Q9BTM1 (H2AJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 78.
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: Histone H2A.J Short name=H2a/j | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 129 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Core component of nucleosome. 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. |
| 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. The octamer wraps approximately 147 bp of DNA. |
| Subcellular location | Nucleus By similarity. Chromosome By similarity. |
| Post-translational modification | Monoubiquitination of Lys-120 gives a specific tag for epigenetic transcriptional repression By similarity. Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription By similarity. |
| Sequence similarities | Belongs to the histone H2A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosome Nucleosome core Nucleus |
| Coding sequence diversity | Alternative splicing |
| Ligand | DNA-binding |
| PTM | Acetylation Isopeptide bond Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | nucleosome assembly Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9BTM1-1) 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 2 (identifier: Q9BTM1-2) The sequence of this isoform differs from the canonical sequence as follows: 119-129: KKTESQKTKSK → VCEHSGPSSGKIPSDRAELGAGSVCGHIFQKVE |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 129 | 128 | Histone H2A.J | PRO_0000344247 | |||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 2 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 6 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 96 | 1 | N6-acetyllysine Ref.4 | ||||||
| Cross-link | 120 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
Natural variations | |||||||||
| Alternative sequence | 119 – 129 | 11 | KKTESQKTKSK → VCEHSGPSSGKIPSDRAELG AGSVCGHIFQKVE in isoform 2. | VSP_034750 | |||||
Sequences
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References
| [1] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Ovarian carcinoma. |
| [2] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye. |
| [4] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK001765 mRNA. Translation: BAA91894.1. CH471094 Genomic DNA. Translation: EAW96326.1. BC003602 mRNA. Translation: AAH03602.1. |
| IPI | IPI00102165. IPI00220855. |
| RefSeq | NP_808760.1. NM_177925.2. |
| UniGene | Hs.524280. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TZY based on UniProtKB P02263. |
| ProteinModelPortal | Q9BTM1. |
| SMR | Q9BTM1. Positions 14-119. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9BTM1. |
PTM databases | |
| PhosphoSite | Q9BTM1. |
Polymorphism databases | |
| DMDM | 74733131. |
Proteomic databases | |
| PRIDE | Q9BTM1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000389078; ENSP00000373730; ENSG00000111332. |
| GeneID | 55766. |
| KEGG | hsa:55766. |
| UCSC | uc009zia.1. human. |
Organism-specific databases | |
| CTD | 55766. |
| GeneCards | GC12P014827. |
| HGNC | HGNC:14456. H2AFJ. |
| neXtProt | NX_Q9BTM1. |
| PharmGKB | PA29108. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG15995. |
| GeneTree | ENSGT00590000082849. |
| HOVERGEN | HBG009342. |
| PhylomeDB | Q9BTM1. |
Gene expression databases | |
| ArrayExpress | Q9BTM1. |
| Bgee | Q9BTM1. |
| CleanEx | HS_H2AFJ. |
| Genevestigator | Q9BTM1. |
Family and domain databases | |
| InterPro | IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view] |
| Gene3D | G3DSA:1.10.20.10. Histone-fold. 1 hit. |
| KO | K11251. |
| Pfam | PF00125. Histone. 1 hit. [Graphical view] |
| PRINTS | PR00620. HISTONEH2A. |
| SMART | SM00414. H2A. 1 hit. [Graphical view] |
| SUPFAM | SSF47113. Histone-fold. 1 hit. |
| PROSITE | PS00046. HISTONE_H2A. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 60813. |
Entry information
| Entry name | H2AJ_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9BTM1 Secondary accession number(s): Q9NV63 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| SIMILARITY comments Index of protein domains and families |

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