Search Results

Overview

Uniprot IDO00267
Protein NameTranscription elongation factor SPT5
Gene NameSUPT5H
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
143 ELGEYYMKKYAKSSV
144 LGEYYMKKYAKSSVG
147 YYMKKYAKSSVGETV
323 IKARMSLKDWFAKRK
601 IHVKDIVKVIDGPHS
650 LVLAGGSKPRDVTNF
718 RISQGPYKGYIGVVK

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)

Protein Sequence

10 MSDSEDSNFS 20 EEEDSERSSD 30 GEEAEVDEER 40 RSAAGSEKEE 50 EPEDEEEEEE 60 EEEYDEEEEE 70 EDDDRPPKKP 80 RHGGFILDEA 90 DVDDEYEDED 100 QWEDGAEDIL 110 EKEEIEASNI 120 DNVVLDEDRS 130 GARRLQNLWR 140 DQREEELGEY 150 YMKKYAKSSV 160 GETVYGGSDE 170 LSDDITQQQL 180 LPGVKDPNLW 190 TVKCKIGEER 200 ATAISLMRKF 210 IAYQFTDTPL 220 QIKSVVAPEH 230 VKGYIYVEAY 240 KQTHVKQAIE 250 GVGNLRLGYW 260 NQQMVPIKEM 270 TDVLKVVKEV 280 ANLKPKSWVR 290 LKRGIYKDDI 300 AQVDYVEPSQ 310 NTISLKMIPR 320 IDYDRIKARM 330 SLKDWFAKRK 340 KFKRPPQRLF 350 DAEKIRSLGG 360 DVASDGDFLI 370 FEGNRYSRKG 380 FLFKSFAMSA 390 VITEGVKPTL 400 SELEKFEDQP 410 EGIDLEVVTE 420 STGKEREHNF 430 QPGDNVEVCE 440 GELINLQGKI 450 LSVDGNKITI 460 MPKHEDLKDM 470 LEFPAQELRK 480 YFKMGDHVKV 490 IAGRFEGDTG 500 LIVRVEENFV 510 ILFSDLTMHE 520 LKVLPRDLQL 530 CSETASGVDV 540 GGQHEWGELV 550 QLDPQTVGVI 560 VRLERETFQV 570 LNMYGKVVTV 580 RHQAVTRKKD 590 NRFAVALDSE 600 QNNIHVKDIV 610 KVIDGPHSGR 620 EGEIRHLFRS 630 FAFLHCKKLV 640 ENGGMFVCKT 650 RHLVLAGGSK 660 PRDVTNFTVG 670 GFAPMSPRIS 680 SPMHPSAGGQ 690 RGGFGSPGGG 700 SGGMSRGRGR 710 RDNELIGQTV 720 RISQGPYKGY 730 IGVVKDATES 740 TARVELHSTC 750 QTISVDRQRL 760 TTVGSRRPGG 770 MTSTYGRTPM 780 YGSQTPMYGS 790 GSRTPMYGSQ 800 TPLQDGSRTP 810 HYGSQTPLHD 820 GSRTPAQSGA 830 WDPNNPNTPS 840 RAEEEYEYAF 850 DDEPTPSPQA 860 YGGTPNPQTP 870 GYPDPSSPQV 880 NPQYNPQTPG 890 TPAMYNTDQF 900 SPYAAPSPQG 910 SYQPSPSPQS 920 YHQVAPSPAG 930 YQNTHSPASY 940 HPTPSPMAYQ 950 ASPSPSPVGY 960 SPMTPGAPSP 970 GGYNPHTPGS 980 GIEQNSSDWV 990 TTDIQVKVRD 1000 TYLDTQVVGQ 1010 TGVIRSVTGG 1020 MCSVYLKDSE 1030 KVVSISSEHL 1040 EPITPTKNNK 1050 VKVILGEDRE 1060 ATGVLLSIDG 1070 EDGIVRMDLD 1080 EQLKILNLRF LGKLLEA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0032044 DSIF complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0032785 negative regulation of DNA-templated transcription, elongation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0032786 positive regulation of DNA-templated transcription, elongation
Biological Process GO:0016239 positive regulation of macroautophagy
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0032968 positive regulation of transcription elongation by RNA polymerase II
Biological Process GO:0034243 regulation of transcription elongation by RNA polymerase II
Biological Process GO:0006368 transcription elongation by RNA polymerase II
Biological Process GO:0160239 transcription pausing by RNA polymerase II

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[3] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.