SUS1_YEAST
ID SUS1_YEAST Reviewed; 96 AA.
AC Q6WNK7; D6VQB1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transcription and mRNA export factor SUS1 {ECO:0000255|HAMAP-Rule:MF_03046};
GN Name=SUS1 {ECO:0000255|HAMAP-Rule:MF_03046}; OrderedLocusNames=YBR111W-A;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP SAGA AND TREX-2 COMPLEXES, AND INTERACTION WITH SAC3 AND THP1.
RX PubMed=14718168; DOI=10.1016/s0092-8674(03)01025-0;
RA Rodriguez-Navarro S., Fischer T., Luo M.-J., Antunez O., Brettschneider S.,
RA Lechner J., Perez-Ortin J.E., Reed R., Hurt E.C.;
RT "Sus1, a functional component of the SAGA histone acetylase complex and the
RT nuclear pore-associated mRNA export machinery.";
RL Cell 116:75-86(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [5]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE TREX-2 COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH SAC3.
RX PubMed=15311284; DOI=10.1038/ncb1163;
RA Fischer T., Rodriguez-Navarro S., Pereira G., Racz A., Schiebel E.,
RA Hurt E.C.;
RT "Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery.";
RL Nat. Cell Biol. 6:840-848(2004).
RN [7]
RP FUNCTION.
RX PubMed=16510898; DOI=10.1101/gr.4355406;
RA Kastenmayer J.P., Ni L., Chu A., Kitchen L.E., Au W.-C., Yang H.,
RA Carter C.D., Wheeler D., Davis R.W., Boeke J.D., Snyder M.A., Basrai M.A.;
RT "Functional genomics of genes with small open reading frames (sORFs) in S.
RT cerevisiae.";
RL Genome Res. 16:365-373(2006).
RN [8]
RP FUNCTION, INTERACTION WITH SGF11 AND UBP8, IDENTIFICATION IN THE SAGA
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16855026; DOI=10.1091/mbc.e06-02-0098;
RA Koehler A., Pascual-Garcia P., Llopis A., Zapater M., Posas F., Hurt E.C.,
RA Rodriguez-Navarro S.;
RT "The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-
RT mediated H2B deubiquitinylation through its interaction with Ubp8 and
RT Sgf11.";
RL Mol. Biol. Cell 17:4228-4236(2006).
RN [9]
RP FUNCTION.
RX PubMed=16760982; DOI=10.1038/nature04752;
RA Cabal G.G., Genovesio A., Rodriguez-Navarro S., Zimmer C., Gadal O.,
RA Lesne A., Buc H., Feuerbach-Fournier F., Olivo-Marin J.-C., Hurt E.C.,
RA Nehrbass U.;
RT "SAGA interacting factors confine sub-diffusion of transcribed genes to the
RT nuclear envelope.";
RL Nature 441:770-773(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH YRA1; MEX67 AND THE RNA POLYMERASE II
RP COMPLEX.
RX PubMed=18923079; DOI=10.1101/gad.483308;
RA Pascual-Garcia P., Govind C.K., Queralt E., Cuenca-Bono B., Llopis A.,
RA Chavez S., Hinnebusch A.G., Rodriguez-Navarro S.;
RT "Sus1 is recruited to coding regions and functions during transcription
RT elongation in association with SAGA and TREX2.";
RL Genes Dev. 22:2811-2822(2008).
RN [11]
RP FUNCTION OF THE TREX-2 COMPLEX.
RX PubMed=18667528; DOI=10.1091/mbc.e08-04-0355;
RA Gonzalez-Aguilera C., Tous C., Gomez-Gonzalez B., Huertas P., Luna R.,
RA Aguilera A.;
RT "The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA
RT export preventing RNA-mediated genome instability.";
RL Mol. Biol. Cell 19:4310-4318(2008).
RN [12]
RP IDENTIFICATION IN THE SAGA AND TREX-2 COMPLEXES.
RX PubMed=18488019; DOI=10.1038/ncb1733;
RA Koehler A., Schneider M., Cabal G.G., Nehrbass U., Hurt E.;
RT "Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA
RT export.";
RL Nat. Cell Biol. 10:707-715(2008).
