MBK2_CAEEL
ID MBK2_CAEEL Reviewed; 817 AA.
AC Q9XTF3; H9G2V8; H9G2V9; J7SF89; Q20604; Q27GP3; Q2EEP1; Q9TVF4;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2 {ECO:0000250|UniProtKB:Q13627};
DE EC=2.7.12.1 {ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:25535836};
DE AltName: Full=Dual specificity Yak1-related kinase mbk-2 {ECO:0000250|UniProtKB:Q13627};
DE AltName: Full=Minibrain Kinase 2 {ECO:0000303|PubMed:14697358};
GN Name=mbk-2 {ECO:0000312|WormBase:F49E11.1b};
GN ORFNames=F49E11.1 {ECO:0000312|WormBase:F49E11.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM09088.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12618396; DOI=10.1093/genetics/163.2.571;
RA Raich W.B., Moorman C., Lacefield C.O., Lehrer J., Bartsch D.,
RA Plasterk R.H., Kandel E.R., Hobert O.;
RT "Characterization of Caenorhabditis elegans homologs of the Down syndrome
RT candidate gene DYRK1A.";
RL Genetics 163:571-580(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA94353.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA94353.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14697358; DOI=10.1016/j.ydbio.2003.09.024;
RA Pang K.M., Ishidate T., Nakamura K., Shirayama M., Trzepacz C.,
RA Schubert C.M., Priess J.R., Mello C.C.;
RT "The minibrain kinase homolog, mbk-2, is required for spindle positioning
RT and asymmetric cell division in early C. elegans embryos.";
RL Dev. Biol. 265:127-139(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16289132; DOI=10.1016/j.ydbio.2005.09.053;
RA Nishi Y., Lin R.;
RT "DYRK2 and GSK-3 phosphorylate and promote the timely degradation of OMA-1,
RT a key regulator of the oocyte-to-embryo transition in C. elegans.";
RL Dev. Biol. 288:139-149(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-490.
RX PubMed=16338136; DOI=10.1016/j.cub.2005.11.063;
RA Stitzel M.L., Pellettieri J., Seydoux G.;
RT "The C. elegans DYRK Kinase MBK-2 marks oocyte proteins for degradation in
RT response to meiotic maturation.";
RL Curr. Biol. 16:56-62(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH EGG-3, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-490.
RX PubMed=17869113; DOI=10.1016/j.cub.2007.08.049;
RA Stitzel M.L., Cheng K.C., Seydoux G.;
RT "Regulation of MBK-2/Dyrk kinase by dynamic cortical anchoring during the
RT oocyte-to-zygote transition.";
RL Curr. Biol. 17:1545-1554(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18854162; DOI=10.1016/j.cell.2008.07.040;
RA Guven-Ozkan T., Nishi Y., Robertson S.M., Lin R.;
RT "Global transcriptional repression in C. elegans germline precursors by
RT regulated sequestration of TAF-4.";
RL Cell 135:149-160(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DISRUPTION PHENOTYPE.
RX PubMed=18199581; DOI=10.1242/dev.013425;
RA Nishi Y., Rogers E., Robertson S.M., Lin R.;
RT "Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-
RT primed MEX-5 and MEX-6.";
RL Development 135:687-697(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION IN A COMPLEX WITH EGG-3;
RP EGG-4 AND EGG-5, INTERACTION WITH EGG-3; EGG-4 AND EGG-5, SUBCELLULAR
RP LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-362 AND TYR-621, AND
RP MUTAGENESIS OF SER-362; LYS-490; TYR-619; TYR-621 AND THR-764.
RX PubMed=19879842; DOI=10.1016/j.cell.2009.08.047;
RA Cheng K.C., Klancer R., Singson A., Seydoux G.;
RT "Regulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and
RT EGG-5 during the oocyte-to-embryo transition.";
RL Cell 139:560-572(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25535836; DOI=10.7554/elife.04591;
RA Wang J.T., Smith J., Chen B.C., Schmidt H., Rasoloson D., Paix A.,
RA Lambrus B.G., Calidas D., Betzig E., Seydoux G.;
RT "Regulation of RNA granule dynamics by phosphorylation of serine-rich,
RT intrinsically disordered proteins in C. elegans.";
RL Elife 3:e04591-e04591(2014).
