SPT5H_HUMAN
ID SPT5H_HUMAN Reviewed; 1087 AA.
AC O00267; O43279; Q59G52; Q99639;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Transcription elongation factor SPT5;
DE Short=hSPT5;
DE AltName: Full=DRB sensitivity-inducing factor 160 kDa subunit;
DE Short=DSIF p160;
DE AltName: Full=DRB sensitivity-inducing factor large subunit;
DE Short=DSIF large subunit;
DE AltName: Full=Tat-cotransactivator 1 protein;
DE Short=Tat-CT1 protein;
GN Name=SUPT5H; Synonyms=SPT5, SPT5H;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8975720; DOI=10.1006/geno.1996.0646;
RA Chiang P.-W., Fogel E., Jackson C.L., Lieuallen K., Lennon G., Qu X.,
RA Wang S.-Q., Kurnit D.M.;
RT "Isolation, sequencing, and mapping of the human homologue of the yeast
RT transcription factor, SPT5.";
RL Genomics 38:421-424(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 116-152;
RP 288-319; 461-471; 529-542; 580-587; 746-761; 795-809; 841-885; 888-922 AND
RP 1068-1087, DOMAINS CTR1 AND CTR2, AND PHOSPHORYLATION.
RX PubMed=9199507; DOI=10.1016/s0014-5793(97)00486-9;
RA Stachora A.A., Schaefer R.E., Pohlmeier M., Maier G., Ponstingl H.;
RT "Human Supt5h protein, a putative modulator of chromatin structure, is
RT reversibly phosphorylated in mitosis.";
RL FEBS Lett. 409:74-78(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 277-282;
RP 324-328; 459-470 AND 580-597, FUNCTION, AND INTERACTION WITH SUPT4H1 AND
RP RNA POLYMERASE II.
RX PubMed=9450929; DOI=10.1101/gad.12.3.343;
RA Wada T., Takagi T., Yamaguchi Y., Ferdous A., Imai T., Hirose S.,
RA Sugimoto S., Yano K., Hartzog G.A., Winston F., Buratowski S., Handa H.;
RT "DSIF, a novel transcription elongation factor that regulates RNA
RT polymerase II processivity, is composed of human Spt4 and Spt5 homologs.";
RL Genes Dev. 12:343-356(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 199-213;
RP 247-258 AND 799-811, AND FUNCTION.
RX PubMed=9514752; DOI=10.1006/jmbi.1997.1601;
RA Wu-Baer F., Lane W.S., Gaynor R.B.;
RT "Role of the human homolog of the yeast transcription factor SPT5 in HIV-1
RT Tat-activation.";
RL J. Mol. Biol. 277:179-197(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH RNA POLYMERASE II.
RX PubMed=9857195; DOI=10.1093/emboj/17.24.7395;
RA Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.;
RT "Evidence that P-TEFb alleviates the negative effect of DSIF on RNA
RT polymerase II-dependent transcription in vitro.";
RL EMBO J. 17:7395-7403(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH THE NELF COMPLEX.
RX PubMed=10199401; DOI=10.1016/s0092-8674(00)80713-8;
RA Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S.,
RA Hasegawa J., Handa H.;
RT "NELF, a multisubunit complex containing RD, cooperates with DSIF to
RT repress RNA polymerase II elongation.";
RL Cell 97:41-51(1999).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH NCL; CCNT1; RNA POL II;
RP HTATSF1 AND CDK9.
RX PubMed=10393184; DOI=10.1093/emboj/18.13.3688;
RA Parada C.A., Roeder R.G.;
RT "A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-
RT 1 transcription.";
RL EMBO J. 18:3688-3701(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH RNGTT.
RX PubMed=10421630; DOI=10.1101/gad.13.14.1774;
RA Wen Y., Shatkin A.J.;
RT "Transcription elongation factor hSPT5 stimulates mRNA capping.";
RL Genes Dev. 13:1774-1779(1999).
RN [11]
RP FUNCTION, INTERACTION WITH RNA POLYMERASE II AND SUPT4H1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10075709; DOI=10.1074/jbc.274.12.8085;
RA Yamaguchi Y., Wada T., Watanabe D., Takagi T., Hasegawa J., Handa H.;
RT "Structure and function of the human transcription elongation factor
RT DSIF.";
RL J. Biol. Chem. 274:8085-8092(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH HTATSF1 AND RNA POLYMERASE II.
