SUPT5H
entrez
6829
canonical
uniprot
O00267
canonical
ensembl
ENSG00000196235
resolver
ensp
ENSP00000384505
resolver
ensp
ENSP00000404029
resolver
ensp
ENSP00000469090
resolver
ensp
ENSP00000616339
resolver
genesymbol
SUPT5H
resolver
genesymbol_syn
SPT5
resolver
genesymbol_syn
SPT5H
resolver
hgnc
HGNC:11469
resolver
uniprot
O43279
resolver
uniprot
Q59G52
resolver
uniprot
Q99639
resolver
uniprot_entry
SPT5H_HUMAN
resolver
uniprot_sec
O43279
resolver
uniprot_sec
Q59G52
resolver
uniprot_sec
Q99639
resolver
amino_acid_sequence
MSDSEDSNFSEEEDSERSSDGEEAEVDEERRSAAGSEKEEEPEDEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKILSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPQTVGVIVRLERETFQVLNMYGKVVTVRHQAVTRKKDNRFAVALDSEQNNIHVKDIVKVIDGPHSGREGEIRHLFRSFAFLHCKKLVENGGMFVCKTRHLVLAGGSKPRDVTNFTVGGFAPMSPRISSPMHPSAGGQRGGFGSPGGGSGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQVVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIVRMDLDEQLKILNLRFLGKLLEA
uniprot
proteins
function
FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A (PubMed:10075709, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter (PubMed:10075709, PubMed:10199401, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex (PubMed:10075709, PubMed:10199401, PubMed:10421630, PubMed:10757782, PubMed:10912001, PubMed:11112772, PubMed:11553615, PubMed:12653964, PubMed:12718890, PubMed:15136722, PubMed:15380072, PubMed:9450929, PubMed:9857195). DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II (PubMed:16214896). 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). Following phosphorylation by CDK9, DSIF can also positively regulate transcriptional elongation (PubMed:16427012). Required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat (PubMed:10393184, PubMed:10454543, PubMed:11809800, PubMed:9514752). 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, PubMed:14701750). {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10421630, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:16427012, ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9514752, ECO:0000269|PubMed:9857195}.
uniprot
proteins
mass_dalton
121000
uniprot
proteins
mutagenesis
MUTAGEN 246; /note="R->A: Reduces the affinity for Pol II elongation complex; when associated with A-247, A-249, A-250 and A-251."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 247; /note="L->A: Reduces the affinity for Pol II elongation complex; when associated with A-246, A-249, A-250 and A-251."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 249; /note="Y->A: Reduces the affinity for Pol II elongation complex; when associated with A-246, A-247, A-250 and A-251."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 250; /note="W->A: Reduces the affinity for Pol II elongation complex; when associated with A-246, A-247, A-249 and A-251."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 251; /note="N->A: Reduces the affinity for Pol II elongation complex; when associated with A-246, A-247, A-249 and A-250."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 577; /note="R->A: Reduces the affinity for Pol II elongation complex; when associated with A-578, A-579 and A-582."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 577; /note="R->E: Reduces the affinity for Pol II elongation complex; when associated with E-578, E-579 and E-582."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 578; /note="K->A: Reduces the affinity for Pol II elongation complex; when associated with A-577, A-579 and A-582."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 578; /note="K->E: Reduces the affinity for Pol II elongation complex; when associated with E-577, E-579 and E-582."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 579; /note="K->A: Reduces the affinity for Pol II elongation complex; when associated with A-577, A-578 and A-582."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 579; /note="K->E: Reduces the affinity for Pol II elongation complex; when associated with E-577, E-578 and E-582."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 582; /note="R->A: Reduces the affinity for Pol II elongation complex; when associated with A-577, A-578 and A-579."