SPP1_YEAST
ID SPP1_YEAST Reviewed; 353 AA.
AC Q03012; D6W3N0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=COMPASS component SPP1;
DE AltName: Full=Complex proteins associated with SET1 protein SPP1;
DE AltName: Full=Set1C component SPP1;
DE AltName: Full=Suppressor of PRP protein 1;
GN Name=SPP1; Synonyms=CPS40, SAF41; OrderedLocusNames=YPL138C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [4]
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 [5]
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 [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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, 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).
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 Q03012; P21651: REC107; NbExp=3; IntAct=EBI-32540, EBI-10742;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U43703; AAB68222.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11296.1; -; Genomic_DNA.
DR PIR; S69047; S69047.
DR RefSeq; NP_015187.1; NM_001183952.1.
DR PDB; 6BX3; EM; 4.30 A; F=117-353.
DR PDB; 6J2P; X-ray; 2.85 A; A/B/C/D=1-124.
DR PDB; 6VEN; EM; 3.37 A; R=2-353.
DR PDBsum; 6BX3; -.
DR PDBsum; 6J2P; -.
DR PDBsum; 6VEN; -.
DR AlphaFoldDB; Q03012; -.
DR SMR; Q03012; -.
DR BioGRID; 36044; 152.
DR ComplexPortal; CPX-1039; COMPASS complex.
DR DIP; DIP-2946N; -.
DR IntAct; Q03012; 12.
DR MINT; Q03012; -.
DR STRING; 4932.YPL138C; -.
DR iPTMnet; Q03012; -.
DR MaxQB; Q03012; -.
DR PaxDb; Q03012; -.
DR PRIDE; Q03012; -.
DR EnsemblFungi; YPL138C_mRNA; YPL138C; YPL138C.
DR GeneID; 855965; -.
DR KEGG; sce:YPL138C; -.
DR SGD; S000006059; SPP1.
DR VEuPathDB; FungiDB:YPL138C; -.
DR eggNOG; KOG1632; Eukaryota.
DR HOGENOM; CLU_045707_0_0_1; -.
DR InParanoid; Q03012; -.
DR OMA; WCPPYSS; -.
DR BioCyc; YEAST:G3O-34036-MON; -.
DR PRO; PR:Q03012; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03012; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:SGD.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1903341; P:regulation of meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037869; Spp1/CFP1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46174; PTHR46174; 2.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..353
FT /note="COMPASS component SPP1"
FT /id="PRO_0000059338"
FT ZN_FING 22..72
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 235..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6J2P"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6J2P"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6J2P"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6J2P"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6J2P"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6J2P"
FT HELIX 203..240
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6VEN"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6VEN"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:6VEN"
FT HELIX 311..348
FT /evidence="ECO:0007829|PDB:6VEN"
SQ SEQUENCE 353 AA; 41468 MW; F4B8DFE0CB358CA4 CRC64;
MSLPQWCPPH STLKRNPTTG EDVYCICKRP DYGELMVGCD GCDDWFHFTC LHIPEQFKDL
VFSFYCPYCQ AGITGKNKDA IINGEGSLPK TLWKRKCRIS DCYKPCLQDS KYCSEEHGRE
FVNDIWSRLK TDEDRAVVKK MVEQTGHIDK FKKFGQLDFI DNNIVVKTDD EKEIFDQIVV
RDMTLKTLED DLQEVQEISL PLFKKKLELL EVYLGWLDNV YTEMRKLDDD AASHVECGKE
DSKGTKRKKK KNSSRSRARK NICGYCSTYE RIPCSVEEFV RDFGSNEEAT KIHEVCTKWK
CNRHLDWVST NQEQYLQQID SLESMQERLQ HLIQARKKQL NIQYYEEILR RGL