RN [13]
RP FUNCTION OF THE TREX-2 COMPLEX.
RX PubMed=18003937; DOI=10.1261/rna.764108;
RA Chekanova J.A., Abruzzi K.C., Rosbash M., Belostotsky D.A.;
RT "Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active
RT genes to the nuclear rim as well as to non-nascent mRNP.";
RL RNA 14:66-77(2008).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20230609; DOI=10.1186/1471-2121-11-19;
RA Cuenca-Bono B., Garcia-Molinero V., Pascual-Garcia P., Garcia-Oliver E.,
RA Llopis A., Rodriguez-Navarro S.;
RT "A novel link between Sus1 and the cytoplasmic mRNA decay machinery
RT suggests a broad role in mRNA metabolism.";
RL BMC Cell Biol. 11:19-19(2010).
RN [15]
RP FUNCTION, AND INDUCTION.
RX PubMed=21749979; DOI=10.1093/nar/gkr496;
RA Cuenca-Bono B., Garcia-Molinero V., Pascual-Garcia P., Dopazo H.,
RA Llopis A., Vilardell J., Rodriguez-Navarro S.;
RT "SUS1 introns are required for efficient mRNA nuclear export in yeast.";
RL Nucleic Acids Res. 39:8599-8611(2011).
RN [16]
RP FUNCTION, AND INDUCTION.
RX PubMed=21749978; DOI=10.1093/nar/gkr497;
RA Hossain M.A., Rodriguez C.M., Johnson T.L.;
RT "Key features of the two-intron Saccharomyces cerevisiae gene SUS1
RT contribute to its alternative splicing.";
RL Nucleic Acids Res. 39:8612-8627(2011).
RN [17]
RP IDENTIFICATION IN THE TREX-2 COMPLEX, AND INTERACTION WITH SEM1.
RX PubMed=23599000; DOI=10.1093/nar/gkt272;
RA Garcia-Oliver E., Pascual-Garcia P., Garcia-Molinero V., Lenstra T.L.,
RA Holstege F.C., Rodriguez-Navarro S.;
RT "A novel role for Sem1 and TREX-2 in transcription involves their impact on
RT recruitment and H2B deubiquitylation activity of SAGA.";
RL Nucleic Acids Res. 41:5655-5668(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH CDC31 AND SAC3.
RX PubMed=19328066; DOI=10.1016/j.molcel.2009.01.033;
RA Jani D., Lutz S., Marshall N.J., Fischer T., Kohler A., Ellisdon A.M.,
RA Hurt E., Stewart M.;
RT "Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform
RT that promotes nuclear pore association and mRNA export.";
RL Mol. Cell 33:727-737(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH SGF11; SGF73 AND
RP UBP8.
RX PubMed=20434206; DOI=10.1016/j.cell.2010.04.026;
RA Kohler A., Zimmerman E., Schneider M., Hurt E., Zheng N.;
RT "Structural basis for assembly and activation of the heterotetrameric SAGA
RT histone H2B deubiquitinase module.";
RL Cell 141:606-617(2010).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SGF11.
RX PubMed=20007317; DOI=10.1074/jbc.m109.070839;
RA Ellisdon A.M., Jani D., Kohler A., Hurt E., Stewart M.;
RT "Structural basis for the interaction between yeast Spt-Ada-Gcn5
RT acetyltransferase (SAGA) complex components Sgf11 and Sus1.";
RL J. Biol. Chem. 285:3850-3856(2010).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH SGF11; SGF73 AND
RP UBP8.
RX PubMed=20395473; DOI=10.1126/science.1190049;
RA Samara N.L., Datta A.B., Berndsen C.E., Zhang X., Yao T., Cohen R.E.,
RA Wolberger C.;
RT "Structural insights into the assembly and function of the SAGA
RT deubiquitinating module.";
RL Science 328:1025-1029(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH SGF11; SGF73 AND
RP UBP8.
RX PubMed=22771212; DOI=10.1016/j.str.2012.05.015;
RA Samara N.L., Ringel A.E., Wolberger C.;
RT "A role for intersubunit interactions in maintaining SAGA deubiquitinating
RT module structure and activity.";
RL Structure 20:1414-1424(2012).
