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P02263

- H2A4_CHICK

UniProt

P02263 - H2A4_CHICK

Protein

Histone H2A-IV

Gene
N/A
Organism
Gallus gallus (Chicken)
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-IV
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 1

    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 – 11Removed1 Publication
    Chaini2 – 129128Histone H2A-IVPRO_0000055215Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei6 – 61N6-acetyllysine1 Publication
    Modified residuei10 – 101N6-acetyllysine1 Publication
    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)1 Publication

    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

    PaxDbiP02263.
    PRIDEiP02263.

    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

    BioGridi676813. 2 interactions.
    IntActiP02263. 3 interactions.
    STRINGi9031.ENSGALP00000035358.

    Structurei

    Secondary structure

    1
    129
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 144
    Helixi18 – 214
    Helixi28 – 3710
    Beta strandi40 – 445
    Helixi47 – 7327
    Beta strandi77 – 793
    Helixi81 – 899
    Helixi92 – 976
    Turni98 – 1003
    Beta strandi101 – 1033
    Turni104 – 1063
    Helixi114 – 1163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EQZX-ray2.50A/E1-129[»]
    1HIOX-ray3.10A16-110[»]
    1HQ3X-ray2.15A/E1-129[»]
    1TZYX-ray1.90A/E1-129[»]
    2AROX-ray2.10A/E1-129[»]
    2HIOX-ray3.10A2-129[»]
    2XQLelectron microscopy19.50A/C/E/G/I16-106[»]
    3C9Kelectron microscopy20.00A/E2-129[»]
    ProteinModelPortaliP02263.
    SMRiP02263. Positions 3-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02263.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    HOVERGENiHBG009342.
    InParanoidiP02263.
    KOiK11251.
    PhylomeDBiP02263.
    TreeFamiTF300137.

    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.

    P02263-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
    YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK 100
    VTIAQGGVLP NIQAVLLPKK TDSHKAKAK 129
    Length:129
    Mass (Da):13,940
    Last modified:January 23, 2007 - v2
    Checksum:iC148297D1C525360
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501V → L in CAA23704. (PubMed:6269072)Curated
    Sequence conflicti127 – 1282KA → AG AA sequence (PubMed:667168)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11055 Genomic DNA. Translation: BAA01798.1.
    V00413 Genomic DNA. Translation: CAA23704.1.
    X02218 Genomic DNA. Translation: CAA26139.1.
    PIRiB93556. HSCH2A.
    RefSeqiNP_001072943.1. NM_001079475.1.
    NP_001264997.1. NM_001278068.1.
    NP_001268410.1. NM_001281481.1.
    XP_004937728.1. XM_004937671.1.
    XP_004937731.1. XM_004937674.1.
    XP_425455.2. XM_425455.3.
    XP_425465.1. XM_425465.2.
    XP_425469.1. XM_425469.4.
    UniGeneiGga.39224.
    Gga.47290.
    Gga.50534.

