SPT6H_MOUSE
ID SPT6H_MOUSE Reviewed; 1726 AA.
AC Q62383; Q5SYM0; Q6GQS3; Q6ZQI0; Q8BQY6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Transcription elongation factor SPT6;
GN Name=Supt6h; Synonyms=Kiaa0162, Supt6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster;
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., Glover T.W.,
RA Miller D.E., Tsai C.-H., Blackburn C.C., Chen X.-N., Sun Z., Cheng J.-F.,
RA Korenberg J.R., Kurnit D.M.;
RT "Identification and analysis of the human and murine putative chromatin
RT structure regulator SUPT6H and Supt6h.";
RL Genomics 34:328-333(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 498-1726.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1359-1726.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP FUNCTION, INTERACTION WITH POLR2A AND IWS1, AND MUTAGENESIS OF ARG-1358.
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 [7]
RP INTERACTION WITH IWS1 AND POLR2A.
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 biosynthesis and
RT HYPB/Setd2-mediated histone H3K36 methylation.";
RL Genes Dev. 22:3422-3434(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-78; SER-91; SER-125;
RP THR-1532; SER-1535; THR-1539; SER-1701; SER-1703; THR-1709 AND THR-1718,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, AND 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., Iemura S.,
RA Honjo T.;
RT "Histone chaperone Spt6 is required for class switch recombination but not
RT somatic hypermutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011).
RN [10]
RP FUNCTION, AND INTERACTION WITH SETD1A.
RX PubMed=22843687; DOI=10.1074/jbc.m112.351569;
RA Begum N.A., Stanlie A., Nakata M., Akiyama H., Honjo T.;
RT "The histone chaperone Spt6 is required for activation-induced cytidine
RT deaminase target determination through H3K4me3 regulation.";
RL J. Biol. Chem. 287:32415-32429(2012).
RN [11]
RP FUNCTION, AND INTERACTION WITH KDM6A.
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 and
RT myogenesis.";
RL EMBO J. 32:1075-1086(2013).
RN [12]
RP INTERACTION WITH WDR43.
RX PubMed=31128943; DOI=10.1016/j.molcel.2019.05.007;
RA Bi X., Xu Y., Li T., Li X., Li W., Shao W., Wang K., Zhan G., Wu Z.,
RA Liu W., Lu J.Y., Wang L., Zhao J., Wu J., Na J., Li G., Li P., Shen X.;
RT "RNA Targets Ribogenesis Factor WDR43 to Chromatin for Transcription and
RT Pluripotency Control.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Transcription elongation factor which binds histone H3 and
CC plays a key role in the regulation of transcription elongation and mRNA
CC processing. Enhances the transcription elongation by RNA polymerase II
CC (RNAPII) and is also required for the efficient activation of
CC transcriptional elongation by the HIV-1 nuclear transcriptional
CC activator, Tat. Besides chaperoning histones in transcription, acts to
CC transport and splice mRNA by forming a complex with IWS1 and the C-
CC terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The
CC SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4,
CC EXOSC10) as well as histone modifying enzymes (such as SETD2), to
CC ensure proper mRNA splicing, efficient mRNA export and elongation-
CC coupled H3K36 methylation, a signature chromatin mark of active
CC transcription. SUPT6H via its association with SETD1A, regulates both
CC class-switch recombination and somatic hypermutation through formation
CC of H3K4me3 epigenetic marks on activation-induced cytidine deaminase
CC (AICDA) target loci. Promotes the activation of the myogenic gene
CC program by entailing erasure of the repressive H3K27me3 epigenetic mark
CC through stabilization of the chromatin interaction of the H3K27
CC demethylase KDM6A. {ECO:0000269|PubMed:17234882,
CC ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22843687,
CC ECO:0000269|PubMed:23503590}.
CC -!- SUBUNIT: Interacts with RNA polymerase II and the DRB sensitivity-
CC inducing factor complex (DSIF complex), which is composed of SUPT5H and
CC SUPT4H1 or SUPT4H2 (By similarity). Interacts with PAAF1 (By
CC similarity). Interacts with histone H2B and H3 (By similarity).
CC Interacts (via SH2 domain) with POLR2A phosphorylated at 'Ser-2'.
CC Interacts (via SH2 domain) with SETD1A. Interacts with IWS1, KDM6A and
CC AICDA. Interacts with WDR43 (PubMed:31128943). {ECO:0000250,
CC ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:19141475,
CC ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22843687,
CC ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:31128943}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR EMBL; U40375; AAB18950.1; -; mRNA.
DR EMBL; AL591070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072657; AAH72657.1; -; mRNA.
DR EMBL; AK129069; BAC97879.1; -; mRNA.
DR EMBL; AK046156; BAC32616.1; -; mRNA.
DR CCDS; CCDS25095.1; -.
DR PIR; T30810; T30810.
DR RefSeq; NP_033323.2; NM_009297.2.
DR AlphaFoldDB; Q62383; -.
DR SMR; Q62383; -.
DR BioGRID; 203576; 9.
DR IntAct; Q62383; 5.
DR MINT; Q62383; -.
DR STRING; 10090.ENSMUSP00000002121; -.
