Hmdb loader

Showing Protein Histone H2A type 2-B (HMDBP07730)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP07730
Secondary Accession Numbers
  • 13439
Name Histone H2A type 2-B
Synonyms Not Available
Gene Name HIST2H2AB
Protein Type Unknown
Biological Properties
General Function Involved in DNA binding
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
macromolecular complex
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
nucleosome
protein-dna complex
Function
binding
nucleic acid binding
dna binding
Process
cellular process
cellular component organization at cellular level
organelle organization
chromosome organization
chromatin organization
nucleosome assembly
nucleosome organization
Cellular Location
  1. Nucleus
  2. Chromosome
Gene Properties
Chromosome Location Chromosome:1
Locus 1q21
SNPs HIST2H2AB
Gene Sequence 
>393 bp
ATGTCAGGACGCGGAAAGCAGGGAGGCAAGGCCCGCGCTAAGGCCAAGTCGCGCTCGTCC
CGCGCTGGTCTCCAGTTCCCGGTGGGGCGAGTGCACCGCTTGCTGCGCAAAGGCAACTAC
GCGGAGCGGGTCGGGGCAGGCGCCCCGGTGTACCTGGCGGCGGTCCTCGAGTACCTGACC
GCGGAAATTCTGGAGCTGGCGGGCAACGCGGCTCGGGACAACAAGAAGACGCGCATCATC
CCTCGCCATCTGCAACTAGCCGTGAGGAATGACGAAGAGCTCAACAAGTTACTCGGGGGT
GTCACCATTGCCCAGGGCGGCGTCTTGCCCAATATCCAGGCTGTCCTGTTGCCCAAGAAA
ACGGAGAGTCACAAGCCTGGCAAGAACAAGTAA
Protein Properties
Number of Residues 130
Molecular Weight 13995.2
Theoretical pI 11.53
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Histone H2A type 2-B
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKK
TESHKPGKNK
GenBank ID Protein 24496255
UniProtKB/Swiss-Prot ID Q8IUE6
UniProtKB/Swiss-Prot Entry Name H2A2B_HUMAN
PDB IDs
GenBank Gene ID AY131972
GeneCard ID HIST2H2AB
GenAtlas ID HIST2H2AB
HGNC ID HGNC:20508
References
General References
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  4. Zhang Y, Griffin K, Mondal N, Parvin JD: Phosphorylation of histone H2A inhibits transcription on chromatin templates. J Biol Chem. 2004 May 21;279(21):21866-72. Epub 2004 Mar 9. [PubMed:15010469 ]
  5. Mailand N, Bekker-Jensen S, Faustrup H, Melander F, Bartek J, Lukas C, Lukas J: RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell. 2007 Nov 30;131(5):887-900. Epub 2007 Nov 20. [PubMed:18001824 ]
  6. Huen MS, Grant R, Manke I, Minn K, Yu X, Yaffe MB, Chen J: RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell. 2007 Nov 30;131(5):901-14. Epub 2007 Nov 20. [PubMed:18001825 ]
  7. Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, Pepperkok R, Ellenberg J, Panier S, Durocher D, Bartek J, Lukas J, Lukas C: RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell. 2009 Feb 6;136(3):435-46. doi: 10.1016/j.cell.2008.12.041. [PubMed:19203579 ]
  8. Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ: The human and mouse replication-dependent histone genes. Genomics. 2002 Nov;80(5):487-98. [PubMed:12408966 ]
  9. Aihara H, Nakagawa T, Yasui K, Ohta T, Hirose S, Dhomae N, Takio K, Kaneko M, Takeshima Y, Muramatsu M, Ito T: Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo. Genes Dev. 2004 Apr 15;18(8):877-88. Epub 2004 Apr 12. [PubMed:15078818 ]
  10. Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y: Role of histone H2A ubiquitination in Polycomb silencing. Nature. 2004 Oct 14;431(7010):873-8. Epub 2004 Sep 22. [PubMed:15386022 ]
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