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UniProtKB/Swiss-Prot entry O00267

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SPT5H_HUMAN
Primary accession number O00267
Secondary accession numbers O43279 Q59G52 Q99639
Integrated into Swiss-Prot on November 22, 2005
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 73)
Name and origin of the protein
Protein name Transcription elongation factor SPT5
Synonyms hSPT5
DRB sensitivity-inducing factor large subunit
DSIF large subunit
DSIF p160
Tat-cotransactivator 1 protein
Tat-CT1 protein
Gene name
Name: SUPT5H
Synonyms: SPT5, SPT5H
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
DOI=10.1006/geno.1996.0646; PubMed=8975720 [NCBI, ExPASy, EBI, Israel, Japan]
Chiang P.-W., Fogel E., Jackson C.L., Lieuallen K., Lennon G., Qu X., Wang S.-Q., Kurnit D.M.;
"Isolation, sequencing, and mapping of the human homologue of the yeast transcription factor, SPT5.";
Genomics 38:421-424(1996).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 116-152; 288-319; 461-471; 529-542; 580-587; 746-761; 795-809; 841-885; 888-922 AND 1068-1087, DOMAINS CTR1 AND CTR2, AND PHOSPHORYLATION.
DOI=10.1016/S0014-5793(97)00486-9; PubMed=9199507 [NCBI, ExPASy, EBI, Israel, Japan]
Stachora A.A., Schaefer R.E., Pohlmeier M., Maier G., Ponstingl H.;
"Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosis.";
FEBS Lett. 409:74-78(1997).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 277-282; 324-328; 459-470 AND 580-597, FUNCTION, AND INTERACTION WITH SUPT4H1 AND RNA POLYMERASE II.
PubMed=9450929 [NCBI, ExPASy, EBI, Israel, Japan]
Wada T., Takagi T., Yamaguchi Y., Ferdous A., Imai T., Hirose S., Sugimoto S., Yano K., Hartzog G.A., Winston F., Buratowski S., Handa H.;
"DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs.";
Genes Dev. 12:343-356(1998).
[4]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 199-213; 247-258 AND 799-811, AND FUNCTION.
DOI=10.1006/jmbi.1997.1601; PubMed=9514752 [NCBI, ExPASy, EBI, Israel, Japan]
Wu-Baer F., Lane W.S., Gaynor R.B.;
"Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation.";
J. Mol. Biol. 277:179-197(1998).
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
 FUNCTION, AND INTERACTION WITH RNA POLYMERASE II.
DOI=10.1093/emboj/17.24.7395; PubMed=9857195 [NCBI, ExPASy, EBI, Israel, Japan]
Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.;
"Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro.";
EMBO J. 17:7395-7403(1998).
[8]
 FUNCTION, AND INTERACTION WITH THE NELF COMPLEX.
DOI=10.1016/S0092-8674(00)80713-8; PubMed=10199401 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S., Hasegawa J., Handa H.;
"NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation.";
Cell 97:41-51(1999).
[9]
 FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH NCL; CCNT1; RNA POL II; HTATSF1 AND CDK9.
DOI=10.1093/emboj/18.13.3688; PubMed=10393184 [NCBI, ExPASy, EBI, Israel, Japan]
Parada C.A., Roeder R.G.;
"A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription.";
EMBO J. 18:3688-3701(1999).
[10]
 FUNCTION, AND INTERACTION WITH RNGTT.
PubMed=10421630 [NCBI, ExPASy, EBI, Israel, Japan]
Wen Y., Shatkin A.J.;
"Transcription elongation factor hSPT5 stimulates mRNA capping.";
Genes Dev. 13:1774-1779(1999).
