Histone H2A type 1-C


NameHistone H2A type 1-C
SynonymsH2AFL Histone H2A/l
Gene NameHIST1H2AC
OrganismHuman
Amino acid sequence
>lcl|BSEQ0013488|Histone H2A type 1-C
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKK
TESHHKAKGK
Number of residues130
Molecular Weight14105.355
Theoretical pINone
GO Classification
Functions
    DNA binding
Processes
    chromatin silencing
    negative regulation of cell proliferation
    chromatin organization
Components
    nucleosome
    nucleus
    extracellular exosome
    nuclear chromatin
General FunctionDna binding
Specific FunctionCore 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ93077
UniProtKB Entry NameH2A1C_HUMAN
Cellular LocationNucleus
Gene sequence
>lcl|BSEQ0013489|Histone H2A type 1-C (HIST1H2AC)
ATGTCTGGACGTGGTAAGCAAGGAGGCAAAGCTCGCGCCAAAGCGAAATCCCGCTCTTCT
CGCGCTGGTCTCCAGTTCCCGGTGGGCCGAGTGCACCGCCTGCTCCGTAAAGGCAACTAC
GCAGAGCGGGTTGGGGCAGGCGCGCCGGTGTACCTGGCGGCGGTGTTAGAGTACCTGACC
GCCGAGATCCTGGAGCTGGCCGGCAACGCGGCTCGCGACAACAAGAAGACTCGCATCATC
CCGCGCCACTTGCAGCTGGCCATCCGCAACGACGAGGAGCTCAACAAACTGCTAGGCCGG
GTGACCATTGCTCAGGGCGGCGTCCTTCCTAACATCCAGGCCGTGCTTCTGCCTAAGAAG
ACCGAGAGTCACCACAAGGCCAAGGGCAAGTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:4733
Chromosome Location6
LocusNone
References
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  19. Tessarz P, Santos-Rosa H, Robson SC, Sylvestersen KB, Nelson CJ, Nielsen ML, Kouzarides T: Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification. Nature. 2014 Jan 23;505(7484):564-8. doi: 10.1038/nature12819. Epub 2013 Dec 18.[24352239 ]
  20. Bhatnagar S, Gazin C, Chamberlain L, Ou J, Zhu X, Tushir JS, Virbasius CM, Lin L, Zhu LJ, Wajapeyee N, Green MR: TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein. Nature. 2014 Dec 4;516(7529):116-20. doi: 10.1038/nature13955. Epub 2014 Nov 24.[25470042 ]
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