SPT7_SCHPO
ID SPT7_SCHPO Reviewed; 992 AA.
AC P87152;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transcriptional activator spt7;
GN Name=spt7; ORFNames=SPBC25H2.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP REVISION OF GENE MODEL, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation. At
CC the promoters, SAGA is required for recruitment of the basal
CC transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction and promoter selectivity, interaction with transcription
CC activators, and chromatin modification through histone acetylation and
CC deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent
CC (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA
CC via upstream activating sequences (UASs). SALSA, an altered form of
CC SAGA, may be involved in positive transcriptional regulation. SLIK is
CC proposed to have partly overlapping functions with SAGA. It
CC preferentially acetylates methylated histone H3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the SAGA, SALSA and SLIK complexes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAB08777.2; -; Genomic_DNA.
DR PIR; T40006; T40006.
DR RefSeq; NP_596356.2; NM_001022276.2.
DR AlphaFoldDB; P87152; -.
DR SMR; P87152; -.
DR BioGRID; 276936; 23.
DR IntAct; P87152; 2.
DR MINT; P87152; -.
DR STRING; 4896.SPBC25H2.11c.1; -.
DR iPTMnet; P87152; -.
DR MaxQB; P87152; -.
DR PaxDb; P87152; -.
DR PRIDE; P87152; -.
DR EnsemblFungi; SPBC25H2.11c.1; SPBC25H2.11c.1:pep; SPBC25H2.11c.
DR GeneID; 2540408; -.
DR KEGG; spo:SPBC25H2.11c; -.
DR PomBase; SPBC25H2.11c; spt7.
DR VEuPathDB; FungiDB:SPBC25H2.11c; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_006198_0_1_1; -.
DR InParanoid; P87152; -.
DR OMA; CHKISLI; -.
DR PRO; PR:P87152; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; EXP:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:GOC.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037782; Spt7.
DR PANTHER; PTHR47343; PTHR47343; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00576; BTP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..992
FT /note="Transcriptional activator spt7"
FT /id="PRO_0000310328"
FT DOMAIN 329..399
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 124..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 992 AA; 112901 MW; 461B9F7A1848CBC9 CRC64;
METNFEDSKS LDEPVLHDIA IALLKNDYWS LYLSPEQKRK YISILNDTLL WNRFINVIEW
DKLCDEKDSN GSNDDEEDDL DITTLFRCRC MIFDAKINPA LFDLSSTSSG SIEHVDHQNI
SLEASLAEEE ERKKGDAKKS EATGRQLFDD DDFDESDAED SSKATITLDL QKDKSLRKSI
IDLKSVDIDD MDTSGFAAIE SNKALSNISF NYVYYTLEND SENINEVKKF EDEEDTSTPN
TSSFQNNSSS LDLSDNLSLN SKFGSLTSSF KYLLQYLEGN RSKINATDAD VKQLLSDVKK
NKSKWANDQR IGQEELYEAA EKVVLELRSY TEHSLAFLTK VSKRDAPDYY TVIKEPMDLG
TILRNLKNLH YNSKKEFVHD LMLIWSNCFL YNSHPDHPLR VHAQFMKDKS LELINLIPDI
VIQSRKDYDD SLIEAELESD EESTAETSKH VTSKKTSSRG GQTQQAVEVH TDANSPEENN
TPVTKKEVET SKPPAVSGST PPVNEAAVIE SSNTLEKEPL SDVATEYWKI KTKDIRESHI
LNNRRILKSL QFIETELPMI RKPTAMSAFI DREVAYGSID CLPMDKGDFE PIMKLDTTPL
LEYDVGSGVP MTAGSVLETE SEEDLYFRDY SLFEINRNTP GVPSLMYKNI AKMQEIRKLC
NKIQTVRQLQ LPQPFYYEHH KSHVPFANNE PILLDIPQNY DNMSSFKPLA HDVLKKLCTI
ILFHAGFESF QMGALDALTE IAADYMAKMG AVMDQYLIYG KDKSQQEIVG QTLGELGVDD
VNDLISYVYH DVERQSVKLL EIHQRLQRHF VELLRPALSE RNDEEAIFNQ NGESFVTGNF
SYETGDDFFG LRELGLDREL GLDSLSVPLH LLQSRLRSNM SWQPEATIKG DQEYAPPPKY
PPITAESISN EIGLIQGFLK KNLEEFGLDE LLEDEDIRPR SKPPRPRLPP NGKITTGRKR
IASSVFLNQS LRKKRCLKEN EQGTEVTTLP EE
