ID SPT6H_HUMAN Reviewed; 1726 AA. AC Q7KZ85; A7E2B4; Q15737; Q6GMQ4; Q7KYW9; Q7LDK4; Q8N526; Q92775; AC Q96AH3; Q9BTH9; Q9BTI2; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 2. DT 12-APR-2017, entry version 136. DE RecName: Full=Transcription elongation factor SPT6; DE Short=hSPT6; DE AltName: Full=Histone chaperone suppressor of Ty6; DE AltName: Full=Tat-cotransactivator 2 protein; DE Short=Tat-CT2 protein; GN Name=SUPT6H; Synonyms=KIAA0162, SPT6H; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8786132; DOI=10.1006/geno.1996.0294; RA Chiang P.-W., Wang S., Smithivas P., Song W.-J., Ramamoorthy S., RA Hillman J., Puett S., Van Keuren M.L., Crombez E., Kumar A., RA Glover T.W., Miller D.E., Tsai C.-H., Blackburn C.C., Chen X.-N., RA Sun Z., Cheng J.-F., Korenberg J.R., Kurnit D.M.; RT "Identification and analysis of the human and murine putative RT chromatin structure regulator SUPT6H and Supt6h."; RL Genomics 34:328-333(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Cervix, Lung, Melanoma, Placenta, and Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1460-1726 (ISOFORMS 1/2). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP 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 RT HIV-1 Tat-activation."; RL J. Mol. Biol. 277:179-197(1998). RN [7] RP INTERACTION WITH HISTONE H2B; H3 AND HHV-5 PROTEIN UL69. RX PubMed=10933715; DOI=10.1128/JVI.74.17.8053-8064.2000; RA Winkler M., aus Dem Siepen T., Stamminger T.; RT "Functional interaction between pleiotropic transactivator pUL69 of RT human cytomegalovirus and the human homolog of yeast chromatin RT regulatory protein SPT6."; RL J. Virol. 74:8053-8064(2000). RN [8] RP FUNCTION, AND INTERACTION WITH THE DSIF COMPLEX AND RNA POLYMERASE II. 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., RA Inukai N., Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., RA Mandal S.S., Reinberg D., Wada T., Handa H.; RT "Human Spt6 stimulates transcription elongation by RNA polymerase II RT in vitro."; RL Mol. Cell. Biol. 24:3324-3336(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION RP BY 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP FUNCTION, AND INTERACTION WITH POLR2A. RX PubMed=17234882; DOI=10.1101/gad.1503107; RA Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.; RT "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA RT splicing and export."; RL Genes Dev. 21:160-174(2007). RN [11] RP INTERACTION WITH IWS1. RX PubMed=19141475; DOI=10.1101/gad.1720008; RA Yoh S.M., Lucas J.S., Jones K.A.; RT "The Iws1:Spt6:CTD complex controls cotranscriptional mRNA RT biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation."; RL Genes Dev. 22:3422-3434(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1535; THR-1539 AND RP THR-1718, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-1523; SER-1535; RP THR-1539; SER-1701; SER-1703 AND THR-1718, AND IDENTIFICATION BY MASS RP 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; THR-1532; SER-1535; RP THR-1539; THR-1697; SER-1701; SER-1703 AND THR-1718, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-743 AND LYS-1676, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; THR-1523; THR-1532; RP SER-1701; SER-1703 AND THR-1718, AND IDENTIFICATION BY MASS RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] 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., RA Buerckstuemmer T., 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 [19] RP REVIEW. RX PubMed=22567361; DOI=10.4061/2011/625210; RA