SPT2_YEAST
ID SPT2_YEAST Reviewed; 333 AA.
AC P06843; D3DM69;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein SPT2;
DE AltName: Full=Negative regulator of Ty transcription;
GN Name=SPT2;
GN Synonyms=SIN1 {ECO:0000303|PubMed:2072912, ECO:0000303|PubMed:8654588},
GN SPM2; OrderedLocusNames=YER161C;
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=2991744; DOI=10.1128/mcb.5.7.1543-1553.1985;
RA Roeder G.S., Beard C., Smith M., Keranen S.;
RT "Isolation and characterization of the SPT2 gene, a negative regulator of
RT Ty-controlled yeast gene expression.";
RL Mol. Cell. Biol. 5:1543-1553(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DNA-BINDING.
RX PubMed=2072912; DOI=10.1128/mcb.11.8.4135-4146.1991;
RA Kruger W., Herskowitz I.;
RT "A negative regulator of HO transcription, SIN1 (SPT2), is a nonspecific
RT DNA-binding protein related to HMG1.";
RL Mol. Cell. Biol. 11:4135-4146(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
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 [5]
RP INTERACTION WITH SAP1.
RX PubMed=8654588; DOI=10.1016/0014-5793(96)00500-5;
RA Liberzon A., Shpungin S., Bangio H., Yona E., Katcoff D.J.;
RT "Association of yeast SAP1, a novel member of the 'AAA' ATPase family of
RT proteins, with the chromatin protein SIN1.";
RL FEBS Lett. 388:5-10(1996).
RN [6]
RP INTERACTION WITH CDC23.
RX PubMed=8710860; DOI=10.1073/pnas.93.16.8274;
RA Shpungin S., Liberzon A., Bangio H., Yona E., Katcoff D.J.;
RT "Association of yeast SIN1 with the tetratrico peptide repeats of CDC23.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8274-8277(1996).
RN [7]
RP IDENTIFICATION IN A SAGA COMPLEX WITH SPT7; HFI1; SPT8; GCN5; SPT20; ADA2;
RP ADA3 AND TRA1.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [11]
RP INTERACTION WITH HISTONE H3 AND H4, DOMAIN, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 289-MET-GLU-290; 299-GLU-GLU-300 AND 310-GLU-ASP-311.
RX PubMed=26109053; DOI=10.1101/gad.261115.115;
RA Chen S., Rufiange A., Huang H., Rajashankar K.R., Nourani A., Patel D.J.;
RT "Structure-function studies of histone H3/H4 tetramer maintenance during
RT transcription by chaperone Spt2.";
RL Genes Dev. 29:1326-1340(2015).
CC -!- FUNCTION: Histone chaperone that stabilizes pre-existing histone
CC tetramers and regulates replication-independent histone exchange on
CC chromatin (PubMed:26109053). Required for normal chromatin refolding in
CC the coding region of transcribed genes, and for the suppression of
CC spurious transcription (PubMed:26109053). Global regulatory protein
CC that plays positive as well as negative regulatory roles in
CC transcription (PubMed:2072912). {ECO:0000269|PubMed:2072912,
CC ECO:0000269|PubMed:26109053}.
CC -!- SUBUNIT: Interacts with tetramers formed by histone H3 and H4
CC (PubMed:26109053). Interacts with SAP1 and CDC23 (PubMed:8654588,
CC PubMed:8710860). Component of the SAGA complex, a large multiprotein
CC complex that modifies the chromatin, at least composed of SPT2, SPT7,
CC SPT8, SPT20/ADA5, HFI1/ADA1, ADA2, ADA3/NGG1, TRA1 and GCN5
CC (PubMed:9885573). {ECO:0000269|PubMed:26109053,
CC ECO:0000269|PubMed:8654588, ECO:0000269|PubMed:8710860,
CC ECO:0000269|PubMed:9885573}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2072912,
CC ECO:0000269|PubMed:26109053}.
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000269|PubMed:26109053}.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M11165; AAA35083.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64688.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07823.1; -; Genomic_DNA.
DR PIR; A23438; A23438.
DR RefSeq; NP_011088.1; NM_001179051.1.
DR AlphaFoldDB; P06843; -.
DR SMR; P06843; -.
DR BioGRID; 36914; 308.
DR DIP; DIP-1657N; -.
DR IntAct; P06843; 40.
DR MINT; P06843; -.
DR STRING; 4932.YER161C; -.
DR iPTMnet; P06843; -.
DR MaxQB; P06843; -.
DR PaxDb; P06843; -.
DR PRIDE; P06843; -.
DR EnsemblFungi; YER161C_mRNA; YER161C; YER161C.
DR GeneID; 856908; -.
DR KEGG; sce:YER161C; -.
DR SGD; S000000963; SPT2.
DR VEuPathDB; FungiDB:YER161C; -.
DR eggNOG; ENOG502QRG5; Eukaryota.
DR HOGENOM; CLU_069667_1_0_1; -.
DR InParanoid; P06843; -.
DR OMA; IWAMFNR; -.
DR BioCyc; YEAST:G3O-30322-MON; -.
DR PRO; PR:P06843; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P06843; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0000217; F:DNA secondary structure binding; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; IMP:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0043631; P:RNA polyadenylation; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..333
FT /note="Protein SPT2"
FT /id="PRO_0000072163"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..333
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000269|PubMed:26109053"
FT REGION 312..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..242
FT /evidence="ECO:0000255"
FT COILED 292..316
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 289..290
FT /note="ME->AA: Strongly reduces histone binding."
FT /evidence="ECO:0000269|PubMed:26109053"
FT MUTAGEN 299..300
FT /note="EE->AA: Strongly reduces histone binding."
FT /evidence="ECO:0000269|PubMed:26109053"
FT MUTAGEN 310..311
FT /note="ED->AA: Strongly reduces histone binding."
FT /evidence="ECO:0000269|PubMed:26109053"
SQ SEQUENCE 333 AA; 38551 MW; 60C3BED7EEA99535 CRC64;
MSFLSKLSQI RKSTTASKAQ VQDPLPKKND EEYSLLPKNY IRDEDPAVKR LKELRRQELL
KNGALAKKSG VKRKRGTSSG SEKKKIERND DDEGGLGIRF KRSIGASHAP LKPVVRKKPE
PIKKMSFEEL MKQAENNEKQ PPKVKSSEPV TKERPHFNKP GFKSSKRPQK KASPGATLRG
VSSGGNSIKS SDSPKPVKLN LPTNGFAQPN RRLKEKLESR KQKSRYQDDY DEEDNDMDDF
IEDDEDEGYH SKSKHSNGPG YDRDEIWAMF NRGKKRSEYD YDELEDDDME ANEMEILEEE
EMARKMARLE DKREEAWLKK HEEEKRRRKK GIR