DR iPTMnet; Q62383; -.
DR PhosphoSitePlus; Q62383; -.
DR EPD; Q62383; -.
DR jPOST; Q62383; -.
DR MaxQB; Q62383; -.
DR PaxDb; Q62383; -.
DR PeptideAtlas; Q62383; -.
DR PRIDE; Q62383; -.
DR ProteomicsDB; 261636; -.
DR Antibodypedia; 3242; 163 antibodies from 23 providers.
DR DNASU; 20926; -.
DR Ensembl; ENSMUST00000002121; ENSMUSP00000002121; ENSMUSG00000002052.
DR GeneID; 20926; -.
DR KEGG; mmu:20926; -.
DR UCSC; uc007kip.2; mouse.
DR CTD; 20926; -.
DR MGI; MGI:107726; Supt6.
DR VEuPathDB; HostDB:ENSMUSG00000002052; -.
DR eggNOG; KOG1856; Eukaryota.
DR GeneTree; ENSGT00510000047446; -.
DR HOGENOM; CLU_001680_4_0_1; -.
DR InParanoid; Q62383; -.
DR OMA; LCNGFKT; -.
DR OrthoDB; 56990at2759; -.
DR PhylomeDB; Q62383; -.
DR TreeFam; TF105956; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 20926; 46 hits in 113 CRISPR screens.
DR ChiTaRS; Supt6; mouse.
DR PRO; PR:Q62383; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q62383; protein.
DR Bgee; ENSMUSG00000002052; Expressed in floor plate of midbrain and 274 other tissues.
DR Genevisible; Q62383; MM.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; 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; IMP:UniProtKB.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; IMP:UniProtKB.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 1.10.10.2740; -; 1.
DR Gene3D; 1.10.10.650; -; 1.
DR Gene3D; 1.10.3500.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.420.140; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR041692; HHH_9.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028083; Spt6_acidic_N_dom.
DR InterPro; IPR042066; Spt6_death-like.
DR InterPro; IPR032706; Spt6_HHH.
DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR InterPro; IPR035420; Spt6_SH2.
DR InterPro; IPR035018; Spt6_SH2_C.
DR InterPro; IPR035019; Spt6_SH2_N.
DR InterPro; IPR028231; Spt6_YqgF.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR017072; TF_Spt6.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; PTHR10145; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF17674; HHH_9; 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; Chaperone; Coiled coil; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT CHAIN 2..1726
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000072172"
FT DOMAIN 1213..1282
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1325..1431
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..916
FT /note="Interaction with PAAF1"
FT /evidence="ECO:0000250"
FT REGION 2..485
FT /note="Interaction with IWS1"
FT REGION 317..1300
FT /note="Interaction with KDM6A"
FT /evidence="ECO:0000269|PubMed:23503590"
FT REGION 489..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1726
FT /note="Interaction with histone H2B and H3"
FT /evidence="ECO:0000250"
FT REGION 1636..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..51
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 743
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 1515
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 1523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 1526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 1532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1539
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1676
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 1697
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7KZ85"
FT MOD_RES 1701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1709
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1718
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 1358
FT /note="R->K: Loss of binding to POLR2A. Retains the ability
FT to support transcription elongation but the resulting
FT transcripts contain splicing defects and accumulate to high
FT levels within the nucleus."
FT /evidence="ECO:0000269|PubMed:17234882"
FT CONFLICT 609
FT /note="T -> A (in Ref. 1; AAB18950)"
FT /evidence="ECO:0000305"
FT CONFLICT 1520
FT /note="P -> Q (in Ref. 5; BAC32616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1726 AA; 199086 MW; 98BD891493372166 CRC64;
MSDFVESEAE ESEEEYNHEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE RGNLKDFIND
DDDEEEGEED EGSDSGDSED DVGHKKRKRP SFDDRLEDDD FDLIEENLGV KVKRGQKYRR
VKKMSDDDED DEEEYGKEEH EKEAIAGEIF QDEEGEEGQE AVEAPMAPPD EEEEDDEESD
IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEDY
EYEDDETEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL
RSIPVKAAED DELEEEADWI YRNAFATPTI SLQDSCDYLD RGQPTSSFSR KGPSTVQKIK
EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM
QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN
AAKASRKKLK RIKEDGDEEG EGEEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG
LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP
LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD DQFLKIGLAE
DEGLLTIDIS IDMKGVEGYG NDQTYFEEIK QFYYRDEFSH QVQEWNRQRT MAIERALQQF
LYVQMAKELK NKLLAEARES VVKACSRKLY NWLRVAPYRP DQQVEEDDDF MDENQGKGIR
VLGIAFSSAR DHPVFCALVN GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL
VNKKPHVVTI AGENRDAQML TEDVKRIVHE 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 WKVSAGIYQH
VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR
KKLEELLIKT KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI
FPTVNGLFRW FKDHYQDPVP GITPSSSNRT RTPASINATP ANINLADLTR AVNALPQNMT
SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA YHVFPTPAQQ PVATPLMTPS
YSYTTPSQPI TTPQYHQLQA STTPQSTQAQ PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ
WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR
