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DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A (PubMed:15136722). DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter (PubMed:10199401, PubMed:10912001, PubMed:11112772). Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex (PubMed:10199401, PubMed:10912001, PubMed:11112772). DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II (PubMed:10199401, PubMed:10912001, PubMed:11112772). TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme (PubMed:16214896). 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 (PubMed:16214896). 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 (PubMed:11112772). 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 (PubMed:11112772)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10075709"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10757782"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12653964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12718890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15060154"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19860741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28892040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9450929"}],"value":"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 (Pol II); forms DNA and RNA clamps that stabilize Pol II elongation complex while maintaining the nontemplate DNA strand in the transcription bubble and nascent RNA in the exit channel. 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 NELFA, NELFB, NELFD and NELFE, and this interaction occurs following prior binding of DSIF to RNA polymerase II. DSIF also interacts with PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P63272","intActId":"EBI-727250"},"interactantTwo":{"uniProtKBAccession":"O00267","geneName":"SUPT5H","intActId":"EBI-710464"},"numberOfExperiments":17,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8649394"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8649394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8786137"}],"value":"Widely expressed"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37478862"}],"value":"Ubiquitinated by UBR5 when not assembled in the DSIF complex, leading to its 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