Search Results

Overview

Uniprot IDP78347
Protein NameGeneral transcription factor II-I
Gene NameGTF2I
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
130 CYGKALGKSTVVPVP
192 KRPFLEPKKHVGGRV
219 GGSCGPIKVKTEPTE
221 SCGPIKVKTEPTEDS
343 PEPANAGKRKVREFN
353 VREFNFEKWNARITD
378 RKYAQAIKAKGPVTI
380 YAQAIKAKGPVTIPY
450 REDLQLDKPASGVKE
456 DKPASGVKEEWYARI
477 VDQLFCKKFAEALGS
561 PRTNTPVKEDWNVRI
660 LPPGMASKINTKALQ
664 MASKINTKALQSPKR
670 TKALQSPKRPRSPGS
729 SFEAWNAKITDLKQK
827 SSKSPPRKINSSPNV
92 EKAAEMHKMKSTTQA
94 AAEMHKMKSTTQANR

Function

Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation

Protein Sequence

10 MAQVAMSTLP 20 VEDEESSESR 30 MVVTFLMSAL 40 ESMCKELAKS 50 KAEVACIAVY 60 ETDVFVVGTE 70 RGRAFVNTRK 80 DFQKDFVKYC 90 VEEEEKAAEM 100 HKMKSTTQAN 110 RMSVDAVEIE 120 TLRKTVEDYF 130 CFCYGKALGK 140 STVVPVPYEK 150 MLRDQSAVVV 160 QGLPEGVAFK 170 HPENYDLATL 180 KWILENKAGI 190 SFIIKRPFLE 200 PKKHVGGRVM 210 VTDADRSILS 220 PGGSCGPIKV 230 KTEPTEDSGI 240 SLEMAAVTVK 250 EESEDPDYYQ 260 YNIQAGPSET 270 DDVDEKQPLS 280 KPLQGSHHSS 290 EGNEGTEMEV 300 PAEDSTQHVP 310 SETSEDPEVE 320 VTIEDDDYSP 330 PSKRPKANEL 340 PQPPVPEPAN 350 AGKRKVREFN 360 FEKWNARITD 370 LRKQVEELFE 380 RKYAQAIKAK 390 GPVTIPYPLF 400 QSHVEDLYVE 410 GLPEGIPFRR 420 PSTYGIPRLE 430 RILLAKERIR 440 FVIKKHELLN 450 STREDLQLDK 460 PASGVKEEWY 470 ARITKLRKMV 480 DQLFCKKFAE 490 ALGSTEAKAV 500 PYQKFEAHPN 510 DLYVEGLPEN 520 IPFRSPSWYG 530 IPRLEKIIQV 540 GNRIKFVIKR 550 PELLTHSTTE 560 VTQPRTNTPV 570 KEDWNVRITK 580 LRKQVEEIFN 590 LKFAQALGLT 600 EAVKVPYPVF 610 ESNPEFLYVE 620 GLPEGIPFRS 630 PTWFGIPRLE 640 RIVRGSNKIK 650 FVVKKPELVI 660 SYLPPGMASK 670 INTKALQSPK 680 RPRSPGSNSK 690 VPEIEVTVEG 700 PNNNNPQTSA 710 VRTPTQTNGS 720 NVPFKPRGRE 730 FSFEAWNAKI 740 TDLKQKVENL 750 FNEKCGEALG 760 LKQAVKVPFA 770 LFESFPEDFY 780 VEGLPEGVPF 790 RRPSTFGIPR 800 LEKILRNKAK 810 IKFIIKKPEM 820 FETAIKESTS 830 SKSPPRKINS 840 SPNVNTTASG 850 VEDLNIIQVT 860 IPDDDNERLS 870 KVEKARQLRE 880 QVNDLFSRKF 890 GEAIGMGFPV 900 KVPYRKITIN 910 PGCVVVDGMP 920 PGVSFKAPSY 930 LEISSMRRIL 940 DSAEFIKFTV 950 IRPFPGLVIN 960 NQLVDQSESE 970 GPVIQESAEP 980 SQLEVPATEE 990 IKETDGSSQI KQEPDPTW

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific
Molecular Function GO:0003700 DNA-binding transcription factor activity
Molecular Function GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Biological Process GO:0016525 negative regulation of angiogenesis
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0006366 transcription by RNA polymerase II

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[6] 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.

[7] 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.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] 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.

[10] 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.

[11] 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.

[12] 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.