MPH1L_SCHPO
ID MPH1L_SCHPO Reviewed; 678 AA.
AC O94235; Q9P7Z5; Q9URW0;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein kinase mph1;
DE EC=2.7.12.1;
GN Name=mph1; ORFNames=SPBC106.01, SPBC1271.16c, SPBC243.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9601094; DOI=10.1242/jcs.111.12.1635;
RA He X., Jones M.H., Winey M., Sazer S.;
RT "Mph1, a member of the Mps1-like family of dual specificity protein
RT kinases, is required for the spindle checkpoint in S. pombe.";
RL J. Cell Sci. 111:1635-1647(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Involved in the regulation of the onset of mitosis. Involved
CC in a pathway that coordinates cell proliferation and differentiation.
CC {ECO:0000269|PubMed:9601094}.
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 -!- 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;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF020705; AAD01648.1; -; mRNA.
DR EMBL; CU329671; CAB72266.1; -; Genomic_DNA.
DR PIR; T43539; T43539.
DR RefSeq; NP_595150.2; NM_001021059.3.
DR AlphaFoldDB; O94235; -.
DR SMR; O94235; -.
DR BioGRID; 276598; 253.
DR DIP; DIP-61850N; -.
DR IntAct; O94235; 1.
DR STRING; 4896.SPBC106.01.1; -.
DR iPTMnet; O94235; -.
DR MaxQB; O94235; -.
DR PaxDb; O94235; -.
DR PRIDE; O94235; -.
DR EnsemblFungi; SPBC106.01.1; SPBC106.01.1:pep; SPBC106.01.
DR GeneID; 2540060; -.
DR KEGG; spo:SPBC106.01; -.
DR PomBase; SPBC106.01; mph1.
DR VEuPathDB; FungiDB:SPBC106.01; -.
DR eggNOG; KOG0596; Eukaryota.
DR HOGENOM; CLU_406608_0_0_1; -.
DR InParanoid; O94235; -.
DR OMA; APFAHLK; -.
DR PhylomeDB; O94235; -.
DR PRO; PR:O94235; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IDA:PomBase.
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: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:0007127; P:meiosis I; IMP:PomBase.
DR GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:PomBase.
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; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..678
FT /note="Serine/threonine-protein kinase mph1"
FT /id="PRO_0000086389"
FT DOMAIN 316..607
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 39..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 322..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 678 AA; 75354 MW; C943950DE001E8E3 CRC64;
MSKRNPPVTN IADLVSDSSL DEDSLSFLEE LQDPELYFKN DTFSSKSSHS DGTVTGDTLR
RQSSGATALE RLVSHPRTKN FDLQGNGGQN SALKEVNTPA YQSMHHFEHL ITPLPSTNAS
HSEVSLSAGV NDLNSNSEHD LLPKSVNKTP GSLSISRRRR IGRIGLGPPK RAEYTLTDPS
KTSDTKNSTE ADEDIEMKSR EVSPASNSVA ATTLKPLQLH NTPLQTSQEH PKPSFHPSQF
ESSFSPRVQF DHDVERRASE LHSRPVTVFQ EPQRSASQPY ESHALSPKVA PLFDNSQATP
IPKRQQDVVT VANLQFIKLG VVGKGGSSMV YRIFSPDNSR LYALKEVNFI NADQTTIQGY
KNEIALLRKL SGNDRIIKLY AAEVNDTLGQ LNMVMECGET DLANLLMKNM KKPINLNFIR
MYWEQMLEAV QVVHDQNIVH SDLKPANFLL VEGNLKLIDF GIAKAIGNDT TNIHRDSHIG
TINYMAPEAL TDMNAHTNSG VKLVKLGRPS DVWSLGCILY QMVYGRAPFA HLKMIQAIAA
IPNEQYHIHF PEVALPANAV QEKEGSLPGV TVGPDLMDVM KRCLERDQRK RLTIPELLVH
PFLNPLPSYL TPLAKKPLPV SGHTNNAHPL RLSTEISASQ LSMIIERSVE LSKHKRLNKE
LIDSMAYDCV SNLRKMPE