[11]
 FUNCTION, INTERACTION WITH RNA POLYMERASE II AND SUPT4H1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.274.12.8085; PubMed=10075709 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi Y., Wada T., Watanabe D., Takagi T., Hasegawa J., Handa H.;
"Structure and function of the human transcription elongation factor DSIF.";
J. Biol. Chem. 274:8085-8092(1999).
[12]
 FUNCTION, AND INTERACTION WITH HTATSF1 AND RNA POLYMERASE II.
PubMed=10454543 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.;
"Tat-SF1 protein associates with RAP30 and human SPT5 proteins.";
Mol. Cell. Biol. 19:5960-5968(1999).
[13]
 FUNCTION.
DOI=10.1016/S1097-2765(00)80272-5; PubMed=10912001 [NCBI, ExPASy, EBI, Israel, Japan]
Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.;
"FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH.";
Mol. Cell 5:1067-1072(2000).
[14]
 FUNCTION, INTERACTION WITH RNA POLYMERASE II AND SUPT4H1, AND PHOSPHORYLATION AT THR-775 AND THR-784.
DOI=10.1128/MCB.20.9.2970-2983.2000; PubMed=10757782 [NCBI, ExPASy, EBI, Israel, Japan]
Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.;
"Domains in the SPT5 protein that modulate its transcriptional regulatory properties.";
Mol. Cell. Biol. 20:2970-2983(2000).
[15]
 PHOSPHORYLATION BY CDK9.
DOI=10.1074/jbc.M010908200; PubMed=11145967 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.B., Sharp P.A.;
"Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase.";
J. Biol. Chem. 276:12317-12323(2001).
[16]
 FUNCTION, AND PHOSPHORYLATION BY CDK9.
DOI=10.1074/jbc.M006130200; PubMed=11112772 [NCBI, ExPASy, EBI, Israel, Japan]
Ping Y.-H., Rana T.M.;
"DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation.";
J. Biol. Chem. 276:12951-12958(2001).
[17]
 FUNCTION.
DOI=10.1074/jbc.M104967200; PubMed=11553615 [NCBI, ExPASy, EBI, Israel, Japan]
Renner D.B., Yamaguchi Y., Wada T., Handa H., Price D.H.;
"A highly purified RNA polymerase II elongation control system.";
J. Biol. Chem. 276:42601-42609(2001).
[18]
 INTERACTION WITH PIN1, AND PHOSPHORYLATION.
DOI=10.1006/jmbi.2001.4991; PubMed=11575923 [NCBI, ExPASy, EBI, Israel, Japan]
Lavoie S.B., Albert A.L., Handa H., Vincent M., Bensaude O.;
"The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9.";
J. Mol. Biol. 312:675-685(2001).
[19]
 FUNCTION, AND PHOSPHORYLATION BY CDK9.
DOI=10.1128/MCB.22.4.1079-1093.2002; PubMed=11809800 [NCBI, ExPASy, EBI, Israel, Japan]
Bourgeois C.F., Kim Y.K., Churcher M.J., West M.J., Karn J.;
"Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences.";
Mol. Cell. Biol. 22:1079-1093(2002).
[20]
 INTERACTION WITH THE NELF COMPLEX.
DOI=10.1128/MCB.22.9.2918-2927.2002; PubMed=11940650 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi Y., Inukai N., Narita T., Wada T., Handa H.;
"Evidence that negative elongation factor represses transcription elongation through binding to a DRB sensitivity-inducing factor/RNA polymerase II complex and RNA.";
Mol. Cell. Biol. 22:2918-2927(2002).
[21]
 FUNCTION, AND INTERACTION WITH SUPT4H1.
DOI=10.1046/j.1365-2443.2003.00638.x; PubMed=12653964 [NCBI, ExPASy, EBI, Israel, Japan]
Kim D.-K., Inukai N., Yamada T., Furuya A., Sato H., Yamaguchi Y., Wada T., Handa H.;
"Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex.";
Genes Cells 8:371-378(2003).
