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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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A-IV
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000552152 – 129Histone H2A-IVAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei2PhosphoserineBy similarity1
Modified residuei6N6-acetyllysine1 Publication1
Modified residuei10N6-acetyllysine1 Publication1
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei105N5-methylglutamineBy similarity1
Cross-linki120Glycyl 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

BgeeiENSGALG00000026738.
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.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi676813. 3 interactors.
IntActiP02263. 3 interactors.
STRINGi9031.ENSGALP00000029990.

Structurei

Secondary structure

1129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Helixi18 – 21Combined sources4
Helixi28 – 37Combined sources10
Beta strandi40 – 44Combined sources5
Helixi47 – 73Combined sources27
Beta strandi77 – 79Combined sources3
Helixi81 – 89Combined sources9
Helixi92 – 97Combined sources6
Turni98 – 100Combined sources3
Beta strandi101 – 103Combined sources3
Turni104 – 106Combined sources3
Helixi114 – 116Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02263.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1756. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
ENSGT00760000118934.
ENSGT00880000137879.
HOVERGENiHBG009342.
InParanoidiP02263.
KOiK11251.
OMAiMPNIHQT.
OrthoDBiEOG091G0XGD.
PhylomeDBiP02263.
TreeFamiTF300137.

Family and domain databases

InterProiView protein in InterPro
IPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
PfamiView protein in Pfam
PF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
PRINTSiPR00620. HISTONEH2A.
SMARTiView protein in SMART
SM00414. H2A. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiView protein in PROSITE
PS00046. HISTONE_H2A. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti50V → L in CAA23704 (PubMed:6269072).Curated1
Sequence conflicti127 – 128KA → AG AA sequence (PubMed:667168).Curated2

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_004937671.2.
XP_425455.2. XM_425455.4.
XP_425465.1. XM_425465.3.
XP_425469.1. XM_425469.5.
UniGeneiGga.39224.
Gga.47290.
Gga.50534.

Genome annotation databases

EnsembliENSGALT00000044624; ENSGALP00000043258; ENSGALG00000027315.
ENSGALT00000045120; ENSGALP00000041766; ENSGALG00000028372.
ENSGALT00000045162; ENSGALP00000040715; ENSGALG00000035715.
ENSGALT00000045191; ENSGALP00000040653; ENSGALG00000029941.
ENSGALT00000045842; ENSGALP00000041269; ENSGALG00000027113.
ENSGALT00000046827; ENSGALP00000056288; ENSGALG00000032645.
ENSGALT00000058977; ENSGALP00000044632; ENSGALG00000031571.
GeneIDi100858459.
101749238.
404299.
417955.
427881.
427891.
427895.
KEGGigga:100858459.
gga:101749238.
gga:404299.
gga:417955.
gga:427881.
gga:427891.
gga:427895.

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 one 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.

Entry informationi

Entry nameiH2A4_CHICK
AccessioniPrimary (citable) accession number: P02263
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 158 of the entry and version 2 of the sequence. See 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