Search Results

Overview

Uniprot ID	P43243
Protein Name	Matrin-3
Gene Name	MATR3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
146	PQILLQLKRRRTEEG
181	PRDDWEEKRHFRRDS
245	ETSHNYHKFDSEYER
3	*****MSKSFQQSSL
473	VRVHLSQKYKRIKKP
491	PDQKFDQKQELGRVI
522	KLAEPYGKIKNYILM
524	AEPYGKIKNYILMRM
554	AMVDHCLKKALWFQG
555	MVDHCLKKALWFQGR
571	VKVDLSEKYKKLVLR
588	NRGIDLLKKDKSRKR
589	RGIDLLKKDKSRKRS
617	SKTDGSQKTESSTEG
698	GKKEPSDKAVKKDGS
711	GSASAAAKKKLKKVD
716	AAKKKLKKVDKIEEL
719	KKLKKVDKIEELDQE
836	KLKKFLNKLAEERRQ

Function

May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. 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). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233)

Protein Sequence

10 MSKSFQQSSL 20 SRDSQGHGRD 30 LSAAGIGLLA 40 AATQSLSMPA 50 SLGRMNQGTA 60 RLASLMNLGM 70 SSSLNQQGAH 80 SALSSASTSS 90 HNLQSIFNIG 100 SRGPLPLSSQ 110 HRGDADQASN 120 ILASFGLSAR 130 DLDELSRYPE 140 DKITPENLPQ 150 ILLQLKRRRT 160 EEGPTLSYGR 170 DGRSATREPP 180 YRVPRDDWEE 190 KRHFRRDSFD 200 DRGPSLNPVL 210 DYDHGSRSQE 220 SGYYDRMDYE 230 DDRLRDGERC 240 RDDSFFGETS 250 HNYHKFDSEY 260 ERMGRGPGPL 270 QERSLFEKKR 280 GAPPSSNIED 290 FHGLLPKGYP 300 HLCSICDLPV 310 HSNKEWSQHI 320 NGASHSRRCQ 330 LLLEIYPEWN 340 PDNDTGHTMG 350 DPFMLQQSTN 360 PAPGILGPPP 370 PSFHLGGPAV 380 GPRGNLGAGN 390 GNLQGPRHMQ 400 KGRVETSRVV 410 HIMDFQRGKN 420 LRYQLLQLVE 430 PFGVISNHLI 440 LNKINEAFIE 450 MATTEDAQAA 460 VDYYTTTPAL 470 VFGKPVRVHL 480 SQKYKRIKKP 490 EGKPDQKFDQ 500 KQELGRVIHL 510 SNLPHSGYSD 520 SAVLKLAEPY 530 GKIKNYILMR 540 MKSQAFIEME 550 TREDAMAMVD 560 HCLKKALWFQ 570 GRCVKVDLSE 580 KYKKLVLRIP 590 NRGIDLLKKD 600 KSRKRSYSPD 610 GKESPSDKKS 620 KTDGSQKTES 630 STEGKEQEEK 640 SGEDGEKDTK 650 DDQTEQEPNM 660 LLESEDELLV 670 DEEEAAALLE 680 SGSSVGDETD 690 LANLGDVASD 700 GKKEPSDKAV 710 KKDGSASAAA 720 KKKLKKVDKI 730 EELDQENEAA 740 LENGIKNEEN 750 TEPGAESSEN 760 ADDPNKDTSE 770 NADGQSDENK 780 DDYTIPDEYR 790 IGPYQPNVPV 800 GIDYVIPKTG 810 FYCKLCSLFY 820 TNEEVAKNTH 830 CSSLPHYQKL 840 KKFLNKLAEE RRQKKET

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005637	nuclear inner membrane
Cellular Component	GO:0016363	nuclear matrix
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0035198	miRNA binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0005198	structural molecule activity
Molecular Function	GO:0008270	zinc ion binding
Biological Process	GO:0002218	activation of innate immune response
Biological Process	GO:0003170	heart valve development
Biological Process	GO:0045087	innate immune response
Biological Process	GO:0010608	post-transcriptional regulation of gene expression
Biological Process	GO:0003281	ventricular septum development

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] 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.

[9] 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.

[10] 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.

[11] 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.