SPT10_YEAST
ID SPT10_YEAST Reviewed; 640 AA.
AC P35208; D6VW59;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein SPT10;
GN Name=SPT10; Synonyms=CRE1, SUD1; OrderedLocusNames=YJL127C; ORFNames=J0702;
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], AND MUTAGENESIS.
RX PubMed=8138180; DOI=10.1093/genetics/136.1.93;
RA Natsoulis G., Winston F., Boeke J.D.;
RT "The SPT10 and SPT21 genes of Saccharomyces cerevisiae.";
RL Genetics 136:93-105(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-640.
RC STRAIN=S288c / GRF88;
RX PubMed=8264536; DOI=10.1007/bf00279904;
RA Yamashita I.;
RT "Isolation and characterization of the SUD1 gene, which encodes a global
RT repressor of core promoter activity in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 241:616-626(1993).
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 DISRUPTION PHENOTYPE.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
CC -!- FUNCTION: Required for normal transcription at a number of loci in
CC yeast. Affects transcription at Ty1 elements, at PHO5, STE6 and ADH2.
CC -!- DISRUPTION PHENOTYPE: Decreases HTA1 RNA level.
CC {ECO:0000269|PubMed:19683497}.
CC -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L24435; AAA35077.1; -; Genomic_DNA.
DR EMBL; Z49402; CAA89422.1; -; Genomic_DNA.
DR EMBL; X65186; CAA46300.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08675.1; -; Genomic_DNA.
DR PIR; S47865; S47865.
DR RefSeq; NP_012408.1; NM_001181560.1.
DR AlphaFoldDB; P35208; -.
DR SMR; P35208; -.
DR BioGRID; 33629; 392.
DR IntAct; P35208; 32.
DR MINT; P35208; -.
DR STRING; 4932.YJL127C; -.
DR iPTMnet; P35208; -.
DR MaxQB; P35208; -.
DR PaxDb; P35208; -.
DR PRIDE; P35208; -.
DR EnsemblFungi; YJL127C_mRNA; YJL127C; YJL127C.
DR GeneID; 853315; -.
DR KEGG; sce:YJL127C; -.
DR SGD; S000003663; SPT10.
DR VEuPathDB; FungiDB:YJL127C; -.
DR eggNOG; ENOG502QRFX; Eukaryota.
DR HOGENOM; CLU_013985_42_4_1; -.
DR InParanoid; P35208; -.
DR OMA; THITKSI; -.
DR BioCyc; YEAST:G3O-31577-MON; -.
DR PRO; PR:P35208; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P35208; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:SGD.
DR GO; GO:0032931; F:histone acetyltransferase activity (H3-K56 specific); IC:SGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0016573; P:histone acetylation; IMP:SGD.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IMP:SGD.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IGI:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR015416; Znf_H2C2_histone_UAS-bd.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF09337; zf-H2C2; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..640
FT /note="Protein SPT10"
FT /id="PRO_0000072160"
FT DOMAIN 121..259
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 388
FT /note="C->S: Loss of complementation of the suppression
FT phenotype."
FT /evidence="ECO:0000269|PubMed:8138180"
SQ SEQUENCE 640 AA; 72922 MW; 9E81C87E2A66D6C5 CRC64;
MLNQHTSSVP DDEHLQMAHQ NSSSEVRNEA AVPDQLLTPL QPYTILLKDG ETIATMYPIP
AYPDLLPLGL LNFLLDEFNM EVEKGDSFPY YETLSLEEFK NVWFHNDGHV CIMVLGEIPE
LDYSMDTEAD TNDNFGTEIE TTKHTTQYKK RKERRNLNLS MQWEKQCLGI FDLKPAYPGR
SAHVVTGTFL VNAGIRGKGI GKTLMETFIE WSKKLGFTSS FFPLIYGTNV GIRRILEGLN
FRRIGKLPEA GILKGFDVPV DSFMYGKEFT HITKSIDLLR DPQKSIEIGK YERLKHFLET
GKYPLHCDRN EKARLRVLSK THSVLNGKLM TKGKEIIYDT DQQIQIALEI HLMEHLGINK
VTSKIGEKYH WRGIKSTVSE VISRCQKCKM RYKDGTGVII EQKRAVKQAH MLPTQHIETI
NNPRKSKKHD NALLGQAINF PQNIISSTLN DVEGEPTPPD TNIVQPTFQN ATNSPATTAE
ANEANKRSEF LSSIQSTPLL DDEQSMNSFN RFVEEENSRK RRKYLDVASN GIVPHLTNNE
SQDHANPVNR DERDMNHSVP DLDRNDHTIM NDAMLSLEDN VMAALEMVQK EQQQKINHRG
EDVTGQQIDL NNSEGNENSV TKIVNNESNT FTEHNSNIYY
