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P02263

- H2A4_CHICK

UniProt

P02263 - H2A4_CHICK

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Protein

Histone H2A-IV

Gene
N/A
Organism
Gallus gallus (Chicken)
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-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
Complete GO annotation...

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 – 21Phosphoserine By 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-methylglutamine By similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Inferred

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

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.

Miscellaneous databases

EvolutionaryTraceiP02263.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501V → L in CAA23704. 1 Publication
Sequence conflicti127 – 1282KA → AG AA sequence 1 Publication

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: July 9, 2014
This is version 129 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

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