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Database: UniProt
Entry: Q03656
LinkDB: Q03656
Original site: Q03656 
ID   SKY1_YEAST              Reviewed;         742 AA.
AC   Q03656; D6W041;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Serine/threonine-protein kinase SKY1;
DE            Short=SRPK;
DE            EC=2.7.11.1;
GN   Name=SKY1; OrderedLocusNames=YMR216C; ORFNames=YM8261.10C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-383; SER-393; SER-449 AND
RP   SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-432; SER-445;
RP   SER-449 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-383; THR-386; SER-388;
RP   SER-393; SER-410; SER-427; SER-432; SER-445; SER-449 AND SER-453, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 138-742, AND FUNCTION.
RX   PubMed=11175909; DOI=10.1038/84178;
RA   Nolen B., Yun C.Y., Wong C.F., McCammon J.A., Fu X.-D., Ghosh G.;
RT   "The structure of Sky1p reveals a novel mechanism for constitutive
RT   activity.";
RL   Nat. Struct. Biol. 8:176-183(2001).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 138-742 ALONE AND IN COMPLEX WITH
RP   ADP AND ATP.
RX   PubMed=12911299; DOI=10.1021/bi0344331;
RA   Nolen B., Ngo J., Chakrabarti S., Vu D., Adams J.A., Ghosh G.;
RT   "Nucleotide-induced conformational changes in the Saccharomyces cerevisiae
RT   SR protein kinase, Sky1p, revealed by X-ray crystallography.";
RL   Biochemistry 42:9575-9585(2003).
CC   -!- FUNCTION: Constitutively active kinase, specifically and sequentially
CC       phosphorylates serine/arginine (SR)-type shuttling mRNA binding
CC       proteins in their RS dipeptide repeats. {ECO:0000269|PubMed:11175909}.
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   -!- INTERACTION:
CC       Q03656; P35169: TOR1; NbExp=2; IntAct=EBI-9800, EBI-19374;
CC   -!- MISCELLANEOUS: Present with 2420 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; Z49809; CAA89931.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10115.1; -; Genomic_DNA.
DR   PIR; S55098; S55098.
DR   RefSeq; NP_013943.1; NM_001182723.1.
DR   PDB; 1HOW; X-ray; 2.10 A; A=138-304, A=539-742.
DR   PDB; 1Q8Y; X-ray; 2.05 A; A/B=138-304, A/B=539-742.
DR   PDB; 1Q8Z; X-ray; 2.35 A; A/B=138-304, A/B=539-742.
DR   PDB; 1Q97; X-ray; 2.30 A; A/B=138-304, A/B=539-742.
DR   PDB; 1Q99; X-ray; 2.11 A; A/B=138-304, A/B=539-742.
DR   PDB; 2JD5; X-ray; 2.50 A; A/B=138-742.
DR   PDBsum; 1HOW; -.
DR   PDBsum; 1Q8Y; -.
DR   PDBsum; 1Q8Z; -.
DR   PDBsum; 1Q97; -.
DR   PDBsum; 1Q99; -.
DR   PDBsum; 2JD5; -.
DR   AlphaFoldDB; Q03656; -.
DR   SMR; Q03656; -.
DR   BioGRID; 35394; 419.
DR   DIP; DIP-2884N; -.
DR   IntAct; Q03656; 16.
DR   MINT; Q03656; -.
DR   STRING; 4932.YMR216C; -.
DR   GlyGen; Q03656; 18 sites, 1 O-linked glycan (18 sites).
DR   iPTMnet; Q03656; -.
DR   MaxQB; Q03656; -.
DR   PaxDb; 4932-YMR216C; -.
DR   PeptideAtlas; Q03656; -.
DR   EnsemblFungi; YMR216C_mRNA; YMR216C; YMR216C.
DR   GeneID; 855256; -.
DR   KEGG; sce:YMR216C; -.
DR   AGR; SGD:S000004829; -.
DR   SGD; S000004829; SKY1.
DR   VEuPathDB; FungiDB:YMR216C; -.
