Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P84229 (H32_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.2
Alternative name(s):
Histone H3 class I
Gene names
Name:H3-I
AND
Name:H3-II
AND
Name:H3-III
AND
Name:H3-IV
AND
Name:H3-V
AND
Name:H3-VI
AND
Name:H3-VII
AND
Name:H3-VIII
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Interacts with HMGB1. Ref.8

Subcellular location

Nucleus. Chromosome.

Developmental stage

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

Post-translational modification

Acetylation is generally linked to gene activation. Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability By similarity. Ref.7

Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene activation Probable. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters By similarity.

Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120' Probable. Ref.7

Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1 RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin By similarity.

Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity.

Lysine deamination at Lys-5 (H3K4all) to form allysine only takes place on H3K4me3 and results in gene repression By similarity.

Sequence similarities

Belongs to the histone H3 family.

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 136135Histone H3.2
PRO_0000221260

Sites

Site37 – 382Involved in HMGB1-binding

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6 By similarity
Modified residue41Phosphothreonine; by GSG2 By similarity
Modified residue51Allysine; alternate By similarity
Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.7
Modified residue51N6,N6-dimethyllysine; alternate Ref.7
Modified residue51N6-acetyllysine; alternate By similarity
Modified residue51N6-methyllysine Ref.7
Modified residue71Phosphothreonine; by PKC By similarity
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.7
Modified residue101N6,N6-dimethyllysine; alternate Ref.7
Modified residue101N6-methyllysine; alternate Ref.7
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 By similarity
Modified residue121Phosphothreonine; by PKC By similarity
Modified residue151N6,N6-dimethyllysine; alternate Ref.7
Modified residue151N6-acetyllysine; alternate Ref.7
Modified residue181Asymmetric dimethylarginine By similarity
Modified residue191N6-acetyllysine; alternate Ref.7
Modified residue191N6-methylated lysine; alternate By similarity
Modified residue241N6-acetyllysine Ref.7
Modified residue281N6-acetyllysine; alternate By similarity
Modified residue281N6-methylated lysine; alternate Ref.7
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 By similarity
Modified residue371N6-acetyllysine; alternate By similarity
Modified residue371N6-methylated lysine; alternate Ref.7
Modified residue421Phosphotyrosine By similarity
Modified residue581Phosphoserine By similarity
Modified residue651N6-methylated lysine By similarity
Modified residue801N6,N6-dimethyllysine; alternate Ref.7
Modified residue801N6-methyllysine; alternate Ref.7
Modified residue811Phosphothreonine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-methyllysine; alternate By similarity

Secondary structure

.............. 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84229 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6FD8508EA50A0EEC

FASTA13615,388
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

« Hide

References

[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]"A chicken histone H3 gene contains intervening sequences."
Engel J.D., Sugarman B.J., Dodgson J.B.
Nature 297:434-436(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide sequences of two members of the chicken H3 histone-encoding gene family."
Nakayama T.
Gene 102:289-290(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-II AND H3-III).
[4]"Nucleotide sequences of new members (H3-IV and H3-V) of the chicken H3 histone-encoding gene family."
Setoguchi Y., Nakayama T.
Nucleic Acids Res. 19:6327-6327(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-IV AND H3-V).
Strain: White leghorn.
[5]"Organization of the chicken histone genes in a major gene cluster and generation of an almost complete set of the core histone protein sequences."
Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.
DNA Res. 3:95-99(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3-VI; H3-VII AND H3-VIII).
Strain: White leghorn.
Tissue: Liver.
[6]"The determination of the primary structure of histone F3 from chicken erythrocytes by automatic Edman degradation. 2. Sequence analysis of histone F3."
Brandt W.F., von Holt C.
Eur. J. Biochem. 46:419-429(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-136.
[7]"Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization-postsource decay, and nanoelectrospray ionization tandem mass spectrometry."
Zhang K., Tang H., Huang L., Blankenship J.W., Jones P.R., Xiang F., Yau P.M., Burlingame A.L.
Anal. Biochem. 306:259-269(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37 AND LYS-80, ACETYLATION AT LYS-15; LYS-19 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Distinct domains in HMGB1 are involved in specific intramolecular and nucleosomal interactions."
Kawase T., Sato K., Ueda T., Yoshida M.
Biochemistry 47:13991-13996(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HMGB1.
[9]"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).
[10]"Asymmetries in the nucleosome core particle at 2.5 A resolution."
Harp J.M., Hanson B.L., Timm D.E., Bunick G.J.
Acta Crystallogr. D 56:1513-1534(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH H2A; H2B AND H4.
[11]"Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A resolution."
Chantalat L., Nicholson J.M., Lambert S.J., Reid A.J., Donovan M.J., Reynolds C.D., Wood C.M., Baldwin J.P.
Acta Crystallogr. D 59:1395-1407(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH H2A AND H2B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02218 Genomic DNA. Translation: CAA26138.1.
J00869 Genomic DNA. Translation: AAA48795.1. Sequence problems.
M61154 Genomic DNA. Translation: AAA48796.1.
M61155 Genomic DNA. Translation: AAA48797.1.
X62291 Genomic DNA. Translation: CAA44180.1.
X62292 Genomic DNA. Translation: CAA44181.1.
U37577 Genomic DNA. Translation: AAC60003.1.
U37578 Genomic DNA. Translation: AAC60004.1.
U37579 Genomic DNA. Translation: AAC60005.1.
PIRHSCH3. S18716.
RefSeqNP_001268409.1. NM_001281480.1.
NP_001268438.1. NM_001281509.1.
XP_001232833.1. XM_001232832.3.
XP_001233028.1. XM_001233027.3.
XP_004937729.1. XM_004937672.1.
XP_416193.2. XM_416193.3.
UniGeneGga.5274.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQZX-ray2.50C/G1-136[»]
1HIOX-ray3.10C44-136[»]
1HQ3X-ray2.15C/G1-136[»]
1TZYX-ray1.90C/G1-136[»]
2AROX-ray2.10C/G1-136[»]
2HIOX-ray3.10C1-136[»]
3C9Kelectron microscopy20.00C/G2-136[»]
ProteinModelPortalP84229.
SMRP84229. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid687084. 3 interactions.
IntActP84229. 3 interactions.
STRING9031.ENSGALP00000019185.

Proteomic databases

PaxDbP84229.
PRIDEP84229.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000042655; ENSGALP00000042290; ENSGALG00000027064.
ENSGALT00000043934; ENSGALP00000040958; ENSGALG00000027257.
GeneID100858681.
417953.
768333.
769809.
769852.
770022.
KEGGgga:100858681.
gga:417953.
gga:768333.
gga:769809.
gga:769852.
gga:770022.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00750000117468.
HOGENOMHOG000155290.
HOVERGENHBG001172.
InParanoidP84229.
KOK11253.
PhylomeDBP84229.
TreeFamTF314241.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP84229.
NextBio20821179.

Entry information

Entry nameH32_CHICK
AccessionPrimary (citable) accession number: P84229
Secondary accession number(s): P02295 expand/collapse secondary AC list , P02297, P16105, P17269, P17320
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references