P06897 (H2A1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Histone H2A type 1
Organism	Xenopus laevis (African clawed frog)
Taxonomic identifier	8355 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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.
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.
Sequence similarities	Belongs to the histone H2A family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure
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

Chain

2 – 130

129

Histone H2A type 1

PRO_0000055294

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

2

1

Phosphoserine By similarity

Modified residue

6

1

N6-acetyllysine 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) By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

130

Helix Strand Turn

Details...

Helix

6 – 8

3

Beta strand

9 – 13

5

Helix

18 – 22

5

Helix

28 – 37

10

Beta strand

42 – 44

3

Helix

47 – 73

27

Beta strand

77 – 79

3

Helix

81 – 89

9

Helix

92 – 97

6

Turn

98 – 100

3

Beta strand

101 – 103

3

Helix

114 – 116

3

Beta strand

117 – 119

3

Helix

120 – 122

3

Turn

124 – 126

3

Sequences

	Sequence		Length	Mass (Da)
	P06897 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 09946ABF27FA52A9	FASTA	130	13,966
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

HSXLA1. H24510.

RefSeq

NP_001089684.1. NM_001096215.1.

UniGene

Xl.19141.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AOI	X-ray	2.80	C/G	5-120	[»]
1KX3	X-ray	2.00	C/G	2-126	[»]
1KX4	X-ray	2.60	C/G	2-126	[»]
1KX5	X-ray	1.94	C/G	2-126	[»]
1M18	X-ray	2.45	C/G	2-129	[»]
1M19	X-ray	2.30	C/G	2-129	[»]
1M1A	X-ray	2.65	C/G	2-129	[»]
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	2-126	[»]
3B6G	X-ray	3.45	C/G	2-126	[»]
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	2-126	[»]
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	[»]

ProteinModelPortal

P06897.

SMR

P06897. Positions 2-126.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39144N.

Proteomic databases

PRIDE

P06897.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

734746.

KEGG

xla:734746.

Organism-specific databases

CTD

3014.

Xenbase

XB-GENE-6493983. h2afx.

Phylogenomic databases

HOVERGEN

HBG009342.

KO

K11251.

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

EvolutionaryTrace

P06897.

Entry information

Entry name

H2A1_XENLA

Accession

Primary (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:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program