Details for: MACROH2A1

Gene ID: 9555

Symbol: MACROH2A1

Ensembl ID: ENSG00000113648

Description: macroH2A.1 histone

Associated with

Other Information

Genular Protein ID: 1969928789

Symbol: H2AY_HUMAN

Name: Core histone macro-H2A.1

UniProtKB Accession Codes:

O75367 O75377 Q503A8 Q7Z5E3 Q96D41 Q9H8P3 Q9UP96

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 3 CDD 2 CORUM 1 CPTAC 2 CTD 1 ChEBI 16 ChiTaRS 1 DIP 1 DNASU 1 DisGeNET 1 ELM 1 EMBL 8 EPD 1 Ensembl 4 EvolutionaryTrace 1 ExpressionAtlas 1 GO 50 Gene3D 2 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 HGNC 2 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 8 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MalaCards 1 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PDB 19 PDBsum 13 PIRSF 1 PRIDE 1 PRINTS 1 PRO 1 PROSITE 1 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 3 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 3 Pumba 1 RNAct 1 RefSeq 6 SAM 1 SIGNOR 1 SMART 2 SMR 1 STRING 1 SUPFAM 2 SWISS-2DPAGE 1 SignaLink 1 SwissPalm 1 TopDownProteomics 2 TreeFam 1 UCSC 1 UniProtKB 3 VEuPathDB 1 eggNOG 2 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 9714746

Title: Isolation of cDNA clones encoding human histone macroH2A1 subtypes.

PubMed ID: 9714746

DOI: 10.1016/s0167-4781(98)00098-0

PubMed ID: 9653160

Title: Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning.

PubMed ID: 9653160

DOI: 10.1073/pnas.95.14.8175

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

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: 12800201

Title: Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries.

PubMed ID: 12800201

DOI: 10.1002/ijc.11208

PubMed ID: 9634239

Title: Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals.

PubMed ID: 9634239

DOI: 10.1038/31275

PubMed ID: 12718888

Title: The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling.

PubMed ID: 12718888

DOI: 10.1016/s1097-2765(03)00100-x

PubMed ID: 16129414

Title: Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain.

PubMed ID: 16129414

DOI: 10.1016/j.bbrc.2005.08.046

PubMed ID: 15621527

Title: Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA.

PubMed ID: 15621527

DOI: 10.1016/j.devcel.2004.10.019

PubMed ID: 15902274

Title: The macro domain is an ADP-ribose binding module.

PubMed ID: 15902274

DOI: 10.1038/sj.emboj.7600664

PubMed ID: 15897469

Title: Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase.

PubMed ID: 15897469

DOI: 10.1073/pnas.0408918102

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: 16428466

Title: Mechanism of polymerase II transcription repression by the histone variant macroH2A.

PubMed ID: 16428466

DOI: 10.1128/mcb.26.3.1156-1164.2006

PubMed ID: 16210244

Title: Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry.

PubMed ID: 16210244

DOI: 10.1074/mcp.m500285-mcp200

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

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: 20068231

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

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21211722

Title: DNA repair factor APLF is a histone chaperone.

PubMed ID: 21211722

DOI: 10.1016/j.molcel.2010.12.008

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: 23022728

Title: Splicing switch of an epigenetic regulator by RNA helicases promotes tumor-cell invasiveness.

PubMed ID: 23022728

DOI: 10.1038/nsmb.2390

PubMed ID: 23186163

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

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23474714

Title: Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.

PubMed ID: 23474714

DOI: 10.1038/nsmb.2521

PubMed ID: 29905837

Title: DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface.

PubMed ID: 29905837

DOI: 10.1093/nar/gky507

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: 16107708

Title: Structural characterization of the histone variant macroH2A.

PubMed ID: 16107708

DOI: 10.1128/mcb.25.17.7616-7624.2005

PubMed ID: 15965484

Title: Splicing regulates NAD metabolite binding to histone macroH2A.

PubMed ID: 15965484

DOI: 10.1038/nsmb956

PubMed ID: 19818708

Title: Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases.

PubMed ID: 19818708

DOI: 10.1016/j.molcel.2009.09.022

Sequence Information:

  • Length: 369
  • Mass: 39184
  • Checksum: D21A4CE6C7AA3BB1
  • Sequence:
    • MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI 
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS 
KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA 
DGFTVLSTKS LFLGQKLQVV QADIASIDSD AVVHPTNTDF YIGGEVGNTL EKKGGKEFVE 
AVLELRKKNG PLEVAGAAVS AGHGLPAKFV IHCNSPVWGA DKCEELLEKT VKNCLALADD 
KKLKSIAFPS IGSGRNGFPK QTAAQLILKA ISSYFVSTMS SSIKTVYFVL FDSESIGIYV 
QEMAKLDAN

Genular Protein ID: 4176396830

Symbol: A0A994J4J7_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A994J4J7

Database IDs:

ARBA 6 CDD 1 CTD 1 EMBL 1 EPD 1 Ensembl 2 GO 5 Gene3D 1 GeneTree 1 HGNC 1 InterPro 4 MaxQB 1 NCBI Taxonomy 1 PANTHER 2 PRINTS 1 Pfam 4 Proteomes 2 RefSeq 1 RuleBase 1 SAM 1 SMART 1 SMR 1 SUPFAM 1

Citations:

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

Sequence Information:

  • Length: 199
  • Mass: 21045
  • Checksum: 09179AC79704AB54
  • Sequence:
    • MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI 
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS 
KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA 
DGFTVLSTKS LFLGQKPPQ

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.