    Genome annotation databases

    EnsembliENSGALT00000043392; ENSGALP00000040820; ENSGALG00000026738.
    ENSGALT00000044624; ENSGALP00000043258; ENSGALG00000027315.
    ENSGALT00000045120; ENSGALP00000041766; ENSGALG00000028372.
    ENSGALT00000045162; ENSGALP00000040715; ENSGALG00000027425.
    ENSGALT00000045191; ENSGALP00000040653; ENSGALG00000028417.
    ENSGALT00000045842; ENSGALP00000041269; ENSGALG00000027113.
    GeneIDi100858459.
    101749238.
    404299.
    417955.
    427881.
    427891.
    427895.
    KEGGigga:100858459.
    gga:101749238.
    gga:404299.
    gga:417955.
    gga:427881.
    gga:427891.
    gga:427895.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11055 Genomic DNA. Translation: BAA01798.1 .
    V00413 Genomic DNA. Translation: CAA23704.1 .
    X02218 Genomic DNA. Translation: CAA26139.1 .
    PIRi B93556. HSCH2A.
    RefSeqi NP_001072943.1. NM_001079475.1.
    NP_001264997.1. NM_001278068.1.
    NP_001268410.1. NM_001281481.1.
    XP_004937728.1. XM_004937671.1.
    XP_004937731.1. XM_004937674.1.
    XP_425455.2. XM_425455.3.
    XP_425465.1. XM_425465.2.
    XP_425469.1. XM_425469.4.
    UniGenei Gga.39224.
    Gga.47290.
    Gga.50534.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EQZ X-ray 2.50 A/E 1-129 [» ]
    1HIO X-ray 3.10 A 16-110 [» ]
    1HQ3 X-ray 2.15 A/E 1-129 [» ]
    1TZY X-ray 1.90 A/E 1-129 [» ]
    2ARO X-ray 2.10 A/E 1-129 [» ]
    2HIO X-ray 3.10 A 2-129 [» ]
    2XQL electron microscopy 19.50 A/C/E/G/I 16-106 [» ]
    3C9K electron microscopy 20.00 A/E 2-129 [» ]
    ProteinModelPortali P02263.
    SMRi P02263. Positions 3-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676813. 2 interactions.
    IntActi P02263. 3 interactions.
    STRINGi 9031.ENSGALP00000035358.

    Proteomic databases

    PaxDbi P02263.
    PRIDEi P02263.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000043392 ; ENSGALP00000040820 ; ENSGALG00000026738 .
    ENSGALT00000044624 ; ENSGALP00000043258 ; ENSGALG00000027315 .
    ENSGALT00000045120 ; ENSGALP00000041766 ; ENSGALG00000028372 .
    ENSGALT00000045162 ; ENSGALP00000040715 ; ENSGALG00000027425 .
    ENSGALT00000045191 ; ENSGALP00000040653 ; ENSGALG00000028417 .
    ENSGALT00000045842 ; ENSGALP00000041269 ; ENSGALG00000027113 .
    GeneIDi 100858459.
    101749238.
    404299.
    417955.
    427881.
    427891.
    427895.
    KEGGi gga:100858459.
    gga:101749238.
    gga:404299.
    gga:417955.
    gga:427881.
    gga:427891.
    gga:427895.

    Organism-specific databases

    CTDi 100858459.
    404299.
    417955.
    427881.
    427891.
    427895.

    Phylogenomic databases

    eggNOGi COG5262.
    HOVERGENi HBG009342.
    InParanoidi P02263.
    KOi K11251.
    PhylomeDBi P02263.
    TreeFami TF300137.

    Miscellaneous databases

    EvolutionaryTracei P02263.
    NextBioi 20817644.

    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. "Inverted duplication of histone genes in chicken and disposition of regulatory sequences."
      Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.
      Nucleic Acids Res. 13:1369-1387(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Takechi S., Ohsige T., Nakayama T.
      Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Vertebrate histone genes: nucleotide sequence of a chicken H2A gene and regulatory flanking sequences."
      D'Andrea R., Harvey R.P., Wells J.R.E.
      Nucleic Acids Res. 9:3119-3128(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Primary structure of chicken erythrocyte histone H2A."
      Laine B., Kmiecik D., Sautiere P., Biserte G.
      Biochimie 60:147-150(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-129.
      Tissue: Erythrocyte.
    5. "Analysis of core histones by liquid chromatography-mass spectrometry and peptide mapping."
      Zhang K., Tang H.
      J. Chromatogr. B 783:173-179(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-12, ACETYLATION AT LYS-6 AND LYS-10, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin."
      Nickel B.E., Allis C.D., Davie J.R.
      Biochemistry 28:958-963(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    7. "The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix."
      Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.
      Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).

    Entry informationi

    Entry nameiH2A4_CHICK
    AccessioniPrimary (citable) accession number: P02263
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 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, Complete proteome, Direct protein sequencing, Reference proteome

    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