ID:SPT5H_HUMAN DESCRIPTION: RecName: Full=Transcription elongation factor SPT5; Short=hSPT5; AltName: Full=DRB sensitivity-inducing factor 160 kDa subunit; Short=DSIF p160; AltName: Full=DRB sensitivity-inducing factor large subunit; Short=DSIF large subunit; AltName: Full=Tat-cotransactivator 1 protein; Short=Tat-CT1 protein; 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 SUPT4H1 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 PRMT1/HRMT1L2, HTATSF1/TATSF1, RNGTT/CAP1A, PRMT5/SKB1, SUPT6H, and can interact with PIN1. Component of a complex which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. INTERACTION: P24928:POLR2A; NbExp=2; IntAct=EBI-710464, EBI-295301; P62937:PPIA; NbExp=2; IntAct=EBI-710464, EBI-437708; P63272:SUPT4H1; NbExp=3; IntAct=EBI-710464, EBI-727250; SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Ubiquitously expressed. PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II. PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing and can stimulate transcriptional elongation from the HIV-1 LTR. P-TEFb dependent phosphorylation is stimulated by the HIV-1 Tat protein. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis. SIMILARITY: Belongs to the SPT5 family. SIMILARITY: Contains 5 KOW domains. SEQUENCE CAUTION: Sequence=BAD92494.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O00267
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000122 negative regulation of transcription from RNA polymerase II promoter GO:0006351 transcription, DNA-templated GO:0006355 regulation of transcription, DNA-templated GO:0006357 regulation of transcription from RNA polymerase II promoter GO:0006366 transcription from RNA polymerase II promoter GO:0006368 transcription elongation from RNA polymerase II promoter GO:0006370 7-methylguanosine mRNA capping GO:0016239 positive regulation of macroautophagy GO:0032784 regulation of DNA-templated transcription, elongation GO:0032785 negative regulation of DNA-templated transcription, elongation GO:0032786 positive regulation of DNA-templated transcription, elongation GO:0045944 positive regulation of transcription from RNA polymerase II promoter GO:1900364 negative regulation of mRNA polyadenylation
AB000516 - Homo sapiens mRNA for DSIF p160, complete cds. AK295137 - Homo sapiens cDNA FLJ52493 complete cds, highly similar to Transcription elongation factor SPT5. AK296117 - Homo sapiens cDNA FLJ54005 complete cds, highly similar to Transcription elongation factor SPT5. AK302954 - Homo sapiens cDNA FLJ55629 complete cds, highly similar to Transcription elongation factor SPT5. Y12790 - H.sapiens mRNA for supt5h protein. U56402 - Human chromatin structural protein homolog (SUPT5H) mRNA, complete cds. BC024203 - Homo sapiens suppressor of Ty 5 homolog (S. cerevisiae), mRNA (cDNA clone MGC:3826 IMAGE:3532191), complete cds. AB209257 - Homo sapiens mRNA for suppressor of Ty 5 homolog variant protein. AF040253 - Homo sapiens transcription factor Tat-CT1 mRNA, complete cds. JD106484 - Sequence 87508 from Patent EP1572962. AB463294 - Synthetic construct DNA, clone: pF1KB4095, Homo sapiens SUPT5H gene for suppressor of Ty 5 homolog, without stop codon, in Flexi system. DQ896795 - Synthetic construct Homo sapiens clone IMAGE:100011255; FLH199443.01L; RZPDo839H0981D suppressor of Ty 5 homolog (S. cerevisiae) (SUPT5H) gene, encodes complete protein. KJ897624 - Synthetic construct Homo sapiens clone ccsbBroadEn_07018 SUPT5H gene, encodes complete protein. AK303480 - Homo sapiens cDNA FLJ61516 complete cds, highly similar to Transcription elongation factor SPT5. AK091476 - Homo sapiens cDNA FLJ34157 fis, clone FCBBF3013506, highly similar to H.sapiens mRNA for supt5h protein. AF052165 - Homo sapiens clone 24522 mRNA sequence. JD255887 - Sequence 236911 from Patent EP1572962. JD087589 - Sequence 68613 from Patent EP1572962. JD402541 - Sequence 383565 from Patent EP1572962.