CC -!- FUNCTION: Required for oocyte-to-zygote transition in which it
CC phosphorylates oocyte proteins, including mei-1, oma-1, oma-2, mex-5,
CC and mex-6, modifying their activity and/or stability following meiosis
CC (PubMed:16289132, PubMed:16338136, PubMed:17869113, PubMed:18854162,
CC PubMed:18199581, PubMed:19879842). Through phosphorylation of P granule
CC components including meg-1, promotes the disassembly of zygotic P
CC granules in the anterior cytoplasm during zygote polarization, and thus
CC plays a role in P granule distribution and segregation in early stage
CC embryos following meiosis (PubMed:25535836). Functions in both spindle
CC positioning and in the posterior localization of cytoplasmic
CC determinants, including pie-1, pos-1, and pgl-1, in early embryos
CC (PubMed:14697358). Involved in the asymmetric distribution of plk-1 at
CC the 2-cell embryonic stage (PubMed:18199581).
CC {ECO:0000269|PubMed:14697358, ECO:0000269|PubMed:16289132,
CC ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:17869113,
CC ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18854162,
CC ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:25535836}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:25535836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1; Evidence={ECO:0000269|PubMed:17869113,
CC ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:19879842,
CC ECO:0000269|PubMed:25535836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:19879842};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:19879842};
CC -!- ACTIVITY REGULATION: Activated during oocyte maturation by
CC phosphorylation on Ser-362 by cdk-1. The pseudotyrosine phosphatases
CC egg-4 and egg-5 sequester activated mbk-2 until the meiotic divisions
CC and inhibit mbk-2 kinase activity directly, using a mixed-inhibition
CC mechanism that does not involve tyrosine dephosphorylation.
CC {ECO:0000269|PubMed:19879842}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for mei-1 (Isoform a) {ECO:0000269|PubMed:19879842};
CC Note=The presence of egg-4 in the assay increases the KM of mbk-2 for
CC mei-1. {ECO:0000269|PubMed:19879842};
CC -!- SUBUNIT: Part of a complex, consisting of pseudophosphatases egg-3,
CC egg-4, egg-5 and kinase mbk-2; this complex is required for the oocyte-
CC to-zygote transition (PubMed:19879842). Interacts (via Tyr-619 and Tyr-
CC 621) with egg-4 (via tyrosine-protein phosphatase domain) and egg-5
CC (via tyrosine-protein phosphatase domain); mbk-2 tyrosine
CC phosphorylation enhances the interaction (PubMed:19879842). The
CC interaction inhibits mbk-2 kinase activity and is required for mbk-2
CC oocyte cortex localization. Interacts (via N-terminus) with egg-3 (via
CC tyrosine-protein phosphatase domain); the interaction does not affect
CC mbk-2 kinase activity, is enhanced by mbk-2 tyrosine phosphorylation
CC status and requires prior binding of mbk-2 to egg-4 and egg-5
CC (PubMed:17869113, PubMed:19879842). {ECO:0000269|PubMed:17869113,
CC ECO:0000269|PubMed:19879842}.
CC -!- INTERACTION:
CC Q9XTF3; Q20402: egg-3; NbExp=9; IntAct=EBI-2005616, EBI-2476895;
CC Q9XTF3-2; P34808: mei-1; NbExp=2; IntAct=EBI-2565597, EBI-323248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12618396, ECO:0000269|PubMed:16338136,
CC ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:18854162}.
CC Note=Maintained at the cortex by the cortical anchor egg-3 before
CC meiotic divisions. During anaphase of meiosis I, egg-3 translocates
CC into the cytoplasm on vesicles and is slowly degraded, releasing mbk-2.
