CPLM-009731

Genbank Nucleotide ID

Transcription elongation factor SPT4

Protein Synonyms/Alias

hSPT4; DRB sensitivity-inducing factor 14 kDa subunit; DSIF p14; DRB sensitivity-inducing factor small subunit; DSIF small subunit

Homo sapiens (Human)

Position	Peptide	Type	References
8	MALETVPKDLRHLRA	ubiquitination	[1, 2, 3, 4, 5]
43	CDAYLQMKGNREMVY	ubiquitination	[4, 6]
81	WQRVSNFKPGVYAVS	ubiquitination	[2, 3, 4, 5, 7]

[1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]

Functional Description

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.

ZN_FING 16 36 C4-type (Potential).
REGION 1 40 Interaction with SUPT5H.

3D-structure; Activator; Complete proteome; Metal-binding; Nucleus; Reference proteome; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0032044; C:DSIF complex; IDA:UniProtKB.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0006338; P:chromatin remodeling; TAS:ProtInc.
GO:0032785; P:negative regulation of DNA-dependent transcription, elongation; IDA:UniProtKB.
GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IEA:Compara.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO:0032786; P:positive regulation of DNA-dependent transcription, elongation; IDA:UniProtKB.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
GO:0022415; P:viral reproductive process; TAS:Reactome.

IPR009287; Spt4.
IPR016046; Spt4-like.
IPR022800; Spt4/RpoE2_Znf.