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Reviewed, UniProtKB/Swiss-Prot P63272 (SPT4H_HUMAN)

Last modified September 2, 2008. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Transcription elongation factor SPT4
      Short name=hSPT4
Alternative name(s):
    DRB sensitivity-inducing factor small subunit
      Short name=DSIF small subunit
    DSIF p14
Gene names
Name: SUPT4H1
Synonyms: SPT4H, SUPT4H
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (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 structure

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.

Sequence similarities

Belongs to the SPT4 family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

SUPT5HO002673EBI-727250,EBI-710464

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 117117Transcription elongation factor SPT4

Regions

Zinc finger16 – 3621C4-type Potential
Region1 – 4040Interaction with SUPT5H

Experimental info

Sequence conflict95 – 11723QGIVR…TAIKT → HAKDSRSNVNKYEPRESSEG HDTCLASLFHSLRHSNSLFA L in BAC85230. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P63272-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 09EDF007501D0F03

FASTA11713,193
        10         20         30         40         50         60 
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI 

        70         80         90        100        110 
IAMMSPEDSW VSKWQRVSNF KPGVYAVSVT GRLPQGIVRE LKSRGVAYKS RDTAIKT

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References

« Hide 'large scale' references
[1]"Isolation and characterization of the human and mouse homologues (SUPT4H and Supt4h) of the yeast SPT4 gene."
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.
Genomics 34:368-375(1996) [PubMed: 8786137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Identification and analysis of a functional human homolog of the SPT4 gene of Saccharomyces cerevisiae."
Hartzog G.A., Basrai M.A., Ricupero-Hovasse S.L., Hieter P., Winston F.
Mol. Cell. Biol. 16:2848-2856(1996) [PubMed: 8649394] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Dermoid cancer.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[6]"Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro."
Wada T., Takagi T., Yamaguchi Y., Watanabe D., Handa H.
EMBO J. 17:7395-7403(1998) [PubMed: 9857195] [Abstract]
Cited for: FUNCTION.
[7]"DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs."
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.
Genes Dev. 12:343-356(1998) [PubMed: 9450929] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUPT5H.
[8]"NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation."
Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S., Hasegawa J., Handa H.
Cell 97:41-51(1999) [PubMed: 10199401] [Abstract]
Cited for: FUNCTION.
[9]"Structure and function of the human transcription elongation factor DSIF."
Yamaguchi Y., Wada T., Watanabe D., Takagi T., Hasegawa J., Handa H.
J. Biol. Chem. 274:8085-8092(1999) [PubMed: 10075709] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUPT5H.
[10]"Tat-SF1 protein associates with RAP30 and human SPT5 proteins."
Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.
Mol. Cell. Biol. 19:5960-5968(1999) [PubMed: 10454543] [Abstract]
Cited for: FUNCTION.
[11]"FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH."
Wada T., Orphanides G., Hasegawa J., Kim D.-K., Shima D., Yamaguchi Y., Fukuda A., Hisatake K., Oh S., Reinberg D., Handa H.
Mol. Cell 5:1067-1072(2000) [PubMed: 10912001] [Abstract]
Cited for: FUNCTION.
[12]"Domains in the SPT5 protein that modulate its transcriptional regulatory properties."
Ivanov D., Kwak Y.T., Guo J., Gaynor R.B.
Mol. Cell. Biol. 20:2970-2983(2000) [PubMed: 10757782] [Abstract]
Cited for: INTERACTION WITH SUPT5H.
[13]"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."
Ping Y.-H., Rana T.M.
J. Biol. Chem. 276:12951-12958(2001) [PubMed: 11112772] [Abstract]
Cited for: FUNCTION.
[14]"A highly purified RNA polymerase II elongation control system."
Renner D.B., Yamaguchi Y., Wada T., Handa H., Price D.H.
J. Biol. Chem. 276:42601-42609(2001) [PubMed: 11553615] [Abstract]
Cited for: FUNCTION.
[15]"Structure-function analysis of human Spt4: evidence that hSpt4 and hSpt5 exert their roles in transcriptional elongation as parts of the DSIF complex."
Kim D.-K., Inukai N., Yamada T., Furuya A., Sato H., Yamaguchi Y., Wada T., Handa H.
Genes Cells 8:371-378(2003) [PubMed: 12653964] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUPT5H.
[16]"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.
Mol. Cell 11:1055-1066(2003) [PubMed: 12718890] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SUPT5H.
[17]"Locus-specific requirements for Spt5 in transcriptional activation and repression in Drosophila."
Jennings B.H., Shah S., Yamaguchi Y., Seki M., Phillips R.G., Handa H., Ish-Horowicz D.
Curr. Biol. 14:1680-1684(2004) [PubMed: 15380072] [Abstract]
Cited for: FUNCTION.
[18]"Human Spt6 stimulates transcription elongation by RNA polymerase II in vitro."
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.
Mol. Cell. Biol. 24:3324-3336(2004) [PubMed: 15060154] [Abstract]
Cited for: INTERACTION WITH SUPT5H.
[19]"Functional interactions of RNA-capping enzyme with factors that positively and negatively regulate promoter escape by RNA polymerase II."
Mandal S.S., Chu C., Wada T., Handa H., Shatkin A.J., Reinberg D.
Proc. Natl. Acad. Sci. U.S.A. 101:7572-7577(2004) [PubMed: 15136722] [Abstract]
Cited for: FUNCTION.
[20]"A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS."
Palangat M., Renner D.B., Price D.H., Landick R.
Proc. Natl. Acad. Sci. U.S.A. 102:15036-15041(2005) [PubMed: 16214896] [Abstract]
Cited for: FUNCTION.

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Cross-references

Sequence databases

U38818 mRNA. Translation: AAB18674.1.
U38817 mRNA. Translation: AAB18675.1.
U43923 mRNA. Translation: AAB07814.1.
AK129758 mRNA. Translation: BAC85230.1.
CR407663 mRNA. Translation: CAG28591.1.
BC002802 mRNA. Translation: AAH02802.1.
RefSeqNP_003159.1.
UniGeneHs.439481

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP63272.

Proteomic databases

PeptideAtlasP63272.

Genome annotation databases

EnsemblENSG00000213246. Homo sapiens. [Contig view]
GeneID6827.
KEGGhsa:6827.

Organism-specific databases

H-InvDBHIX0014029.
HGNCHGNC:11467. SUPT4H1.
MIM603555. gene.
PharmGKBPA36253.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP63272.

Enzyme and pathway databases

ReactomeREACT_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.

Gene expression databases

ArrayExpressP63272.
CleanExHS_SUPT4H1.
GermOnlineENSG00000108375. Homo sapiens.

Family and domain databases

InterProIPR009287. Spt4.
IPR016046. Spt4-like.
[Graphical view]
PANTHERPTHR12882. Spt4. 1 hit.
PfamPF06093. Spt4. 1 hit.
[Graphical view]
PIRSFPIRSF025023. Spt4. 1 hit.
ProDomP63272.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubP63272.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameSPT4H_HUMAN
AccessionPrimary (citable) accession number: P63272
Secondary accession number(s): Q16550, Q62387, Q6ZP89
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: September 2, 2008
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents