SPT4H_HUMAN
ID SPT4H_HUMAN Reviewed; 117 AA.
AC P63272; B2R4X8; D3DTZ4; Q16550; Q62387; Q6ZP89;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcription elongation factor SPT4;
DE Short=hSPT4;
DE AltName: Full=DRB sensitivity-inducing factor 14 kDa subunit;
DE Short=DSIF p14;
DE AltName: Full=DRB sensitivity-inducing factor small subunit;
DE Short=DSIF small subunit;
GN Name=SUPT4H1; Synonyms=SPT4H, SUPT4H;
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], AND TISSUE SPECIFICITY.
RX PubMed=8786137; DOI=10.1006/geno.1996.0299;
RA Chiang P.-W., Wang S.-Q., Smithivas P., Song W.-J., Crombez E., Akhtar A.,
RA Im R., Greenfield J., Ramamoorthy S., van Keuren M.L., Blackburn C.C.,
RA Tsai C.-H., Kurnit D.M.;
RT "Isolation and characterization of the human and mouse homologues (SUPT4H
RT and Supt4h) of the yeast SPT4 gene.";
RL Genomics 34:368-375(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8649394; DOI=10.1128/mcb.16.6.2848;
RA Hartzog G.A., Basrai M.A., Ricupero-Hovasse S.L., Hieter P., Winston F.;
RT "Identification and analysis of a functional human homolog of the SPT4 gene
RT of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:2848-2856(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dermoid cancer, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [7]
RP FUNCTION.
RX PubMed=9857195; DOI=10.1093/emboj/17.24.7395;
RA Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.;
RT "Evidence that P-TEFb alleviates the negative effect of DSIF on RNA
RT polymerase II-dependent transcription in vitro.";
RL EMBO J. 17:7395-7403(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH SUPT5H.
RX PubMed=9450929; DOI=10.1101/gad.12.3.343;
RA Wada T., Takagi T., Yamaguchi Y., Ferdous A., Imai T., Hirose S.,
RA Sugimoto S., Yano K., Hartzog G.A., Winston F., Buratowski S., Handa H.;
RT "DSIF, a novel transcription elongation factor that regulates RNA
RT polymerase II processivity, is composed of human Spt4 and Spt5 homologs.";
RL Genes Dev. 12:343-356(1998).
RN [9]
RP FUNCTION.
RX PubMed=10199401; DOI=10.1016/s0092-8674(00)80713-8;
RA Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S.,
RA Hasegawa J., Handa H.;
RT "NELF, a multisubunit complex containing RD, cooperates with DSIF to
RT repress RNA polymerase II elongation.";
RL Cell 97:41-51(1999).
RN [10]
RP FUNCTION, AND INTERACTION WITH SUPT5H.
RX PubMed=10075709; DOI=10.1074/jbc.274.12.8085;
RA Yamaguchi Y., Wada T., Watanabe D., Takagi T., Hasegawa J., Handa H.;
RT "Structure and function of the human transcription elongation factor
RT DSIF.";
RL J. Biol. Chem. 274:8085-8092(1999).
RN [11]
RP FUNCTION.
RX PubMed=10454543; DOI=10.1128/mcb.19.9.5960;
RA Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.;
RT "Tat-SF1 protein associates with RAP30 and human SPT5 proteins.";
RL Mol. Cell. Biol. 19:5960-5968(1999).
RN [12]
RP FUNCTION.
RX PubMed=10912001; DOI=10.1016/s1097-2765(00)80272-5;
RA Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y.,
RA Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.;
RT "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation
RT and reveals functional differences between P-TEFb and TFIIH.";
RL Mol. Cell 5:1067-1072(2000).
RN [13]
RP INTERACTION WITH SUPT5H.
RX PubMed=10757782; DOI=10.1128/mcb.20.9.2970-2983.2000;
RA Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.;
RT "Domains in the SPT5 protein that modulate its transcriptional regulatory
RT properties.";
RL Mol. Cell. Biol. 20:2970-2983(2000).
RN [14]
RP FUNCTION.
RX PubMed=11112772; DOI=10.1074/jbc.m006130200;
RA Ping Y.-H., Rana T.M.;
RT "DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1
RT Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and
RT DSIF during transcription elongation.";
RL J. Biol. Chem. 276:12951-12958(2001).
RN [15]
RP FUNCTION.
RX PubMed=11553615; DOI=10.1074/jbc.m104967200;
RA Renner D.B., Yamaguchi Y., Wada T., Handa H., Price D.H.;
RT "A highly purified RNA polymerase II elongation control system.";
RL J. Biol. Chem. 276:42601-42609(2001).
RN [16]
RP FUNCTION, AND INTERACTION WITH SUPT5H.
RX PubMed=12653964; DOI=10.1046/j.1365-2443.2003.00638.x;
RA Kim D.-K., Inukai N., Yamada T., Furuya A., Sato H., Yamaguchi Y., Wada T.,
RA Handa H.;
RT "Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5
RT exert their roles in transcriptional elongation as parts of the DSIF
RT complex.";
RL Genes Cells 8:371-378(2003).
RN [17]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SUPT5H.
RX PubMed=12718890; DOI=10.1016/s1097-2765(03)00101-1;
RA Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B.,
RA Gehrig P., Gaynor R.B.;
RT "Methylation of SPT5 regulates its interaction with RNA polymerase II and
RT transcriptional elongation properties.";
RL Mol. Cell 11:1055-1066(2003).
RN [18]
RP FUNCTION.
RX PubMed=15380072; DOI=10.1016/j.cub.2004.08.066;
RA Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H.,
RA Ish-Horowicz D.;
RT "Locus-specific requirements for Spt5 in transcriptional activation and
RT repression in Drosophila.";
RL Curr. Biol. 14:1680-1684(2004).
RN [19]
RP INTERACTION WITH SUPT5H.
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 [20]
RP FUNCTION.
RX PubMed=15136722; DOI=10.1073/pnas.0401493101;
RA Mandal S.S., Chu C., Wada T., Handa H., Shatkin A.J., Reinberg D.;
RT "Functional interactions of RNA-capping enzyme with factors that positively
RT and negatively regulate promoter escape by RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7572-7577(2004).
RN [21]
RP FUNCTION.
RX PubMed=16214896; DOI=10.1073/pnas.0409405102;
RA Palangat M., Renner D.B., Price D.H., Landick R.;
RT "A negative elongation factor for human RNA polymerase II inhibits the
RT anti-arrest transcript-cleavage factor TFIIS.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15036-15041(2005).
RN [22]
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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-117 IN COMPLEX WITH SPT5H.
RX PubMed=19860741; DOI=10.1042/bj20091422;
RA Wenzel S., Martins B.M., Rosch P., Wohrl B.M.;
RT "Crystal structure of the human transcription elongation factor DSIF hSpt4
RT subunit in complex with the hSpt5 dimerization interface.";
RL Biochem. J. 425:373-380(2010).
CC -!- FUNCTION: Component of the DRB sensitivity-inducing factor complex
CC (DSIF complex), which regulates mRNA processing and transcription
CC elongation by RNA polymerase II. DSIF positively regulates mRNA capping
CC by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A.
CC DSIF also acts cooperatively with the negative elongation factor
CC complex (NELF complex) to enhance transcriptional pausing at sites
CC proximal to the promoter. Transcriptional pausing may facilitate the
CC assembly of an elongation competent RNA polymerase II complex. DSIF and
CC NELF promote pausing by inhibition of the transcription elongation
CC factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at
CC transcription pause sites and stimulates the weak intrinsic nuclease
CC activity of the enzyme. Cleavage of blocked transcripts by RNA
CC polymerase II promotes the resumption of transcription from the new 3'
CC terminus and may allow repeated attempts at transcription through
CC natural pause sites. DSIF can also positively regulate transcriptional
CC elongation and is required for the efficient activation of
CC transcriptional elongation by the HIV-1 nuclear transcriptional
CC activator, Tat. DSIF acts to suppress transcriptional pausing in
CC transcripts derived from the HIV-1 LTR and blocks premature release of
CC HIV-1 transcripts at terminator sequences.
CC {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401,
CC ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10912001,
CC ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615,
CC ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890,
CC ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072,
CC ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:9450929,
CC ECO:0000269|PubMed:9857195}.
CC -!- SUBUNIT: Interacts with SUPT5H to form DSIF. DSIF interacts with the
CC positive transcription elongation factor b complex (P-TEFb complex),
CC which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts
CC with RNA polymerase II, and this interaction is reduced by
CC phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb.
CC DSIF also interacts with the NELF complex, which is composed of NELFA,
CC NELFB, NELFD and NELFE, and this interaction occurs following prior
CC binding of DSIF to RNA polymerase II. DSIF also interacts with
CC PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can
CC interact with PIN1. {ECO:0000269|PubMed:10075709,
CC ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:12653964,
CC ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15060154,
CC ECO:0000269|PubMed:19860741, ECO:0000269|PubMed:9450929}.
CC -!- INTERACTION:
CC P63272; O00267: SUPT5H; NbExp=15; IntAct=EBI-727250, EBI-710464;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8649394}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8649394,
CC ECO:0000269|PubMed:8786137}.
CC -!- SIMILARITY: Belongs to the SPT4 family. {ECO:0000305}.
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DR EMBL; U38818; AAB18674.1; -; mRNA.
DR EMBL; U38817; AAB18675.1; -; mRNA.
DR EMBL; U43923; AAB07814.1; -; mRNA.
DR EMBL; AK129758; BAC85230.1; -; mRNA.
DR EMBL; AK311986; BAG34925.1; -; mRNA.
DR EMBL; CR407663; CAG28591.1; -; mRNA.
DR EMBL; CH471109; EAW94464.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94466.1; -; Genomic_DNA.
DR EMBL; BC002802; AAH02802.1; -; mRNA.
DR CCDS; CCDS11606.1; -.
DR RefSeq; NP_003159.1; NM_003168.2.
DR PDB; 3H7H; X-ray; 1.55 A; A=2-117.
DR PDB; 5OIK; EM; 3.70 A; Y=1-117.
DR PDB; 6GMH; EM; 3.10 A; Y=1-117.
DR PDB; 6GML; EM; 3.20 A; Y=1-117.
DR PDB; 6TED; EM; 3.10 A; Y=1-117.
DR PDB; 7OKY; EM; 4.14 A; Y=1-117.
DR PDBsum; 3H7H; -.
DR PDBsum; 5OIK; -.
DR PDBsum; 6GMH; -.
DR PDBsum; 6GML; -.
DR PDBsum; 6TED; -.
DR PDBsum; 7OKY; -.
DR AlphaFoldDB; P63272; -.
DR SMR; P63272; -.
DR BioGRID; 112695; 45.
DR ComplexPortal; CPX-891; DSIF transcription elongation factor complex.
DR CORUM; P63272; -.
DR DIP; DIP-40644N; -.
DR IntAct; P63272; 17.
DR MINT; P63272; -.
DR STRING; 9606.ENSP00000225504; -.
DR iPTMnet; P63272; -.
DR PhosphoSitePlus; P63272; -.
DR BioMuta; SUPT4H1; -.
DR DMDM; 54039624; -.
DR EPD; P63272; -.
DR jPOST; P63272; -.
DR MassIVE; P63272; -.
DR MaxQB; P63272; -.
DR PaxDb; P63272; -.
DR PeptideAtlas; P63272; -.
DR PRIDE; P63272; -.
DR ProteomicsDB; 57516; -.
DR Antibodypedia; 18387; 173 antibodies from 27 providers.
DR DNASU; 6827; -.
DR Ensembl; ENST00000225504.8; ENSP00000225504.3; ENSG00000213246.7.
DR Ensembl; ENST00000580947.1; ENSP00000462670.1; ENSG00000213246.7.
DR GeneID; 6827; -.
DR KEGG; hsa:6827; -.
DR MANE-Select; ENST00000225504.8; ENSP00000225504.3; NM_003168.3; NP_003159.1.
DR UCSC; uc002iwe.3; human.
DR CTD; 6827; -.
DR DisGeNET; 6827; -.
DR GeneCards; SUPT4H1; -.
DR HGNC; HGNC:11467; SUPT4H1.
DR HPA; ENSG00000213246; Low tissue specificity.
DR MIM; 603555; gene.
DR neXtProt; NX_P63272; -.
DR OpenTargets; ENSG00000213246; -.
DR PharmGKB; PA36253; -.
DR VEuPathDB; HostDB:ENSG00000213246; -.
DR eggNOG; KOG3490; Eukaryota.
DR GeneTree; ENSGT00390000018559; -.
DR HOGENOM; CLU_138052_3_0_1; -.
DR InParanoid; P63272; -.
DR OMA; FDGMIAV; -.
DR OrthoDB; 1617752at2759; -.
DR PhylomeDB; P63272; -.
DR TreeFam; TF300105; -.
DR PathwayCommons; P63272; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; P63272; -.
DR BioGRID-ORCS; 6827; 418 hits in 1077 CRISPR screens.
DR ChiTaRS; SUPT4H1; human.
DR EvolutionaryTrace; P63272; -.
DR GeneWiki; SUPT4H1; -.
DR GenomeRNAi; 6827; -.
DR Pharos; P63272; Tbio.
DR PRO; PR:P63272; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P63272; protein.
DR Bgee; ENSG00000213246; Expressed in monocyte and 104 other tissues.
DR ExpressionAtlas; P63272; baseline and differential.
DR Genevisible; P63272; HS.
DR GO; GO:0032044; C:DSIF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd07973; Spt4; 1.
DR Gene3D; 3.30.40.210; -; 1.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR009287; Spt4.
DR InterPro; IPR022800; Spt4/RpoE2_Znf.
DR InterPro; IPR038510; Spt4_sf.
DR PANTHER; PTHR12882; PTHR12882; 1.
DR Pfam; PF06093; Spt4; 1.
DR PIRSF; PIRSF025023; Spt4; 1.
DR SMART; SM01389; Spt4; 1.
DR SUPFAM; SSF63393; SSF63393; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..117
FT /note="Transcription elongation factor SPT4"
FT /id="PRO_0000210325"
FT ZN_FING 16..36
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 2..40
FT /note="Interaction with SUPT5H"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 95..117
FT /note="QGIVRELKSRGVAYKSRDTAIKT -> HAKDSRSNVNKYEPRESSEGHDTCL
FT ASLFHSLRHSNSLFAL (in Ref. 3; BAC85230)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3H7H"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:3H7H"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:3H7H"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:3H7H"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:3H7H"
SQ SEQUENCE 117 AA; 13193 MW; 09EDF007501D0F03 CRC64;
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI
IAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE LKSRGVAYKS RDTAIKT
