MTA2 | ENSG00000149480 | NCBI 9219

Details for: MTA2

Gene ID: 9219

Symbol: MTA2

Ensembl ID: ENSG00000149480

Description: metastasis associated 1 family member 2

Associated with

Chromatin modifying enzymes
(R-HSA-3247509)
Disease
(R-HSA-1643685)
Epigenetic regulation of gene expression
(R-HSA-212165)
Ercc6 (csb) and ehmt2 (g9a) positively regulate rrna expression
(R-HSA-427389)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hdacs deacetylate histones
(R-HSA-3214815)
Infectious disease
(R-HSA-5663205)
Intracellular signaling by second messengers
(R-HSA-9006925)
Pip3 activates akt signaling
(R-HSA-1257604)
Positive epigenetic regulation of rrna expression
(R-HSA-5250913)
Potential therapeutics for sars
(R-HSA-9679191)
Pten regulation
(R-HSA-6807070)
Regulation of pten gene transcription
(R-HSA-8943724)
Regulation of tp53 activity
(R-HSA-5633007)
Regulation of tp53 activity through acetylation
(R-HSA-6804758)
Rna polymerase ii transcription
(R-HSA-73857)
Rna polymerase i promoter clearance
(R-HSA-73854)
Rna polymerase i transcription
(R-HSA-73864)
Rna polymerase i transcription initiation
(R-HSA-73762)
Sars-cov infections
(R-HSA-9679506)
Signal transduction
(R-HSA-162582)
Transcriptional regulation by tp53
(R-HSA-3700989)
Viral infection pathways
(R-HSA-9824446)
Chromatin
(GO:0000785)
Chromatin organization
(GO:0006325)
Chromatin remodeling
(GO:0006338)
Chromosome, telomeric region
(GO:0000781)
Dna methylation
(GO:0006306)
Histone deacetylase activity
(GO:0004407)
Histone deacetylase binding
(GO:0042826)
Histone deacetylase complex
(GO:0000118)
Membrane
(GO:0016020)
Metal ion binding
(GO:0046872)
Negative regulation of dna-templated transcription
(GO:0045892)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nucleoplasm
(GO:0005654)
Nucleosomal dna binding
(GO:0031492)
Nucleus
(GO:0005634)
Nurd complex
(GO:0016581)
Positive regulation of dna-templated transcription
(GO:0045893)
Positive regulation of transcription by rna polymerase ii
(GO:0045944)
Protein-containing complex
(GO:0032991)
Protein binding
(GO:0005515)
Regulation of cell fate specification
(GO:0042659)
Regulation of fibroblast migration
(GO:0010762)
Regulation of stem cell differentiation
(GO:2000736)
Rna polymerase ii-specific dna-binding transcription factor binding
(GO:0061629)
Sequence-specific dna binding
(GO:0043565)
Transcription coactivator activity
(GO:0003713)
Transcription corepressor activity
(GO:0003714)
Transcription regulator complex
(GO:0005667)

Other Information

Proteins

Metastasis-associated protein MTA2

Genular Protein ID: 1421960127

Symbol: MTA2_HUMAN

Name: Metastasis-associated protein MTA2

UniProtKB Accession Codes:

O94776 Q68DB1 Q9UQB5

Database IDs:

Citations:

PubMed ID: 9929979

Title: Molecular cloning, mapping and characterization of a novel human gene, MTA1-L1. showing homology to a metastasis-associated gene, MTA1.

PubMed ID: 9929979

DOI: 10.1007/s100380050107

PubMed ID: 11099047

Title: Deacetylation of p53 modulates its effect on cell growth and apoptosis.

PubMed ID: 11099047

DOI: 10.1038/35042612

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 16554811

Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.

PubMed ID: 16554811

DOI: 10.1038/nature04632

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11331609

Title: Sharp, an inducible cofactor that integrates nuclear receptor repression and activation.

PubMed ID: 11331609

DOI: 10.1101/gad.871201

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16428440

Title: MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties.

PubMed ID: 16428440

DOI: 10.1128/mcb.26.3.843-851.2006

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18757745

Title: RCS1, a substrate of APC/C, controls the metaphase to anaphase transition.

PubMed ID: 18757745

DOI: 10.1073/pnas.0709227105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21965678

Title: SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function.

PubMed ID: 21965678

DOI: 10.1074/jbc.m111.267237

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 22926524

Title: RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene.

PubMed ID: 22926524

DOI: 10.1038/onc.2012.386

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26030138

Title: Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.

PubMed ID: 26030138

DOI: 10.1371/journal.pone.0128558

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 28977666

Title: CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality.

PubMed ID: 28977666

DOI: 10.1093/nar/gkx711

PubMed ID: 33283408

Title: Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex.

PubMed ID: 33283408

DOI: 10.1111/febs.15650

Sequence Information:

Length: 668
Mass: 75023
Checksum: 65087AF798BA64EC
Sequence:

MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD 
SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILSQY 
LEKEDCFFYS LVFDPVQKTL LADQGEIRVG CKYQAEIPDR LVEGESDNRN QQKMEMKVWD 
PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR 
NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL 
ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG 
FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGATRGTTEP 
HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR 
RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT 
PINRNQLSQN RGLGGIMVKR AYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD 
APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLIAVRPPVP LPAPSHPAST 
NEPIVLED

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: MTA2

Associated with

Other Information

Molecular cloning, mapping and characterization of a novel human gene, MTA1-L1. showing homology to a metastasis-associated gene, MTA1. PubMed ID: 9929979

Deacetylation of p53 modulates its effect on cell growth and apoptosis. PubMed ID: 11099047

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

Human chromosome 11 DNA sequence and analysis including novel gene identification. PubMed ID: 16554811

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. PubMed ID: 11331609

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties. PubMed ID: 16428440

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

RCS1, a substrate of APC/C, controls the metaphase to anaphase transition. PubMed ID: 18757745

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function. PubMed ID: 21965678

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene. PubMed ID: 22926524

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics. PubMed ID: 26030138

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality. PubMed ID: 28977666

Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex. PubMed ID: 33283408