MBK1_CAEEL
ID MBK1_CAEEL Reviewed; 882 AA.
AC Q8WQL7; Q22155;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase mbk-1 {ECO:0000250|UniProtKB:Q13627};
DE EC=2.7.12.1 {ECO:0000269|PubMed:12618396};
DE AltName: Full=Dual specificity Yak1-related kinase mbk-1 {ECO:0000250|UniProtKB:Q13627, ECO:0000312|EMBL:AAL40874.1};
DE AltName: Full=Minibrain Kinase 1 {ECO:0000250|UniProtKB:Q9XTF3};
GN Name=mbk-1 {ECO:0000312|EMBL:AAL40874.1, ECO:0000312|WormBase:T04C10.1};
GN ORFNames=T04C10.1;
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:AAL40874.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, 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:0000312|EMBL:CAA93756.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA93756.2};
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).
CC -!- FUNCTION: Possible role in the function of olfactory neurons.
CC {ECO:0000269|PubMed:12618396}.
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:12618396};
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:12618396};
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:12618396};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:12618396};
CC -!- INTERACTION:
CC Q8WQL7; Q7K7J0: gei-18; NbExp=3; IntAct=EBI-329013, EBI-2315822;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12618396}.
CC -!- TISSUE SPECIFICITY: Expressed in all somatic cells.
CC {ECO:0000269|PubMed:12618396}.
CC -!- DEVELOPMENTAL STAGE: First observed during early cell morphogenesis in
CC the embryo, levels increase during later embryonic development and
CC remain at comparable levels throughout larval and adult stages.
CC {ECO:0000269|PubMed:12618396}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:12618396}.
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; AY064464; AAL40874.1; -; mRNA.
DR EMBL; Z69885; CAA93756.2; -; Genomic_DNA.
DR PIR; T24445; T24445.
DR RefSeq; NP_510460.2; NM_078059.4.
DR AlphaFoldDB; Q8WQL7; -.
DR SMR; Q8WQL7; -.
DR BioGRID; 46475; 139.
DR IntAct; Q8WQL7; 3.
DR MINT; Q8WQL7; -.
DR STRING; 6239.T04C10.1; -.
DR EPD; Q8WQL7; -.
DR PaxDb; Q8WQL7; -.
DR PeptideAtlas; Q8WQL7; -.
DR EnsemblMetazoa; T04C10.1.1; T04C10.1.1; WBGene00003149.
DR GeneID; 181578; -.
DR KEGG; cel:CELE_T04C10.1; -.
DR UCSC; T04C10.1; c. elegans.
DR CTD; 181578; -.
DR WormBase; T04C10.1; CE33442; WBGene00003149; mbk-1.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000170191; -.
DR HOGENOM; CLU_014959_0_0_1; -.
DR InParanoid; Q8WQL7; -.
DR OMA; DGIYYCK; -.
DR OrthoDB; 870358at2759; -.
DR PhylomeDB; Q8WQL7; -.
DR Reactome; R-CEL-1538133; G0 and Early G1.
DR PRO; PR:Q8WQL7; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003149; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR CDD; cd14226; PKc_DYRK1; 1.
DR InterPro; IPR028318; DYRK1A/B_MNB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR044131; PKc_DYR1A/1B.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24058:SF121; PTHR24058:SF121; 2.
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 ATP-binding; Kinase; Magnesium; Nucleotide-binding; Nucleus; Olfaction;
KW Reference proteome; Sensory transduction; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..882
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase mbk-1"
FT /id="PRO_0000390715"
FT DOMAIN 328..649
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 334..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTF3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 882 AA; 101244 MW; DD5C9DD354DA7098 CRC64;
MNTADVPDNL QSWGQQPSSS YSNTQQHSQM TNLPPINHNN LCDTEPMNED FQLQDVQADE
LQKQQKQQEQ QHIQQQNAQR FIAQSRQPHS NILRFPQPPI TSIKTNSHAF YPQQEVTQVR
PKKHRVSMTN AEAALTPGMP PEKQAAKKRN IGQFSTDTVP AGIGMIGIPF ESTSKPLQIQ
QFRNPQDAPV RKLTSDLIKT YKAINESFYL RKQVRRDRHK SQDAGKPKGS KDGSGASLTD
TFSIHNAIPI TSSDNHYQQD AHQNAPPLLD TNAPPTSTMV VPMRTETDLQ QQQRQKSSRG
GPYNNGYDDQ NYDYILKNGE IFDKRYVILS DTPVGKGSFG QVTKAYDTLN KEEVAIKIIK
NKKTFFDQAQ IEIHLLELTN AHDKDNKYNI VTLKGHFVHR AHLCLVFELL SYNLYDLLKN
TSFRGVSLNL ARKFAQQLGK TLLFLSSPEL SIIHCDLKPE NVLLVNAKRS QIRVIDFGSS
CQTGHRIYQY IQSRFYRSPE VLLGIAYDTK IDMWSLGCIL VEMHTGEPLF AGSSEVDQMM
KIVEVLGMPP KEMLDIGPKT HKYFDKTEDG IYYCKKTRDG YRHTYKAPGA RKLHEILGVT
SGGPGGRRLG EPGHSVEDYS KFKDLIKRML QFDPKQRISP YYVVRHPFLK QKEERVPSQP
PVSHSNLQQQ QQLYIQQPSS QMSQVMESPS VGSVYVEDNG MYRQAPGSSA NPISVTSSFD
EGDAMEVDAG RRRFSAHQQN YHNPNYQYSQ PQQQQQQQYQ QTQRTQLEQQ QKQAQLQQQL
QQQQMQQQQQ QQQQRQHMPQ AQSSSQQHLQ SRARPRQQDQ NEWRNQFELD DTFQQKQRKV
DDSVSNQISR NQFNPQQVSM THGNVNANNR EMEKLDYPNN KL
