Hmdb loader

Showing Protein Histone H2A type 2-C (HMDBP01943)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP01943
Secondary Accession Numbers
  • 7354
Name Histone H2A type 2-C
Synonyms
  1. Histone H2A-GL101
  2. Histone H2A/q
Gene Name HIST2H2AC
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 1q21.2
SNPs HIST2H2AC
Gene Sequence 
>390 bp
ATGTCTGGTCGTGGCAAACAAGGAGGCAAGGCCCGCGCCAAGGCCAAGTCGCGCTCGTCC
CGCGCTGGCCTCCAGTTCCCGGTAGGGCGAGTGCACCGCTTGCTGCGCAAAGGCAACTAC
GCGGAGCGGGTGGGGGCCGGCGCGCCCGTCTACATGGCGGCGGTCCTCGAGTACCTGACC
GCCGAGATCCTGGAGCTGGCGGGCAACGCGGCTCGGGACAACAAGAAGACGCGCATCATC
CCTCGTCACCTCCAGCTGGCCATCCGCAACGACGAGGAACTGAACAAGCTGCTGGGCAAA
GTCACCATCGCCCAGGGCGGCGTTTTGCCTAACATCCAGGCCGTTCTGTTACCAAAGAAA
ACCGAAAGCCACAAAGCCAAAAGCAAATAA
Protein Properties
Number of Residues 129
Molecular Weight 13988.3
Theoretical pI 11.55
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Histone H2A type 2-C
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKK
TESHKAKSK
GenBank ID Protein 37994721
UniProtKB/Swiss-Prot ID Q16777
UniProtKB/Swiss-Prot Entry Name H2A2C_HUMAN
PDB IDs
GenBank Gene ID BC060324
GeneCard ID HIST2H2AC
GenAtlas ID HIST2H2AC
HGNC ID HGNC:4738
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES, Nakada S, Ylanko J, Olivarius S, Mendez M, Oldreive C, Wildenhain J, Tagliaferro A, Pelletier L, Taubenheim N, Durandy A, Byrd PJ, Stankovic T, Taylor AM, Durocher D: The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell. 2009 Feb 6;136(3):420-34. doi: 10.1016/j.cell.2008.12.042. [PubMed:19203578 ]
  5. 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 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. 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 ]
  10. 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 ]
  11. 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 ]
  12. Hagiwara T, Hidaka Y, Yamada M: Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes. Biochemistry. 2005 Apr 19;44(15):5827-34. [PubMed:15823041 ]
  13. Cao R, Tsukada Y, Zhang Y: Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell. 2005 Dec 22;20(6):845-54. [PubMed:16359901 ]
  14. Bergink S, Salomons FA, Hoogstraten D, Groothuis TA, de Waard H, Wu J, Yuan L, Citterio E, Houtsmuller AB, Neefjes J, Hoeijmakers JH, Vermeulen W, Dantuma NP: DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A. Genes Dev. 2006 May 15;20(10):1343-52. [PubMed:16702407 ]
  15. Boyne MT 2nd, Pesavento JJ, Mizzen CA, Kelleher NL: Precise characterization of human histones in the H2A gene family by top down mass spectrometry. J Proteome Res. 2006 Feb;5(2):248-53. [PubMed:16457589 ]
  16. Bonenfant D, Coulot M, Towbin H, Schindler P, van Oostrum J: Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry. Mol Cell Proteomics. 2006 Mar;5(3):541-52. Epub 2005 Nov 30. [PubMed:16319397 ]
  17. Braastad CD, Hovhannisyan H, van Wijnen AJ, Stein JL, Stein GS: Functional characterization of a human histone gene cluster duplication. Gene. 2004 Nov 10;342(1):35-40. [PubMed:15527963 ]
  18. Collart D, Romain PL, Huebner K, Pockwinse S, Pilapil S, Cannizzaro LA, Lian JB, Croce CM, Stein JL, Stein GS: A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing. J Cell Biochem. 1992 Dec;50(4):374-85. [PubMed:1469070 ]