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Protein

Histone H2A-IV

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A-IV
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

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 – 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.

Expressioni

Gene expression databases

ExpressionAtlasiP02263. baseline.

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. 3 interactions.
IntActiP02263. 3 interactions.
STRINGi9031.ENSGALP00000029990.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiKANSQEY.
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

        10         20         30         40         50
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK
110 120
VTIAQGGVLP NIQAVLLPKK TDSHKAKAK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi676813. 3 interactions.
IntActiP02263. 3 interactions.
STRINGi9031.ENSGALP00000029990.

Proteomic databases

PaxDbiP02263.
PRIDEiP02263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi100858459.
404299.
417955.
427881.
427891.
427895.

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiP02263.
NextBioi20817644.
PROiP02263.

Gene expression databases

ExpressionAtlasiP02263. baseline.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.