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Overview

Uniprot ID	Q99856
Protein Name	AT-rich interactive domain-containing protein 3A
Gene Name	ARID3A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
176	TTALFPRKAQPPQAF

Function

Transcription factor which may be involved in the control of cell cycle progression by the RB1/E2F1 pathway and in B-cell differentiation

Protein Sequence

10 MKLQAVMETL 20 LQRQQRARQE 30 LEARQQLPPD 40 PPAAPPGRAR 50 AAPDEDREPE 60 SARMQRAQMA 70 ALAAMRAAAA 80 GLGHPASPGG 90 SEDGPPGSEE 100 EDAAREGTPG 110 SPGRGREGPG 120 EEHFEDMASD 130 EDMKPKWEEE 140 EMEEDLGEDE 150 EEEEEDYEDE 160 EEEEDEEGLG 170 PPGPASLGTT 180 ALFPRKAQPP 190 QAFRGDGVPR 200 VLGGQERPGP 210 GPAHPGGAAH 220 VAPQLQPPDH 230 GDWTYEEQFK 240 QLYELDGDPK 250 RKEFLDDLFS 260 FMQKRGTPVN 270 RIPIMAKQVL 280 DLFMLYVLVT 290 EKGGLVEVIN 300 KKLWREITKG 310 LNLPTSITSA 320 AFTLRTQYMK 330 YLYPYECEKR 340 GLSNPNELQA 350 AIDSNRREGR 360 RQSFGGSLFA 370 YSPGGAHGML 380 SSPKLPVSSL 390 GLAASTNGSS 400 ITPAPKIKKE 410 EDSAIPITVP 420 GRLPVSLAGH 430 PVVAAQAAAV 440 QAAAAQAAVA 450 AQAAALEQLR 460 EKLESAEPPE 470 KKMALVADEQ 480 QRLMQRALQQ 490 NFLAMAAQLP 500 MSIRINSQAS 510 ESRQDSAVNL 520 TGTNGSNSIS 530 MSVEINGIMY 540 TGVLFAQPPA 550 PTPTSAPNKG 560 GGGGGGSSSN 570 AGGRGGNTGT 580 SGGQAGPAGL 590 STPSTSTSNN SLP

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0045121	membrane raft
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0003682	chromatin binding
Molecular Function	GO:0003677	DNA binding
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0003712	transcription coregulator activity
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:0006357	regulation of 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] 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.

[5] 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.

[6] 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.

[7] 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.