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P06897 (H2A1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. 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 namesRecommended name:
Histone H2A type 1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length130 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

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 130129Histone H2A type 1
PRO_0000055294

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine By similarity
Modified residue61N6-acetyllysine By similarity
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) By similarity

Secondary structure

.......................... 130
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06897 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 09946ABF27FA52A9

FASTA13013,966
        10         20         30         40         50         60 
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT 

        70         80         90        100        110        120 
AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG VTIAQGGVLP NIQSVLLPKK 

       130 
TESAKSAKSK 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization and nucleotide sequence of two distinct histone gene clusters from Xenopus laevis. Identification of novel conserved upstream sequence elements."
Perry M., Thomsen G.H., Roeder R.G.
J. Mol. Biol. 185:479-499(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GENE CLUSTER X1H3).
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"Crystal structure of the nucleosome core particle at 2.8 A resolution."
Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J.
Nature 389:251-260(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03018 Genomic DNA. Translation: CAA26817.1.
M21287 Genomic DNA. Translation: AAA49769.1.
BC106331 mRNA. Translation: AAI06332.1.
PIRHSXLA1. H24510.
RefSeqNP_001089684.1. NM_001096215.1.
UniGeneXl.19141.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80C/G5-120[»]
1KX3X-ray2.00C/G2-126[»]
1KX4X-ray2.60C/G2-126[»]
1KX5X-ray1.94C/G2-126[»]
1M18X-ray2.45C/G2-129[»]
1M19X-ray2.30C/G2-129[»]
1M1AX-ray2.65C/G2-129[»]
1P34X-ray2.70C/G2-130[»]
1P3AX-ray3.00C/G2-130[»]
1P3BX-ray3.00C/G2-130[»]
1P3FX-ray2.90C/G2-130[»]
1P3GX-ray2.70C/G2-130[»]
1P3IX-ray2.30C/G2-130[»]
1P3KX-ray2.90C/G2-130[»]
1P3LX-ray2.40C/G2-130[»]
1P3MX-ray2.90C/G2-130[»]
1P3OX-ray2.75C/G2-130[»]
1P3PX-ray2.70C/G2-130[»]
1S32X-ray2.05C/G2-120[»]
1ZBBX-ray9.00C/G/c/g2-130[»]
1ZLAX-ray2.90C/G2-130[»]
2FJ7X-ray3.20C/G2-130[»]
2NZDX-ray2.65C/G2-120[»]
3B6FX-ray3.45C/G2-126[»]
3B6GX-ray3.45C/G2-126[»]
3C1BX-ray2.20C/G2-130[»]
3C1CX-ray3.15C/G2-130[»]
3KUYX-ray2.90C/G2-120[»]
3KWQX-ray3.50C/G15-121[»]
3LJAX-ray2.75C/G2-130[»]
3MNNX-ray2.50C/G2-120[»]
3O62X-ray3.22C/G2-126[»]
3REHX-ray2.50C/G2-130[»]
3REIX-ray2.65C/G2-130[»]
3REJX-ray2.55C/G2-130[»]
3REKX-ray2.60C/G2-130[»]
3RELX-ray2.70C/G2-130[»]
3TU4X-ray3.00C/G2-130[»]
3UT9X-ray2.20C/G2-130[»]
3UTAX-ray2.07C/G2-130[»]
3UTBX-ray2.20C/G2-130[»]
4J8UX-ray2.38C/G2-126[»]
4J8VX-ray2.58C/G2-126[»]
4J8WX-ray2.41C/G2-126[»]
4J8XX-ray2.87C/G2-126[»]
4LD9X-ray3.31C/G2-130[»]
ProteinModelPortalP06897.
SMRP06897. Positions 2-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-39144N.

Proteomic databases

PRIDEP06897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID734746.
KEGGxla:734746.

Organism-specific databases

CTD3014.
XenbaseXB-GENE-6493983. h2afx.

Phylogenomic databases

HOVERGENHBG009342.
KOK11251.

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

EvolutionaryTraceP06897.

Entry information

Entry nameH2A1_XENLA
AccessionPrimary (citable) accession number: P06897
Secondary accession number(s): Q3B8I8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 111 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