[22]
 FUNCTION, INTERACTION WITH CDK9; PRMT1; RNA POLYMERASE II; PRMT5 AND SUPT4H1, METHYLATION AT ARG-681; ARG-696 AND ARG-698, AND MUTAGENESIS OF ARG-681; ARG-696 AND ARG-698.
DOI=10.1016/S1097-2765(03)00101-1; PubMed=12718890 [NCBI, ExPASy, EBI, Israel, Japan]
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.;
"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties.";
Mol. Cell 11:1055-1066(2003).
[23]
 INTERACTION WITH THE NELF COMPLEX.
DOI=10.1128/MCB.23.6.1863-1873.2003; PubMed=12612062 [NCBI, ExPASy, EBI, Israel, Japan]
Narita T., Yamaguchi Y., Yano K., Sugimoto S., Chanarat S., Wada T., Kim D.-K., Hasegawa J., Omori M., Inukai N., Endoh M., Yamada T., Handa H.;
"Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex.";
Mol. Cell. Biol. 23:1863-1873(2003).
[24]
 FUNCTION, AND MUTAGENESIS OF GLY-1002.
DOI=10.1016/j.cub.2004.08.066; PubMed=15380072 [NCBI, ExPASy, EBI, Israel, Japan]
Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H., Ish-Horowicz D.;
"Locus-specific requirements for Spt5 in transcriptional activation and repression in Drosophila.";
Curr. Biol. 14:1680-1684(2004).
[25]
 PHOSPHORYLATION BY CDK9.
DOI=10.1128/JVI.78.24.13522-13533.2004; PubMed=15564463 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou M., Deng L., Lacoste V., Park H.U., Pumfery A., Kashanchi F., Brady J.N., Kumar A.;
"Coordination of transcription factor phosphorylation and histone methylation by the P-TEFb kinase during human immunodeficiency virus type 1 transcription.";
J. Virol. 78:13522-13533(2004).
[26]
 FUNCTION.
DOI=10.1128/MCB.24.2.787-795.2004; PubMed=14701750 [NCBI, ExPASy, EBI, Israel, Japan]
Fujinaga K., Irwin D., Huang Y., Taube R., Kurosu T., Peterlin B.M.;
"Dynamics of human immunodeficiency virus transcription: P-TEFb phosphorylates RD and dissociates negative effectors from the transactivation response element.";
Mol. Cell. Biol. 24:787-795(2004).
[27]
 INTERACTION WITH RNA POLYMERASE II; SUPT4H1 AND SUPT6H.
DOI=10.1128/MCB.24.8.3324-3336.2004; PubMed=15060154 [NCBI, ExPASy, EBI, Israel, Japan]
Endoh M., Zhu W., Hasegawa J., Watanabe H., Kim D.-K., Aida M., Inukai N., Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., Mandal S.S., Reinberg D., Wada T., Handa H.;
"Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro.";
Mol. Cell. Biol. 24:3324-3336(2004).
[28]
 FUNCTION.
DOI=10.1073/pnas.0401493101; PubMed=15136722 [NCBI, ExPASy, EBI, Israel, Japan]
Mandal S.S., Chu C., Wada T., Handa H., Shatkin A.J., Reinberg D.;
"Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II.";
Proc. Natl. Acad. Sci. U.S.A. 101:7572-7577(2004).
[29]
 FUNCTION.
DOI=10.1073/pnas.0409405102; PubMed=16214896 [NCBI, ExPASy, EBI, Israel, Japan]
Palangat M., Renner D.B., Price D.H., Landick R.;
"A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS.";
Proc. Natl. Acad. Sci. U.S.A. 102:15036-15041(2005).
[30]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[31]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-709; TYR-717 AND THR-1034, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[32]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[33]
 STRUCTURE BY NMR OF 420-757.
RIKEN structural genomics initiative (RSGI);
"Solution structure of KOW motifs of human transcription elongation factor SPT5.";
Submitted (JUL-2007) to the PDB data bank.
Comments
  • FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.
