Search Results

Overview

Uniprot IDO94992
Protein NameProtein HEXIM1
Gene NameHEXIM1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
165 SKKKRHWKPYYKLTW
196 IRAEMFAKGQPVAPY
227 LKTGLYSKRAAAKSD
356 QERAPLSKFGD****

Function

Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor (PubMed:14580347, PubMed:15201869, PubMed:15713661). Core component of the 7SK RNP complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (PubMed:12832472, PubMed:14580347, PubMed:15201869, PubMed:15713661). May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity (PubMed:15940264, PubMed:15941832, PubMed:17088550). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728)

Protein Sequence

10 MAEPFLSEYQ 20 HQPQTSNCTG 30 AAAVQEELNP 40 ERPPGAEERV 50 PEEDSRWQSR 60 AFPQLGGRPG 70 PEGEGSLESQ 80 PPPLQTQACP 90 ESSCLREGEK 100 GQNGDDSSAG 110 GDFPPPAEVE 120 PTPEAELLAQ 130 PCHDSEASKL 140 GAPAAGGEEE 150 WGQQQRQLGK 160 KKHRRRPSKK 170 KRHWKPYYKL 180 TWEEKKKFDE 190 KQSLRASRIR 200 AEMFAKGQPV 210 APYNTTQFLM 220 DDHDQEEPDL 230 KTGLYSKRAA 240 AKSDDTSDDD 250 FMEEGGEEDG 260 GSDGMGGDGS 270 EFLQRDFSET 280 YERYHTESLQ 290 NMSKQELIKE 300 YLELEKCLSR 310 MEDENNRLRL 320 ESKRLGGDDA 330 RVRELELELD 340 RLRAENLQLL 350 TENELHRQQE RAPLSKFGD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0120259 7SK snRNP
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0097322 7SK snRNA binding
Molecular Function GO:0004861 cyclin-dependent protein serine/threonine kinase inhibitor activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0106140 P-TEFb complex binding
Molecular Function GO:0004860 protein kinase inhibitor activity
Molecular Function GO:0017069 snRNA binding
Molecular Function GO:0140416 transcription regulator inhibitor activity
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0045087 innate immune response
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0034244 negative regulation of transcription elongation by RNA polymerase II
Biological Process GO:0032897 negative regulation of viral transcription
Biological Process GO:1901798 positive regulation of signal transduction by p53 class mediator

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] 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.

[5] 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.