UniProtKB - P84229 (H32_CHICK)
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 37 – 38 | Involved in HMGB1-binding | 2 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- protein heterodimerization activity Source: InterPro
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
Reactomei | R-GGA-1266695, Interleukin-7 signaling R-GGA-201722, Formation of the beta-catenin:TCF transactivating complex R-GGA-212300, PRC2 methylates histones and DNA R-GGA-2559580, Oxidative Stress Induced Senescence R-GGA-3214815, HDACs deacetylate histones R-GGA-3214847, HATs acetylate histones R-GGA-3247509, Chromatin modifying enzymes R-GGA-5250924, B-WICH complex positively regulates rRNA expression R-GGA-5578749, Transcriptional regulation by small RNAs R-GGA-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 R-GGA-68616, Assembly of the ORC complex at the origin of replication R-GGA-73728, RNA Polymerase I Promoter Opening R-GGA-73772, RNA Polymerase I Promoter Escape R-GGA-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-GGA-9018519, Estrogen-dependent gene expression R-GGA-983231, Factors involved in megakaryocyte development and platelet production |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H3.2Alternative name(s): Histone H3 class I |
Gene namesi | 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 |
Organismi | Gallus gallus (Chicken) |
Taxonomic identifieri | 9031 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus |
Proteomesi |
|
Subcellular locationi
Nucleus
Other locations
Nucleus
- nucleus Source: GO_Central
Other locations
- nucleosome Source: UniProtKB-KW
Keywords - Cellular componenti
Chromosome, Nucleosome core, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000221260 | 2 – 136 | Histone H3.2Add BLAST | 135 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 3 | Asymmetric dimethylarginine; by PRMT6; alternateBy similarity | 1 | |
Modified residuei | 3 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 4 | Phosphothreonine; by HASPINBy similarity | 1 | |
Modified residuei | 5 | Allysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6,N6,N6-trimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6,N6-dimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 5 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 5 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 6 | 5-glutamyl dopamine; alternateBy similarity | 1 | |
Modified residuei | 6 | 5-glutamyl serotonin; alternateBy similarity | 1 | |
Modified residuei | 7 | Phosphothreonine; by PKCBy similarity | 1 | |
Modified residuei | 9 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 9 | Symmetric dimethylarginine; by PRMT5; alternateBy similarity | 1 | |
Modified residuei | 10 | N6,N6,N6-trimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6,N6-dimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 10 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 11 | ADP-ribosylserine; alternateBy similarity | 1 | |
Modified residuei | 11 | Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5By similarity | 1 | |
Modified residuei | 12 | Phosphothreonine; by PKCBy similarity | 1 | |
Modified residuei | 15 | N6,N6-dimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 15 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 15 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 15 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 18 | Asymmetric dimethylarginine; by CARM1; alternateBy similarity | 1 | |
Modified residuei | 18 | Citrulline; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 19 | N6-butyryllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 19 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 24 | N6-butyryllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 24 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 27 | CitrullineBy similarity | 1 | |
Modified residuei | 28 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 28 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 29 | ADP-ribosylserine; alternateBy similarity | 1 | |
Modified residuei | 29 | Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5By similarity | 1 | |
Modified residuei | 37 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 38 | N6-methyllysineBy similarity | 1 | |
Modified residuei | 42 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 57 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-methyllysine; by EHMT2; alternateBy similarity | 1 | |
Modified residuei | 57 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 58 | PhosphoserineBy similarity | 1 | |
Modified residuei | 65 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 65 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6,N6,N6-trimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6,N6-dimethyllysine; alternate1 Publication | 1 | |
Modified residuei | 80 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6-lactoyllysine; alternateBy similarity | 1 | |
Modified residuei | 80 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 80 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 81 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 87 | PhosphoserineBy similarity | 1 | |
Modified residuei | 108 | PhosphothreonineBy similarity | 1 | |
Lipidationi | 111 | S-palmitoyl cysteineBy similarity | 1 | |
Modified residuei | 116 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 116 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 123 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 123 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 123 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 123 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 123 | N6-succinyllysine; alternateBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P84229 |
PTM databases
iPTMneti | P84229 |
Expressioni
Developmental stagei
Gene expression databases
Bgeei | ENSGALG00000027064, Expressed in granulocyte and 11 other tissues |
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.
Interacts with HMGB1.