  • SUBUNIT: Interacts with SUPT4H1 to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. DSIF also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin.
  • INTERACTION:
    P24928:POLR2A; NbExp=2; IntAct=EBI-710464, EBI-295301;
    P62937:PPIA; NbExp=1; IntAct=EBI-710464, EBI-437708;
    P63272:SUPT4H1; NbExp=3; IntAct=EBI-710464, EBI-727250;
  • SUBCELLULAR LOCATION: Nucleus.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO00267-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDO00267-2
    Features which should be applied to build the isoform sequence: VSP_016282.
  • TISSUE SPECIFICITY: Ubiquitously expressed.
  • PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II.
  • PTM: Phosphorylated. Phosphorylation by P-TEFb alleviates transcriptional pausing and can stimulate transcriptional elongation from the HIV-1 LTR. P-TEFb dependent phosphorylation is stimulated by the HIV-1 Tat protein. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis.
  • SIMILARITY: Belongs to the SPT5 family.
  • SIMILARITY: Contains 5 KOW domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U56402; AAC51102.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y12790; CAA73326.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB000516; BAA24075.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF040253; AAD02179.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209257; BAD92494.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024203; AAH24203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001104490.1; -.
NP_001124296.1; -.
NP_001124297.1; -.
NP_003160.2; -.
UniGene Hs.631604
3D structure databases
PDB
2DO3; NMR; -; A=462-523.[ExPASy / RCSB / EBI]
2E6Z; NMR; -; A=420-471.[ExPASy / RCSB / EBI]
2E70; NMR; -; A=690-757.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2DO3; -.
2E6Z; -.
2E70; -.
ModBase O00267.
Protein-protein interaction databases
DIP DIP:29014N; -.
IntAct O00267; -.
PTM databases
PhosphoSite O00267; -.
Enzyme and pathway databases
Reactome REACT_1788; Transcription.
REACT_1892; Elongation arrest and recovery.
REACT_6143; Pausing and recovery of Tat-mediated HIV-1 elongation.
REACT_6185; HIV Infection.
REACT_6244; Pausing and recovery of HIV-1 elongation.
REACT_6259; HIV-1 elongation arrest and recovery.
REACT_6344; Tat-mediated HIV-1 elongation arrest and recovery.
REACT_71; Gene Expression.
REACT_769; Pausing and recovery of elongation.
Organism-specific databases
H-InvDB HIX0015120; -.
HGNC HGNC:11469; SUPT5H.
GenAtlas SUPT5H.
MIM 602102; gene. [NCBI / EBI]
PharmGKB PA36255; -.
GeneCards O00267.
Gene expression databases
ArrayExpress O00267; -.
CleanEx HS_SUPT5H; -.
GermOnline ENSG00000196235; Homo sapiens.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0019899; Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0008148; Molecular function: negative transcription elongation factor activity (inferred from direct assay from UniProtKB).
GO:0008159; Molecular function: positive transcription elongation factor activity (inferred from direct assay from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0007049; Biological process: cell cycle (non-traceable author statement from UniProtKB).
GO:0006338; Biological process: chromatin remodeling (non-traceable author statement from UniProtKB).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0032968; Biological process: positive regulation of RNA elongation from RNA polymerase II promoter (inferred from electronic annotation from InterPro).
GO:0045944; Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0010033; Biological process: response to organic substance (traceable author statement from UniProtKB).
GO:0045090; Biological process: retroviral genome replication (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR005824; KOW.
IPR005100; Supt5.
IPR017071; TF_Spt5.
IPR006645; Transcrpt_antiterm_NusG_N.
Graphical view of domain structure.
Pfam PF00467; KOW; 2.
PF03439; Supt5; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF036945; Spt5; 1.
ProDom PD005267; Ribosomal_NusG; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00739; KOW; 6.
SM00738; NGN; 1.
SMART graphical view of domain structure.
BLOCKS O00267.
