[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. DOI=10.1006/geno.1996.0299; PubMed=8786137 [NCBI, ExPASy, EBI, Israel, Japan] Chiang P.-W., Wang S.-Q., Smithivas P., Song W.-J., Crombez E., Akhtar A., Im R., Greenfield J., Ramamoorthy S., van Keuren M.L., Blackburn C.C., Tsai C.-H., Kurnit D.M.; "Isolation and characterization of the human and mouse homologues (SUPT4H and Supt4h) of the yeast SPT4 gene."; Genomics 34:368-375(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. PubMed=8649394 [NCBI, ExPASy, EBI, Israel, Japan] Hartzog G.A., Basrai M.A., Ricupero-Hovasse S.L., Hieter P., Winston F.; "Identification and analysis of a functional human homolog of the SPT4 gene of Saccharomyces cerevisiae."; Mol. Cell. Biol. 16:2848-2856(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Dermoid cancer; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	FUNCTION. DOI=10.1093/emboj/17.24.7395; PubMed=9857195 [NCBI, ExPASy, EBI, Israel, Japan] Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.; "Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro."; EMBO J. 17:7395-7403(1998).
[7]	FUNCTION, AND INTERACTION WITH SUPT5H. PubMed=9450929 [NCBI, ExPASy, EBI, Israel, Japan] Wada T., Takagi T., Yamaguchi Y., Ferdous A., Imai T., Hirose S., Sugimoto S., Yano K., Hartzog G.A., Winston F., Buratowski S., Handa H.; "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs."; Genes Dev. 12:343-356(1998).
[8]	FUNCTION. DOI=10.1016/S0092-8674(00)80713-8; PubMed=10199401 [NCBI, ExPASy, EBI, Israel, Japan] Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S., Hasegawa J., Handa H.; "NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation."; Cell 97:41-51(1999).
[9]	FUNCTION, AND INTERACTION WITH SUPT5H. DOI=10.1074/jbc.274.12.8085; PubMed=10075709 [NCBI, ExPASy, EBI, Israel, Japan] Yamaguchi Y., Wada T., Watanabe D., Takagi T., Hasegawa J., Handa H.; "Structure and function of the human transcription elongation factor DSIF."; J. Biol. Chem. 274:8085-8092(1999).
[10]	FUNCTION. PubMed=10454543 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.; "Tat-SF1 protein associates with RAP30 and human SPT5 proteins."; Mol. Cell. Biol. 19:5960-5968(1999).
[11]	FUNCTION. DOI=10.1016/S1097-2765(00)80272-5; PubMed=10912001 [NCBI, ExPASy, EBI, Israel, Japan] Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.; "FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH."; Mol. Cell 5:1067-1072(2000).
[12]	INTERACTION WITH SUPT5H. DOI=10.1128/MCB.20.9.2970-2983.2000; PubMed=10757782 [NCBI, ExPASy, EBI, Israel, Japan] Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.; "Domains in the SPT5 protein that modulate its transcriptional regulatory properties."; Mol. Cell. Biol. 20:2970-2983(2000).
[13]	FUNCTION. DOI=10.1074/jbc.M006130200; PubMed=11112772 [NCBI, ExPASy, EBI, Israel, Japan] Ping Y.-H., Rana T.M.; "DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation."; J. Biol. Chem. 276:12951-12958(2001).
[14]	FUNCTION. DOI=10.1074/jbc.M104967200; PubMed=11553615 [NCBI, ExPASy, EBI, Israel, Japan] Renner D.B., Yamaguchi Y., Wada T., Handa H., Price D.H.; "A highly purified RNA polymerase II elongation control system."; J. Biol. Chem. 276:42601-42609(2001).
[15]	FUNCTION, AND INTERACTION WITH SUPT5H. DOI=10.1046/j.1365-2443.2003.00638.x; PubMed=12653964 [NCBI, ExPASy, EBI, Israel, Japan] Kim D.-K., Inukai N., Yamada T., Furuya A., Sato H., Yamaguchi Y., Wada T., Handa H.; "Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex."; Genes Cells 8:371-378(2003).
[16]	FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SUPT5H. DOI=10.1016/S1097-2765(03)00101-1; PubMed=12718890 [NCBI, ExPASy, EBI, Israel, Japan] Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.; "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."; Mol. Cell 11:1055-1066(2003).
[17]	FUNCTION. DOI=10.1016/j.cub.2004.08.066; PubMed=15380072 [NCBI, ExPASy, EBI, Israel, Japan] Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H., Ish-Horowicz D.; "Locus-specific requirements for Spt5 in transcriptional activation and repression in Drosophila."; Curr. Biol. 14:1680-1684(2004).
[18]	INTERACTION WITH SUPT5H. DOI=10.1128/MCB.24.8.3324-3336.2004; PubMed=15060154 [NCBI, ExPASy, EBI, Israel, Japan] Endoh M., Zhu W., Hasegawa J., Watanabe H., Kim D.-K., Aida M., Inukai N., Narita T., Yamada T., Furuya A., Sato H., Yamaguchi Y., Mandal S.S., Reinberg D., Wada T., Handa H.; "Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro."; Mol. Cell. Biol. 24:3324-3336(2004).
[19]	FUNCTION. DOI=10.1073/pnas.0401493101; PubMed=15136722 [NCBI, ExPASy, EBI, Israel, Japan] Mandal S.S., Chu C., Wada T., Handa H., Shatkin A.J., Reinberg D.; "Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II."; Proc. Natl. Acad. Sci. U.S.A. 101:7572-7577(2004).
[20]	FUNCTION. DOI=10.1073/pnas.0409405102; PubMed=16214896 [NCBI, ExPASy, EBI, Israel, Japan] Palangat M., Renner D.B., Price D.H., Landick R.; "A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS."; Proc. Natl. Acad. Sci. U.S.A. 102:15036-15041(2005).

Comments

FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences.
SUBUNIT: Interacts with SUPT5H to form DSIF. DSIF interacts with the positive transcription elongation factor b complex (P-TEFb complex), which is composed of CDK9 and cyclin-T (CCNT1 or CCNT2). DSIF interacts with RNA polymerase II, and this interaction is reduced by phosphorylation of the C-terminal domain (CTD) of POLR2A by P-TEFb. DSIF also interacts with the NELF complex, which is composed of WHSC2/NELFA, COBRA1/NELFB, TH1L/NELFD and RDBP/NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. DSIF also interacts with HRMT1L2/PRMT1, HTATSF1/TATSF1, RNGTT/CAP1A, SKB1/PRMT5, SUPT6H, and can interact with PIN1.
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Widely expressed.
SIMILARITY: Belongs to the SPT4 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U38818; AAB18674.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U38817; AAB18675.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U43923; AAB07814.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK129758; BAC85230.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407663; CAG28591.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002802; AAH02802.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_003159.1; -.

UniGene

Hs.439481

3D structure databases

ModBase

P63272.

Enzyme and pathway databases

Reactome

REACT_1788; Transcription.
REACT_1892; Elongation arrest and recovery.
REACT_6143; Pausing and recovery of Tat-mediated HIV-1 elongation.
REACT_6185; HIV Infection.
REACT_6244; Pausing and recovery of HIV-1 elongation.
REACT_6259; HIV-1 elongation arrest and recovery.
REACT_6344; Tat-mediated HIV-1 elongation arrest and recovery.
REACT_71; Gene Expression.
REACT_769; Pausing and recovery of elongation.

Organism-specific databases

H-InvDB

HIX0014029; -.

HGNC

HGNC:11467; SUPT4H1.

GeneLynx

SUPT4H1; Homo sapiens.

GenAtlas

SUPT4H1.

MIM

603555; gene. [NCBI / EBI]

PharmGKB

PA36253; -.

GeneCards

P63272.

Gene expression databases

ArrayExpress

P63272; -.

CleanEx

HS_SUPT4H1; -.

GermOnline

ENSG00000108375; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0008148;	Molecular function: negative transcription elongation factor activity (inferred from direct assay from UniProtKB).
GO:0008159;	Molecular function: positive transcription elongation factor activity (inferred from direct assay from UniProtKB).
GO:0046982;	Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0003700;	Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0006338;	Biological process: chromatin remodeling (traceable author statement from ProtInc).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0045944;	Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0006368;	Biological process: RNA elongation from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR009287; Spt4.
IPR016046; Spt4-like.
Graphical view of domain structure.

PANTHER

PTHR12882; Spt4; 1.

Pfam

PF06093; Spt4; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF025023; Spt4; 1.

BLOCKS

P63272.

Proteomic databases

PeptideAtlas

P63272; -.

Genome annotation databases

Ensembl

ENSG00000213246; Homo sapiens. [Contig view]

GeneID

6827; -.

KEGG

hsa:6827; -.

Other

LinkHub

P63272; -.

SOURCE

SUPT4H1; Homo sapiens.

ProtoNet

P63272.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Activator; Metal-binding; Nucleus; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 117`	`117`	`Transcription elongation factor SPT4.`	`PRO_0000210325`
`ZN_FING`	`16 36`	`21`	`C4-type (Potential).`
`REGION`	`1 40`	`40`	`Interaction with SUPT5H.`
`CONFLICT`	`95 117`		`QGIVRELKSRGVAYKSRDTAIKT -> HAKDSRSNVNKYEPRESSEGHDTCLASLFHSLRHSN` `SLFAL (in Ref. 3; BAC85230).`

Sequence information

Length: 117 AA [This is the length of the unprocessed precursor]

Molecular weight: 13193 Da [This is the MW of the unprocessed precursor]

CRC64: 09EDF007501D0F03 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI 

        70         80         90        100        110 
IAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE LKSRGVAYKS RDTAIKT

P63272 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools