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P06897

- H2A1_XENLA

UniProt

P06897 - H2A1_XENLA

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Protein

Histone H2A type 1

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. nucleosome assembly Source: InterPro
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

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 130129Histone H2A type 1PRO_0000055294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei6 – 61N6-acetyllysine By 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-methylglutamine By 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.
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.

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

DIPiDIP-39144N.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP06897.
SMRiP06897. Positions 2-126.

Miscellaneous databases

EvolutionaryTraceiP06897.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

Phylogenomic databases

HOVERGENiHBG009342.
KOiK11251.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 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

MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG 100
VTIAQGGVLP NIQSVLLPKK TESAKSAKSK 130
Length:130
Mass (Da):13,966
Last modified:January 23, 2007 - v2
Checksum:i09946ABF27FA52A9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X03018 Genomic DNA. Translation: CAA26817.1 .
M21287 Genomic DNA. Translation: AAA49769.1 .
BC106331 mRNA. Translation: AAI06332.1 .
PIRi H24510. HSXLA1.
RefSeqi NP_001089684.1. NM_001096215.1.
UniGenei Xl.19141.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOI X-ray 2.80 C/G 5-120 [» ]
1KX3 X-ray 2.00 C/G 2-130 [» ]
1KX4 X-ray 2.60 C/G 2-130 [» ]
1KX5 X-ray 1.94 C/G 2-130 [» ]
1M18 X-ray 2.45 C/G 2-130 [» ]
1M19 X-ray 2.30 C/G 2-130 [» ]
1M1A X-ray 2.65 C/G 2-130 [» ]
1P34 X-ray 2.70 C/G 2-130 [» ]
1P3A X-ray 3.00 C/G 2-130 [» ]
1P3B X-ray 3.00 C/G 2-130 [» ]
1P3F X-ray 2.90 C/G 2-130 [» ]
1P3G X-ray 2.70 C/G 2-130 [» ]
1P3I X-ray 2.30 C/G 2-130 [» ]
1P3K X-ray 2.90 C/G 2-130 [» ]
1P3L X-ray 2.40 C/G 2-130 [» ]
1P3M X-ray 2.90 C/G 2-130 [» ]
1P3O X-ray 2.75 C/G 2-130 [» ]
1P3P X-ray 2.70 C/G 2-130 [» ]
1S32 X-ray 2.05 C/G 2-120 [» ]
1ZBB X-ray 9.00 C/G/c/g 2-130 [» ]
1ZLA X-ray 2.90 C/G 2-130 [» ]
2FJ7 X-ray 3.20 C/G 2-130 [» ]
2NZD X-ray 2.65 C/G 2-120 [» ]
3B6F X-ray 3.45 C/G 2-130 [» ]
3B6G X-ray 3.45 C/G 2-130 [» ]
3C1B X-ray 2.20 C/G 2-130 [» ]
3C1C X-ray 3.15 C/G 2-130 [» ]
3KUY X-ray 2.90 C/G 2-120 [» ]
3KWQ X-ray 3.50 C/G 15-121 [» ]
3LJA X-ray 2.75 C/G 2-130 [» ]
3MNN X-ray 2.50 C/G 2-120 [» ]
3O62 X-ray 3.22 C/G 2-130 [» ]
3REH X-ray 2.50 C/G 2-130 [» ]
3REI X-ray 2.65 C/G 2-130 [» ]
3REJ X-ray 2.55 C/G 2-130 [» ]
3REK X-ray 2.60 C/G 2-130 [» ]
3REL X-ray 2.70 C/G 2-130 [» ]
3TU4 X-ray 3.00 C/G 2-130 [» ]
3UT9 X-ray 2.20 C/G 2-130 [» ]
3UTA X-ray 2.07 C/G 2-130 [» ]
3UTB X-ray 2.20 C/G 2-130 [» ]
4J8U X-ray 2.38 C/G 2-130 [» ]
4J8V X-ray 2.58 C/G 2-130 [» ]
4J8W X-ray 2.41 C/G 2-130 [» ]
4J8X X-ray 2.87 C/G 2-130 [» ]
4LD9 X-ray 3.31 C/G 1-130 [» ]
ProteinModelPortali P06897.
SMRi P06897. Positions 2-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-39144N.

Proteomic databases

PRIDEi P06897.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 734746.
KEGGi xla:734746.

Organism-specific databases

CTDi 3014.
Xenbasei XB-GENE-6493983. h2afx.

Phylogenomic databases

HOVERGENi HBG009342.
KOi K11251.

Miscellaneous databases

EvolutionaryTracei P06897.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00620. HISTONEH2A.
SMARTi SM00414. H2A. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00046. HISTONE_H2A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).

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: July 9, 2014
This is version 112 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

External Data

Dasty 3

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