Biochemical and Signaling Pathways
Reactome (by CSHL, EBI, and GO)
Protein O00267 (Reactome details) participates in the following event(s):
R-HSA-77073 SPT5 subunit of Pol II binds the RNA triphosphatase (RTP) R-HSA-112434 Formation of DSIF complex R-HSA-167153 SPT5 subunit of Pol II binds the RNA triphosphatase (RTP) R-HSA-77090 Methylation of GMP-cap by RNA Methyltransferase R-HSA-77077 Capping complex formation R-HSA-113407 DSIF complex binds to RNA Pol II (hypophosphorylated) R-HSA-167083 DSIF complex binds to RNA Pol II (hypophosphorylated) R-HSA-113429 Elongating transcript encounters a lesion in the template R-HSA-77078 Hydrolysis of the 5'-end of the nascent transcript by the capping enzyme R-HSA-77081 Formation of the CE:GMP intermediate complex R-HSA-77085 Dissociation of transcript with 5'-GMP from GT R-HSA-77083 Transfer of GMP from the capping enzyme GT site to 5'-end of mRNA R-HSA-113402 Formation of DSIF:NELF:early elongation complex R-HSA-112379 Recruitment of elongation factors to form elongation complex R-HSA-112381 Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex R-HSA-113411 2-4 nt.backtracking of Pol II complex on the template leading to elongation pausing R-HSA-113412 Pol II elongation complex moves on the template as transcript elongates R-HSA-113414 7-14 nt. Backtracking of Pol II complex on the template leading to elongation arrest R-HSA-112385 Addition of nucleotides leads to transcript elongation R-HSA-112392 Resumption of elongation after recovery from pausing R-HSA-113413 TFIIS-mediated recovery of elongation from arrest R-HSA-112395 Abortive termination of elongation after arrest R-HSA-112396 Separation of elongating transcript from template R-HSA-167085 Formation of DSIF:NELF:HIV-1 early elongation complex R-HSA-167150 Resumption of elongation of HIV-1 transcript after recovery from pausing R-HSA-167076 2-4 nt.backtracking of Pol II complex on the HIV-1 template leading to elongation pausing R-HSA-167077 Recruitment of elongation factors to form HIV-1 elongation complex R-HSA-167084 Hyperphosphorylation (Ser2) of RNA Pol II CTD by P-TEFb complex R-HSA-167282 2-4 nt.backtracking of Pol II complex on the HIV-1 template leading to elongation pausing R-HSA-167284 7-14 nt. Backtracking of Pol II complex on the HIV-1 template leading to elongation arrest R-HSA-167288 TFIIS-mediated recovery of HIV-1 elongation from arrest R-HSA-167292 Resumption of elongation of HIV-1 transcript after recovery from pausing R-HSA-167148 TFIIS-mediated recovery of elongation from arrest R-HSA-167459 Abortive termination of HIV-1 elongation after arrest (Tat-containing elongation complex) R-HSA-167090 7-14 nt. Backtracking of Pol II complex on the HIV-1 template leading to elongation arrest R-HSA-170706 Phosphorylation of NEFL by the P-TEFb(Cyclin T1:Cdk9) complex R-HSA-167191 Hyperphosphorylation (Ser2) of RNA Pol II CTD by the P-TEFb(Cyclin T1:Cdk9) complex R-HSA-167192 Pol II elongation complex moves on the HIV-1 template as transcript elongates R-HSA-167181 Addition of nucleotides leads to HIV-1 transcript elongation R-HSA-167197 Separation of elongating HIV-1 transcript from template R-HSA-167481 Abortive termination of HIV-1 elongation after arrest R-HSA-170704 Phosphorylation of DSIF by the P-TEFb(Cyclin T1:Cdk9) complex R-HSA-167196 Recruitment of elongation factors to form HIV-1 elongation complex R-HSA-113409 Abortive termination of early transcription elongation by DSIF:NELF R-HSA-167087 Limited elongation of the HIV-1 transcript R-HSA-167478 Abortive termination of HIV-1 early transcription elongation by DSIF:NELF R-HSA-167147 Separation of abortive HIV-1 transcript from template R-HSA-6797616 CCNK:CDK12 binds RNA Pol II at DNA repair genes R-HSA-6797606 CDK12 phosphorylates RNA Pol II CTD at DNA repair genes R-HSA-72086 mRNA Capping R-HSA-77075 RNA Pol II CTD phosphorylation and interaction with CE R-HSA-674695 RNA Polymerase II Pre-transcription Events R-HSA-167160 RNA Pol II CTD phosphorylation and interaction with CE during HIV infection R-HSA-113418 Formation of the Early Elongation Complex R-HSA-167158 Formation of the HIV-1 Early Elongation Complex R-HSA-8953854 Metabolism of RNA R-HSA-73857 RNA Polymerase II Transcription R-HSA-167172 Transcription of the HIV genome R-HSA-112382 Formation of RNA Pol II elongation complex R-HSA-75955 RNA Polymerase II Transcription Elongation R-HSA-167238 Pausing and recovery of Tat-mediated HIV elongation R-HSA-167152 Formation of HIV elongation complex in the absence of HIV Tat R-HSA-167290 Pausing and recovery of HIV elongation R-HSA-167287 HIV elongation arrest and recovery R-HSA-167243 Tat-mediated HIV elongation arrest and recovery R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat R-HSA-167246 Tat-mediated elongation of the HIV-1 transcript R-HSA-167169 HIV Transcription Elongation R-HSA-74160 Gene expression (Transcription) R-HSA-162599 Late Phase of HIV Life Cycle R-HSA-167242 Abortive elongation of HIV-1 transcript in the absence of Tat R-HSA-6796648 TP53 Regulates Transcription of DNA Repair Genes R-HSA-162587 HIV Life Cycle R-HSA-3700989 Transcriptional Regulation by TP53 R-HSA-162906 HIV Infection R-HSA-212436 Generic Transcription Pathway R-HSA-5663205 Infectious disease R-HSA-1643685 Disease
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
