SHG1_YEAST
ID SHG1_YEAST Reviewed; 142 AA.
AC P38337; D6VQQ5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=COMPASS component SHG1;
DE AltName: Full=Complex proteins associated with SET1 protein SHG1;
DE AltName: Full=Set1C component SHG1;
GN Name=SHG1; Synonyms=CPS15; OrderedLocusNames=YBR258C; ORFNames=YBR1726;
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=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11742990; DOI=10.1093/emboj/20.24.7137;
RA Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,
RA Aasland R., Stewart A.F.;
RT "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and
RT methylates histone 3 lysine 4.";
RL EMBO J. 20:7137-7148(2001).
RN [6]
RP FUNCTION.
RX PubMed=11805083; DOI=10.1074/jbc.c200023200;
RA Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J.,
RA Johnston M., Shilatifard A.;
RT "COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric
RT silencing of gene expression.";
RL J. Biol. Chem. 277:10753-10755(2002).
RN [7]
RP SUBUNIT.
RX PubMed=11687631; DOI=10.1073/pnas.231473398;
RA Miller T., Krogan N.J., Dover J., Erdjument-Bromage H., Tempst P.,
RA Johnston M., Greenblatt J.F., Shilatifard A.;
RT "COMPASS: a complex of proteins associated with a trithorax-related SET
RT domain protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001).
RN [8]
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 [9]
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: The COMPASS (Set1C) complex specifically mono-, di- and
CC trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays
CC a role in telomere length maintenance and transcription elongation
CC regulation. {ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11805083}.
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex which consists of
CC SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and
CC SWD3(1). {ECO:0000269|PubMed:11687631, ECO:0000269|PubMed:11742990}.
CC -!- INTERACTION:
CC P38337; P38827: SET1; NbExp=5; IntAct=EBI-21106, EBI-16977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHG1 family. {ECO:0000305}.
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DR EMBL; X70529; CAA49922.1; -; Genomic_DNA.
DR EMBL; Z36127; CAA85221.1; -; Genomic_DNA.
DR EMBL; AY557639; AAS55965.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07375.1; -; Genomic_DNA.
DR PIR; S32960; S32960.
DR RefSeq; NP_009817.3; NM_001178606.3.
DR AlphaFoldDB; P38337; -.
DR BioGRID; 32954; 211.
DR ComplexPortal; CPX-1039; COMPASS complex.
DR DIP; DIP-6843N; -.
DR IntAct; P38337; 7.
DR MINT; P38337; -.
DR STRING; 4932.YBR258C; -.
DR iPTMnet; P38337; -.
DR MaxQB; P38337; -.
DR PaxDb; P38337; -.
DR PRIDE; P38337; -.
DR EnsemblFungi; YBR258C_mRNA; YBR258C; YBR258C.
DR GeneID; 852561; -.
DR KEGG; sce:YBR258C; -.
DR SGD; S000000462; SHG1.
DR VEuPathDB; FungiDB:YBR258C; -.
DR eggNOG; ENOG502S9A4; Eukaryota.
DR HOGENOM; CLU_139264_0_0_1; -.
DR InParanoid; P38337; -.
DR OMA; MEMHASK; -.
DR BioCyc; YEAST:G3O-29182-MON; -.
DR PRO; PR:P38337; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38337; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:SGD.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome.
FT CHAIN 1..142
FT /note="COMPASS component SHG1"
FT /id="PRO_0000212515"
SQ SEQUENCE 142 AA; 16429 MW; 12E73F0C3DD225D7 CRC64;
MAYNQEDSKR LSDKYKKEGH FDKLKREILS NPWNNTEENS ESFEQALRKR VASTVKEMVN
EDEELIFKNR GLTSALIESQ LVKDNYLKLG SKMEGDNGDG EKKFDLDVYV RSKLQDPKLL
EMIKGQLQET LNSYEEEANG ST