RX PubMed=10454543; DOI=10.1128/mcb.19.9.5960;
RA Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.;
RT "Tat-SF1 protein associates with RAP30 and human SPT5 proteins.";
RL Mol. Cell. Biol. 19:5960-5968(1999).
RN [13]
RP FUNCTION.
RX PubMed=10912001; DOI=10.1016/s1097-2765(00)80272-5;
RA Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y.,
RA Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.;
RT "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation
RT and reveals functional differences between P-TEFb and TFIIH.";
RL Mol. Cell 5:1067-1072(2000).
RN [14]
RP FUNCTION, INTERACTION WITH RNA POLYMERASE II AND SUPT4H1, AND
RP PHOSPHORYLATION AT THR-775 AND THR-784.
RX PubMed=10757782; DOI=10.1128/mcb.20.9.2970-2983.2000;
RA Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.;
RT "Domains in the SPT5 protein that modulate its transcriptional regulatory
RT properties.";
RL Mol. Cell. Biol. 20:2970-2983(2000).
RN [15]
RP PHOSPHORYLATION BY CDK9.
RX PubMed=11145967; DOI=10.1074/jbc.m010908200;
RA Kim J.B., Sharp P.A.;
RT "Positive transcription elongation factor B phosphorylates hSPT5 and RNA
RT polymerase II carboxyl-terminal domain independently of cyclin-dependent
RT kinase-activating kinase.";
RL J. Biol. Chem. 276:12317-12323(2001).
RN [16]
RP FUNCTION, AND PHOSPHORYLATION BY CDK9.
RX PubMed=11112772; DOI=10.1074/jbc.m006130200;
RA Ping Y.-H., Rana T.M.;
RT "DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1
RT Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and
RT DSIF during transcription elongation.";
RL J. Biol. Chem. 276:12951-12958(2001).
RN [17]
RP FUNCTION.
RX PubMed=11553615; DOI=10.1074/jbc.m104967200;
RA Renner D.B., Yamaguchi Y., Wada T., Handa H., Price D.H.;
RT "A highly purified RNA polymerase II elongation control system.";
RL J. Biol. Chem. 276:42601-42609(2001).
RN [18]
RP INTERACTION WITH PIN1, AND PHOSPHORYLATION.
RX PubMed=11575923; DOI=10.1006/jmbi.2001.4991;
RA Lavoie S.B., Albert A.L., Handa H., Vincent M., Bensaude O.;
RT "The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by
RT Cdk9.";
RL J. Mol. Biol. 312:675-685(2001).
RN [19]
RP FUNCTION, AND PHOSPHORYLATION BY CDK9.
RX PubMed=11809800; DOI=10.1128/mcb.22.4.1079-1093.2002;
RA Bourgeois C.F., Kim Y.K., Churcher M.J., West M.J., Karn J.;
RT "Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing
RT premature RNA release at terminator sequences.";
RL Mol. Cell. Biol. 22:1079-1093(2002).
RN [20]
RP INTERACTION WITH THE NELF COMPLEX.
RX PubMed=11940650; DOI=10.1128/mcb.22.9.2918-2927.2002;
RA Yamaguchi Y., Inukai N., Narita T., Wada T., Handa H.;
RT "Evidence that negative elongation factor represses transcription
RT elongation through binding to a DRB sensitivity-inducing factor/RNA
RT polymerase II complex and RNA.";
RL Mol. Cell. Biol. 22:2918-2927(2002).
RN [21]
RP FUNCTION, AND INTERACTION WITH SUPT4H1.
RX PubMed=12653964; DOI=10.1046/j.1365-2443.2003.00638.x;
RA Kim D.-K., Inukai N., Yamada T., Furuya A., Sato H., Yamaguchi Y., Wada T.,
RA Handa H.;
RT "Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5
RT exert their roles in transcriptional elongation as parts of the DSIF
RT complex.";
RL Genes Cells 8:371-378(2003).
RN [22]
RP FUNCTION, INTERACTION WITH CDK9; PRMT1; RNA POLYMERASE II; PRMT5 AND
RP SUPT4H1, METHYLATION AT ARG-681; ARG-696 AND ARG-698, AND MUTAGENESIS OF
RP ARG-681; ARG-696 AND ARG-698.
