SKY1_YEAST
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 03-AUG-2022, entry version 187.
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; 412.
DR DIP; DIP-2884N; -.
DR IntAct; Q03656; 16.
DR MINT; Q03656; -.
DR STRING; 4932.YMR216C; -.
DR iPTMnet; Q03656; -.
DR MaxQB; Q03656; -.
DR PaxDb; Q03656; -.
DR PRIDE; Q03656; -.
DR EnsemblFungi; YMR216C_mRNA; YMR216C; YMR216C.
DR GeneID; 855256; -.
DR KEGG; sce:YMR216C; -.
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; NTTGKHV; -.
DR BioCyc; YEAST:G3O-32899-MON; -.
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:cellular cation homeostasis; IMP:SGD.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006376; P:mRNA splice site selection; IGI:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:SGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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 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; 2.
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 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
