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Database: UniProt
Entry: SKM1_YEAST
LinkDB: SKM1_YEAST
Original site: SKM1_YEAST 
ID   SKM1_YEAST              Reviewed;         655 AA.
AC   Q12469; D6W1V4; E9P934; Q06940;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Serine/threonine-protein kinase SKM1;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase 75490 D;
GN   Name=SKM1; OrderedLocusNames=YOL113W; ORFNames=HRA655;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / GRF88;
RX   PubMed=9044278; DOI=10.1046/j.1365-2958.1997.d01-1870.x;
RA   Martin H., Mendoza A., Rodriguez-Pachon J.M., Molina M., Nombela C.;
RT   "Characterization of SKM1, a Saccharomyces cerevisiae gene encoding a novel
RT   Ste20/PAK-like protein kinase.";
RL   Mol. Microbiol. 23:431-444(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7502582; DOI=10.1002/yea.320111108;
RA   Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT   "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT   the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT   tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL   Yeast 11:1069-1075(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: May be involved in cellular signaling or cytoskeletal
CC       functions. May play a role in morphogenetic control.
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=2.7.11.1;
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=2.7.11.1;
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR   EMBL; X69322; CAA49163.1; -; Genomic_DNA.
DR   EMBL; Z48149; CAA88147.1; -; Genomic_DNA.
DR   EMBL; Z74855; CAA99132.1; -; Genomic_DNA.
DR   EMBL; AY693219; AAT93238.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10670.1; -; Genomic_DNA.
DR   PIR; S51884; S51884.
DR   RefSeq; NP_014528.1; NM_001183367.1.
DR   AlphaFoldDB; Q12469; -.
DR   SMR; Q12469; -.
DR   BioGRID; 34287; 138.
DR   DIP; DIP-4217N; -.
DR   IntAct; Q12469; 13.
DR   MINT; Q12469; -.
DR   STRING; 4932.YOL113W; -.
DR   iPTMnet; Q12469; -.
DR   MaxQB; Q12469; -.
DR   PaxDb; 4932-YOL113W; -.
DR   PeptideAtlas; Q12469; -.
DR   EnsemblFungi; YOL113W_mRNA; YOL113W; YOL113W.
DR   GeneID; 854036; -.
DR   KEGG; sce:YOL113W; -.
DR   AGR; SGD:S000005473; -.
DR   SGD; S000005473; SKM1.
DR   VEuPathDB; FungiDB:YOL113W; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   GeneTree; ENSGT00940000176572; -.
DR   HOGENOM; CLU_000288_26_2_1; -.
DR   InParanoid; Q12469; -.
DR   OMA; KEGWISY; -.
DR   OrthoDB; 460351at2759; -.
DR   BioCyc; YEAST:G3O-33510-MONOMER; -.
DR   BRENDA; 2.7.11.1; 984.
DR   Reactome; R-SCE-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-SCE-5627123; RHO GTPases activate PAKs.
DR   Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR   Reactome; R-SCE-9013406; RHOQ GTPase cycle.
DR   Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR   Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR   BioGRID-ORCS; 854036; 0 hits in 13 CRISPR screens.
DR   PRO; PR:Q12469; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12469; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:SGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR   GO; GO:0035376; P:sterol import; IMP:SGD.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd13279; PH_Cla4_Ste20; 1.
DR   CDD; cd06614; STKc_PAK; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   PANTHER; PTHR48015:SF6; SERINE_THREONINE-PROTEIN KINASE CLA4-RELATED; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..655
FT                   /note="Serine/threonine-protein kinase SKM1"
FT                   /id="PRO_0000086656"
FT   DOMAIN          3..118
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          123..136
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          360..639
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          265..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        507
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         366..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        150
FT                   /note="S -> R (in Ref. 5; AAT93238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="S -> A (in Ref. 1; CAA49163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="R -> K (in Ref. 1; CAA49163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="H -> Y (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="S -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="M -> T (in Ref. 1; CAA49163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="A -> V (in Ref. 1; CAA49163)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   655 AA;  75331 MW;  1F6CBC85FE10D385 CRC64;
     MKGVKKEGWI SYKVDGLFSF LWQKRYLVLN DSYLAFYKSD KCNEEPVLSV PLTSITNVSR
     IQLKQNCFEI LRATDQKENI SPINSYFYES NSKRSIFIST RTERDLHGWL DAIFAKCPLL
     SGVSSPTNFT HKVHVGFDPK VGNFVGVPDS WAKLLQTSEI TYDDWNRNSK AVIKALQFYE
     DYNGLDTMQF NDHLNTSLDL KPLKSPTRYI INKRTNSIKR SVSRTLRKGK TDSILPVYQS
     ELKPFPRPSD DDYKFTNIED NKVREEGRVH VSKESTADSQ TKQLGKKEQK VIQSHLRRHD
     NNSTFRPHRL APSAPATKNH DSKTKWHKED LLELKNNDDS NEIIMKMKTV AIDVNPRPYF
     QLVEKAGQGA SGAVYLSKRI KLPQENDPRF LKSHCHRVVG ERVAIKQIRL SEQPKKQLIM
     NELLVMNDSR QENIVNFLEA YIIDDEELWV IMEYMEGGCL TDILDAVARS NTGEHSSPLN
     ENQMAYIVKE TCQGLKFLHN KKIIHRDIKS DNILLNSQGL VKITDFGFCV ELTEKRSKRA
     TMVGTPYWMA PEIVNQKGYD EKVDVWSLGI MLIEMIEGEP PYLNEDPLKA LYLIANNGSP
     KLRHPESVSK QTKQFLDACL QVNVESRASV RKLLTFEFLS MACSPEQLKV SLKWH
//
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