RX PubMed=12718890; DOI=10.1016/s1097-2765(03)00101-1;
RA Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B.,
RA Gehrig P., Gaynor R.B.;
RT "Methylation of SPT5 regulates its interaction with RNA polymerase II and
RT transcriptional elongation properties.";
RL Mol. Cell 11:1055-1066(2003).
RN [23]
RP INTERACTION WITH THE NELF COMPLEX.
RX PubMed=12612062; DOI=10.1128/mcb.23.6.1863-1873.2003;
RA Narita T., Yamaguchi Y., Yano K., Sugimoto S., Chanarat S., Wada T.,
RA Kim D.-K., Hasegawa J., Omori M., Inukai N., Endoh M., Yamada T., Handa H.;
RT "Human transcription elongation factor NELF: identification of novel
RT subunits and reconstitution of the functionally active complex.";
RL Mol. Cell. Biol. 23:1863-1873(2003).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF GLY-1002.
RX PubMed=15380072; DOI=10.1016/j.cub.2004.08.066;
RA Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H.,
RA Ish-Horowicz D.;
RT "Locus-specific requirements for Spt5 in transcriptional activation and
RT repression in Drosophila.";
RL Curr. Biol. 14:1680-1684(2004).
RN [25]
RP PHOSPHORYLATION BY CDK9.
RX PubMed=15564463; DOI=10.1128/jvi.78.24.13522-13533.2004;
RA Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F.,
RA Brady J.N., Kumar A.;
RT "Coordination of transcription factor phosphorylation and histone
RT methylation by the P-TEFb kinase during human immunodeficiency virus type 1
RT transcription.";
RL J. Virol. 78:13522-13533(2004).
RN [26]
RP FUNCTION.
RX PubMed=14701750; DOI=10.1128/mcb.24.2.787-795.2004;
RA Fujinaga K., Irwin D., Huang Y., Taube R., Kurosu T., Peterlin B.M.;
RT "Dynamics of human immunodeficiency virus transcription: P-TEFb
RT phosphorylates RD and dissociates negative effectors from the
RT transactivation response element.";
RL Mol. Cell. Biol. 24:787-795(2004).
RN [27]
RP INTERACTION WITH RNA POLYMERASE II; SUPT4H1 AND SUPT6H.
RX PubMed=15060154; DOI=10.1128/mcb.24.8.3324-3336.2004;
RA Endoh M., Zhu W., Hasegawa J., Watanabe H., Kim D.-K., Aida M., Inukai N.,
RA Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., Mandal S.S.,
RA Reinberg D., Wada T., Handa H.;
RT "Human Spt6 stimulates transcription elongation by RNA polymerase II in
RT vitro.";
RL Mol. Cell. Biol. 24:3324-3336(2004).
RN [28]
RP FUNCTION.
RX PubMed=15136722; DOI=10.1073/pnas.0401493101;
RA Mandal S.S., Chu C., Wada T., Handa H., Shatkin A.J., Reinberg D.;
RT "Functional interactions of RNA-capping enzyme with factors that positively
RT and negatively regulate promoter escape by RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7572-7577(2004).
RN [29]
RP FUNCTION.
RX PubMed=16214896; DOI=10.1073/pnas.0409405102;
RA Palangat M., Renner D.B., Price D.H., Landick R.;
RT "A negative elongation factor for human RNA polymerase II inhibits the
RT anti-arrest transcript-cleavage factor TFIIS.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15036-15041(2005).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [31]
RP PHOSPHORYLATION BY CDK7.
RX PubMed=16327805; DOI=10.1038/nsmb1028;
RA Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C.,
RA Blethrow J.D., Shokat K.M., Fisher R.P.;
RT "Dichotomous but stringent substrate selection by the dual-function Cdk7
RT complex revealed by chemical genetics.";
RL Nat. Struct. Mol. Biol. 13:55-62(2006).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666 AND THR-1034, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666 AND THR-1034, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-686; SER-789;
RP THR-791; SER-804; THR-806 AND THR-1034, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP INTERACTION WITH MCM3AP.
