Database: UniProt
Original site: SUS1_SCHPO 
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   11-NOV-2015, entry version 65.
DE   RecName: 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;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Involved in mRNA export coupled transcription activation
CC       by association with both the TREX-2 and the SAGA complexes. At the
CC       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
CC       transcription activators, and chromatin modification through
CC       histone acetylation and deubiquitination. Within the SAGA complex,
CC       participates in a subcomplex required for deubiquitination of H2B
CC       and for the maintenance of steady-state H3 methylation levels. The
CC       TREX-2 complex functions in docking export-competent
CC       ribonucleoprotein particles (mRNPs) to the nuclear entrance of the
CC       nuclear pore complex (nuclear basket). TREX-2 participates in mRNA
CC       export and accurate chromatin positioning in the nucleus by
CC       tethering genes to the nuclear periphery. May also be involved in
CC       cytoplasmic mRNA decay by interaction with components of P-bodies
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated
CC       TREX-2 complex (transcription and export complex 2), composed of
CC       at least sus1, sac3, thp1, sem1, and cdc31. TREX-2 contains 2 sus1
CC       chains. The TREX-2 complex interacts with the nucleoporin nup1.
CC       Component of the 1.8 MDa SAGA transcription coactivator-HAT
CC       complex. SAGA is built of 5 distinct domains with specialized
CC       functions. Within the SAGA complex, sus1, sgf11, sgf73 and ubp8
CC       form an additional subcomplex of SAGA called the DUB module
CC       (deubiquitination module). Interacts directly with thp1, sac3,
CC       sgf11, and with the RNA polymerase II. {ECO:0000255|HAMAP-
CC       Rule:MF_03046}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03046}. Nucleus, nuclear pore complex {ECO:0000255|HAMAP-
CC       Rule:MF_03046}. Cytoplasm, P-body {ECO:0000255|HAMAP-
CC       Rule:MF_03046}.
CC   -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03046}.
DR   EMBL; CU329671; CAF28466.1; -; Genomic_DNA.
DR   RefSeq; NP_001018822.1; NM_001022002.2.
DR   BioGrid; 280381; 7.
DR   IntAct; Q7LL15; 2.
DR   MINT; MINT-8207616; -.
DR   MaxQB; Q7LL15; -.
DR   EnsemblFungi; SPBC6B1.12c.1; SPBC6B1.12c.1:pep; SPBC6B1.12c.
DR   GeneID; 3361305; -.
DR   KEGG; spo:SPBC6B1.12c; -.
DR   EuPathDB; FungiDB:SPBC6B1.12c; -.
DR   PomBase; SPBC6B1.12c; sus1.
DR   InParanoid; Q7LL15; -.
DR   KO; K11368; -.
DR   OrthoDB; EOG7RNKCD; -.
DR   PhylomeDB; Q7LL15; -.
DR   NextBio; 20811385; -.
DR   PRO; PR:Q7LL15; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR   GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0070390; C:transcription export complex 2; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR   GO; GO:0016573; P:histone acetylation; IC:PomBase.
DR   GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; EXP:PomBase.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_03046; ENY2_Sus1; 1.
DR   InterPro; IPR018783; TF_enhancer_of_yellow_2.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Complete proteome; Cytoplasm;
KW   mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Translocation; Transport.
FT   CHAIN         1    108       Transcription and mRNA export factor
FT                                sus1.
FT                                /FTId=PRO_0000350748.
SQ   SEQUENCE   108 AA;  12313 MW;  91F54D90F0469567 CRC64;
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