CC -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC association with both the TREX-2 and the SAGA complexes. The
CC transcription regulatory histone acetylation (HAT) complex SAGA is
CC involved in RNA polymerase II-dependent regulation of approximately 10%
CC of yeast genes. At the promoters, SAGA is required for recruitment of
CC the basal transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
CC interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1),
CC and chromatin modification through histone acetylation (GCN5) and
CC deubiquitination (UBP8). 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. SUS1 has also a role in mRNP biogenesis
CC and maintenance of genome integrity through preventing RNA-mediated
CC genome instability. Has a role in response to DNA damage induced by
CC methyl methane sulfonate (MMS) and replication arrest induced by
CC hydroxyurea. May also be involved in cytoplasmic mRNA decay by
CC interaction with components of P-bodies. {ECO:0000269|PubMed:15311284,
CC ECO:0000269|PubMed:16510898, ECO:0000269|PubMed:16760982,
CC ECO:0000269|PubMed:16855026, ECO:0000269|PubMed:18003937,
CC ECO:0000269|PubMed:18667528, ECO:0000269|PubMed:18923079,
CC ECO:0000269|PubMed:20230609, ECO:0000269|PubMed:21749978,
CC ECO:0000269|PubMed:21749979}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2), composed of at least
CC SUS1, SAC3, THP1, SEM1, and CDC31. TREX-2 contains 2 SUS1 chains. The
CC TREX-2 complex interacts with the mRNA export factors MEX67, MTR2 and
CC SUB2, and the nucleoporin NUP1. Component of the 1.8 MDa SAGA
CC transcription coactivator-HAT complex, which consists of at least of
CC TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6,
CC HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1.
CC TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies.
CC SAGA is built of 5 distinct domains with specialized functions. Domain
CC I (containing TRA1) probably represents the activator interaction
CC surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and
CC TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and
CC probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and
CC TAF6, and probably TAF9) are believed to play primarily an
CC architectural role. Domain III also harbors the HAT activity. Domain V
CC (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an additional
CC subcomplex of SAGA called the DUB module (deubiquitination module).
CC Interacts directly with THP1, SAC3, SGF11 and with the RNA polymerase
CC II. Interacts with YRA1 and MEX67. {ECO:0000269|PubMed:14718168,
CC ECO:0000269|PubMed:15311284, ECO:0000269|PubMed:16855026,
CC ECO:0000269|PubMed:18488019, ECO:0000269|PubMed:18923079,
CC ECO:0000269|PubMed:19328066, ECO:0000269|PubMed:20007317,
CC ECO:0000269|PubMed:20395473, ECO:0000269|PubMed:20434206,
CC ECO:0000269|PubMed:22771212, ECO:0000269|PubMed:23599000}.
CC -!- INTERACTION:
CC Q6WNK7; P06704: CDC31; NbExp=6; IntAct=EBI-1251050, EBI-4259;
CC Q6WNK7; P46674: SAC3; NbExp=11; IntAct=EBI-1251050, EBI-16425;
CC Q6WNK7; Q03067: SGF11; NbExp=12; IntAct=EBI-1251050, EBI-34550;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16855026}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:20230609}. Note=The nucleoplasm localization
CC requires the presence of UBP8 and SGF11 to bind part of SUS1 to the
CC SAGA complex. {ECO:0000269|PubMed:16855026}.
CC -!- INDUCTION: The gene for SUS1 bears 2 introns, and its expression is
CC highly regulated by splicing, translation and decay. The presence of
CC the introns thereby play a key role for SUS1 function in yeast.
CC {ECO:0000269|PubMed:21749978, ECO:0000269|PubMed:21749979}.
CC -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03046}.
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DR EMBL; AY278445; AAQ19492.1; -; mRNA.
DR EMBL; Z35980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z35981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006936; DAA07231.1; -; Genomic_DNA.
DR RefSeq; NP_878049.2; NM_001184520.1.
DR PDB; 3FWB; X-ray; 2.50 A; C=1-96.
DR PDB; 3FWC; X-ray; 2.70 A; C/D/G/H/K/L/O/P=1-96.