RX PubMed=23652018; DOI=10.1038/ncomms2823;
RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA Goodman M.F., Sakaguchi N.;
RT "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT modulating transcription and nucleosome occupancy.";
RL Nat. Commun. 4:1830-1830(2013).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-143 AND LYS-1037, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [43]
RP STRUCTURE BY NMR OF 420-523 AND 690-757.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of KOW motifs of human transcription elongation factor
RT SPT5.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 176-273 IN COMPLEX WITH SPT4H1.
RX PubMed=19860741; DOI=10.1042/bj20091422;
RA Wenzel S., Martins B.M., Rosch P., Wohrl B.M.;
RT "Crystal structure of the human transcription elongation factor DSIF hSpt4
RT subunit in complex with the hSpt5 dimerization interface.";
RL Biochem. J. 425:373-380(2010).
CC -!- FUNCTION: Component of the DRB sensitivity-inducing factor complex
CC (DSIF complex), which regulates mRNA processing and transcription
CC elongation by RNA polymerase II. DSIF positively regulates mRNA capping
CC by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A.
CC DSIF also acts cooperatively with the negative elongation factor
CC complex (NELF complex) to enhance transcriptional pausing at sites
CC proximal to the promoter. Transcriptional pausing may facilitate the
CC assembly of an elongation competent RNA polymerase II complex. DSIF and
CC NELF promote pausing by inhibition of the transcription elongation
CC factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at
CC transcription pause sites and stimulates the weak intrinsic nuclease
CC activity of the enzyme. Cleavage of blocked transcripts by RNA
CC polymerase II promotes the resumption of transcription from the new 3'
CC terminus and may allow repeated attempts at transcription through
CC natural pause sites. DSIF can also positively regulate transcriptional
CC elongation and is required for the efficient activation of
CC transcriptional elongation by the HIV-1 nuclear transcriptional
CC activator, Tat. DSIF acts to suppress transcriptional pausing in
CC transcripts derived from the HIV-1 LTR and blocks premature release of
CC HIV-1 transcripts at terminator sequences.
CC {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401,
CC ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10421630,
CC ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10757782,
CC ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772,
CC ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:11809800,
CC ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890,
CC ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15136722,
CC ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896,
CC ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9514752,
CC ECO:0000269|PubMed:9857195}.
CC -!- SUBUNIT: Interacts with SUPT4H1 to form DSIF. DSIF interacts with the
CC positive transcription elongation factor b complex (P-TEFb complex),
CC which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts
CC with RNA polymerase II, and this interaction is reduced by
CC phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb.
CC DSIF also interacts with the NELF complex, which is composed of NELFA,
CC NELFB, NELFD and NELFE, and this interaction occurs following prior
CC binding of DSIF to RNA polymerase II. DSIF also interacts with
CC PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can
CC interact with PIN1. Component of a complex which is at least composed
CC of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA
CC polymerase II, SUPT5H, and NCL/nucleolin. Interacts with MCM3AP isoform
CC GANP (PubMed:23652018). {ECO:0000269|PubMed:10075709,
CC ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10393184,
CC ECO:0000269|PubMed:10421630, ECO:0000269|PubMed:10454543,
CC ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:11575923,
CC ECO:0000269|PubMed:11940650, ECO:0000269|PubMed:12612062,
CC ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890,
CC ECO:0000269|PubMed:15060154, ECO:0000269|PubMed:19860741,
CC ECO:0000269|PubMed:23652018, ECO:0000269|PubMed:9450929,
CC ECO:0000269|PubMed:9857195}.
CC -!- INTERACTION:
CC O00267; P50613: CDK7; NbExp=3; IntAct=EBI-710464, EBI-1245958;
CC O00267; Q13526: PIN1; NbExp=4; IntAct=EBI-710464, EBI-714158;
CC O00267; P24928: POLR2A; NbExp=5; IntAct=EBI-710464, EBI-295301;
CC O00267; P62937: PPIA; NbExp=2; IntAct=EBI-710464, EBI-437708;
CC O00267; P63272: SUPT4H1; NbExp=15; IntAct=EBI-710464, EBI-727250;
CC O00267; P54274: TERF1; NbExp=2; IntAct=EBI-710464, EBI-710997;
CC O00267; Q5EP34: PA; Xeno; NbExp=3; IntAct=EBI-710464, EBI-25772799;
CC O00267; G3MZY8: POLR2A; Xeno; NbExp=2; IntAct=EBI-710464, EBI-6551200;
CC O00267; A5PJW8: POLR2B; Xeno; NbExp=8; IntAct=EBI-710464, EBI-15586776;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10075709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00267-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00267-2; Sequence=VSP_016282;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:8975720}.