CC {ECO:0000269|PubMed:12618396, ECO:0000269|PubMed:16338136,
CC ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879842}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q9XTF3-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q9XTF3-2; Sequence=VSP_053183, VSP_053184, VSP_053186;
CC Name=c {ECO:0000269|PubMed:12618396, ECO:0000269|PubMed:9851916};
CC IsoId=Q9XTF3-3; Sequence=VSP_053187;
CC Name=d {ECO:0000269|PubMed:9851916};
CC IsoId=Q9XTF3-4; Sequence=VSP_053181, VSP_053186;
CC Name=e {ECO:0000269|PubMed:9851916};
CC IsoId=Q9XTF3-5; Sequence=VSP_053182, VSP_053185, VSP_053186;
CC Name=f;
CC IsoId=Q9XTF3-6; Sequence=VSP_053625, VSP_053628, VSP_053629,
CC VSP_053630;
CC Name=g;
CC IsoId=Q9XTF3-7; Sequence=VSP_053627;
CC Name=h;
CC IsoId=Q9XTF3-8; Sequence=VSP_053626;
CC -!- TISSUE SPECIFICITY: In L1 larvae, expressed widely in the nervous
CC system, including head neurons and the ventral nerve cord. In adult
CC animals, continues to be expressed in the nervous system and is also
CC expressed in body wall muscle. {ECO:0000269|PubMed:12618396}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:12618396}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:19879842}.
CC -!- DISRUPTION PHENOTYPE: Maternal-effect embryonic lethality due to
CC defects in spindle positioning and cytokinesis in the early embryo
CC (PubMed:12618396, PubMed:14697358). Microtubules are fragmented and
CC disordered (PubMed:14697358). Abolishes phosphorylation of RNA-binding
CC protein oma-1 in embryos (PubMed:16289132). RNAi-mediated knockdown
CC causes an increase in taf-4 nuclear localization in the one-cell embryo
CC (PubMed:18854162). RNAi-mediated knockdown causes a loss in plk-1
CC asymmetric localization in 2-cell stage embryo without affecting mex-5
CC polarization (PubMed:18199581). RNAi-mediated knockdown disrupts P
CC granule distribution in zygotes after meiosis whereby zygotic P
CC granules fail to disassemble in the anterior cytoplasm during zygote
CC polarization, however new P granules assemble and accumulate in the
CC posterior cytoplasm as in wild-type (PubMed:25535836).
CC {ECO:0000269|PubMed:12618396, ECO:0000269|PubMed:14697358,
CC ECO:0000269|PubMed:16289132, ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:25535836}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000255}.
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DR EMBL; AY090019; AAM09088.1; -; mRNA.
DR EMBL; Z70308; CAA94352.1; -; Genomic_DNA.
DR EMBL; Z70308; CAA94353.1; -; Genomic_DNA.
DR EMBL; Z81121; CAA94353.1; JOINED; Genomic_DNA.
DR EMBL; Z81146; CAA94353.1; JOINED; Genomic_DNA.
DR EMBL; Z70308; CAB54254.2; -; Genomic_DNA.
DR EMBL; Z81121; CAB54254.2; JOINED; Genomic_DNA.
DR EMBL; Z81146; CAB54254.2; JOINED; Genomic_DNA.
DR EMBL; Z70308; CAJ76942.1; -; Genomic_DNA.
DR EMBL; Z70308; CAJ80814.1; -; Genomic_DNA.
DR EMBL; Z81121; CAJ80814.1; JOINED; Genomic_DNA.
DR EMBL; Z70308; CCG28133.1; -; Genomic_DNA.
DR EMBL; Z81121; CCG28133.1; JOINED; Genomic_DNA.
DR EMBL; Z81146; CCG28133.1; JOINED; Genomic_DNA.
DR EMBL; Z70308; CCG28134.1; -; Genomic_DNA.
DR EMBL; Z81121; CCG28134.1; JOINED; Genomic_DNA.
DR EMBL; Z70308; CCM09396.1; -; Genomic_DNA.
DR EMBL; Z81121; CCM09396.1; JOINED; Genomic_DNA.
DR PIR; T22440; T22440.
DR PIR; T22442; T22442.
DR RefSeq; NP_001023207.1; NM_001028036.2. [Q9XTF3-1]
DR RefSeq; NP_001023208.1; NM_001028037.2. [Q9XTF3-3]
DR RefSeq; NP_001040950.1; NM_001047485.3. [Q9XTF3-4]
DR RefSeq; NP_001040951.1; NM_001047486.2. [Q9XTF3-5]
DR RefSeq; NP_001255694.1; NM_001268765.1.