Duina A.A.; RT "Histone chaperones Spt6 and FACT: Similarities and differences in RT modes of action at transcribed genes."; RL Genet. Res. Int. 2011:625210-625210(2011). RN [20] RP INTERACTION WITH AICDA. RX PubMed=21518874; DOI=10.1073/pnas.1104423108; RA Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S., RA Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T., RA Iemura S., Honjo T.; RT "Histone chaperone Spt6 is required for class switch recombination but RT not somatic hypermutation."; RL Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-7; SER-12; SER-125 AND SER-1535, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP INTERACTION WITH HHV-5 PROTEIN UL69. RX PubMed=22171252; DOI=10.1128/JVI.06776-11; RA Cygnar D., Hagemeier S., Kronemann D., Bresnahan W.A.; RT "The cellular protein SPT6 is required for efficient replication of RT human cytomegalovirus."; RL J. Virol. 86:2011-2020(2012). RN [23] RP FUNCTION, AND INTERACTION WITH PAAF1. RX PubMed=22316138; DOI=10.1186/1742-4690-9-13; RA Nakamura M., Basavarajaiah P., Rousset E., Beraud C., Latreille D., RA Henaoui I.S., Lassot I., Mari B., Kiernan R.; RT "Spt6 levels are modulated by PAAF1 and proteasome to regulate the RT HIV-1 LTR."; RL Retrovirology 9:13-13(2012). RN [24] RP FUNCTION. RX PubMed=23503590; DOI=10.1038/emboj.2013.54; RA Wang A.H., Zare H., Mousavi K., Wang C., Moravec C.E., Sirotkin H.I., RA Ge K., Gutierrez-Cruz G., Sartorelli V.; RT "The histone chaperone Spt6 coordinates histone H3K27 demethylation RT and myogenesis."; RL EMBO J. 32:1075-1086(2013). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; THR-1523; SER-1526; RP SER-1528 AND SER-1535, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND TYR-1515, AND 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Transcription elongation factor which binds histone H3 CC and plays a key role in the regulation of transcription elongation CC and mRNA processing. Enhances the transcription elongation by RNA CC polymerase II (RNAPII) and is also required for the efficient CC activation of transcriptional elongation by the HIV-1 nuclear CC transcriptional activator, Tat. Besides chaperoning histones in CC transcription, acts to transport and splice mRNA by forming a CC complex with IWS1 and the C-terminal domain (CTD) of the RNAPII CC subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA CC export factors (ALYREF/THOC4, EXOSC10) as well as histone CC modifying enzymes (such as SETD2), to ensure proper mRNA splicing, CC efficient mRNA export and elongation-coupled H3K36 methylation, a CC signature chromatin mark of active transcription. SUPT6H via its CC association with SETD1A, regulates both class-switch recombination CC and somatic hypermutation through formation of H3K4me3 epigenetic CC marks on activation-induced cytidine deaminase (AICDA) target CC loci. Promotes the activation of the myogenic gene program by CC entailing erasure of the repressive H3K27me3 epigenetic mark CC through stabilization of the chromatin interaction of the H3K27 CC demethylase KDM6A. {ECO:0000269|PubMed:15060154, CC ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:22316138, CC ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:9514752}. CC -!