CC -!- PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively
CC regulates interaction with P-TEFb and RNA polymerase II.
CC {ECO:0000269|PubMed:12718890}.
CC -!- PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb
CC alleviates transcriptional pausing and can stimulate transcriptional
CC elongation from the HIV-1 LTR. P-TEFb dependent phosphorylation is
CC stimulated by the HIV-1 Tat protein. Phosphorylation may also stimulate
CC interaction with PIN1. Bulk phosphorylation occurs predominantly in
CC mitosis. {ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:11112772,
CC ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923,
CC ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:15564463,
CC ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:9199507}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92494.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U56402; AAC51102.1; -; mRNA.
DR EMBL; Y12790; CAA73326.1; -; mRNA.
DR EMBL; AB000516; BAA24075.1; -; mRNA.
DR EMBL; AF040253; AAD02179.1; -; mRNA.
DR EMBL; AB209257; BAD92494.1; ALT_INIT; mRNA.
DR EMBL; BC024203; AAH24203.1; -; mRNA.
DR CCDS; CCDS12536.1; -. [O00267-1]
DR CCDS; CCDS46072.1; -. [O00267-2]
DR RefSeq; NP_001104490.1; NM_001111020.2. [O00267-1]
DR RefSeq; NP_001124296.1; NM_001130824.1. [O00267-1]
DR RefSeq; NP_001124297.1; NM_001130825.1. [O00267-2]
DR RefSeq; NP_001306919.1; NM_001319990.1. [O00267-1]
DR RefSeq; NP_001306920.1; NM_001319991.1. [O00267-2]
DR RefSeq; NP_003160.2; NM_003169.3. [O00267-1]
DR PDB; 2DO3; NMR; -; A=462-523.
DR PDB; 2E6Z; NMR; -; A=420-471.
DR PDB; 2E70; NMR; -; A=694-757.
DR PDB; 3H7H; X-ray; 1.55 A; B=176-273.
DR PDB; 4L1U; X-ray; 2.42 A; G/H/I/J=778-790.
DR PDB; 5OHO; X-ray; 1.60 A; A/B=536-646.
DR PDB; 5OHQ; X-ray; 1.10 A; A=979-1087.
DR PDB; 5OIK; EM; 3.70 A; Z=1-1087.
DR PDB; 5U98; X-ray; 2.00 A; C/F=980-988.
DR PDB; 6EQY; NMR; -; A=522-647.
DR PDB; 6ER0; NMR; -; A=961-1087.
DR PDB; 6GMH; EM; 3.10 A; Z=1-1087.
DR PDB; 6GML; EM; 3.20 A; Z=1-1087.
DR PDB; 6TED; EM; 3.10 A; Z=1-1087.
DR PDB; 7OKX; EM; 3.30 A; Z=1-1087.
DR PDB; 7OKY; EM; 4.14 A; Z=1-1087.
DR PDB; 7OL0; EM; 3.00 A; Z=1-1087.
DR PDB; 7PKS; EM; 3.60 A; Z=1-1087.
DR PDBsum; 2DO3; -.
DR PDBsum; 2E6Z; -.
DR PDBsum; 2E70; -.
DR PDBsum; 3H7H; -.
DR PDBsum; 4L1U; -.
DR PDBsum; 5OHO; -.
DR PDBsum; 5OHQ; -.
DR PDBsum; 5OIK; -.
DR PDBsum; 5U98; -.
DR PDBsum; 6EQY; -.
DR PDBsum; 6ER0; -.
DR PDBsum; 6GMH; -.
DR PDBsum; 6GML; -.
DR PDBsum; 6TED; -.
DR PDBsum; 7OKX; -.
DR PDBsum; 7OKY; -.
DR PDBsum; 7OL0; -.
DR PDBsum; 7PKS; -.
DR AlphaFoldDB; O00267; -.
