TTK_MACFA
ID TTK_MACFA Reviewed; 856 AA.
AC Q4R945;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Dual specificity protein kinase TTK;
DE EC=2.7.12.1 {ECO:0000250|UniProtKB:P33981};
GN Name=TTK; ORFNames=QtsA-10742;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates proteins on serine, threonine, and tyrosine
CC (By similarity). Probably associated with cell proliferation (By
CC similarity). Phosphorylates MAD1L1 to promote mitotic checkpoint
CC signaling (By similarity). Essential for chromosome alignment by
CC enhancing AURKB activity (via direct CDCA8 phosphorylation) at the
CC centromere, and for the mitotic checkpoint (By similarity).
CC {ECO:0000250|UniProtKB:P33981}.
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:P33981};
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:P33981};
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:P33981};
CC -!- ACTIVITY REGULATION: Inhibited by the ATP-competitive kinase inhibitor,
CC SP600125. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TPR; the interactions occurs in a microtubule-
CC independent manner (By similarity). Interacts with MAD1L1 and MAD2L1
CC (By similarity). {ECO:0000250|UniProtKB:P33981}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB168252; BAE00376.1; -; mRNA.
DR AlphaFoldDB; Q4R945; -.
DR SMR; Q4R945; -.
DR STRING; 9541.XP_005552546.1; -.
DR eggNOG; KOG0596; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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; IEA:UniProtKB-KW.
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:0051304; P:chromosome separation; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR Gene3D; 1.25.40.10; -; 1.
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; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48452; SSF48452; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..856
FT /note="Dual specificity protein kinase TTK"
FT /id="PRO_0000311351"
FT DOMAIN 524..790
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 369..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 646
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 530..538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33981"
SQ SEQUENCE 856 AA; 96783 MW; 194168C4A238E22B CRC64;
MESEDLSGRE LTIDSIMNKV RDIKNKFKNE DLTDELSLNK ISADTTDNSG TVNQIMMMAN
SPEDWLSLLL KLEKNSVPLS DALLNKLIGR YSQAIEALPP DKYGQNESFA RIQVRFAELK
AIQEPDDARD YFQMARANCK KFAFVHISFA QFELSQGNVK KSKQLLQEAV ERGAVPLEML
EIALRNLNLQ KKQLLSEEEK KTLSASMVLT AQESFSSSLG HLQNRNNSCD SRGQTTKARF
LYGENMPPQD AEIGYRNSLK QTNKTKQSCP FGRVPVNLLN SPDCDVKTDD SVVPCFIKRQ
TSRSECRDLV VAGSKPSGND SCELRNLKSV QNINCKEPLV SDEKSSELII TDSVTLKNKT
ESSLRAKLEE TKEYQEPEVP ESNQKQWQSK RKSACINENP VASSNQWQIP ELARKVNIEK
HTTFEQPVFS VSKQSPPMSA SKWFDPKSIC KTPSSNTLDD YMSCFRTPVV KNDFPPACQL
STPYGQPACF QQQQQQIPAT PLQNLQVLAS SSANECISVK GRIYSILKQI GSGGSSKVFQ
VLNEKKQIYA IKFVNLEEAD NQTLDSYRNE IAYLNKLQQH SDKIIRLYDY EITDQYIYMV
MECGNIDLNS WLKKKKSIDP WERKSYWKNM LEAVHTIHQH GIVHSDLKPA NFLIVDGMLK
LIDFGIANQM QPDTTSIVKD SQVGTVNYMP PEAIKDMSSS RENGKSKSKI SPKSDVWSLG
CILYYMTYGK TPFQHIINQI SKLHAIIDPN HEIEFPDIPE KDLQDVLKCC LKRDPKQRIS
IPELLAHPYV QIQTHPGNQM AKGTTEEMKY VLGQLVGLNS PNSILKAAKT LYEHYSGGES
HNSSSSKTFG KKREKK
