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 02-MAR-2010, entry version 67. DE RecName: Full=Transcription elongation factor SPT6; DE Short=hSPT6; 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 MEDLINE=96374824; 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 MEDLINE=96281124; 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 MEDLINE=98181020; 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 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78 AND RP SER-125, AND MASS SPECTROMETRY. RC TISSUE=Epithelium; 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS RP SPECTROMETRY. RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1532; SER-1535; RP THR-1539; SER-1701 AND THR-1718, AND MASS SPECTROMETRY. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78; RP SER-179; SER-267; THR-1523; SER-1526; THR-1532; SER-1535; THR-1539; RP SER-1701; SER-1703 AND THR-1718, AND MASS SPECTROMETRY. 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 [12] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-12; THR-1697 AND RP THR-1718, AND MASS SPECTROMETRY. 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78; RP THR-1532; SER-1535; THR-1539; THR-1697; SER-1701; SER-1703 AND RP THR-1718, AND MASS SPECTROMETRY. RC TISSUE=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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-743 AND LYS-1676, AND MASS RP SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). CC -!- FUNCTION: Acts to stimulate transcriptional elongation by RNA CC polymerase II. 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. CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). 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. CC -!- SIMILARITY: Contains 1 S1 motif domain. CC -!- SIMILARITY: Contains 1 SH2 domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAB18949.1; Type=Frameshift; Positions=988; 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 IPI; IPI00430770; -. DR IPI; IPI00456683; -. DR IPI; IPI00784161; -. DR RefSeq; NP_003161.2; -. DR UniGene; Hs.250429; -. DR STRING; Q7KZ85; -. DR PhosphoSite; Q7KZ85; -. DR PeptideAtlas; Q7KZ85; -. DR PRIDE; Q7KZ85; -. DR Ensembl; ENST00000314616; ENSP00000319104; ENSG00000109111; Homo sapiens. DR GeneID; 6830; -. DR KEGG; hsa:6830; -. DR UCSC; uc002hby.1; human. DR CTD; 6830; -. DR GeneCards; GC17P024013; -. DR H-InvDB; HIX0013656; -. DR HGNC; HGNC:11470; SUPT6H. DR HPA; CAB012416; -. DR MIM; 601333; gene. DR PharmGKB; PA36256; -. DR eggNOG; prNOG07888; -. DR HOVERGEN; HBG093994; -. DR InParanoid; Q7KZ85; -. DR OMA; QHFEVPF; -. DR OrthoDB; EOG9G4K8M; -. DR PhylomeDB; Q7KZ85; -. DR NextBio; 26667; -. DR PMAP-CutDB; Q7KZ85; -. DR ArrayExpress; Q7KZ85; -. DR Bgee; Q7KZ85; -. DR Genevestigator; Q7KZ85; -. DR GermOnline; ENSG00000109111; Homo sapiens. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003711; F:transcription elongation regulator activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription from RNA polyme...; IEA:InterPro. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR016027; NA-bd_OB-fold-like. DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom. DR InterPro; IPR006641; Resolv_RNaseH-like. DR InterPro; IPR000980; SH2. DR InterPro; IPR017072; TF_Spt6. DR Pfam; PF00575; S1; 1. DR Pfam; PF00017; SH2; 1. DR PIRSF; PIRSF036947; Spt6; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00732; YqgFc; 1. DR SUPFAM; SSF50249; Nucleic_acid_OB; 1. DR PROSITE; PS50126; S1; 1. DR PROSITE; PS50001; SH2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Nucleus; KW Phosphoprotein; Transcription; Transcription regulation. FT CHAIN 1 1726 Transcription elongation factor SPT6. FT /FTId=PRO_0000072171. FT DOMAIN 1213 1282 S1 motif. FT DOMAIN 1325 1431 SH2. FT COMPBIAS 6 250 Asp/Glu-rich. FT COMPBIAS 1525 1528 Poly-Ser. FT COMPBIAS 1654 1657 Poly-Ser. FT MOD_RES 7 7 Phosphoserine. FT MOD_RES 12 12 Phosphoserine. FT MOD_RES 73 73 Phosphoserine. FT MOD_RES 75 75 Phosphoserine. FT MOD_RES 78 78 Phosphoserine. FT MOD_RES 125 125 Phosphoserine. FT MOD_RES 179 179 Phosphoserine. FT MOD_RES 267 267 Phosphoserine. FT MOD_RES 743 743 N6-acetyllysine. FT MOD_RES 1523 1523 Phosphothreonine. FT MOD_RES 1526 1526 Phosphoserine. FT MOD_RES 1532 1532 Phosphothreonine. FT MOD_RES 1535 1535 Phosphoserine. FT MOD_RES 1539 1539 Phosphothreonine. FT MOD_RES 1676 1676 N6-acetyllysine. FT MOD_RES 1697 1697 Phosphothreonine. FT MOD_RES 1701 1701 Phosphoserine. FT MOD_RES 1703 1703 Phosphoserine. FT MOD_RES 1718 1718 Phosphothreonine. FT VAR_SEQ 1 1181 Missing (in isoform 2). FT /FTId=VSP_011505. FT VAR_SEQ 617 1616 Missing (in isoform 3). FT /FTId=VSP_011507. FT VAR_SEQ 1182 1211 ESYDQAIRNDETGLWQCPFCQQDNFPELSE -> MPSRGTR FT PEDSSVLIPTDNSTPHKEDLSSK (in isoform 2). FT /FTId=VSP_011506. FT CONFLICT 61 73 DDDEDEGEEDEGS -> ATAPGHPKLSEGR (in Ref. FT 1; AAC50821). FT CONFLICT 100 109 DFDLIEENLG -> LEDDDFLLNE (in Ref. 4; FT AAH33074). FT CONFLICT 988 994 YVCGLGP -> VCLWPGT (in Ref. 1). FT CONFLICT 1545 1545 L -> P (in Ref. 4; AAH17105). FT CONFLICT 1627 1627 S -> I (in Ref. 4; AAH17105). 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 //