Search Results

Overview

Uniprot IDO94776
Protein NameMetastasis-associated protein MTA2
Gene NameMTA2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
460 TFLLQTTKLTRLARR
504 IRLPKAAKTPLKIHP
508 KAAKTPLKIHPLVRL
522 LPLATIVKDLVAQAP
531 LVAQAPLKPKTPRGT
533 AQAPLKPKTPRGTKT
539 PKTPRGTKTPINRNQ
559 GLGGIMVKRAYETMA
592 SSSQPAAKRQKLNPA
595 QPAAKRQKLNPADAP
618 KDTRALRKALTHLEM

Function

May function as a transcriptional coregulator (PubMed:16428440, PubMed:28977666). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666)

Protein Sequence

10 MAANMYRVGD 20 YVYFENSSSN 30 PYLVRRIEEL 40 NKTANGNVEA 50 KVVCLFRRRD 60 ISSSLNSLAD 70 SNAREFEEES 80 KQPGVSEQQR 90 HQLKHRELFL 100 SRQFESLPAT 110 HIRGKCSVTL 120 LNETDILSQY 130 LEKEDCFFYS 140 LVFDPVQKTL 150 LADQGEIRVG 160 CKYQAEIPDR 170 LVEGESDNRN 180 QQKMEMKVWD 190 PDNPLTDRQI 200 DQFLVVARAV 210 GTFARALDCS 220 SSIRQPSLHM 230 SAAAASRDIT 240 LFHAMDTLQR 250 NGYDLAKAMS 260 TLVPQGGPVL 270 CRDEMEEWSA 280 SEAMLFEEAL 290 EKYGKDFNDI 300 RQDFLPWKSL 310 ASIVQFYYMW 320 KTTDRYIQQK 330 RLKAAEADSK 340 LKQVYIPTYT 350 KPNPNQIISV 360 GSKPGMNGAG 370 FQKGLTCESC 380 HTTQSAQWYA 390 WGPPNMQCRL 400 CASCWIYWKK 410 YGGLKTPTQL 420 EGATRGTTEP 430 HSRGHLSRPE 440 AQSLSPYTTS 450 ANRAKLLAKN 460 RQTFLLQTTK 470 LTRLARRMCR 480 DLLQPRRAAR 490 RPYAPINANA 500 IKAECSIRLP 510 KAAKTPLKIH 520 PLVRLPLATI 530 VKDLVAQAPL 540 KPKTPRGTKT 550 PINRNQLSQN 560 RGLGGIMVKR 570 AYETMAGAGV 580 PFSANGRPLA 590 SGIRSSSQPA 600 AKRQKLNPAD 610 APNPVVFVAT 620 KDTRALRKAL 630 THLEMRRAAR 640 RPNLPLKVKP 650 TLIAVRPPVP 660 LPAPSHPAST NEPIVLED

Gene Ontology

Classification GO ID Description
Biological Process GO:2000736 regulation of stem cell differentiation
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0000118 histone deacetylase complex
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016581 NuRD complex
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0005667 transcription regulator complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0004407 histone deacetylase activity
Molecular Function GO:0042826 histone deacetylase binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0043565 sequence-specific DNA binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006325 chromatin organization
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0042659 regulation of cell fate specification
Biological Process GO:0010762 regulation of fibroblast migration

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] 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.