Histone H2A peptide - unmodified (ab13202)
- FO108H2AH2a 615
- H2A GL101H2A histone family member AH2A.1H2A.2H2A/aH2A/mH2A/OH2A/qH2A1B_HUMANH2AFAH2AFEH2AFLH2AFMH2AFOH2AFQH4 histone family 2H4 histone family member NH4F2H4FNHIST1H2AEHIST1H2AJHIST2H2AAHIST2H2AA3HIST2H2ABHIST2H2ACHistH2AHistone 1 H2aeHistone 2 H2aa3Histone 2 H2abHistone 2 H2acHistone H2A type 1 BHistone H2A type 1 CHistone H2A type 1 EHistone H2A type 1 JHistone H2A type 1-B/EHistone H2A.2Histone H2A/aHistone H2A/mMGC74460
modificationsThe chromatin-associated form is phosphorylated on Thr-121 during mitosis.
Deiminated on Arg-4 in granulocytes upon calcium entry.
Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3. Monoubiquitination of Lys-120 by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Monoubiquitination and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events.
Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
Histone H2A peptide - unmodified images
References for Histone H2A peptide - unmodified (ab13202)
ab13202 has not yet been referenced specifically in any publications.