DR RefSeq; NP_001255695.1; NM_001268766.1. [Q9XTF3-6]
DR RefSeq; NP_001263802.1; NM_001276873.1.
DR RefSeq; NP_502492.2; NM_070091.6.
DR AlphaFoldDB; Q9XTF3; -.
DR SMR; Q9XTF3; -.
DR BioGRID; 43342; 132.
DR ComplexPortal; CPX-3381; Egg-3/4/5 MBK-2 complex.
DR IntAct; Q9XTF3; 11.
DR STRING; 6239.F49E11.1b; -.
DR iPTMnet; Q9XTF3; -.
DR EPD; Q9XTF3; -.
DR PaxDb; Q9XTF3; -.
DR PeptideAtlas; Q9XTF3; -.
DR EnsemblMetazoa; F49E11.1a.1; F49E11.1a.1; WBGene00003150. [Q9XTF3-2]
DR EnsemblMetazoa; F49E11.1b.1; F49E11.1b.1; WBGene00003150. [Q9XTF3-1]
DR EnsemblMetazoa; F49E11.1c.1; F49E11.1c.1; WBGene00003150. [Q9XTF3-3]
DR EnsemblMetazoa; F49E11.1d.1; F49E11.1d.1; WBGene00003150. [Q9XTF3-4]
DR EnsemblMetazoa; F49E11.1e.1; F49E11.1e.1; WBGene00003150. [Q9XTF3-5]
DR EnsemblMetazoa; F49E11.1f.1; F49E11.1f.1; WBGene00003150. [Q9XTF3-6]
DR EnsemblMetazoa; F49E11.1g.1; F49E11.1g.1; WBGene00003150. [Q9XTF3-7]
DR EnsemblMetazoa; F49E11.1h.1; F49E11.1h.1; WBGene00003150. [Q9XTF3-8]
DR GeneID; 178250; -.
DR KEGG; cel:CELE_F49E11.1; -.
DR UCSC; F49E11.1c; c. elegans.
DR CTD; 178250; -.
DR WormBase; F49E11.1a; CE05897; WBGene00003150; mbk-2. [Q9XTF3-2]
DR WormBase; F49E11.1b; CE19878; WBGene00003150; mbk-2. [Q9XTF3-1]
DR WormBase; F49E11.1c; CE23751; WBGene00003150; mbk-2. [Q9XTF3-3]
DR WormBase; F49E11.1d; CE39735; WBGene00003150; mbk-2. [Q9XTF3-4]
DR WormBase; F49E11.1e; CE39938; WBGene00003150; mbk-2. [Q9XTF3-5]
DR WormBase; F49E11.1f; CE47098; WBGene00003150; mbk-2. [Q9XTF3-6]
DR WormBase; F49E11.1g; CE47427; WBGene00003150; mbk-2. [Q9XTF3-7]
DR WormBase; F49E11.1h; CE47790; WBGene00003150; mbk-2. [Q9XTF3-8]
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000166363; -.
DR InParanoid; Q9XTF3; -.
DR OMA; CTATSMP; -.
DR OrthoDB; 870358at2759; -.
DR PhylomeDB; Q9XTF3; -.
DR Reactome; R-CEL-6804756; Regulation of TP53 Activity through Phosphorylation.
DR SignaLink; Q9XTF3; -.
DR PRO; PR:Q9XTF3; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003150; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9XTF3; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005694; C:chromosome; IDA:WormBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; ISS:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IMP:UniProtKB.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:WormBase.
DR GO; GO:0007017; P:microtubule-based process; IMP:WormBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0001556; P:oocyte maturation; IC:ComplexPortal.
DR GO; GO:1903864; P:P granule disassembly; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:WormBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:WormBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR Gene3D; 3.30.10.30; -; 1.
