Search Results

Overview

Uniprot IDQ13330
Protein NameMetastasis-associated protein MTA1
Gene NameMTA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
125 PATHIRGKCSVTLLN
462 ARSSGSPKFAMKTRQ
477 AFYLHTTKLTRIARR
527 SQSPLVLKQAVRKPL
532 VLKQAVRKPLEAVLR
567 LSSLTPAKVAPVINN
582 GSPTILGKRSYEQHN
596 NGVDGNMKKRLLMPS
597 GVDGNMKKRLLMPSR
626 RNLLLNGKSYPTKVR
631 NGKSYPTKVRLIRGG
644 GGSLPPVKRRRMNWI
670 EETRKIRKLLSSSET

Function

Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator (PubMed:16617102, PubMed:17671180, PubMed:17922032, PubMed:21965678, PubMed:24413532). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). In the NuRD complex, regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA (PubMed:17671180). In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A (PubMed:17922032, PubMed:24413532). Acts as a transcriptional coactivator of BCAS3, and SUMO2, independent of the NuRD complex (PubMed:16617102, PubMed:17671180, PubMed:21965678). Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3 (By similarity). Regulates p53-dependent and -independent DNA repair processes following genotoxic stress (PubMed:19837670). Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair (PubMed:19837670). Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles (By similarity). Positively regulates the CLOCK-BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1 (By similarity). Regulates deacetylation of BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression (By similarity). With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity)

Protein Sequence

10 MAANMYRVGD 20 YVYFENSSSN 30 PYLIRRIEEL 40 NKTANGNVEA 50 KVVCFYRRRD 60 ISSTLIALAD 70 KHATLSVCYK 80 AGPGADNGEE 90 GEIEEEMENP 100 EMVDLPEKLK 110 HQLRHRELFL 120 SRQLESLPAT 130 HIRGKCSVTL 140 LNETESLKSY 150 LEREDFFFYS 160 LVYDPQQKTL 170 LADKGEIRVG 180 NRYQADITDL 190 LKEGEEDGRD 200 QSRLETQVWE 210 AHNPLTDKQI 220 DQFLVVARSV 230 GTFARALDCS 240 SSVRQPSLHM 250 SAAAASRDIT 260 LFHAMDTLHK 270 NIYDISKAIS 280 ALVPQGGPVL 290 CRDEMEEWSA 300 SEANLFEEAL 310 EKYGKDFTDI 320 QQDFLPWKSL 330 TSIIEYYYMW 340 KTTDRYVQQK 350 RLKAAEAESK 360 LKQVYIPNYN 370 KPNPNQISVN 380 NVKAGVVNGT 390 GAPGQSPGAG 400 RACESCYTTQ 410 SYQWYSWGPP 420 NMQCRLCASC 430 WTYWKKYGGL 440 KMPTRLDGER 450 PGPNRSNMSP 460 HGLPARSSGS 470 PKFAMKTRQA 480 FYLHTTKLTR 490 IARRLCREIL 500 RPWHAARHPY 510 LPINSAAIKA 520 ECTARLPEAS 530 QSPLVLKQAV 540 RKPLEAVLRY 550 LETHPRPPKP 560 DPVKSVSSVL 570 SSLTPAKVAP 580 VINNGSPTIL 590 GKRSYEQHNG 600 VDGNMKKRLL 610 MPSRGLANHG 620 QARHMGPSRN 630 LLLNGKSYPT 640 KVRLIRGGSL 650 PPVKRRRMNW 660 IDAPDDVFYM 670 ATEETRKIRK 680 LLSSSETKRA 690 ARRPYKPIAL 700 RQSQALPPRP 710 PPPAPVNDEP IVIED

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005874 microtubule
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016581 NuRD complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0042826 histone deacetylase binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor 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:0006338 chromatin remodeling
Biological Process GO:0032922 circadian regulation of gene expression
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0043153 entrainment of circadian clock by photoperiod
Biological Process GO:0045475 locomotor rhythm
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0045814 negative regulation of gene expression, epigenetic
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:1902499 positive regulation of protein autoubiquitination
Biological Process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process GO:0042659 regulation of cell fate specification
Biological Process GO:2000736 regulation of stem cell differentiation
Biological Process GO:0010212 response to ionizing radiation
Biological Process GO:0007165 signal transduction

Reference

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[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] 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.

[7] 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.

[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] 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.