DR PDB; 3KIK; X-ray; 2.10 A; A/B/C/D=1-96.
DR PDB; 3KJL; X-ray; 2.70 A; A/B/C/D=1-96.
DR PDB; 3M99; X-ray; 2.70 A; C=1-96.
DR PDB; 3MHH; X-ray; 2.45 A; B=1-96.
DR PDB; 3MHS; X-ray; 1.89 A; B=1-96.
DR PDB; 4C31; X-ray; 3.00 A; B/E=1-96.
DR PDB; 4FIP; X-ray; 2.69 A; B/F=1-96.
DR PDB; 4FJC; X-ray; 2.83 A; B/F=1-96.
DR PDB; 4FK5; X-ray; 2.03 A; B=1-96.
DR PDB; 4MBE; X-ray; 2.61 A; C/F=1-96.
DR PDB; 4WA6; X-ray; 2.36 A; B/F=1-96.
DR PDB; 4ZUX; X-ray; 3.82 A; V/a/f/k=1-96.
DR PDB; 6AQR; X-ray; 2.10 A; B=1-96.
DR PDB; 6T9L; EM; 3.60 A; L=1-96.
DR PDBsum; 3FWB; -.
DR PDBsum; 3FWC; -.
DR PDBsum; 3KIK; -.
DR PDBsum; 3KJL; -.
DR PDBsum; 3M99; -.
DR PDBsum; 3MHH; -.
DR PDBsum; 3MHS; -.
DR PDBsum; 4C31; -.
DR PDBsum; 4FIP; -.
DR PDBsum; 4FJC; -.
DR PDBsum; 4FK5; -.
DR PDBsum; 4MBE; -.
DR PDBsum; 4WA6; -.
DR PDBsum; 4ZUX; -.
DR PDBsum; 6AQR; -.
DR PDBsum; 6T9L; -.
DR AlphaFoldDB; Q6WNK7; -.
DR SMR; Q6WNK7; -.
DR BioGRID; 36987; 422.
DR ComplexPortal; CPX-1686; TREX-2 transcription-export complex.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-45499N; -.
DR IntAct; Q6WNK7; 94.
DR MINT; Q6WNK7; -.
DR STRING; 4932.YBR111W-A; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; Q6WNK7; -.
DR MaxQB; Q6WNK7; -.
DR PaxDb; Q6WNK7; -.
DR PRIDE; Q6WNK7; -.
DR EnsemblFungi; YBR111W-A_mRNA; YBR111W-A; YBR111W-A.
DR GeneID; 1466445; -.
DR KEGG; sce:YBR111W-A; -.
DR SGD; S000028510; SUS1.
DR VEuPathDB; FungiDB:YBR111W-A; -.
DR eggNOG; ENOG502S9WJ; Eukaryota.
DR HOGENOM; CLU_134052_2_1_1; -.
DR InParanoid; Q6WNK7; -.
DR OMA; YESGWFD; -.
DR BioCyc; YEAST:G3O-29255-MON; -.
DR EvolutionaryTrace; Q6WNK7; -.
DR PRO; PR:Q6WNK7; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; Q6WNK7; protein.
DR GO; GO:0071819; C:DUBm complex; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IPI:ComplexPortal.
DR GO; GO:0070390; C:transcription export complex 2; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IMP:SGD.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:SGD.
DR GO; GO:0034729; P:histone H3-K79 methylation; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
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; PTHR12514; 1.
DR Pfam; PF10163; EnY2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromatin regulator; Cytoplasm; Isopeptide bond;
KW mRNA transport; Nucleus; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Translocation; Transport;
KW Ubl conjugation.
FT CHAIN 1..96
FT /note="Transcription and mRNA export factor SUS1"
FT /id="PRO_0000227806"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:3MHS"
FT HELIX 75..92
FT /evidence="ECO:0007829|PDB:3MHS"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4FK5"
SQ SEQUENCE 96 AA; 11085 MW; DB0DA0C9DC13FB21 CRC64;
MTMDTAQLKS QIQQYLVESG NYELISNELK ARLLQEGWVD KVKDLTKSEM NINESTNFTQ
ILSTVEPKAL EMVSDSTRET VLKQIREFLE EIVDTQ
