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Protein

Histone H2A type 1

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A type 1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6493983. h2afx.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 130129Histone H2A type 1PRO_0000055294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei105 – 1051N5-methylglutamineBy similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP06897.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi592527. 1 interaction.
DIPiDIP-39144N.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi9 – 135Combined sources
Helixi18 – 225Combined sources
Helixi28 – 3710Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 7327Combined sources
Beta strandi77 – 793Combined sources
Helixi81 – 899Combined sources
Helixi92 – 976Combined sources
Turni98 – 1003Combined sources
Beta strandi101 – 1033Combined sources
Helixi114 – 1163Combined sources
Beta strandi117 – 1193Combined sources
Helixi120 – 1223Combined sources
Turni124 – 1263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80C/G5-120[»]
1KX3X-ray2.00C/G2-130[»]
1KX4X-ray2.60C/G2-130[»]
1KX5X-ray1.94C/G2-130[»]
1M18X-ray2.45C/G2-130[»]
1M19X-ray2.30C/G2-130[»]
1M1AX-ray2.65C/G2-130[»]
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/G2-130[»]
3B6GX-ray3.45C/G2-130[»]
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/G2-130[»]
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/G2-130[»]
4J8VX-ray2.58C/G2-130[»]
4J8WX-ray2.41C/G2-130[»]
4J8XX-ray2.87C/G2-130[»]
4LD9X-ray3.31C/G1-130[»]
4WU8X-ray2.45C/G2-130[»]
4WU9X-ray2.60C/G2-130[»]
4XUJX-ray3.18C/G2-130[»]
4XZQX-ray2.40C/G15-121[»]
4YS3X-ray3.00C/G15-121[»]
4Z66X-ray2.50C/G15-121[»]
4ZUXX-ray3.82C/G/M/Q1-130[»]
5CP6X-ray2.60C/G2-130[»]
5E5AX-ray2.81C/G1-130[»]
5F99X-ray2.63C/G2-130[»]
5HQ2X-ray4.50G2-130[»]
ProteinModelPortaliP06897.
SMRiP06897. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06897.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

HOVERGENiHBG009342.
KOiK11251.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06897-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG
110 120 130
VTIAQGGVLP NIQSVLLPKK TESAKSAKSK
Length:130
Mass (Da):13,966
Last modified:January 23, 2007 - v2
Checksum:i09946ABF27FA52A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA. Translation: CAA26817.1.
M21287 Genomic DNA. Translation: AAA49769.1.
BC106331 mRNA. Translation: AAI06332.1.
PIRiH24510. HSXLA1.
RefSeqiNP_001089684.1. NM_001096215.1.
UniGeneiXl.19141.

Genome annotation databases

GeneIDi734746.
KEGGixla:734746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA. Translation: CAA26817.1.
M21287 Genomic DNA. Translation: AAA49769.1.
BC106331 mRNA. Translation: AAI06332.1.
PIRiH24510. HSXLA1.
RefSeqiNP_001089684.1. NM_001096215.1.
UniGeneiXl.19141.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80C/G5-120[»]
1KX3X-ray2.00C/G2-130[»]
1KX4X-ray2.60C/G2-130[»]
1KX5X-ray1.94C/G2-130[»]
1M18X-ray2.45C/G2-130[»]
1M19X-ray2.30C/G2-130[»]
1M1AX-ray2.65C/G2-130[»]
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/G2-130[»]
3B6GX-ray3.45C/G2-130[»]
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/G2-130[»]
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/G2-130[»]
4J8VX-ray2.58C/G2-130[»]
4J8WX-ray2.41C/G2-130[»]
4J8XX-ray2.87C/G2-130[»]
4LD9X-ray3.31C/G1-130[»]
4WU8X-ray2.45C/G2-130[»]
4WU9X-ray2.60C/G2-130[»]
4XUJX-ray3.18C/G2-130[»]
4XZQX-ray2.40C/G15-121[»]
4YS3X-ray3.00C/G15-121[»]
4Z66X-ray2.50C/G15-121[»]
4ZUXX-ray3.82C/G/M/Q1-130[»]
5CP6X-ray2.60C/G2-130[»]
5E5AX-ray2.81C/G1-130[»]
5F99X-ray2.63C/G2-130[»]
5HQ2X-ray4.50G2-130[»]
ProteinModelPortaliP06897.
SMRiP06897. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi592527. 1 interaction.
DIPiDIP-39144N.

Proteomic databases

PRIDEiP06897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi734746.
KEGGixla:734746.

Organism-specific databases

CTDi3014.
XenbaseiXB-GENE-6493983. h2afx.

Phylogenomic databases

HOVERGENiHBG009342.
KOiK11251.

Miscellaneous databases

EvolutionaryTraceiP06897.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH2A1_XENLA
AccessioniPrimary (citable) accession number: P06897
Secondary accession number(s): Q3B8I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.