DR InterPro; IPR042521; DYRK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Kinase; Magnesium; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..817
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase mbk-2"
FT /id="PRO_0000390717"
FT DOMAIN 461..774
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 587
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 467..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:17869113,
FT ECO:0000269|PubMed:19879842"
FT MOD_RES 362
FT /note="Phosphoserine; by cdk-1"
FT /evidence="ECO:0000269|PubMed:19879842"
FT MOD_RES 621
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:19879842"
FT VAR_SEQ 1..327
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053181"
FT VAR_SEQ 1..301
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053182"
FT VAR_SEQ 1..297
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_053625"
FT VAR_SEQ 1..294
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053183"
FT VAR_SEQ 1..282
FT /note="Missing (in isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_053626"
FT VAR_SEQ 148..164
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_053627"
FT VAR_SEQ 295..310
FT /note="AAQATGLPNVGTSSSN -> MTLFEPSTSGNRMGYR (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053184"
FT VAR_SEQ 298..310
FT /note="ATGLPNVGTSSSN -> MFAIPFHRFYSDE (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_053628"
FT VAR_SEQ 302..310
FT /note="PNVGTSSSN -> MYSSLFELR (in isoform e)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053185"
FT VAR_SEQ 797..817
FT /note="KKTETLPNIDSNANILMRKKF -> VCFIIF (in isoform a,
FT isoform d and isoform e)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053186"
FT VAR_SEQ 797..817
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:12618396,
FT ECO:0000303|PubMed:9851916"
FT /id="VSP_053187"
FT VAR_SEQ 797..802
FT /note="KKTETL -> VCFIIF (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_053629"
FT VAR_SEQ 803..817
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_053630"
FT MUTAGEN 362
FT /note="S->A: Loss of phosphorylation by cdk-1. Loss of
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 362
FT /note="S->E: Constitutively active."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 490
FT /note="K->R: Loss of autophosphorylation activity. Slight
FT loss of binding to egg-4 and egg-5."
FT /evidence="ECO:0000269|PubMed:16338136,
FT ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879842"
FT MUTAGEN 619
FT /note="Y->F: Reduced binding to egg-4 and egg-5 and
FT translocation to the cytoplasm; when associated with F-
FT 621."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 621
FT /note="Y->F: Loss of tyrosine phosphorylation. Reduced
FT binding to egg-4 and egg-5 and translocation to the
FT cytoplasm; when associated with F-619."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 764
FT /note="T->A: No loss of phosphorylation by cdk-1."
FT /evidence="ECO:0000269|PubMed:19879842"
SQ SEQUENCE 817 AA; 89885 MW; 74903C85CB68C428 CRC64;
MAALASFTRN SRSYGQQPID VTQQGQRDRS VMSLDAQGRS VSHECPTSTT LVRQLYLPQI
PQSASFAAAP TSFSGASSSS SNHHHPVYHS QNSLPPNLLG SSQNSASSNS LVQGHRNPAL
GSGNTLTRSY HQPSSTNSST NNLYGPLGTI SRDLKQSIRD ISPPVINSSA NPHLVNYVQT
SSFDNGSYEF PSGQAQQQRR LGGSQQHLAP LQQTASSLYS NPQSSSSQLL GQQQAVRPNY
AYQQSLPRQQ HINSHQTQAF FGTVRGPTNS TNIVTPLRAS KTMIDVLAPV RDTVAAQATG
LPNVGTSSSN GSSNSSSGVG SGGSGSLMTQ SIGGPNKHLS ASHSTLNTAS THDMMHSKIP
KSPSNESLSR SHTSSSGGSQ GGHNSNSGSN SGFRPEDAVQ TFGAKLVPFE KNEIYNYTRV
FFVGSHAKKQ AGVIGGANNG GYDDENGSYQ LVVHDHIAYR YEVLKVIGKG SFGQVIKAFD
HKYQQYVALK LVRNEKRFHR QADEEIRILD HLRRQDSDGT HNIIHMLDYF NFRNHKCITF
ELLSINLYEL IKRNKFQGFS LMLVRKFAYS MLLCLDLLQK NRLIHCDLKP ENVLLKQQGR
SGIKVIDFGS SCFDDQRIYT YIQSRFYRAP EVILGTKYGM PIDMWSLGCI LAELLTGYPL
LPGEDENDQL ALIIELLGMP PPKSLETAKR ARTFITSKGY PRYCTATSMP DGSVVLAGAR
SKRGKMRGPP ASRSWSTALK NMGDELFVDF LKRCLDWDPE TRMTPAQALK HKWLRRRLPN
PPRDGLESMG GLADHEKKTE TLPNIDSNAN ILMRKKF