DR SMR; O00267; -.
DR BioGRID; 112697; 304.
DR ComplexPortal; CPX-891; DSIF transcription elongation factor complex.
DR CORUM; O00267; -.
DR DIP; DIP-29014N; -.
DR IntAct; O00267; 122.
DR MINT; O00267; -.
DR STRING; 9606.ENSP00000470252; -.
DR GlyGen; O00267; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O00267; -.
DR MetOSite; O00267; -.
DR PhosphoSitePlus; O00267; -.
DR BioMuta; SUPT5H; -.
DR EPD; O00267; -.
DR jPOST; O00267; -.
DR MassIVE; O00267; -.
DR MaxQB; O00267; -.
DR PaxDb; O00267; -.
DR PeptideAtlas; O00267; -.
DR PRIDE; O00267; -.
DR ProteomicsDB; 47816; -. [O00267-1]
DR ProteomicsDB; 47817; -. [O00267-2]
DR Antibodypedia; 16797; 188 antibodies from 29 providers.
DR DNASU; 6829; -.
DR Ensembl; ENST00000359191.10; ENSP00000352117.6; ENSG00000196235.14. [O00267-2]
DR Ensembl; ENST00000402194.6; ENSP00000384505.2; ENSG00000196235.14. [O00267-2]
DR Ensembl; ENST00000432763.7; ENSP00000404029.4; ENSG00000196235.14. [O00267-1]
DR Ensembl; ENST00000598725.5; ENSP00000469090.1; ENSG00000196235.14. [O00267-1]
DR Ensembl; ENST00000599117.5; ENSP00000470252.1; ENSG00000196235.14. [O00267-1]
DR GeneID; 6829; -.
DR KEGG; hsa:6829; -.
DR MANE-Select; ENST00000432763.7; ENSP00000404029.4; NM_001111020.3; NP_001104490.1.
DR UCSC; uc002olo.5; human. [O00267-1]
DR CTD; 6829; -.
DR DisGeNET; 6829; -.
DR GeneCards; SUPT5H; -.
DR HGNC; HGNC:11469; SUPT5H.
DR HPA; ENSG00000196235; Low tissue specificity.
DR MIM; 602102; gene.
DR neXtProt; NX_O00267; -.
DR OpenTargets; ENSG00000196235; -.
DR PharmGKB; PA36255; -.
DR VEuPathDB; HostDB:ENSG00000196235; -.
DR eggNOG; KOG1999; Eukaryota.
DR GeneTree; ENSGT00440000037640; -.
DR HOGENOM; CLU_003537_0_0_1; -.
DR InParanoid; O00267; -.
DR OMA; VGYMNTP; -.
DR OrthoDB; 828863at2759; -.
DR PhylomeDB; O00267; -.
DR TreeFam; TF105730; -.
DR BioCyc; MetaCyc:G66-31601-MON; -.
DR PathwayCommons; O00267; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR SignaLink; O00267; -.
DR SIGNOR; O00267; -.
DR BioGRID-ORCS; 6829; 731 hits in 1079 CRISPR screens.
DR ChiTaRS; SUPT5H; human.
DR EvolutionaryTrace; O00267; -.
DR GeneWiki; SUPT5H; -.
DR GenomeRNAi; 6829; -.
DR Pharos; O00267; Tbio.
DR PRO; PR:O00267; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O00267; protein.
DR Bgee; ENSG00000196235; Expressed in right testis and 201 other tissues.
DR ExpressionAtlas; O00267; baseline and differential.
DR Genevisible; O00267; HS.
