Search Results

Overview

Uniprot IDQ96HW7
Protein NameIntegrator complex subunit 4
Gene NameINTS4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
26 PQEEIATKKLRLTKP
27 QEEIATKKLRLTKPS
35 LRLTKPSKSAALHID
353 GEFSSGRKWGDDAPK

Function

Component of the integrator complex, a multiprotein complex that terminates RNA polymerase II (Pol II) transcription in the promoter-proximal region of genes (PubMed:29471365, PubMed:33243860, PubMed:33548203, PubMed:38570683). The integrator complex provides a quality checkpoint during transcription elongation by driving premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: the complex terminates transcription by (1) catalyzing dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, (2) degrading the exiting nascent RNA transcript via endonuclease activity and (3) promoting the release of Pol II from bound DNA (PubMed:33243860, PubMed:38570683). The integrator complex is also involved in terminating the synthesis of non-coding Pol II transcripts, such as enhancer RNAs (eRNAs), small nuclear RNAs (snRNAs), telomerase RNAs and long non-coding RNAs (lncRNAs) (PubMed:16239144). Within the integrator complex, INTS4 acts as an scaffold that links INTS9 and INTS11 (PubMed:29471365, PubMed:33548203). Mediates recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the integrator complex (PubMed:23904267)

Protein Sequence

10 MAAHLKKRVY 20 EEFTKVVQPQ 30 EEIATKKLRL 40 TKPSKSAALH 50 IDLCKATSPA 60 DALQYLLQFA 70 RKPVEAESVE 80 GVVRILLEHY 90 YKENDPSVRL 100 KIASLLGLLS 110 KTAGFSPDCI 120 MDDAINILQN 130 EKSHQVLAQL 140 LDTLLAIGTK 150 LPENQAIQMR 160 LVDVACKHLT 170 DTSHGVRNKC 180 LQLLGNLGSL 190 EKSVTKDAEG 200 LAARDVQKII 210 GDYFSDQDPR 220 VRTAAIKAML 230 QLHERGLKLH 240 QTIYNQACKL 250 LSDDYEQVRS 260 AAVQLIWVVS 270 QLYPESIVPI 280 PSSNEEIRLV 290 DDAFGKICHM 300 VSDGSWVVRV 310 QAAKLLGSME 320 QVSSHFLEQT 330 LDKKLMSDLR 340 RKRTAHERAK 350 ELYSSGEFSS 360 GRKWGDDAPK 370 EEVDTGAVNL 380 IESGACGAFV 390 HGLEDEMYEV 400 RIAAVEALCM 410 LAQSSPSFAE 420 KCLDFLVDMF 430 NDEIEEVRLQ 440 SIHTMRKISN 450 NITLREDQLD 460 TVLAVLEDSS 470 RDIREALHEL 480 LCCTNVSTKE 490 GIHLALVELL 500 KNLTKYPTDR 510 DSIWKCLKFL 520 GSRHPTLVLP 530 LVPELLSTHP 540 FFDTAEPDMD 550 DPAYIAVLVL 560 IFNAAKTCPT 570 MPALFSDHTF 580 RHYAYLRDSL 590 SHLVPALRLP 600 GRKLVSSAVS 610 PSIIPQEDPS 620 QQFLQQSLER 630 VYSLQHLDPQ 640 GAQELLEFTI 650 RDLQRLGELQ 660 SELAGVADFS 670 ATYLRCQLLL 680 IKALQEKLWN 690 VAAPLYLKQS 700 DLASAAAKQI 710 MEETYKMEFM 720 YSGVENKQVV 730 IIHHMRLQAK 740 ALQLIVTART 750 TRGLDPLFGM 760 CEKFLQEVDF 770 FQRYFIADLP 780 HLQDSFVDKL 790 LDLMPRLMTS 800 KPAEVVKILQ 810 TMLRQSAFLH 820 LPLPEQIHKA 830 SATIIEPAGE 840 SDNPLRFTSG 850 LVVALDVDAT 860 LEHVQDPQNT 870 VKVQVLYPDG 880 QAQMIHPKPA 890 DFRNPGPGRH 900 RLITQVYLSH 910 TAWTEACQVE 920 VRLLLAYNSS 930 ARIPKCPWME 940 GGEMSPQVET 950 SIEGTIPFSK 960 PVKVYIMPKP ARR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0160232 INTAC complex
Cellular Component GO:0032039 integrator complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Biological Process GO:0034243 regulation of transcription elongation by RNA polymerase II
Biological Process GO:0160240 RNA polymerase II transcription initiation surveillance
Biological Process GO:0016180 snRNA processing

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] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] 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.

[4] 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.

[5] 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.

[6] 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.