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 582; /note="R->E: Reduces the affinity for Pol II elongation complex; when associated with E-577, E-578 and E-579."; /evidence="ECO:0000269|PubMed:28892040"; MUTAGEN 681; /note="R->A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698."; /evidence="ECO:0000269|PubMed:12718890"; MUTAGEN 681; /note="R->K: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698."; /evidence="ECO:0000269|PubMed:12718890"; MUTAGEN 696; /note="R->A: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698."; /evidence="ECO:0000269|PubMed:12718890"; MUTAGEN 696; /note="R->K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698."; /evidence="ECO:0000269|PubMed:12718890"; MUTAGEN 698; /note="R->A: Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696."; /evidence="ECO:0000269|PubMed:12718890"; MUTAGEN 698; /note="R->K: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696."; /evidence="ECO:0000269|PubMed:12718890"; MUTAGEN 775; /note="T->A: Decreased ability to promote transcription elongation; when associated with A-784, A-791, A-799, A-806 and A-814."; /evidence="ECO:0000269|PubMed:16427012"; MUTAGEN 784; /note="T->A: Decreased ability to promote transcription elongation; when associated with A-775, A-791, A-799, A-806 and A-814."; /evidence="ECO:0000269|PubMed:16427012"; MUTAGEN 791; /note="T->A: Decreased ability to promote transcription elongation; when associated with A-775, A-784, A-799, A-806 and A-814."; /evidence="ECO:0000269|PubMed:16427012"; MUTAGEN 799; /note="T->A: Decreased ability to promote transcription elongation; when associated with A-775, A-784, A-791, A-806 and A-814."; /evidence="ECO:0000269|PubMed:16427012"; MUTAGEN 806; /note="T->A: Decreased ability to promote transcription elongation; when associated with A-775, A-784, A-791, A-799 and A-814."; /evidence="ECO:0000269|PubMed:16427012"; MUTAGEN 814; /note="T->A: Decreased ability to promote transcription elongation; when associated with A-775, A-784, A-791, A-799 and A-806."; /evidence="ECO:0000269|PubMed:16427012"; MUTAGEN 1002; /note="G->D: Defective in regulation of transcriptional elongation."; /evidence="ECO:0000269|PubMed:15380072
uniprot
proteins
post_translational_modification
PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II. {ECO:0000269|PubMed:12718890}.; PTM: Phosphorylated by CDK7 and CDK9 (PubMed:10757782, PubMed:11112772, PubMed:11145967, PubMed:11809800, PubMed:15564463, PubMed:16327805). Phosphorylation by P-TEFb (CDK9) at Thr residues of the C-terminal repeats alleviates transcriptional pausing and promotes transcription elongation (PubMed:11112772, PubMed:11145967, PubMed:11809800, PubMed:15564463). Dephosphorylated by the INTAC complex when transcripts are unfavorably configured for transcriptional elongation, leading to premature transcription termination: dephosphorylation is mediated by the PPP2CA component of the INTAC complex (PubMed:34004147). Dephosphorylated by the PNUTS-PP1 complex in termination zones downstream of poly(A) sites, thereby promoting deceleration of RNA polymerase II transcription (PubMed:34004147). Phosphorylation may also stimulate interaction with PIN1 (PubMed:11575923). Bulk phosphorylation occurs predominantly in mitosis (PubMed:9199507). Phosphorylation by P-TEFb can stimulate transcriptional elongation from the HIV-1 LTR (PubMed:11112772, PubMed:11145967, PubMed:11809800, PubMed:15564463). P-TEFb dependent phosphorylation is stimulated by the HIV-1 Tat protein (PubMed:11112772). {ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:15564463, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:34004147, ECO:0000269|PubMed:9199507}.; PTM: Ubiquitinated by UBR5 when not assembled in the DSIF complex, leading to its degradation: UBR5 recognizes and binds a degron that is not accessible when SUPT5H is part of the DSIF complex. {ECO:0000269|PubMed:37478862}.
uniprot
proteins
protein_family
SPT5 family
uniprot
proteins
pubmed
10075709
uniprot
proteins
pubmed
10199401
uniprot
proteins
pubmed
10393184
uniprot
proteins
pubmed
10421630
uniprot
proteins
pubmed
10454543
uniprot
proteins
pubmed
10757782
uniprot
proteins
pubmed
10912001
uniprot
proteins
pubmed
11112772
uniprot
proteins
pubmed
11145967
uniprot
proteins
pubmed
11553615
uniprot
proteins
pubmed
11575923
uniprot
proteins
pubmed
11809800
uniprot
proteins
pubmed
11940650
uniprot
proteins
pubmed
12612062
uniprot
proteins
pubmed
12653964
uniprot
proteins
pubmed
12718890
uniprot
proteins
pubmed
14701750
uniprot
proteins
pubmed
15060154
uniprot
proteins
pubmed
15136722
uniprot
proteins
pubmed
15380072
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15564463
uniprot
proteins
pubmed
16214896
uniprot
proteins
pubmed
16327805
uniprot
proteins
pubmed
16427012
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19860741
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23652018
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28892040
uniprot
proteins
pubmed
31677974
uniprot
proteins
pubmed
34004147
uniprot
proteins
pubmed
37478862
uniprot
proteins
pubmed
8975720
uniprot
proteins
pubmed
9199507
uniprot
proteins
pubmed
9450929
uniprot
proteins
pubmed
9514752
uniprot
proteins
pubmed
9857195
uniprot
proteins
sequence_length
1087
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10075709}.
uniprot
proteins