SPT6H_HUMAN
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};
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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
