SOK2_YEAST
ID SOK2_YEAST Reviewed; 785 AA.
AC P53438; D6VZJ0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein SOK2;
GN Name=SOK2; OrderedLocusNames=YMR016C; ORFNames=YM9711.03C;
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].
RX PubMed=8524252; DOI=10.1128/mcb.15.12.6854;
RA Ward M.P., Gimeno C.J., Fink G.R., Garrett S.;
RT "SOK2 may regulate cyclic AMP-dependent protein kinase-stimulated growth
RT and pseudohyphal development by repressing transcription.";
RL Mol. Cell. Biol. 15:6854-6863(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 SER-771, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a general regulatory role in the cyclic AMP-dependent
CC protein kinase-stimulated (PKA) signal transduction pathway by
CC regulating the expression of genes important in growth and development.
CC May inhibit the switch from unicellular to filamentous growth.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00630}.
CC -!- MISCELLANEOUS: Present with 314 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; S80522; AAB35749.1; -; Genomic_DNA.
DR EMBL; Z49211; CAA89117.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09914.1; -; Genomic_DNA.
DR PIR; S54016; S54016.
DR RefSeq; NP_013729.1; NM_001182512.1.
DR AlphaFoldDB; P53438; -.
DR SMR; P53438; -.
DR BioGRID; 35187; 248.
DR IntAct; P53438; 2.
DR MINT; P53438; -.
DR STRING; 4932.YMR016C; -.
DR iPTMnet; P53438; -.
DR MaxQB; P53438; -.
DR PaxDb; P53438; -.
DR PRIDE; P53438; -.
DR EnsemblFungi; YMR016C_mRNA; YMR016C; YMR016C.
DR GeneID; 855030; -.
DR KEGG; sce:YMR016C; -.
DR SGD; S000004618; SOK2.
DR VEuPathDB; FungiDB:YMR016C; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR GeneTree; ENSGT00940000176596; -.
DR HOGENOM; CLU_357582_0_0_1; -.
DR InParanoid; P53438; -.
DR BioCyc; YEAST:G3O-32722-MON; -.
DR PRO; PR:P53438; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P53438; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PTHR47792; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..785
FT /note="Protein SOK2"
FT /id="PRO_0000072036"
FT DOMAIN 414..520
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 448..469
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 785 AA; 85643 MW; F4E0F224BE84645F CRC64;
MPIGNPINTN DIKSNRMRQE SNMSAVSNSE STIGQSTQQQ QQQQQYLGQS VQPLMPVSYQ
YVVPEQWPYP QYYQQPQSQS QQQLQSQPQM YQVQESFQSS GSDSNASNPP STSVGVPSNA
TATALPNGSA ITTKKSNNST NISNNVPYYY YFPQMQAQQS MAYSYPQAYY YYPANGDGTT
NGATPSVTSN QVQNPNLEKT YSTFEQQQQH QQQQQLQAQT YPAQPPKIGN AFSKFSKSGP
PSDSSSGSMS PNSNRTSRNS NSISSLAQQP PMSNYPQPST YQYPGFHKTS SIPNSHSPIP
PRSLTTPTQG PTSQNGPLSY NLPQVGLLPP QQQQQVSPLY DGNSITPPVK PSTDQETYLT
ANRHGVSDQQ YDSMAKTMNS FQTTTIRHPM PLIATTNATG SNTSGTSASI IRPRVTTTMW
EDEKTLCYQV EANGISVVRR ADNDMVNGTK LLNVTKMTRG RRDGILKAEK IRHVVKIGSM
HLKGVWIPFE RALAIAQREK IADYLYPLFI RDIQSVLKQN NPSNDSSSSS SSTGIKSISP
RTYYQPINNY QNPNGPSNIS AAQLTYSSMN LNNKIIPNNS IPAVSTIAAG EKPLKKCTMP
NSNQLEGHTI TNLQTLSATM PMKQQLMGNI ASPLSYPRNA TMNSASTLGI TPADSKPLTP
SPTTTNTNQS SESNVGSIHT GITLPRVESE SASHSKWSKE ADSGNTVPDN QTLKEPRSSQ
LPISALTSTD TDKIKTSTSD EATQPNEPSE AEPVKESESS KSQVDGAGDV SNEEIAADDT
KKQEK
