BYR1_SCHPO
ID BYR1_SCHPO Reviewed; 340 AA.
AC P10506;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Protein kinase byr1;
DE EC=2.7.12.2;
DE AltName: Full=MAPK kinase;
DE Short=MAPKK;
GN Name=byr1; Synonyms=ste1; ORFNames=SPAC1D4.13;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=3042386; DOI=10.1002/j.1460-2075.1988.tb02905.x;
RA Nadin-Davis S.A., Nasim A.;
RT "A gene which encodes a predicted protein kinase can restore some functions
RT of the ras gene in fission yeast.";
RL EMBO J. 7:985-993(1988).
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).
RN [3]
RP FUNCTION, INTERACTION WITH BOB1 AND SPK1, AND SUBCELLULAR LOCATION.
RX PubMed=11683500; DOI=10.1046/j.1432-0436.2001.670402.x;
RA Henkel J., Du H., Yang P., Qyang Y., Kansra S., Ko M., Kim H., Marcus S.;
RT "Bob1, a Gim5/MM-1/Pfd5 homolog, interacts with the MAP kinase kinase byr1
RT to regulate sexual differentiation in the fission yeast,
RT Schizosaccharomyces pombe.";
RL Differentiation 67:98-106(2001).
CC -!- FUNCTION: Serine/threonine protein kinase involved in conjugation and
CC sporulation. It is thought that it is phosphorylated by the byr2
CC protein kinase and that it can phosphorylate the spk1 kinase. When
CC bound to bob1, is involved in the regulation of sexual differentiation.
CC {ECO:0000269|PubMed:11683500, ECO:0000269|PubMed:3042386}.
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 -!- 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;
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 -!- SUBUNIT: Interacts with bob1 and spk1. {ECO:0000269|PubMed:11683500}.
CC -!- INTERACTION:
CC P10506; O94307: bob1; NbExp=2; IntAct=EBI-2042633, EBI-2042611;
CC P10506; P27638: spk1; NbExp=2; IntAct=EBI-2042633, EBI-2104356;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11683500}.
CC Note=Localizes to the cell tips and septum forming regions.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; X07445; CAA30326.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93222.1; -; Genomic_DNA.
DR PIR; S00473; OKBYR1.
DR RefSeq; NP_593026.1; NM_001018425.2.
DR AlphaFoldDB; P10506; -.
DR SMR; P10506; -.
DR BioGRID; 278613; 18.
DR IntAct; P10506; 7.
DR STRING; 4896.SPAC1D4.13.1; -.
DR MaxQB; P10506; -.
DR PaxDb; P10506; -.
DR EnsemblFungi; SPAC1D4.13.1; SPAC1D4.13.1:pep; SPAC1D4.13.
DR GeneID; 2542137; -.
DR KEGG; spo:SPAC1D4.13; -.
DR PomBase; SPAC1D4.13; byr1.
DR VEuPathDB; FungiDB:SPAC1D4.13; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P10506; -.
DR OMA; ATQELPW; -.
DR PhylomeDB; P10506; -.
DR BRENDA; 2.7.12.2; 5613.
DR Reactome; R-SPO-110056; MAPK3 (ERK1) activation.
DR Reactome; R-SPO-112411; MAPK1 (ERK2) activation.
DR Reactome; R-SPO-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SPO-445144; Signal transduction by L1.
DR Reactome; R-SPO-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-SPO-5674135; MAP2K and MAPK activation.
DR Reactome; R-SPO-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-SPO-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:P10506; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:PomBase.
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:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0071507; P:pheromone response MAPK cascade; IMP:PomBase.
DR GO; GO:0034307; P:regulation of ascospore formation; IMP:PomBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Conjugation; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Sporulation; Transferase.
FT CHAIN 1..340
FT /note="Protein kinase byr1"
FT /id="PRO_0000085688"
FT DOMAIN 66..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 72..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 38189 MW; 2AC885AEE971DB8A CRC64;
MFKRRRNPKG LVLNPNASVK SSDNDHKEEL INNQKSFESN VEAFMEQCAH MNRRPAWISD
LDNSSLEVVR HLGEGNGGAV SLVKHRNIFM ARKTVYVGSD SKLQKQILRE LGVLHHCRSP
YIVGFYGAFQ YKNNISLCME YMDCGSLDAI LREGGPIPLD ILGKIINSMV KGLIYLYNVL
HIIHRDLKPS NVVVNSRGEI KLCDFGVSGE LVNSVAQTFV GTSTYMSPER IRGGKYTVKS
DIWSLGISII ELATQELPWS FSNIDDSIGI LDLLHCIVQE EPPRLPSSFP EDLRLFVDAC
LHKDPTLRAS PQQLCAMPYF QQALMINVDL ASWASNFRSS