3 PublicationsGO - Molecular functioni
- protein heterodimerization activity Source: InterPro
Protein-protein interaction databases
IntActi | P84229, 3 interactors |
STRINGi | 9031.ENSGALP00000040958 |
Structurei
Secondary structure
3D structure databases
SMRi | P84229 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P84229 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 43 | DisorderedSequence analysisAdd BLAST | 43 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1745, Eukaryota |
GeneTreei | ENSGT01040000240403 |
HOGENOMi | CLU_078295_4_0_1 |
InParanoidi | P84229 |
OMAi | LARRIRX |
OrthoDBi | 1564596at2759 |
PhylomeDBi | P84229 |
TreeFami | TF314241 |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000164, Histone_H3/CENP-A |
PANTHERi | PTHR11426, PTHR11426, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00622, HISTONEH3 |
SMARTi | View protein in SMART SM00428, H3, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00322, HISTONE_H3_1, 1 hit PS00959, HISTONE_H3_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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 |
PIRi | S18716, HSCH3 |
RefSeqi | NP_001268409.1, NM_001281480.1 NP_001268438.1, NM_001281509.2 XP_001232833.1, XM_001232832.4 XP_001233028.1, XM_001233027.4 XP_015144912.1, XM_015289426.1 XP_015144926.1, XM_015289440.1 XP_416193.2, XM_416193.4 |
Genome annotation databases
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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 |
PIRi | S18716, HSCH3 |
RefSeqi | NP_001268409.1, NM_001281480.1 NP_001268438.1, NM_001281509.2 XP_001232833.1, XM_001232832.4 XP_001233028.1, XM_001233027.4 XP_015144912.1, XM_015289426.1 XP_015144926.1, XM_015289440.1 XP_416193.2, XM_416193.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EQZ | X-ray | 2.50 | C/G | 1-136 | [»] | |
1HIO | X-ray | 3.10 | C | 44-136 | [»] | |
1HQ3 | X-ray | 2.15 | C/G | 1-136 | [»] | |
1TZY | X-ray | 1.90 | C/G | 1-136 | [»] | |
2ARO | X-ray | 2.10 | C/G | 1-136 | [»] | |
2HIO | X-ray | 3.10 | C | 1-136 | [»] | |
3C9K | electron microscopy | 20.00 | C/G | 2-136 | [»] | |
7BXT | electron microscopy | 4.20 | A/E | 1-64 | [»] | |
7BY0 | electron microscopy | 4.50 | A/E | 1-64 | [»] | |
SMRi | P84229 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P84229, 3 interactors |
STRINGi | 9031.ENSGALP00000040958 |
PTM databases
iPTMneti | P84229 |
Proteomic databases
PaxDbi | P84229 |
Genome annotation databases
Organism-specific databases
CTDi | 100858681 417953 768333 770022 |
Phylogenomic databases
eggNOGi | KOG1745, Eukaryota |
GeneTreei | ENSGT01040000240403 |
HOGENOMi | CLU_078295_4_0_1 |
InParanoidi | P84229 |
OMAi | LARRIRX |
OrthoDBi | 1564596at2759 |
PhylomeDBi | P84229 |
TreeFami | TF314241 |
Enzyme and pathway databases
Reactomei | R-GGA-1266695, Interleukin-7 signaling R-GGA-201722, Formation of the beta-catenin:TCF transactivating complex R-GGA-212300, PRC2 methylates histones and DNA R-GGA-2559580, Oxidative Stress Induced Senescence R-GGA-3214815, HDACs deacetylate histones R-GGA-3214847, HATs acetylate histones R-GGA-3247509, Chromatin modifying enzymes R-GGA-5250924, B-WICH complex positively regulates rRNA expression R-GGA-5578749, Transcriptional regulation by small RNAs R-GGA-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 R-GGA-68616, Assembly of the ORC complex at the origin of replication R-GGA-73728, RNA Polymerase I Promoter Opening R-GGA-73772, RNA Polymerase I Promoter Escape R-GGA-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-GGA-9018519, Estrogen-dependent gene expression R-GGA-983231, Factors involved in megakaryocyte development and platelet production |
Miscellaneous databases
EvolutionaryTracei | P84229 |
PROi | PR:P84229 |
Gene expression databases
Bgeei | ENSGALG00000027064, Expressed in granulocyte and 11 other tissues |
Family and domain databases
Gene3Di | 1.10.20.10, 1 hit |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR007125, Histone_H2A/H2B/H3 IPR000164, Histone_H3/CENP-A |
PANTHERi | PTHR11426, PTHR11426, 1 hit |
Pfami | View protein in Pfam PF00125, Histone, 1 hit |
PRINTSi | PR00622, HISTONEH3 |
SMARTi | View protein in SMART SM00428, H3, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00322, HISTONE_H3_1, 1 hit PS00959, HISTONE_H3_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | H32_CHICK | |
Accessioni | P84229Primary (citable) accession number: P84229 Secondary accession number(s): P02295 P17320 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 152 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families