Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02263

- H2A4_CHICK

UniProt

P02263 - H2A4_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_189773. RNA Polymerase I Chain Elongation.
REACT_194991. Oxidative Stress Induced Senescence.
REACT_197049. Amyloids.
REACT_197579. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_197816. DNA Damage/Telomere Stress Induced Senescence.
REACT_197820. HATs acetylate histones.
REACT_198068. Condensation of Prophase Chromosomes.
REACT_203085. formation of the beta-catenin:TCF transactivating complex.
REACT_204005. PRC2 methylates histones and DNA.
REACT_214700. Senescence-Associated Secretory Phenotype (SASP).
REACT_223091. SIRT1 negatively regulates rRNA Expression.
REACT_223355. NoRC negatively regulates rRNA expression.
REACT_224340. RNA Polymerase I Promoter Opening.
REACT_257247. Packaging Of Telomere Ends.
REACT_259645. Meiotic synapsis.
REACT_269036. DNA methylation.
REACT_270829. Transcriptional regulation by small RNAs.
REACT_271245. HDACs deacetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A-IV
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
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. 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 – 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.
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 .
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:
PDBei
RCSB PDBi
PDBji
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.

Enzyme and pathway databases

Reactomei REACT_189773. RNA Polymerase I Chain Elongation.
REACT_194991. Oxidative Stress Induced Senescence.
REACT_197049. Amyloids.
REACT_197579. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_197816. DNA Damage/Telomere Stress Induced Senescence.
REACT_197820. HATs acetylate histones.
REACT_198068. Condensation of Prophase Chromosomes.
REACT_203085. formation of the beta-catenin:TCF transactivating complex.
REACT_204005. PRC2 methylates histones and DNA.
REACT_214700. Senescence-Associated Secretory Phenotype (SASP).
REACT_223091. SIRT1 negatively regulates rRNA Expression.
REACT_223355. NoRC negatively regulates rRNA expression.
REACT_224340. RNA Polymerase I Promoter Opening.
REACT_257247. Packaging Of Telomere Ends.
REACT_259645. Meiotic synapsis.
REACT_269036. DNA methylation.
REACT_270829. Transcriptional regulation by small RNAs.
REACT_271245. HDACs deacetylate histones.

Miscellaneous databases

EvolutionaryTracei P02263.
NextBioi 20817644.

Gene expression databases

ExpressionAtlasi P02263. baseline.

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: November 26, 2014
This is version 132 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