ProtoNet O00267.
Genome annotation databases
Ensembl ENSG00000196235; Homo sapiens. [Contig view]
GeneID 6829; -.
KEGG hsa:6829; -.
Phylogenomic databases
HOVERGEN O00267; -.
Other
NextBio 26663; -.
SOURCE SUPT5H; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Alternative splicing; Direct protein sequencing; Methylation; Nucleus; Phosphoprotein; Repeat; Repressor; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1087  1087     Transcription elongation factor SPT5. PRO_0000208468
DOMAIN   273    306  34     KOW 1. 
DOMAIN   420    451  32     KOW 2. 
DOMAIN   472    503  32     KOW 3. 
DOMAIN   594    627  34     KOW 4. 
DOMAIN   704    737  34     KOW 5. 
REPEAT   754    759  6     CTR1-1; approximate. 
REPEAT   760    765  6     CTR1-2. 
REPEAT   766    771  6     CTR1-3. 
REPEAT   772    778  7     CTR1-4. 
REPEAT   781    787  7     CTR1-5. 
REPEAT   788    794  7     CTR1-6. 
REPEAT   796    802  7     CTR1-7. 
REPEAT   803    809  7     CTR1-8. 
REPEAT   811    817  7     CTR1-9. 
REPEAT   844    851  8     CTR2-1. 
REPEAT   854    862  9     CTR2-2; approximate. 
REPEAT   863    869  7     CTR2-3; approximate. 
REPEAT   881    885  5     CTR2-4; half-length. 
REPEAT   896    902  7     CTR2-5; approximate. 
REPEAT   904    911  8     CTR2-6. 
REPEAT   916    921  6     CTR2-7; approximate. 
REPEAT   924    930  7     CTR2-8. 
REPEAT   932    939  8     CTR2-9. 
REPEAT   943    950  8     CTR2-10. 
REGION   176    270  95     Interaction with SUPT4H1. 
REGION   313    420  108     Interaction with RNA polymerase II. 
REGION   754    817  64     9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1. 
REGION   844    950  107     10 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2. 
COMPBIAS   11    106  96     Glu-rich. 
COMPBIAS   844    968  125     Pro-rich. 
MOD_RES   666    666        Phosphoserine. 
MOD_RES   681    681        Asymmetric dimethylarginine; by PRMT1; alternate. 
MOD_RES   681    681        Omega-N-methylarginine; by PRMT1; alternate. 
MOD_RES   696    696        Asymmetric dimethylarginine; by PRMT1; alternate. 
MOD_RES   696    696        Omega-N-methylarginine; by PRMT1; alternate. 
MOD_RES   698    698        Asymmetric dimethylarginine; by PRMT1; alternate. 
MOD_RES   698    698        Omega-N-methylarginine; by PRMT1 and PRMT5; alternate. 
MOD_RES   698    698        Symmetric dimethylarginine; by PRMT5; alternate. 
MOD_RES   709    709        Phosphothreonine. 
MOD_RES   717    717        Phosphotyrosine. 
MOD_RES   775    775        Phosphothreonine; by CDK9. 
MOD_RES   784    784        Phosphothreonine; by CDK9. 
MOD_RES   1034   1034        Phosphothreonine. 
VAR_SEQ   103    106        Missing (in isoform 2). VSP_016282
MUTAGEN   681    681        R->A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698. 
MUTAGEN   681    681        R->K: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698. 
MUTAGEN   696    696        R->A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698. 
MUTAGEN   696    696        R->K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698. 
MUTAGEN   698    698        R->A: Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696. 
MUTAGEN   698    698        R->K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696. 
MUTAGEN   1002   1002        G->D: Defective in regulation of transcriptional elongation. 
CONFLICT   181    181        T -> I (in Ref. 1; AAC51102). 
CONFLICT   483    483        G -> A (in Ref. 1; AAC51102). 
CONFLICT   820    820    </