DR   eggNOG; KOG1290; Eukaryota.
DR   GeneTree; ENSGT00940000170102; -.
DR   HOGENOM; CLU_000288_81_8_1; -.
DR   InParanoid; Q03656; -.
DR   OMA; NHKGPNG; -.
DR   OrthoDB; 912242at2759; -.
DR   BioCyc; YEAST:G3O-32899-MONOMER; -.
DR   BioGRID-ORCS; 855256; 1 hit in 13 CRISPR screens.
DR   EvolutionaryTrace; Q03656; -.
DR   PRO; PR:Q03656; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03656; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:SGD.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IMP:SGD.
DR   GO; GO:0006873; P:intracellular monoatomic ion homeostasis; IMP:SGD.
DR   GO; GO:0006376; P:mRNA splice site recognition; IGI:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:SGD.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR   GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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   PANTHER; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47634:SF9; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..742
FT                   /note="Serine/threonine-protein kinase SKY1"
FT                   /id="PRO_0000086658"
FT   DOMAIN          158..706
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          13..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         164..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         383
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         386
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         449
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   TURN            154..157
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          158..166
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          168..177
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   TURN            178..181
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          182..189
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           193..211
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           216..222
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          230..236
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          239..246
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           253..259
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   TURN            260..262
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           267..286
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           297..299
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          300..304
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   TURN            539..542
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          543..548
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           551..553
FT                   /evidence="ECO:0007829|PDB:1HOW"
FT   HELIX           568..570
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           573..577
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           584..599
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          610..612
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           615..626
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           631..636
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           640..643
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   STRAND          650..652
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           661..667
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           673..683
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           684..687
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   TURN            691..693
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           697..701
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   HELIX           704..706
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
FT   TURN            710..714
FT                   /evidence="ECO:0007829|PDB:1Q99"
FT   HELIX           726..728
FT                   /evidence="ECO:0007829|PDB:1Q99"
FT   STRAND          732..734
FT                   /evidence="ECO:0007829|PDB:1Q8Y"
SQ   SEQUENCE   742 AA;  83238 MW;  C775F10B30C950FC CRC64;
     MGSSINYPGF VTKSAHLADT STDASISCEE ATSSQEAKKN FFQRDYNMMK KAPAPTKSKL
     SLALQTSKSS SSANGTVQED TSSKTEDFST KSIKKKPDSG VESHVSIQSD SGPQSDSDLD
     SDSSISSCDE RNEESLKDYR PGGYHPAFKG EPYKDARYIL VRKLGWGHFS TVWLAKDMVN
     NTHVAMKIVR GDKVYTEAAE DEIKLLQRVN DADNTKEDSM GANHILKLLD HFNHKGPNGV
     HVVMVFEVLG ENLLALIKKY EHRGIPLIYV KQISKQLLLG LDYMHRRCGI IHTDIKPENV
     LMEIGDVEGI VQMVEALDKQ KREAKRLQRH VSRSSDITAN DSSDEKWAEC QTSMPCGSSS
     NSKSRSIEKD LSKRCFRRPR RHTIITGSQP LPSPISSSNF FEMRAHFCGS SHNSFSSVSG
     NRNIPSSINN NSINNGIGIK NSNNSFLNSV PHSVTRMFIN EDSNDNNNND NSKNKNNNNN
     NSNNNNNEDI MNTPLHEEQL ADSLSTFDIS NISQSSDTNG PYISNTMDSN SNVSTDINSP
     ENLIQIKIAD LGNACWYDEH YTNSIQTREY RSPEVLLGAP WGCGADIWST ACLIFELITG
     DFLFEPDEGH SYTKDDDHIA QIIELLGELP SYLLRNGKYT RTFFNSRGLL RNISKLKFWP
     LEDVLTEKYK FSKDEAKEIS DFLSPMLQLD PRKRADAGGL VNHPWLKDTL GMEEIRVPDR
     ELYGSGSDIP GWFEEVRDHK RH
//
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