- SUBUNIT: Interacts with RNA polymerase II and the DRB sensitivity- CC inducing factor complex (DSIF complex), which is composed of CC SUPT5H and SUPT4H1. Interacts with human cytomegalovirus/HHV-5 CC protein UL69. Interacts with KDM6A (By similarity). Interacts (via CC SH2 domain) with SETD1A (By similarity). Interacts (via SH2 CC domain) with POLR2A phosphorylated at 'Ser-2'. Interacts with CC IWS1, AICDA and PAAF1. Interacts with histone H2B and H3. CC {ECO:0000250, ECO:0000269|PubMed:10933715, CC ECO:0000269|PubMed:15060154, ECO:0000269|PubMed:17234882, CC ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:21518874, CC ECO:0000269|PubMed:22171252, ECO:0000269|PubMed:22316138}. CC -!- INTERACTION: CC P04626:ERBB2; NbExp=2; IntAct=EBI-2515547, EBI-641062; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q7KZ85-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7KZ85-2; Sequence=VSP_011505, VSP_011506; CC Name=3; CC IsoId=Q7KZ85-3; Sequence=VSP_011507; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB18949.1; Type=Frameshift; Positions=988; Evidence={ECO:0000305}; CC Sequence=AAC50821.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAH33074.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAA11479.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U38623; AAC99996.1; -; mRNA. DR EMBL; U38658; AAB18949.1; ALT_FRAME; mRNA. DR EMBL; U46691; AAC50821.1; ALT_INIT; mRNA. DR EMBL; D79984; BAA11479.2; ALT_INIT; mRNA. DR EMBL; CH471159; EAW51117.1; -; Genomic_DNA. DR EMBL; BC003692; AAH03692.1; -; mRNA. DR EMBL; BC003696; AAH03696.1; -; mRNA. DR EMBL; BC017105; AAH17105.1; -; mRNA. DR EMBL; BC033074; AAH33074.1; ALT_INIT; mRNA. DR EMBL; BC073963; AAH73963.1; -; mRNA. DR EMBL; BC136522; AAI36523.1; -; mRNA. DR EMBL; BC136524; AAI36525.1; -; mRNA. DR EMBL; BC150268; AAI50269.1; -; mRNA. DR EMBL; AF070532; AAC28631.1; -; mRNA. DR CCDS; CCDS32596.1; -. [Q7KZ85-1] DR RefSeq; NP_001307684.1; NM_001320755.1. [Q7KZ85-1] DR RefSeq; NP_003161.2; NM_003170.4. [Q7KZ85-1] DR RefSeq; XP_016880467.1; XM_017024978.1. [Q7KZ85-1] DR RefSeq; XP_016880468.1; XM_017024979.1. [Q7KZ85-1] DR RefSeq; XP_016880469.1; XM_017024980.1. DR UniGene; Hs.250429; -. DR UniGene; Hs.735114; -. DR ProteinModelPortal; Q7KZ85; -. DR SMR; Q7KZ85; -. DR BioGrid; 112698; 75. DR DIP; DIP-42615N; -. DR IntAct; Q7KZ85; 30. DR MINT; MINT-1491202; -. DR STRING; 9606.ENSP00000319104; -. DR iPTMnet; Q7KZ85; -. DR PhosphoSitePlus; Q7KZ85; -. DR BioMuta; SUPT6H; -. DR DMDM; 51701986; -. DR EPD; Q7KZ85; -. DR MaxQB; Q7KZ85; -. DR PaxDb; Q7KZ85; -. DR PeptideAtlas; Q7KZ85; -. DR PRIDE; Q7KZ85; -. DR Ensembl; ENST00000314616; ENSP00000319104; ENSG00000109111. [Q7KZ85-1] DR Ensembl; ENST00000347486; ENSP00000338143; ENSG00000109111. [Q7KZ85-1] DR GeneID; 6830; -. DR KEGG; hsa:6830; -. DR UCSC; uc002hby.4; human. [Q7KZ85-1] DR CTD; 6830; -. DR GeneCards; SUPT6H; -. DR HGNC; HGNC:11470; SUPT6H. DR HPA; CAB012416; -. DR HPA; HPA036382; -. DR MIM; 601333; gene. DR neXtProt; NX_Q7KZ85; -. DR OpenTargets; ENSG00000109111; -. DR PharmGKB; PA36256; -. DR eggNOG; KOG1856; Eukaryota. DR eggNOG; COG2183; LUCA. DR GeneTree; ENSGT00510000047446; -. DR HOVERGEN; HBG093994; -. DR InParanoid; Q7KZ85; -. DR KO; K11292; -. DR OMA; HEANEMD; -. DR OrthoDB; EOG091G00SW; -. DR PhylomeDB; Q7KZ85; -. DR TreeFam; TF105956; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-112387; Elongation arrest and recovery. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR SignaLink; Q7KZ85; -. DR ChiTaRS; SUPT6H; human. DR GeneWiki; SUPT6H; -. DR GenomeRNAi; 6830; -. DR PMAP-CutDB; Q7KZ85; -. DR PRO; PR:Q7KZ85; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000109111; -. DR ExpressionAtlas; Q7KZ85; baseline and differential. DR Genevisible; Q7KZ85; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central. DR GO; GO:0035327; C:transcriptionally active chromatin; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0000991; F:transcription factor activity, core RNA polymerase II binding; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc. DR GO; GO:0070827; P:chromatin maintenance; IBA:GO_Central. DR GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB. DR GO; GO:0006342; P:chromatin silencing; IBA:GO_Central. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB. DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central. DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB. DR GO; GO:0045191; P:regulation of isotype switching; ISS:UniProtKB. DR GO; GO:0010793; P:regulation of mRNA export from nucleus; ISS:UniProtKB. DR GO; GO:0050684; P:regulation of mRNA processing; ISS:UniProtKB. DR GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.650; -; 1. DR Gene3D; 1.10.150.310; -; 1. DR Gene3D; 1.10.3500.10; -; 1. DR Gene3D; 3.30.420.140; -; 1. DR Gene3D; 3.30.505.10; -; 2. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR000980; SH2. DR InterPro; IPR028083; Spt6_acidic_N_dom. DR InterPro; IPR027999; Spt6_dom. DR InterPro; IPR032706; Spt6_HHH. DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom. DR InterPro; IPR028231; Spt6_YqgF. DR InterPro; IPR023323; Tex-like_dom. DR InterPro; IPR023319; Tex-like_HTH_dom. DR InterPro; IPR023097; Tex_RuvX-like_dom. DR InterPro; IPR017072; TF_Spt6. DR InterPro; IPR006641; YqgF/RNaseH-like_dom. DR PANTHER; PTHR10145:SF7; PTHR10145:SF7; 1. DR Pfam; PF14878; DLD; 1. DR Pfam; PF14635; HHH_7; 1. DR Pfam; PF14641; HTH_44; 1. DR Pfam; PF00575; S1; 1. DR Pfam; PF14633; SH2_2; 1. DR Pfam; PF14632; SPT6_acidic; 1. DR Pfam; PF14639; YqgF; 1. DR PIRSF; PIRSF036947; Spt6; 1. DR SMART; SM00316; S1; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00732; YqgFc; 1. DR SUPFAM; SSF47781; SSF47781; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR SUPFAM; SSF55550; SSF55550; 1. DR PROSITE; PS50126; S1; 1. DR PROSITE; PS50001; SH2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chaperone; Complete proteome; KW Host-virus interaction; mRNA processing; mRNA splicing; KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Transport. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:21406692}. FT CHAIN 2 1726 Transcription elongation factor SPT6. FT /FTId=PRO_0000072171. FT DOMAIN 1213 1282 S1 motif. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 1325 1431 SH2. {ECO:0000255|PROSITE- FT ProRule:PRU00191}. FT REGION 2 916 Interaction with PAAF1. FT {ECO:0000269|PubMed:22316138}. FT REGION 2 485 Interaction with IWS1. {ECO:0000250}. FT REGION 317 1300 Interaction with KDM6A. {ECO:0000250}. FT REGION 1633 1726 Interaction with histone H2B and H3. FT {ECO:0000269|PubMed:10933715}. FT COMPBIAS 6 250 Asp/Glu-rich. FT COMPBIAS 1525 1528 Poly-Ser. FT COMPBIAS 1654 1657 Poly-Ser. