SGF29_SCHPO
ID SGF29_SCHPO Reviewed; 244 AA.
AC Q9USW9; O74353;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=SAGA-associated factor 29;
GN Name=sgf29; ORFNames=SPBC1921.07c, SPBC21D10.13;
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 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 [3]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=19056896; DOI=10.1101/gad.1719908;
RA Helmlinger D., Marguerat S., Villen J., Gygi S.P., Bahler J., Winston F.;
RT "The S. pombe SAGA complex controls the switch from proliferation to sexual
RT differentiation through the opposing roles of its subunits Gcn5 and Spt8.";
RL Genes Dev. 22:3184-3195(2008).
RN [4]
RP FUNCTION.
RX PubMed=21642955; DOI=10.1038/emboj.2011.181;
RA Helmlinger D., Marguerat S., Villen J., Swaney D.L., Gygi S.P., Bahler J.,
RA Winston F.;
RT "Tra1 has specific regulatory roles, rather than global functions, within
RT the SAGA co-activator complex.";
RL EMBO J. 30:2843-2852(2011).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 202-THR--TYR-205.
RX PubMed=26401015; DOI=10.1073/pnas.1508449112;
RA Ringel A.E., Cieniewicz A.M., Taverna S.D., Wolberger C.;
RT "Nucleosome competition reveals processive acetylation by the SAGA HAT
RT module.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5461-E5470(2015).
CC -!- FUNCTION: Chromatin reader component of the transcription regulatory
CC histone acetylation (HAT) complex SAGA (PubMed:21642955,
CC PubMed:26401015). Sgf29 specifically recognizes and binds methylated
CC 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated
CC form (H3K4me3) (PubMed:26401015). In the SAGA complex, sgf29 is
CC required to facilitate crosstalk between gcn5 acetyltransferase
CC activity and H3K4me3 recognition (PubMed:26401015). At the promoters,
CC SAGA is required for recruitment of the basal transcription machinery
CC (PubMed:19056896). It influences RNA polymerase II transcriptional
CC activity through different activities such as TBP interaction and
CC promoter selectivity, interaction with transcription activators, and
CC chromatin modification through histone acetylation and deubiquitination
CC (PubMed:19056896). SAGA acetylates nucleosomal histone H3 to some
CC extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac)
CC (PubMed:19056896). {ECO:0000269|PubMed:19056896,
CC ECO:0000269|PubMed:21642955, ECO:0000269|PubMed:26401015}.
CC -!- SUBUNIT: Component of the SAGA complex. {ECO:0000269|PubMed:19056896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The SGF29 C-terminal (also named tudor-like) domain mediates
CC binding to methylated 'Lys-4' of histone H3 (H3K4me).
CC {ECO:0000255|PROSITE-ProRule:PRU00851}.
CC -!- SIMILARITY: Belongs to the SGF29 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00851}.
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DR EMBL; CU329671; CAB58973.1; -; Genomic_DNA.
DR PIR; T11685; T11685.
DR RefSeq; NP_596000.2; NM_001021908.2.
DR AlphaFoldDB; Q9USW9; -.
DR SMR; Q9USW9; -.
DR BioGRID; 277306; 222.
DR IntAct; Q9USW9; 2.
DR MINT; Q9USW9; -.
DR STRING; 4896.SPBC1921.07c.1; -.
DR iPTMnet; Q9USW9; -.
DR SwissPalm; Q9USW9; -.
DR MaxQB; Q9USW9; -.
DR PaxDb; Q9USW9; -.
DR PRIDE; Q9USW9; -.
DR EnsemblFungi; SPBC1921.07c.1; SPBC1921.07c.1:pep; SPBC1921.07c.
DR GeneID; 2540787; -.
DR KEGG; spo:SPBC1921.07c; -.
DR PomBase; SPBC1921.07c; sgf29.
DR VEuPathDB; FungiDB:SPBC1921.07c; -.
DR eggNOG; KOG3038; Eukaryota.
DR HOGENOM; CLU_023535_2_0_1; -.
DR InParanoid; Q9USW9; -.
DR OMA; QKECHET; -.
DR PhylomeDB; Q9USW9; -.
DR PRO; PR:Q9USW9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 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; IDA:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR037802; SGF29.
DR InterPro; IPR010750; SGF29_tudor-like_dom.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR21539; PTHR21539; 1.
DR Pfam; PF07039; DUF1325; 1.
DR PROSITE; PS51518; SGF29_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..244
FT /note="SAGA-associated factor 29"
FT /id="PRO_0000116868"
FT DOMAIN 109..244
FT /note="SGF29 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 155..157
FT /note="Histone H3K4me3 N-terminus binding"
FT /evidence="ECO:0000250|UniProtKB:P25554"
FT REGION 200..203
FT /note="Histone H3K4me3 N-terminus binding"
FT /evidence="ECO:0000250|UniProtKB:P25554"
FT REGION 222..225
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:P25554"
FT SITE 198
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:P25554"
FT SITE 205
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:P25554"
FT MUTAGEN 202..205
FT /note="TTFY->ATFV: Impaired ability to bind methylated
FT 'Lys-4' of histone H3 (H3K4me)."
FT /evidence="ECO:0000269|PubMed:26401015"
SQ SEQUENCE 244 AA; 27519 MW; 4FD4DF2BD4D9A6EE CRC64;
MVRPINAEED VTSMWVKFHE SLNPIRSSLI KQEECYKTVD GDDNPIEERI KACDAGIQTS
EEQKKELEHT MQSLEMIINV LEKANEKPVI TNSPLTRSRR NRGTSFTANT VTFTPGMSVA
FKLPYTRHNE GGDWIQCIII KVTGEGAKQR FEVQDPEPDD DGNAGQIYKT TANHLIQIPA
KGTPLPPISP KTNVLARYPE TTTFYRAEVI RTLPDGSCKL RFEGEEEVGK ETVVERHLVL
EYNG
