TTK_DANRE
ID TTK_DANRE Reviewed; 982 AA.
AC Q8AYG3; Q7T2A4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dual specificity protein kinase Ttk;
DE EC=2.7.12.1;
DE AltName: Full=Mitotic checkpoint serine/threonine-protein kinase Mps1;
DE AltName: Full=Monopolar spindle protein 1;
DE AltName: Full=Protein nightcap;
GN Name=ttk; Synonyms=mps1, ncp {ECO:0000303|PubMed:12399306};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN61408.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTAGENESIS OF ILE-783.
RC STRAIN=AB {ECO:0000269|PubMed:12399306};
RX PubMed=12399306; DOI=10.1242/dev.129.22.5141;
RA Poss K.D., Nechiporuk A., Hillam A.M., Johnson S.L., Keating M.T.;
RT "Mps1 defines a proximal blastemal proliferative compartment essential for
RT zebrafish fin regeneration.";
RL Development 129:5141-5149(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH54627.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH54627.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=12481136; DOI=10.1126/science.1077857;
RA Poss K.D., Wilson L.G., Keating M.T.;
RT "Heart regeneration in zebrafish.";
RL Science 298:2188-2190(2002).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15231734; DOI=10.1101/gad.1182604;
RA Poss K.D., Nechiporuk A., Stringer K.F., Lee C., Keating M.T.;
RT "Germ cell aneuploidy in zebrafish with mutations in the mitotic checkpoint
RT gene mps1.";
RL Genes Dev. 18:1527-1532(2004).
CC -!- FUNCTION: Phosphorylates proteins on serine, threonine, and tyrosine
CC (By similarity). Involved in mitotic cell cycle checkpoint control.
CC Required for fin and heart regeneration. Required to prevent chromosome
CC segregation errors during meiosis. {ECO:0000250,
CC ECO:0000269|PubMed:12399306, ECO:0000269|PubMed:12481136,
CC ECO:0000269|PubMed:15231734}.
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:0000305};
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:0000305};
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:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q86UE8};
CC -!- TISSUE SPECIFICITY: Barely detectable in adult somatic tissues.
CC Expressed in immature germ cells that have not completed meiosis. In
CC ovary, expressed predominantly in previtellogenic oocytes. In testis,
CC expressed in primary and secondary spermatocytes, but not mature
CC spermatozoa. {ECO:0000269|PubMed:12399306,
CC ECO:0000269|PubMed:15231734}.
CC -!- INDUCTION: Strongly induced in a subpopulation of cells in the proximal
CC blastema during regenerative outgrowth. {ECO:0000269|PubMed:12399306}.
CC -!- DISRUPTION PHENOTYPE: Mutants show anomalies in the chromosome number
CC of male germ cells, leading to aneuploidy and severe developmental
CC defects in their progeny. {ECO:0000269|PubMed:15231734}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF488735; AAN61408.1; -; mRNA.
DR EMBL; BC054627; AAH54627.1; -; mRNA.
DR RefSeq; NP_778207.1; NM_175042.2.
DR AlphaFoldDB; Q8AYG3; -.
DR SMR; Q8AYG3; -.
DR STRING; 7955.ENSDARP00000121369; -.
DR PaxDb; Q8AYG3; -.
DR PRIDE; Q8AYG3; -.
DR GeneID; 317763; -.
DR KEGG; dre:317763; -.
DR CTD; 7272; -.
DR ZFIN; ZDB-GENE-030123-1; ttk.
DR eggNOG; KOG0596; Eukaryota.
DR InParanoid; Q8AYG3; -.
DR OrthoDB; 172948at2759; -.
DR PhylomeDB; Q8AYG3; -.
DR PRO; PR:Q8AYG3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000776; C:kinetochore; 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:0046872; F:metal ion 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; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0060249; P:anatomical structure homeostasis; IMP:ZFIN.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP:ZFIN.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0007060; P:male meiosis chromosome segregation; IMP:ZFIN.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
DR GO; GO:0042246; P:tissue regeneration; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027084; Prot_kin_Mps1_fam.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22974:SF21; PTHR22974:SF21; 3.
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; Cell cycle; Cell division; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..982
FT /note="Dual specificity protein kinase Ttk"
FT /id="PRO_0000086390"
FT DOMAIN 653..916
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 178..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 775
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 659..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 783
FT /note="I->K: In zp1; temperature-sensitive mutation that
FT blocks fin regeneration at the restrictive temperature."
FT /evidence="ECO:0000269|PubMed:12399306"
FT CONFLICT 210
FT /note="N -> S (in Ref. 1; AAN61408)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> SS (in Ref. 1; AAN61408)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..495
FT /note="EH -> DL (in Ref. 1; AAN61408)"
FT /evidence="ECO:0000305"
FT CONFLICT 509..510
FT /note="GM -> YI (in Ref. 1; AAN61408)"
FT /evidence="ECO:0000305"
FT CONFLICT 516..517
FT /note="PV -> SA (in Ref. 1; AAN61408)"
FT /evidence="ECO:0000305"
FT CONFLICT 553..554
FT /note="PV -> SL (in Ref. 1; AAN61408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 110012 MW; 3B9C7D38DDF76C22 CRC64;
MDEEESTERQ MQIAMLCQKL AMMKQLFNED DTDYINQAIS SNSPDTCRTF LSNLEKKGNP
QADPSLLSKL MDSYTRVFSS MPLGKYSQNE SYAKMLVRFA ELKAIQDVND AQTSFDIARS
HCKDFAFVHV AYAQFELLQG NMKKCTMILQ KAFEMNAKPR HVLEAAVRNL KTGKRQLLSH
EDKENLSVSA LDHTQGSRRS DGTCELKPSN TFLHSDQKFS PQEENGPVWR TGSQHRRTAM
AERVPMVPLS IPENETSDSD CAQKAEAPFT HSSGFSRQTS GSSVRSAFSL CSSKKGTPDG
DSYSLNIKPP VISPDYLRED IEEGHTITAL LNRAEKRETA RTEETTDINQ IISTNSTEGC
QAFLKNLEKR ADPHSDAAFL SKLLDCYSKV FARFPLAEHC KTESYARMLV RYAELKGIED
PEDAADDFSI ARSHCKAFAF VHIAHAQFEL SRGNSRKSVS ILQKALSSNA RPIELLQTAI
RNLKSGKTLL LPAEHQESSE AENVEAQNGM KREENPVKAP EDHQKPFSKE TSSEWKIPAL
ITKHTSPEDR KAPVEPVSSS SSHHAVRTPA PLRLNPSLSC QTPNYRQPNP NSFVTPVVKQ
RPVIVSVPAT AQKMCPTALP CTPQSGVSYI QPPTQTPSSA FSNESITIKG KQFFIFKMIG
RGGSSKVYQV FDHKKHVYAV KYVNLEEADA QAVESYKNEI EHLNHLQQYS DQIIKLYDYE
ITSSYIYMLM ECGHLDLNTW LRNRKTVKPL DRKAYWRNML EAVHTIHKHG IVHSDLKPAN
FLIVDGSLKL IDFGIANQIQ PDVTSIMKDS QVGTLNYMPP EAIKDTSSNG KPGSKISAKG
DVWSLGCILY CMTYGKTPFQ NITNQISKIH AIIDPSHEID FPDIPEKDLL DVLKKCLVRN
PRERISIAEL LDHPYLQLQP QPAPEPAETS SSDFKRILNE LVALQSPNSI ARAASNLAMM
CNSGRKLDVS ECVKSSSQTL WK
