MPS1_ARATH
ID MPS1_ARATH Reviewed; 777 AA.
AC Q84VX4; Q8LA38; Q9CA22;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine/threonine-protein kinase MPS1 {ECO:0000305};
DE EC=2.7.12.2 {ECO:0000305};
DE AltName: Full=Monopolar spindle protein 1 homolog {ECO:0000303|PubMed:23049844};
GN Name=MPS1 {ECO:0000303|PubMed:23049844}; Synonyms=PPK1 {ECO:0000305};
GN OrderedLocusNames=At1g77720;
GN ORFNames=T32E8.5 {ECO:0000312|EMBL:AAG51619.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-777.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=23049844; DOI=10.1371/journal.pone.0045707;
RA De Oliveira E.A., Romeiro N.C., Da Silva Ribeiro E., Santa-Catarina C.,
RA Oliveira A.E., Silveira V., De Souza Filho G.A., Venancio T.M., Cruz M.A.;
RT "Structural and functional characterization of the protein kinase Mps1 in
RT Arabidopsis thaliana.";
RL PLoS ONE 7:E45707-E45707(2012).
CC -!- FUNCTION: Involved in the regulation of the onset of mitosis. Involved
CC in a pathway that coordinates cell proliferation and differentiation.
CC Implicated in spindle pole body (SPD) duplication (By similarity). May
CC be a downstream regulator of auxin signaling in the formation of
CC secondary roots (Probable). {ECO:0000250|UniProtKB:P54199,
CC ECO:0000305|PubMed:23049844}.
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=2.7.12.2; Evidence={ECO:0000305};
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=2.7.12.2;
CC 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=2.7.12.2;
CC Evidence={ECO:0000305};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51619.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012193; AAG51619.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36013.1; -; Genomic_DNA.
DR EMBL; BT004636; AAO42882.1; -; mRNA.
DR EMBL; AK227513; BAE99513.1; -; mRNA.
DR EMBL; AY088049; AAM65595.1; -; mRNA.
DR PIR; A96807; A96807.
DR RefSeq; NP_565160.3; NM_106421.5.
DR AlphaFoldDB; Q84VX4; -.
DR SMR; Q84VX4; -.
DR STRING; 3702.AT1G77720.1; -.
DR iPTMnet; Q84VX4; -.
DR PaxDb; Q84VX4; -.
DR PRIDE; Q84VX4; -.
DR ProteomicsDB; 187438; -.
DR EnsemblPlants; AT1G77720.1; AT1G77720.1; AT1G77720.
DR GeneID; 844108; -.
DR Gramene; AT1G77720.1; AT1G77720.1; AT1G77720.
DR KEGG; ath:AT1G77720; -.
DR Araport; AT1G77720; -.
DR TAIR; locus:2203196; AT1G77720.
DR eggNOG; KOG0596; Eukaryota.
DR HOGENOM; CLU_013521_1_0_1; -.
DR InParanoid; Q84VX4; -.
DR OMA; DQTIDEN; -.
DR OrthoDB; 172948at2759; -.
DR PhylomeDB; Q84VX4; -.
DR PRO; PR:Q84VX4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84VX4; baseline and differential.
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:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051304; P:chromosome separation; IEA:InterPro.
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:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
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 PANTHER; PTHR22974:SF21; PTHR22974:SF21; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..777
FT /note="Serine/threonine-protein kinase MPS1"
FT /id="PRO_0000446309"
FT DOMAIN 400..693
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 551
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 406..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 475
FT /note="E -> A (in Ref. 5; AAM65595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 86377 MW; F2C25DA9609A878F CRC64;
MDREDNLPVQ PDKPPKSLVR PILNLETTSS SSSSSSSSPE LLRHLQAAFK RHRPLSKMQT
TSIGPRRSVA PQRQASRNTR LVTAEGQRSQ DVVTLSQSLA ANTLTQDTTN NLAITSVAGE
SASITQPTVS EHFNPSDRQM DFGKSAVTSL ESNLDVQRKS QSLIGTSQDM EWDATNQAEA
SHLDACIGSK HQNLPSVDSE VSLKSEYKDS SSLAKIQGQL GEFPNFLNQP RTRCSAVGSS
WATTTLIHSS SAPMLNATTH VSRSYVEADS NANPHAVQSQ GNLPSCCPSS KVSNILHPNK
DATASEMPAS TNDPEVRVKE TDTSKQQQIT TGLEAPVGSS IYGSDGQANA RLPEELHTSV
SSQPQKSDKH EKVASSKGPS APRKRNYDPD LFFKVNGKLY QRLGKIGSGG SSEVHKVISS
DCTIYALKKI KLKGRDYATA YGFCQEIGYL KKLKGKTNII QLIDYEVTDK TLLQEVLNGT
MSNKDGRVKE DGFIYMVLEY GEIDLAHMLS QKWREIEGSD RTIDENWLRF YWQQILQAVN
TIHEERIVHS DLKPANFLLV RGFLKLIDFG IAKAINSDTT NIQRDSQVGT LSYMSPEAFM
CNESDENGNT IKCGRPSDIW SLGCILYQMV YGRTPFADYK TFWAKFKVIT DPNHEITYNQ
LSNPWLIDLM KKCLAWDRNQ RWRIPELLQH PFLAPPIPHE PQVKTIKLFS LIAESCGSDD
DKANSMISQL EQLLSNPAPL PRNDVLDSRD QNQQLLSRVS ELCIQLQDRL QGLEGEN
