Q02874 (H2AY_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 113.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Core histone macro-H2A.1 Short name=Histone macroH2A1 Short name=mH2A1 Alternative name(s): H2A.y H2A/y | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 371 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation. Ref.5 |
| Subunit structure | The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. Interacts with SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with HDAC1 and HDAC2 By similarity. |
| Subcellular location | Nucleus By similarity. Chromosome By similarity. Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin By similarity. |
| Tissue specificity | Isoform 1 is present only in liver and brain, whereas isoform 2 is present in brain, thymus, testis, liver and kidney (at protein level). Ref.3 |
| Post-translational modification | Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin By similarity. |
| Sequence similarities | Contains 1 histone H2A domain. Contains 1 Macro domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosome Nucleosome core Nucleus |
| Coding sequence diversity | Alternative splicing |
| Ligand | DNA-binding |
| Molecular function | Chromatin regulator |
| PTM | Isopeptide bond Methylation Phosphoprotein Ubl conjugation |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW dosage compensationInferred from electronic annotation. Source: Compara nucleosome assemblyInferred from electronic annotation. Source: InterPro |
| Cellular_component | Barr body Inferred from electronic annotation. Source: Compara condensed chromosomeInferred from electronic annotation. Source: Compara nucleosomeInferred from direct assay Ref.1. Source: RGD |
| Molecular_function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin bindingInferred from electronic annotation. Source: Compara |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 2 (identifier: Q02874-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 1 (identifier: Q02874-2) The sequence of this isoform differs from the canonical sequence as follows: 197-228: NLIHSEISNLAGFEVEAIINPTNADIDLKDDL → QVVQADIASIDSDAVVHPTNADFYIGGEV |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 371 | 371 | Core histone macro-H2A.1 | PRO_0000055319 | ||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||
| Domain | 2 – 117 | 116 | Histone H2A | |||||||||||||||||||||||||||
| Domain | 183 – 369 | 187 | Macro | |||||||||||||||||||||||||||
| Compositional bias | 118 – 161 | 44 | Lys-rich | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 18 | 1 | N6-methyllysine By similarity | |||||||||||||||||||||||||||
| Modified residue | 129 | 1 | Phosphothreonine By similarity | |||||||||||||||||||||||||||
| Modified residue | 169 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||
| Modified residue | 172 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||
| Cross-link | 116 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity | ||||||||||||||||||||||||||||
| Cross-link | 117 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity | ||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||
| Alternative sequence | 197 – 228 | 32 | NLIHS…LKDDL → QVVQADIASIDSDAVVHPTN ADFYIGGEV in isoform 1. | VSP_002057 | ||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 184 – 189 | 6 | ||||||||||||||||||||||||||||
| Helix | 229 – 251 | 23 | ||||||||||||||||||||||||||||
| Beta strand | 259 – 263 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 267 – 275 | 9 | ||||||||||||||||||||||||||||
| Helix | 285 – 302 | 18 | ||||||||||||||||||||||||||||
| Beta strand | 306 – 310 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 314 – 316 | 3 | ||||||||||||||||||||||||||||
| Helix | 322 – 337 | 16 | ||||||||||||||||||||||||||||
| Beta strand | 347 – 351 | 5 | ||||||||||||||||||||||||||||
| Helix | 355 – 365 | 11 | ||||||||||||||||||||||||||||
| Turn | 366 – 369 | 4 | ||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "MacroH2A, a core histone containing a large nonhistone region." Pehrson J.R., Fried V.A. Science 257:1398-1400(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE. Tissue: Liver. |
| [2] | Pehrson J.R. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION (ISOFORM 1). |
| [3] | "Developmental and tissue expression patterns of histone macroH2A1 subtypes." Pehrson J.R., Costanzi C., Dharia C. J. Cell. Biochem. 65:107-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Thymus. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: Brown Norway. Tissue: Kidney. |
| [5] | "Structural characterization of the histone variant macroH2A." Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., Khochbin S., Luger K. Mol. Cell. Biol. 25:7616-7624(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 181-371 (ISOFORM 1), FUNCTION. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M99065 mRNA. Translation: AAA41561.2. M99066 mRNA. Translation: AAA41560.1. U79139 mRNA. Translation: AAB38330.1. BC089093 mRNA. Translation: AAH89093.1. | ||||||||||||
| IPI | IPI00193500. IPI00231507. | ||||||||||||
| PIR | I59567. I80811. | ||||||||||||
| RefSeq | NP_058878.1. NM_017182.2. | ||||||||||||
| UniGene | Rn.11098. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q02874. | ||||||||||||
| SMR | Q02874. Positions 10-117, 180-368. | ||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q02874. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q02874. | ||||||||||||
| PRIDE | Q02874. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOT00000015632; ENSRNOP00000015632; ENSRNOG00000011523. ENSRNOT00000051702; ENSRNOP00000049143; ENSRNOG00000011523. | ||||||||||||
| GeneID | 29384. | ||||||||||||
| KEGG | rno:29384. | ||||||||||||
| UCSC | RGD:621462. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 9555. | ||||||||||||
| RGD | 621462. H2afy. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG2110. | ||||||||||||
| GeneTree | ENSGT00690000101745. | ||||||||||||
| HOGENOM | HOG000234653. | ||||||||||||
| HOVERGEN | HBG009342. | ||||||||||||
| InParanoid | Q02874. | ||||||||||||
| KO | K11251. | ||||||||||||
| OrthoDB | EOG4XH00N. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q02874. | ||||||||||||
| Genevestigator | Q02874. | ||||||||||||
| GermOnline | ENSRNOG00000011523. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 1.10.20.10. 1 hit. | ||||||||||||
| InterPro | IPR002589. A1pp. IPR021171. Core_histone_macro-H2A. IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view] | ||||||||||||
| Pfam | PF00125. Histone. 1 hit. PF01661. Macro. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF037942. Core_histone_macro-H2A. 1 hit. | ||||||||||||
| PRINTS | PR00620. HISTONEH2A. | ||||||||||||
| SMART | SM00506. A1pp. 1 hit. SM00414. H2A. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF47113. Histone-fold. 1 hit. | ||||||||||||
| PROSITE | PS51154. MACRO. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q02874. | ||||||||||||
| NextBio | 608979. | ||||||||||||
Entry information
| Entry name | H2AY_RAT | ||||||||
| Accession | Primary (citable) accession number: Q02874 Secondary accession number(s): O09140, Q63325 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
