ID SPT6H_HUMAN Reviewed; 1726 AA. AC Q7KZ85; A7E2B4; Q15737; Q6GMQ4; Q7KYW9; Q7LDK4; Q8N526; Q92775; Q96AH3; AC Q9BTH9; Q9BTI2; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 2. DT 03-AUG-2022, entry version 176. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., 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 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. The RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of RT 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 HIV-1 RT Tat-activation."; RL J. Mol. Biol. 277:179-197(1998). RN [7] RP INTERACTION WITH HISTONE H2B; H3 AND HHV-5 PROTEIN UL69 (MICROBIAL RP INFECTION). 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 human RT cytomegalovirus and the human homolog of yeast chromatin regulatory protein RT 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., 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, 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 [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 biosynthesis and RT 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 THR-1718, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT 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 SPECTROMETRY RP [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 [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 IDENTIFICATION BY RP 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., Walther T.C., RA 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 SPECTROMETRY RP [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 [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., 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 [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 modes of RT 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., 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 [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-7; SER-12; SER-125 AND SER-1535, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP INTERACTION WITH HHV-5 PROTEIN UL69 (MICROBIAL INFECTION). 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 human RT 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 HIV-1 RT 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 and RT 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 SCALE RP 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., 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). 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: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 SUPT5H and CC SUPT4H1. Interacts with KDM6A (By similarity). Interacts (via SH2 CC domain) with SETD1A (By similarity). Interacts (via SH2 domain) with CC POLR2A phosphorylated at 'Ser-2'. Interacts with IWS1, AICDA and PAAF1. CC Interacts with histone H2B and H3. Interacts with WDR43 (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q62383, CC ECO:0000269|PubMed:10933715, ECO:0000269|PubMed:15060154, CC ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:19141475, CC ECO:0000269|PubMed:21518874, ECO:0000269|PubMed:22316138}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus/HHV-5 protein UL69. {ECO:0000269|PubMed:10933715, CC ECO:0000269|PubMed:22171252}. CC -!- INTERACTION: CC Q7KZ85; 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; Evidence={ECO:0000305}; CC Sequence=AAC50821.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH33074.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA11479.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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 PDB; 6GME; X-ray; 1.80 A; A/B=1338-1520. DR PDB; 6GMH; EM; 3.10 A; M=1-1726. DR PDB; 6TED; EM; 3.10 A; M=1-1726. DR PDB; 7OOP; EM; 2.90 A; M=1-1726. DR PDB; 7OPC; EM; 3.00 A; M=1-1726. DR PDB; 7OPD; EM; 3.00 A; M=1-1726. DR PDBsum; 6GME; -. DR PDBsum; 6GMH; -. DR PDBsum; 6TED; -. DR PDBsum; 7OOP; -. DR PDBsum; 7OPC; -. DR PDBsum; 7OPD; -. DR AlphaFoldDB; Q7KZ85; -. DR SMR; Q7KZ85; -. DR BioGRID; 112698; 197. DR CORUM; Q7KZ85; -. DR DIP; DIP-42615N; -. DR IntAct; Q7KZ85; 58. DR MINT; Q7KZ85; -. DR STRING; 9606.ENSP00000319104; -. DR GlyGen; Q7KZ85; 8 sites, 2 O-linked glycans (8 sites). DR iPTMnet; Q7KZ85; -. DR MetOSite; Q7KZ85; -. DR PhosphoSitePlus; Q7KZ85; -. DR BioMuta; SUPT6H; -. DR DMDM; 51701986; -. DR EPD; Q7KZ85; -. DR jPOST; Q7KZ85; -. DR MassIVE; Q7KZ85; -. DR MaxQB; Q7KZ85; -. DR PaxDb; Q7KZ85; -. DR PeptideAtlas; Q7KZ85; -. DR PRIDE; Q7KZ85; -. DR ProteomicsDB; 68703; -. [Q7KZ85-1] DR ProteomicsDB; 68704; -. [Q7KZ85-2] DR ProteomicsDB; 68705; -. [Q7KZ85-3] DR Antibodypedia; 3242; 163 antibodies from 23 providers. DR DNASU; 6830; -. DR Ensembl; ENST00000314616.11; ENSP00000319104.6; ENSG00000109111.15. [Q7KZ85-1] DR Ensembl; ENST00000347486.8; ENSP00000338143.4; ENSG00000109111.15. [Q7KZ85-1] DR GeneID; 6830; -. DR KEGG; hsa:6830; -. DR MANE-Select; ENST00000314616.11; ENSP00000319104.6; NM_003170.5; NP_003161.2. DR UCSC; uc002hby.4; human. [Q7KZ85-1] DR CTD; 6830; -. DR GeneCards; SUPT6H; -. DR HGNC; HGNC:11470; SUPT6H. DR HPA; ENSG00000109111; Low tissue specificity. DR MIM; 601333; gene. DR neXtProt; NX_Q7KZ85; -. DR OpenTargets; ENSG00000109111; -. DR PharmGKB; PA36256; -. DR VEuPathDB; HostDB:ENSG00000109111; -. DR eggNOG; KOG1856; Eukaryota. DR GeneTree; ENSGT00510000047446; -. DR HOGENOM; CLU_001680_4_0_1; -. DR InParanoid; Q7KZ85; -. DR OMA; LCNGFKT; -. DR OrthoDB; 56990at2759; -. DR PhylomeDB; Q7KZ85; -. DR TreeFam; TF105956; -. DR PathwayCommons; Q7KZ85; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. 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 BioGRID-ORCS; 6830; 800 hits in 1099 CRISPR screens. DR ChiTaRS; SUPT6H; human. DR GeneWiki; SUPT6H; -. DR GenomeRNAi; 6830; -. DR Pharos; Q7KZ85; Tbio. DR PRO; PR:Q7KZ85; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q7KZ85; protein. DR Bgee; ENSG00000109111; Expressed in sural nerve and 197 other tissues. DR ExpressionAtlas; Q7KZ85; baseline and differential. DR Genevisible; Q7KZ85; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 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; IDA:UniProtKB. DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl. 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; 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: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 3D-structure; Acetylation; Alternative splicing; Chaperone; KW Host-virus interaction; mRNA processing; mRNA splicing; mRNA transport; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT CHAIN 2..1726 FT /note="Transcription elongation factor SPT6" FT /id="PRO_0000072171" 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..199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..916 FT /note="Interaction with PAAF1" FT /evidence="ECO:0000269|PubMed:22316138" FT REGION 2..485 FT /note="Interaction with IWS1" FT /evidence="ECO:0000250" FT REGION 317..1300 FT /note="Interaction with KDM6A" FT /evidence="ECO:0000250" FT REGION 484..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:0000269|PubMed:10933715" FT REGION 1636..1726 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..48 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 166..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:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62383" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62383" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 743 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1515 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1523 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1526 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1528 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1532 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1535 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1539 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 1676 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1697 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1701 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT MOD_RES 1703 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT MOD_RES 1709 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q62383" FT MOD_RES 1718 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT VAR_SEQ 1..1181 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011505" FT VAR_SEQ 617..1616 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011507" FT VAR_SEQ 1182..1211 FT /note="ESYDQAIRNDETGLWQCPFCQQDNFPELSE -> MPSRGTRPEDSSVLIPTD FT NSTPHKEDLSSK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011506" FT CONFLICT 61..73 FT /note="DDDEDEGEEDEGS -> ATAPGHPKLSEGR (in Ref. 1; FT AAC50821)" FT /evidence="ECO:0000305" FT CONFLICT 100..109 FT /note="DFDLIEENLG -> LEDDDFLLNE (in Ref. 4; AAH33074)" FT /evidence="ECO:0000305" FT CONFLICT 988..994 FT /note="YVCGLGP -> VCLWPGT (in Ref. 1; AAB18949)" FT /evidence="ECO:0000305" FT CONFLICT 1545 FT /note="L -> P (in Ref. 4; AAH17105)" FT /evidence="ECO:0000305" FT CONFLICT 1627 FT /note="S -> I (in Ref. 4; AAH17105)" FT /evidence="ECO:0000305" FT HELIX 285..291 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:7OPC" FT HELIX 296..300 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 312..324 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 356..367 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 373..379 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 381..384 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 385..387 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 390..426 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 446..449 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 450..453 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 457..460 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 464..469 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:7OPC" FT HELIX 524..529 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 530..532 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 533..538 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 539..541 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 543..552 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 566..570 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 575..578 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 582..598 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 600..612 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 615..619 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 622..626 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 629..632 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 633..635 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 638..644 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 652..662 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 666..670 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 685..692 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 699..701 FT /evidence="ECO:0007829|PDB:6TED" FT HELIX 702..719 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 721..753 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 781..785 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 789..792 FT /evidence="ECO:0007829|PDB:6GMH" FT STRAND 794..799 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 801..803 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 805..811 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 825..842 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 846..850 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 856..869 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 870..874 FT /evidence="ECO:0007829|PDB:6GMH" FT STRAND 875..878 FT /evidence="ECO:0007829|PDB:6GMH" FT STRAND 881..884 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 889..895 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 897..902 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 904..906 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 908..921 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 923..930 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 934..939 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 944..947 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 951..969 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 973..978 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 980..983 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 984..987 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 989..991 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 994..1007 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1012..1014 FT /evidence="ECO:0007829|PDB:6GMH" FT HELIX 1016..1020 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1025..1031 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 1032..1034 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1052..1054 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1055..1058 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1060..1062 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1063..1073 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1079..1084 FT /evidence="ECO:0007829|PDB:6GMH" FT HELIX 1086..1094 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1099..1101 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1104..1113 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1114..1117 FT /evidence="ECO:0007829|PDB:6TED" FT HELIX 1120..1131 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1132..1134 FT /evidence="ECO:0007829|PDB:6GMH" FT HELIX 1146..1154 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 1158..1160 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1166..1171 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1228..1232 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1237..1240 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1242..1245 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1248..1250 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 1253..1255 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1261..1267 FT /evidence="ECO:0007829|PDB:7OOP" FT TURN 1272..1274 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1276..1280 FT /evidence="ECO:0007829|PDB:6GMH" FT HELIX 1283..1286 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 1330..1332 FT /evidence="ECO:0007829|PDB:6GMH" FT HELIX 1340..1349 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1355..1359 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1361..1363 FT /evidence="ECO:0007829|PDB:6GMH" FT STRAND 1367..1374 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1377..1385 FT /evidence="ECO:0007829|PDB:6GME" FT TURN 1386..1388 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1391..1393 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1395..1400 FT /evidence="ECO:0007829|PDB:6GME" FT HELIX 1403..1406 FT /evidence="ECO:0007829|PDB:6GME" FT HELIX 1408..1427 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1430..1432 FT /evidence="ECO:0007829|PDB:6TED" FT HELIX 1435..1438 FT /evidence="ECO:0007829|PDB:6GME" FT HELIX 1440..1453 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1455..1457 FT /evidence="ECO:0007829|PDB:6GMH" FT STRAND 1460..1464 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1466..1468 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1471..1476 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1478..1481 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1483..1490 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1493..1496 FT /evidence="ECO:0007829|PDB:6GME" FT STRAND 1499..1503 FT /evidence="ECO:0007829|PDB:6GME" FT HELIX 1504..1514 FT /evidence="ECO:0007829|PDB:6GME" 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 //