SKH1_SCHPO
ID SKH1_SCHPO Reviewed; 363 AA.
AC Q9Y884; Q9UUK6;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=MAP kinase kinase skh1/pek1;
DE EC=2.7.12.2;
GN Name=skh1; Synonyms=mkk1, pek1; ORFNames=SPBC543.07;
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=10591634; DOI=10.1242/jcs.113.1.153;
RA Loewith R., Hubberstey A., Young D.;
RT "Skh1, the MAPKK component of the mkh1 signaling pathway in
RT Schizosaccharomyces pombe.";
RL J. Cell Sci. 113:153-160(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10365961; DOI=10.1038/20951;
RA Sugiura R., Toda T., Susheela D., Shuntoh H., Kuno T.;
RT "The MAPK kinase Pek1 acts as a phosphorylation-dependent molecular
RT switch.";
RL Nature 399:479-483(1999).
RN [3]
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 mkh1 signal transduction pathway that plays a
CC role in cell wall integrity. Activates spm1/pmk1 via phosphorylation.
CC {ECO:0000269|PubMed:10365961, ECO:0000269|PubMed:10591634}.
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 -!- ACTIVITY REGULATION: Activated by mkh1.
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; AF157632; AAD41399.1; -; Genomic_DNA.
DR EMBL; D82023; BAA82312.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC05249.1; -; Genomic_DNA.
DR PIR; T51294; T51294.
DR PIR; T51992; T51992.
DR RefSeq; NP_596795.1; NM_001023815.2.
DR AlphaFoldDB; Q9Y884; -.
DR SMR; Q9Y884; -.
DR BioGRID; 277435; 104.
DR IntAct; Q9Y884; 2.
DR STRING; 4896.SPBC543.07.1; -.
DR MaxQB; Q9Y884; -.
DR PaxDb; Q9Y884; -.
DR EnsemblFungi; SPBC543.07.1; SPBC543.07.1:pep; SPBC543.07.
DR GeneID; 2540919; -.
DR KEGG; spo:SPBC543.07; -.
DR PomBase; SPBC543.07; -.
DR VEuPathDB; FungiDB:SPBC543.07; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9Y884; -.
DR OMA; IAGWVCK; -.
DR PhylomeDB; Q9Y884; -.
DR BRENDA; 2.7.12.2; 5613.
DR Reactome; R-SPO-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SPO-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-SPO-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:Q9Y884; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA: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:UniProtKB-KW.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IDA:PomBase.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:PomBase.
DR GO; GO:1903340; P:positive regulation of cell wall organization or biogenesis; EXP:PomBase.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..363
FT /note="MAP kinase kinase skh1/pek1"
FT /id="PRO_0000086655"
FT DOMAIN 79..343
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="L -> K (in Ref. 2; BAA82312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40707 MW; 141EA6B8C1D036DC CRC64;
MSKKPVLNLD TSNGFSEEYI SHPERNDNQG IVEITDLVFS SESKLTQRKE SRDSKTFVPS
FLEELDDDHL HELVTNGGIL YMNSLGEGVS GSVRKCRIRG TQMIFAMKTV LAAPNTALQK
QLLRELKINR SCTSPYIVKY YGACYNNAEC QLNIAMEYCG AGSLDAIYKR VRSQGGRTGE
RPLGKIAFGV LSGLSYLHDR KIIHRDIKPS NILLTSKGQV KLCDFGVSGE LVNSLAGTFT
GTSYYMAPER ISGGSYTISS DIWSLGLTLM EVALNRFPFP PEGSPPPMPI ELLSYIINMP
PPLLPQEPGI KWSKSFQHFL CVCLDKDKTR RPGPQKMLTH PWVKAFERIH VDMEEFLRQV
WSD
