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P06897

- H2A1_XENLA

UniProt

P06897 - H2A1_XENLA

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
  1. 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

    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

    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-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

    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.
    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.
    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

    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: October 1, 2014
    This is version 113 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