DR GO; GO:0032044; C:DSIF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR IDEAL; IID00641; -.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 6.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1087
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208468"
FT DOMAIN 273..306
FT /note="KOW 1"
FT DOMAIN 420..451
FT /note="KOW 2"
FT DOMAIN 472..503
FT /note="KOW 3"
FT DOMAIN 594..627
FT /note="KOW 4"
FT DOMAIN 704..737
FT /note="KOW 5"
FT REPEAT 754..759
FT /note="CTR1-1; approximate"
FT REPEAT 760..765
FT /note="CTR1-2"
FT REPEAT 766..771
FT /note="CTR1-3"
FT REPEAT 772..778
FT /note="CTR1-4"
FT REPEAT 781..787
FT /note="CTR1-5"
FT REPEAT 788..794
FT /note="CTR1-6"
FT REPEAT 796..802
FT /note="CTR1-7"
FT REPEAT 803..809
FT /note="CTR1-8"
FT REPEAT 811..817
FT /note="CTR1-9"
FT REPEAT 844..851
FT /note="CTR2-1"
FT REPEAT 854..862
FT /note="CTR2-2; approximate"
FT REPEAT 863..869
FT /note="CTR2-3; approximate"
FT REPEAT 881..885
FT /note="CTR2-4; half-length"
FT REPEAT 896..902
FT /note="CTR2-5; approximate"
FT REPEAT 904..911
FT /note="CTR2-6"
FT REPEAT 916..921
FT /note="CTR2-7; approximate"
FT REPEAT 924..930
FT /note="CTR2-8"
FT REPEAT 932..939
FT /note="CTR2-9"
FT REPEAT 943..950
FT /note="CTR2-10"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..270
FT /note="Interaction with SUPT4H1"
FT REGION 313..420
FT /note="Interaction with RNA polymerase II"
FT REGION 670..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..817
FT /note="9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-
FT X-[YQ], motif CTR1"
FT REGION 844..950
FT /note="10 X 8 AA approximate tandem repeats of P-[TS]-P-S-
FT P-[QA]-[SG]-Y, motif CTR2"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..872
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55201"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55201"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 681
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 681
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 696
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 696
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 698
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 698
FT /note="Omega-N-methylarginine; by PRMT1 and PRMT5;
FT alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 698
FT /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT /evidence="ECO:0000269|PubMed:12718890"
FT MOD_RES 718
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O55201"
FT MOD_RES 775
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000269|PubMed:10757782"
FT MOD_RES 784
FT /note="Phosphothreonine; by CDK9"
FT /evidence="ECO:0000269|PubMed:10757782"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 791
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 806
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1034
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1037
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 103..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_016282"
FT MUTAGEN 681
FT /note="R->A: Enhances interactions with CDK9 and RNA
FT polymerase II and enhances transcriptional elongation; when
FT associated with A-696 and A-698."
FT /evidence="ECO:0000269|PubMed:12718890"
FT MUTAGEN 681
FT /note="R->K: Increases promoter association and enhances
FT transcriptional elongation; when associated with K-696 and
FT K-698."
FT /evidence="ECO:0000269|PubMed:12718890"
FT MUTAGEN 696
FT /note="R->A: Enhances interactions with CDK9 and RNA
FT polymerase II and enhances transcriptional elongation; when
FT associated with A-681 and A-698."
FT /evidence="ECO:0000269|PubMed:12718890"
FT MUTAGEN 696
FT /note="R->K: Increases promoter association and enhances
FT transcriptional elongation; when associated with K-681 and
FT K-698."
FT /evidence="ECO:0000269|PubMed:12718890"
FT MUTAGEN 698
FT /note="R->A: Enhances transcriptional elongation. Enhances
FT interactions with CDK9 and RNA polymerase II and enhances
FT transcriptional elongation; when associated with A-681 and
FT A-696."
FT /evidence="ECO:0000269|PubMed:12718890"
FT MUTAGEN 698
FT /note="R->K: Increases promoter association and enhances
FT transcriptional elongation; when associated with K-681 and
FT K-696."
FT /evidence="ECO:0000269|PubMed:12718890"
FT MUTAGEN 1002
FT /note="G->D: Defective in regulation of transcriptional
FT elongation."
