ID   SUS1_SCHPO              Reviewed;         108 AA.
AC   Q7LL15;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=SAGA complex subunit Sus1;
DE   AltName: Full=Transcription and mRNA export factor sus1 {ECO:0000255|HAMAP-Rule:MF_03046};
GN   Name=sus1; ORFNames=SPBC6B1.12c;
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   IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
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).
CC   -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC       association with both the TREX-2 and the SAGA complexes. SAGA acts as a
CC       general cofactor required for essentially all RNA polymerase II
CC       transcription. At the promoters, SAGA is required for transcription
CC       pre-initiation complex (PIC) recruitment. It influences RNA polymerase
CC       II transcriptional activity through different activities such as TBP
CC       interaction (via core/TAF module) and promoter selectivity, interaction
CC       with transcription activators (via Tra1/SPT module), and chromatin
CC       modification through histone acetylation (via HAT module) and
CC       deubiquitination (via DUB module). SAGA preferentially acetylates
CC       histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and
CC       deubiquitinates histone H2B. SAGA interacts with DNA via upstream
CC       activating sequences (UASs). Within the SAGA complex, participates in a
CC       subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of
CC       H2B and for the maintenance of steady-state H3 methylation levels. The
CC       TREX-2 complex functions in docking export-competent ribonucleoprotein
CC       particles (mRNPs) to the nuclear entrance of the nuclear pore complex
CC       (nuclear basket), by association with components of the nuclear mRNA
CC       export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the
CC       nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA
CC       export and accurate chromatin positioning in the nucleus by tethering
CC       genes to the nuclear periphery. {ECO:0000250|UniProtKB:Q6WNK7}.
CC   -!- SUBUNIT: Component of the 1.8 MDa SAGA (Spt-Ada-Gcn5 acetyltransferase)
CC       complex, which is composed of 19 subunits tra1, spt7, taf5, ngg1/ada3,
CC       sgf73, spt20, spt8, taf12, taf6, hfi1/ada1, ubp8, gcn5, ada2, spt3,
CC       sgf29, taf10, taf9, sgf11 and sus1 (PubMed:19056896). The SAGA complex
CC       is composed of 4 modules, namely the HAT (histone acetyltransferase)
CC       module (gcn5, ada2, ngg1/ada3 and sgf29), the DUB (deubiquitinating)
CC       module (ubp8, sgf11, sgf73 and sus1), the core or TAF (TBP-associated
CC       factor) module (taf5, taf6, taf9, taf10 and taf12), and the Tra1 or SPT
CC       (Suppressor of Ty) module (tra1, hfi1/ada1, spt3, spt7, spt8 and
CC       spt20). The Tra1/SPT module binds activators, the core module recruits
CC       TBP (TATA-binding protein), the HAT module contains the histone H3
CC       acetyltransferase gcn5, and the DUB module comprises the histone H2B
CC       deubiquitinase ubp8 (By similarity). Component of the nuclear pore
CC       complex (NPC)-associated TREX-2 complex (transcription and export
CC       complex 2), composed of at least sus1, sac3, thp1, sem1, and cdc31.
CC       TREX-2 contains 2 sus1 chains. The TREX-2 complex interacts with the
CC       mRNA export factors mex67, mtr2 and sub2, and the nucleoporin nup1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q6WNK7,
CC       ECO:0000269|PubMed:19056896}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03046}. Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03046}.
CC   -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03046}.
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DR   EMBL; CU329671; CAF28466.1; -; Genomic_DNA.
DR   RefSeq; NP_001018822.1; NM_001022002.3.
DR   AlphaFoldDB; Q7LL15; -.
DR   SMR; Q7LL15; -.
DR   BioGRID; 280381; 8.
DR   ComplexPortal; CPX-2718; SAGA complex.
DR   FunCoup; Q7LL15; 33.
DR   IntAct; Q7LL15; 2.
DR   MINT; Q7LL15; -.
DR   STRING; 284812.Q7LL15; -.
DR   iPTMnet; Q7LL15; -.
DR   PaxDb; 284812-Q7LL15; -.
DR   GeneID; 3361305; -.
DR   KEGG; spo:3361305; -.
DR   PomBase; SPBC6B1.12c; sus1.
DR   VEuPathDB; FungiDB:SPBC6B1.12c; -.
DR   HOGENOM; CLU_134052_2_0_1; -.
DR   InParanoid; Q7LL15; -.
DR   OMA; ANELEYK; -.
DR   PhylomeDB; Q7LL15; -.
DR   PRO; PR:Q7LL15; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0070390; C:transcription export complex 2; ISO:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IC:PomBase.
DR   Gene3D; 1.10.246.140; -; 1.
DR   HAMAP; MF_03046; ENY2_Sus1; 1.
DR   InterPro; IPR018783; TF_ENY2.
DR   InterPro; IPR038212; TF_EnY2_sf.
DR   PANTHER; PTHR12514; ENHANCER OF YELLOW 2 TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF10163; EnY2; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Cytoplasm; mRNA transport; Nucleus;
KW   Protein transport; Reference proteome; Transcription;
KW   Transcription regulation; Translocation; Transport.
FT   CHAIN           1..108
FT                   /note="SAGA complex subunit Sus1"
FT                   /id="PRO_0000350748"
SQ   SEQUENCE   108 AA;  12313 MW;  91F54D90F0469567 CRC64;
     MYDLIFSTKM TTEKIVEQLY ETGDYERLAN ELEYKLESCG WTTQLRDYTR GIVNSDSKID
     FQKLYESALQ SATESIPDSV KMDLLKDIKT CVLKLANPPE SANGGNKM
//