERGENiHBG106273.
KOiK08799.

Family and domain databases

Gene3Di3.30.310.80. 1 hit.
InterProiIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Eg3, selected by differential screening encodes a new Xenopus protein kinase."
    Roghi C., Le Guellec R., Paris J., Couturier A., Philippe M.
    Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Egg.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo and Oocyte.
  3. "Cell cycle regulation of pEg3, a new Xenopus protein kinase of the KIN1/PAR-1/MARK family."
    Blot J., Chartrain I., Roghi C., Philippe M., Tassan J.P.
    Dev. Biol. 241:327-338(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  4. "Cell-cycle-dependent cortical localization of pEg3 protein kinase in Xenopus and human cells."
    Chartrain I., Couturier A., Tassan J.P.
    Biol. Cell 98:253-263(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION AT THR-414; THR-449; THR-451; THR-481; THR-483; SER-498; SER-505 AND SER-517.
  6. "Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit."
    Badouel C., Chartrain I., Blot J., Tassan J.P.
    Exp. Cell Res. 316:2166-2173(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, PROTEIN DEGRADATION.
  7. "A functional analysis of MELK in cell division reveals a transition in the mode of cytokinesis during Xenopus development."
    Le Page Y., Chartrain I., Badouel C., Tassan J.P.
    J. Cell Sci. 124:958-968(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMELK_XENLA
AccessioniPrimary (citable) accession number: Q91821
Secondary accession number(s): Q498M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 1, 2001
Last modified: May 11, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.