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 7 7 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 12 12 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 73 73 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 78 78 Phosphoserine. FT {ECO:0000250|UniProtKB:Q62383}. FT MOD_RES 91 91 Phosphoserine. FT {ECO:0000250|UniProtKB:Q62383}. FT MOD_RES 125 125 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 267 267 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 743 743 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 1515 1515 Phosphotyrosine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 1523 1523 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1526 1526 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1528 1528 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 1532 1532 Phosphothreonine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1535 1535 Phosphoserine. FT {ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 1539 1539 Phosphothreonine. FT {ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332}. FT MOD_RES 1676 1676 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 1697 1697 Phosphothreonine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 1701 1701 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1703 1703 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1709 1709 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q62383}. FT MOD_RES 1718 1718 Phosphothreonine. FT {ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT VAR_SEQ 1 1181 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_011505. FT VAR_SEQ 617 1616 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_011507. FT VAR_SEQ 1182 1211 ESYDQAIRNDETGLWQCPFCQQDNFPELSE -> MPSRGTR FT PEDSSVLIPTDNSTPHKEDLSSK (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_011506. FT CONFLICT 61 73 DDDEDEGEEDEGS -> ATAPGHPKLSEGR (in Ref. FT 1; AAC50821). {ECO:0000305}. FT CONFLICT 100 109 DFDLIEENLG -> LEDDDFLLNE (in Ref. 4; FT AAH33074). {ECO:0000305}. FT CONFLICT 988 994 YVCGLGP -> VCLWPGT (in Ref. 1; AAB18949). FT {ECO:0000305}. FT CONFLICT 1545 1545 L -> P (in Ref. 4; AAH17105). FT {ECO:0000305}. FT CONFLICT 1627 1627 S -> I (in Ref. 4; AAH17105). FT {ECO:0000305}. SQ SEQUENCE 1726 AA; 199073 MW; F7EB22FA669EB030 CRC64; MSDFVESEAE ESEEEYNDEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE QGNLKGFIND DDDEDEGEED EGSDSGDSED DVGHKKRKRT SFDDRLEDDD FDLIEENLGV KVKRGQKYRR VKKMSDDEDD DEEEYGKEEH EKEAIAEEIF QDGEGEEGQE AMEAPMAPPE EEEEDDEESD IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEEY EYEDDEAEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL RSIPVKGAED DELEEEADWI YRNAFATPTI SLQESCDYLD RGQPASSFSR KGPSTIQKIK EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN AAKASRKKLK RVREEGDEEG EGDEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD DQFLKICLAE DEGLLTTDIS IDLKGVEGYG NDQTYFEEIK QFYYRDEFSH QVQEWNRQRT MAIERALQQF LYVQMAKELK NKLLAEAKEY VIKACSRKLY NWLRVAPYRP DQQVEEDDDF MDENQGKGIR VLGIAFSSAR DHPVFCALVN GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL LNKKPHVVTV AGENRDAQML IEDVKRIVHE LDQGQQLSSI GVELVDNELA ILYMNSKKSE AEFRDYPPVL RQAVSLARRI QDPLIEFAQV CSSDEDILCL KFHPLQEHVV KEELLNALYC EFINRVNEVG VDVNRAIAHP YSQALIQYVC GLGPRKGTHL LKILKQNNTR LESRTQLVTM CHMGPKVFMN CAGFLKIDTA SLGDSTDSYI EVLDGSRVHP ETYEWARKMA VDALEYDESA EDANPAGALE EILENPERLK DLDLDAFAEE LERQGYGDKH ITLYDIRAEL SCRYKDLRTA YRSPNTEEIF NMLTKETPET FYIGKLIICN VTGIAHRRPQ GESYDQAIRN DETGLWQCPF CQQDNFPELS EVWNHFDSGS CPGQAIGVKT RLDNGVTGFI PTKFLSDKVV KRPEERVKVG MTVHCRIMKI DIEKFSADLT CRTSDLMDRN NEWKLPKDTY YDFDAEAADH KQEEDMKRKQ QRTTYIKRVI AHPSFHNINF KQAEKMMETM DQGDVIIRPS SKGENHLTVT WKVSDGIYQH VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR KKLEELLIKT KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI FPTVNGLFRW FKDHYQDPVP GITPSSSSRT RTPASINATP ANINLADLTR AVNALPQNMT SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA YHVFPTPAQQ PVATPLMTPS YSYTTPSQPI TTPQYHQLQA STTPQSAQAQ PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR //