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 03-AUG-2022, entry version 190.
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; 136.
DR DIP; DIP-4217N; -.
DR IntAct; Q12469; 13.
DR MINT; Q12469; -.
DR STRING; 4932.YOL113W; -.
DR iPTMnet; Q12469; -.
DR MaxQB; Q12469; -.
DR PaxDb; Q12469; -.
DR PRIDE; Q12469; -.
DR EnsemblFungi; YOL113W_mRNA; YOL113W; YOL113W.
DR GeneID; 854036; -.
DR KEGG; sce:YOL113W; -.
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; WYDASAT; -.
DR BioCyc; YEAST:G3O-33510-MON; -.
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-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
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:0006468; P:protein phosphorylation; HDA:SGD.
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 Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.90.810.10; -; 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 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; SSF56112; SSF56112; 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
