P0C170 (H2A1E_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Histone H2A type 1-E
Organism	Rattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier	10116 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	130 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. Chromosome.
Induction	Up-regulated in hepatocytes after treatment with the procarcinogen N-nitrosodiethylamine (NDEA). Ref.3
Post-translational modification	The chromatin-associated form is phosphorylated on Thr-121 during mitosis By similarity. Monoubiquitination of Lys-120 (H2AK119Ub) 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 (H3K27me). H2AK119Ub 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. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events By similarity. 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 By similarity. Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity. Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes By similarity.
Sequence similarities	Belongs to the histone H2A family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing 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 nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 130	129	Histone H2A type 1-E		PRO_0000227511
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Modified residue	2	1	Phosphoserine; by RPS6KA5 By similarity
	Modified residue	4	1	Citrulline; alternate By similarity
	Modified residue	4	1	Symmetric dimethylarginine; alternate By similarity
	Modified residue	6	1	N6-acetyllysine By similarity
	Modified residue	37	1	N6-crotonyl-L-lysine By similarity
	Modified residue	119	1	N6-crotonyl-L-lysine By similarity
	Modified residue	120	1	N6-crotonyl-L-lysine By similarity
	Modified residue	121	1	Phosphothreonine By similarity
	Modified residue	126	1	N6-crotonyl-L-lysine By similarity
	Cross-link	14		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	16		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	120		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Sequences

	Sequence		Length	Mass (Da)
	P0C170 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9CED539793FE9AC7	FASTA	130	14,119
	10 20 30 40 50 60 MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT 70 80 90 100 110 120 AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK 130 TESHHKAKGK

References

[1]	"Primary structure and microheterogeneities of rat chloroleukemia histone H2A (histone ALK, IIbl or F2a2)." Laine B., Sautiere P., Biserte G. Biochemistry 15:1640-1645(1976) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-130. Tissue: Leukemia.
[2]	"Mass spectrometry-compatible silver staining of histones resolved on acetic acid-urea-Triton PAGE." Pramod K.S., Bharat K., Sanjay G. Proteomics 9:2589-2592(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]	"Overexpression of histone variant H2A.1 and cellular transformation are related in N-nitrosodiethylamine-induced sequential hepatocarcinogenesis." Khare S.P., Sharma A., Deodhar K.K., Gupta S. Exp. Biol. Med. 236:30-35(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY NDEA, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
IPI	IPI00560491.
RefSeq	XP_001061734.1. XM_001061734.2. XP_001071473.1. XM_001071473.2. XP_344600.3. XM_344599.4. XP_577573.1. XM_577573.3.
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P0C170.
Proteomic databases
PaxDb	P0C170.
PRIDE	P0C170.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000013790; ENSRNOP00000013790; ENSRNOG00000049649. ENSRNOT00000045512; ENSRNOP00000046383; ENSRNOG00000050266.
GeneID	364723. 502125.
KEGG	rno:364723. rno:502125.
UCSC	RGD:1594367. rat.
Organism-specific databases
CTD	665433. 85235.
RGD	1594367. LOC502125.
Phylogenomic databases
eggNOG	COG5262.
GeneTree	ENSGT00690000101783.
HOVERGEN	HBG009342.
InParanoid	P0C170.
KO	K11251.
OMA	KSRINPR.
OrthoDB	EOG4TXBTD.
Gene expression databases
Genevestigator	P0C170.
GermOnline	ENSRNOG00000032221. Rattus norvegicus. ENSRNOG00000038904. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
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	685918.

Entry information

Entry name

H2A1E_RAT

Accession

Primary (citable) accession number: P0C170

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program