FT /evidence="ECO:0000269|PubMed:15380072"
FT CONFLICT 181
FT /note="T -> I (in Ref. 1; AAC51102)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="G -> A (in Ref. 1; AAC51102)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="A -> G (in Ref. 1; AAC51102)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="P -> R (in Ref. 3; BAA24075)"
FT /evidence="ECO:0000305"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6GMH"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:6GMH"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:6GMH"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:6GMH"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:6GMH"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:2E6Z"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:2E6Z"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:6TED"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:6GMH"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 555..562
FT /evidence="ECO:0007829|PDB:5OHO"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:6EQY"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:5OHO"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:5OHO"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:6EQY"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:5OHO"
FT TURN 606..609
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 611..617
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 619..625
FT /evidence="ECO:0007829|PDB:5OHO"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 635..639
FT /evidence="ECO:0007829|PDB:5OHO"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:5OHO"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:5OHO"
FT TURN 704..707
FT /evidence="ECO:0007829|PDB:7OL0"
FT STRAND 709..712
FT /evidence="ECO:0007829|PDB:7OL0"
FT TURN 716..719
FT /evidence="ECO:0007829|PDB:7OL0"
FT STRAND 721..727
FT /evidence="ECO:0007829|PDB:7OL0"
FT STRAND 729..740
FT /evidence="ECO:0007829|PDB:7OL0"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:7OL0"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:7OL0"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:7OL0"
FT STRAND 984..988
FT /evidence="ECO:0007829|PDB:5OHQ"
FT TURN 995..999
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1001..1008
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1011..1016
FT /evidence="ECO:0007829|PDB:5OHQ"
FT TURN 1017..1020
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1021..1026
FT /evidence="ECO:0007829|PDB:5OHQ"
FT HELIX 1027..1029
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1030..1032
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1040..1043
FT /evidence="ECO:0007829|PDB:5OHQ"
FT TURN 1047..1050
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1052..1059
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1062..1067
FT /evidence="ECO:0007829|PDB:5OHQ"
FT TURN 1068..1070
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1073..1077
FT /evidence="ECO:0007829|PDB:5OHQ"
FT HELIX 1078..1080
FT /evidence="ECO:0007829|PDB:5OHQ"
FT STRAND 1081..1084
FT /evidence="ECO:0007829|PDB:5OHQ"
SQ SEQUENCE 1087 AA; 121000 MW; EC3F402A670A5B7D CRC64;
MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE
EDDDRPPKKP RHGGFILDEA DVDDEYEDED QWEDGAEDIL EKEEIEASNI DNVVLDEDRS
GARRLQNLWR DQREEELGEY YMKKYAKSSV GETVYGGSDE LSDDITQQQL LPGVKDPNLW
TVKCKIGEER ATAISLMRKF IAYQFTDTPL QIKSVVAPEH VKGYIYVEAY KQTHVKQAIE
GVGNLRLGYW NQQMVPIKEM TDVLKVVKEV ANLKPKSWVR LKRGIYKDDI AQVDYVEPSQ
NTISLKMIPR IDYDRIKARM SLKDWFAKRK KFKRPPQRLF DAEKIRSLGG DVASDGDFLI
FEGNRYSRKG FLFKSFAMSA VITEGVKPTL SELEKFEDQP EGIDLEVVTE STGKEREHNF
QPGDNVEVCE GELINLQGKI LSVDGNKITI MPKHEDLKDM LEFPAQELRK YFKMGDHVKV
IAGRFEGDTG LIVRVEENFV ILFSDLTMHE LKVLPRDLQL CSETASGVDV GGQHEWGELV
QLDPQTVGVI VRLERETFQV LNMYGKVVTV RHQAVTRKKD NRFAVALDSE QNNIHVKDIV
KVIDGPHSGR EGEIRHLFRS FAFLHCKKLV ENGGMFVCKT RHLVLAGGSK PRDVTNFTVG
GFAPMSPRIS SPMHPSAGGQ RGGFGSPGGG SGGMSRGRGR RDNELIGQTV RISQGPYKGY
IGVVKDATES TARVELHSTC QTISVDRQRL TTVGSRRPGG MTSTYGRTPM YGSQTPMYGS
GSRTPMYGSQ TPLQDGSRTP HYGSQTPLHD GSRTPAQSGA WDPNNPNTPS RAEEEYEYAF
DDEPTPSPQA YGGTPNPQTP GYPDPSSPQV NPQYNPQTPG TPAMYNTDQF SPYAAPSPQG
SYQPSPSPQS YHQVAPSPAG YQNTHSPASY HPTPSPMAYQ ASPSPSPVGY SPMTPGAPSP
GGYNPHTPGS GIEQNSSDWV TTDIQVKVRD TYLDTQVVGQ TGVIRSVTGG MCSVYLKDSE
KVVSISSEHL EPITPTKNNK VKVILGEDRE ATGVLLSIDG EDGIVRMDLD EQLKILNLRF
LGKLLEA
