Search Results

Overview

Uniprot IDQ16666
Protein NameGamma-interferon-inducible protein 16
Gene NameIFI16
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
128 EATPGAQKRKKSTKE
190 ENPKTVAKCQVTPRR
451 KSEDTISKMNDFMRM
507 KSEDTISKMNDFMRM
561 TTLKPRLKTEPEEVS
90 KKEKLKVKGPALSRK

Function

Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer

Protein Sequence

10 MGKKYKNIVL 20 LKGLEVINDY 30 HFRMVKSLLS 40 NDLKLNLKMR 50 EEYDKIQIAD 60 LMEEKFRGDA 70 GLGKLIKIFE 80 DIPTLEDLAE 90 TLKKEKLKVK 100 GPALSRKRKK 110 EVDATSPAPS 120 TSSTVKTEGA 130 EATPGAQKRK 140 KSTKEKAGPK 150 GSKVSEEQTQ 160 PPSPAGAGMS 170 TAMGRSPSPK 180 TSLSAPPNSS 190 STENPKTVAK 200 CQVTPRRNVL 210 QKRPVIVKVL 220 STTKPFEYET 230 PEMEKKIMFH 240 ATVATQTQFF 250 HVKVLNTSLK 260 EKFNGKKIII 270 ISDYLEYDSL 280 LEVNEESTVS 290 EAGPNQTFEV 300 PNKIINRAKE 310 TLKIDILHKQ 320 ASGNIVYGVF 330 MLHKKTVNQK 340 TTIYEIQDDR 350 GKMDVVGTGQ 360 CHNIPCEEGD 370 KLQLFCFRLR 380 KKNQMSKLIS 390 EMHSFIQIKK 400 KTNPRNNDPK 410 SMKLPQEQRQ 420 LPYPSEASTT 430 FPESHLRTPQ 440 MPPTTPSSSF 450 FTKKSEDTIS 460 KMNDFMRMQI 470 LKEGSHFPGP 480 FMTSIGPAES 490 HPHTPQMPPS 500 TPSSSFLTTK 510 SEDTISKMND 520 FMRMQILKEG 530 SHFPGPFMTS 540 IGPAESHPHT 550 PQMPPSTPSS 560 SFLTTLKPRL 570 KTEPEEVSIE 580 DSAQSDLKEV 590 MVLNATESFV 600 YEPKEQKKMF 610 HATVATENEV 620 FRVKVFNIDL 630 KEKFTPKKII 640 AIANYVCRNG 650 FLEVYPFTLV 660 ADVNADRNME 670 IPKGLIRSAS 680 VTPKINQLCS 690 QTKGSFVNGV 700 FEVHKKNVRG 710 EFTYYEIQDN 720 TGKMEVVVHG 730 RLTTINCEEG 740 DKLKLTCFEL 750 APKSGNTGEL 760 RSVIHSHIKV 770 IKTRKNKKDI 780 LNPDSSMETS PDFFF

Gene Ontology

Classification GO ID Description
Biological Process GO:0006914 autophagy
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008134 transcription factor binding
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0042149 cellular response to glucose starvation
Biological Process GO:0035458 cellular response to interferon-beta
Biological Process GO:0071479 cellular response to ionizing radiation
Biological Process GO:0051607 defense response to virus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006954 inflammatory response
Biological Process GO:0045087 innate immune response
Biological Process GO:0072332 intrinsic apoptotic signaling pathway by p53 class mediator
Biological Process GO:0042771 intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
Biological Process GO:0030224 monocyte differentiation
Biological Process GO:0030099 myeloid cell differentiation
Biological Process GO:0140972 negative regulation of AIM2 inflammasome complex assembly
Biological Process GO:0043392 negative regulation of DNA binding
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0045814 negative regulation of gene expression, epigenetic
Biological Process GO:0045824 negative regulation of innate immune response
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0045071 negative regulation of viral genome replication
Biological Process GO:0001819 positive regulation of cytokine production
Biological Process GO:0032731 positive regulation of interleukin-1 beta production
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0010506 regulation of autophagy
Biological Process GO:0050727 regulation of inflammatory response

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[7] 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.

[8] 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.