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   01-MAY-2013, entry version 48.
DE   RecName: Full=Protein sus1;
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]
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.,
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. The
CC       transcription regulatory histone acetylation (HAT) complex SAGA is
CC       a multiprotein complex that activates transcription by remodeling
CC       chromatin and mediating histone acetylation and deubiquitination.
CC       Within the SAGA complex, participates in a subcomplex that
CC       specifically deubiquitinates histone H2B and is involved in the
CC       maintenance of steady-state H3 methylation levels. The TREX-2
CC       complex functions in docking export-competent ribonucleoprotein
CC       particles (mRNPs) to the nuclear entrance of the nuclear pore
CC       complex (nuclear basket). TREX-2 participates in mRNA export and
CC       accurate chromatin positioning in the nucleus by tethering genes
CC       to the nuclear periphery. Has also a role in mRNP biogenesis and
CC       maintenance of genome integrity through preventing RNA-mediated
CC       genome instability (By similarity).
CC   -!- SUBUNIT: Component of the transcription regulatory histone
CC       acetylation (HAT) complex SAGA and of the mRNA export TREX-2
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC       Nucleus, nuclear pore complex (By similarity).
CC   -!- SIMILARITY: Belongs to the ENY2 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CU329671; CAF28466.1; -; Genomic_DNA.
DR   RefSeq; NP_001018822.1; NM_001022002.2.
DR   STRING; 4896.SPBC6B1.12c-1; -.
DR   EnsemblFungi; SPBC6B1.12c.1; SPBC6B1.12c.1:pep; SPBC6B1.12c.
DR   GeneID; 3361305; -.
DR   KEGG; spo:SPBC6B1.12c; -.
DR   PomBase; SPBC6B1.12c; -.
DR   KO; K11368; -.
DR   OrthoDB; EOG4Z926B; -.
DR   NextBio; 20811385; -.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR   GO; GO:0016573; P:histone acetylation; IC:PomBase.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR018783; TF_enhancer_of_yellow_2.
DR   Pfam; PF10163; EnY2; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Complete proteome; mRNA transport;
KW   Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW   Transcription; Transcription regulation; Translocation; Transport.
FT   CHAIN         1    108       Protein sus1.
FT                                /FTId=PRO_0000350748.
SQ   SEQUENCE   108 AA;  12313 MW;  91F54D90F0469567 CRC64;
     MYDLIFSTKM TTEKIVEQLY ETGDYERLAN ELEYKLESCG WTTQLRDYTR GIVNSDSKID
     FQKLYESALQ SATESIPDSV KMDLLKDIKT CVLKLANPPE SANGGNKM
//