MBK2_CAEBR
ID MBK2_CAEBR Reviewed; 815 AA.
AC A8WJR8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2 {ECO:0000250|UniProtKB:Q13627};
DE EC=2.7.12.1 {ECO:0000250|UniProtKB:Q9XTF3};
DE AltName: Full=Dual specificity Yak1-related kinase mbk-2 {ECO:0000250|UniProtKB:Q13627};
DE AltName: Full=Minibrain Kinase 2 {ECO:0000250|UniProtKB:Q9XTF3};
GN Name=mbk-2 {ECO:0000312|WormBase:CBG23998a};
GN ORFNames=CBG23998 {ECO:0000312|WormBase:CBG23998a};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP20711.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP20711.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 Through phosphorylation of P granule components including meg-1,
CC promotes the disassembly of zygotic P granules in the anterior
CC cytoplasm during zygote polarization, and thus plays a role in P
CC granule distribution and segregation in early stage embryos following
CC meiosis (By similarity). Functions in both spindle positioning and in
CC the posterior localization of cytoplasmic determinants, including pie-
CC 1, pos-1, and pgl-1, in early embryos. Involved in the asymmetric
CC distribution of plk-1 at the 2-cell embryonic stage.
CC {ECO:0000250|UniProtKB:Q9XTF3}.
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:0000250|UniProtKB:Q9XTF3};
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:0000250|UniProtKB:Q9XTF3};
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:0000250|UniProtKB:Q9XTF3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9XTF3};
CC -!- ACTIVITY REGULATION: Activated during oocyte maturation by
CC phosphorylation on Ser-361 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q9XTF3}.
CC -!- SUBUNIT: Part of a complex, consisting of pseudophosphatases egg-3,
CC egg-4, egg-5 and kinase mbk-2. Interacts (via Tyr-618 and Tyr-620) with
CC egg-4 (via tyrosine-protein phosphatase domain) and egg-5 (via
CC tyrosine-protein phosphatase domain); mbk-2 tyrosine phosphorylation
CC enhances the interaction. The interaction inhibits mbk-2 kinase
CC activity and is required for mbk-2 oocyte cortex localization.
CC Interacts (via N-terminus) with egg-3 (via tyrosine-protein phosphatase
CC domain); the interaction does not affect mbk-2 kinase activity, is
CC enhanced by mbk-2 tyrosine phosphorylation status and requires prior
CC binding of mbk-2 to egg-4 and egg-5. {ECO:0000250|UniProtKB:Q9XTF3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9XTF3}. Note=Maintained at the cortex by the
CC cortical anchor egg-3 before meiotic divisions. During anaphase of
CC meiosis I, egg-3 translocates into the cytoplasm on vesicles and is
CC slowly degraded, releasing mbk-2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9XTF3}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9XTF3}.
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; HE601390; CAP20711.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WJR8; -.
DR SMR; A8WJR8; -.
DR STRING; 6238.CBG23998; -.
DR PRIDE; A8WJR8; -.
DR WormBase; CBG23998a; CBP43104; WBGene00042214; Cbr-mbk-2.
DR eggNOG; KOG0667; Eukaryota.
DR HOGENOM; CLU_018023_0_0_1; -.
DR InParanoid; A8WJR8; -.
DR OMA; CTATSMP; -.
DR OrthoDB; 870358at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW Nucleotide-binding; Olfaction; Phosphoprotein; Reference proteome;
KW Sensory transduction; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..815
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase mbk-2"
FT /id="PRO_0000390716"
FT DOMAIN 460..773
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 586
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 466..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTF3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 361
FT /note="Phosphoserine; by cdk-1"
FT /evidence="ECO:0000250|UniProtKB:Q9XTF3"
FT MOD_RES 620
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9XTF3"
SQ SEQUENCE 815 AA; 89584 MW; FE1C1BD9C26AEDF4 CRC64;
MAALASFTRN SRSYGQQPID VTQQGQRDRS VMSLDAQGRS KMSNINYTRP AALSTSDSTI
GVFRRAPSSF SGASSSSSNH HHPVYHSHNS LPPTLIGGSP HSASSNSLAQ GHRNPALGSG
NTLTRSYHQP SSTNSSTSNL HGPLGTYSRD LKQAIRDISP PVINSSANPH LVNYIHTSSF
DNGSYEFPSG QAQQQRRLGG SQQHLAPLQQ TSSSLYSNPQ SSSSQLLGQQ AVRSNYAYQQ
SLPRQQHINS HQTQAFFGTI RAPGNSTNIV TPLRASKTMI DVLAPVRDSV AAQATTGALP
SVGTSSSNGS SNSSSGVGSG GSGSLMTQSI GGPNKHLSAS HSTLNTASTH DSMMHTKIPK
SPSNESLSRS HTSSSGGSQG GHNSNSGSNS GFRPEDAVQT FGAKLVPYEK NEIYNYTRVF
FVGSHAKKQP GVIGGANNGG YDDENGSYQL VVHDHIAYRY EVLKVIGKGS FGQVIKAFDH
KYQQYVALKL VRNEKRFHRQ ADEEIRILDH LRRQDSDGTH NIIHMLDYFN FRNHKCITFE
LLSINLYELI KRNKFQGFSL MLVRKFAYSM LLCLDLLQKN RLIHCDLKPE NVLLKQQGRS
GIKVIDFGSS CFDDQRIYTY IQSRFYRAPE VILGTKYGMP IDMWSLGCIL AELLTGYPLL
PGEDENDQLA LIIELLGMPP PKSLETAKRA RTFITSKGYP RYCTATSMPD GSVVLAGARS
KRGKMRGPPE SRSWSTALKN MGDELFVDFL KRCLDWDPET RMTPAQALKH KWLRRRLPNP
PRDGMDSMGG LADHDKKADL PNIDSNANIL MRKKF
