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P02263 (H2A4_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Post-translational modification

Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events By similarity.

Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription By similarity.

Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex By similarity.

Sequence similarities

Belongs to the histone H2A family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 129128Histone H2A-IV
PRO_0000055215

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue21Phosphoserine By similarity
Modified residue61N6-acetyllysine Ref.5
Modified residue101N6-acetyllysine Ref.5
Modified residue1051N5-methylglutamine By similarity
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Experimental info

Sequence conflict501V → L in CAA23704. Ref.3
Sequence conflict127 – 1282KA → AG AA sequence Ref.4

Secondary structure

...................... 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02263 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C148297D1C525360

FASTA12913,940
        10         20         30         40         50         60 
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT 

        70         80         90        100        110        120 
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK 


TDSHKAKAK 

« Hide

References

[1]"Inverted duplication of histone genes in chicken and disposition of regulatory sequences."
Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.
Nucleic Acids Res. 13:1369-1387(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Takechi S., Ohsige T., Nakayama T.
Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Vertebrate histone genes: nucleotide sequence of a chicken H2A gene and regulatory flanking sequences."
D'Andrea R., Harvey R.P., Wells J.R.E.
Nucleic Acids Res. 9:3119-3128(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Primary structure of chicken erythrocyte histone H2A."
Laine B., Kmiecik D., Sautiere P., Biserte G.
Biochimie 60:147-150(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-129.
Tissue: Erythrocyte.
[5]"Analysis of core histones by liquid chromatography-mass spectrometry and peptide mapping."
Zhang K., Tang H.
J. Chromatogr. B 783:173-179(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 5-12, ACETYLATION AT LYS-6 AND LYS-10, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin."
Nickel B.E., Allis C.D., Davie J.R.
Biochemistry 28:958-963(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[7]"The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix."
Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.
Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D11055 Genomic DNA. Translation: BAA01798.1.
V00413 Genomic DNA. Translation: CAA23704.1.
X02218 Genomic DNA. Translation: CAA26139.1.
PIRHSCH2A. B93556.
RefSeqNP_001072943.1. NM_001079475.1.
NP_001264997.1. NM_001278068.1.
NP_001268410.1. NM_001281481.1.
XP_004937728.1. XM_004937671.1.
XP_004937731.1. XM_004937674.1.
XP_425455.2. XM_425455.3.
XP_425465.1. XM_425465.2.
XP_425469.1. XM_425469.4.
UniGeneGga.39224.
Gga.47290.
Gga.50534.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQZX-ray2.50A/E1-129[»]
1HIOX-ray3.10A16-110[»]
1HQ3X-ray2.15A/E1-129[»]
1TZYX-ray1.90A/E1-129[»]
2AROX-ray2.10A/E1-129[»]
2HIOX-ray3.10A2-129[»]
2XQLelectron microscopy19.50A/C/E/G/I16-106[»]
3C9Kelectron microscopy20.00A/E2-129[»]
ProteinModelPortalP02263.
SMRP02263. Positions 3-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676813. 2 interactions.
IntActP02263. 3 interactions.
STRING9031.ENSGALP00000035358.

Proteomic databases

PaxDbP02263.
PRIDEP02263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000043392; ENSGALP00000040820; ENSGALG00000026738.
ENSGALT00000044624; ENSGALP00000043258; ENSGALG00000027315.
ENSGALT00000045120; ENSGALP00000041766; ENSGALG00000028372.
ENSGALT00000045162; ENSGALP00000040715; ENSGALG00000027425.
ENSGALT00000045191; ENSGALP00000040653; ENSGALG00000028417.
ENSGALT00000045842; ENSGALP00000041269; ENSGALG00000027113.
GeneID100858459.
101749238.
404299.
417955.
427881.
427891.
427895.
KEGGgga:100858459.
gga:101749238.
gga:404299.
gga:417955.
gga:427881.
gga:427891.
gga:427895.

Organism-specific databases

CTD100858459.
404299.
417955.
427881.
427891.
427895.

Phylogenomic databases

eggNOGCOG5262.
HOVERGENHBG009342.
InParanoidP02263.
KOK11251.
PhylomeDBP02263.
TreeFamTF300137.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02263.
NextBio20817644.

Entry information

Entry nameH2A4_CHICK
AccessionPrimary (citable) accession number: P02263
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references