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Protein

Histone H2B 7

Gene

H2B-VII

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

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B 7
Alternative name(s):
H2B VII
Gene namesi
Name:H2B-VII
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

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 methionineiRemovedBy similarity
Chaini2 – 126125Histone H2B 7PRO_0000244865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei13 – 131N6-acetyllysine1 Publication
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei16 – 161N6-acetyllysine1 Publication
Modified residuei21 – 211N6-acetyllysine1 Publication
Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Monoubiquitination of Lys-121 by the BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.By similarity
Phosphorylated on Ser-15 during apoptosis; which facilitates apoptotic chromatin condensation.1 Publication
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP0C1H5.
PRIDEiP0C1H5.

PTM databases

iPTMnetiP0C1H5.

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.3 Publications

Protein-protein interaction databases

IntActiP0C1H5. 1 interaction.
STRINGi9031.ENSGALP00000037260.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 4911Combined sources
Helixi57 – 8428Combined sources
Beta strandi88 – 903Combined sources
Helixi92 – 10211Combined sources
Helixi105 – 12420Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQZX-ray2.50B/F1-126[»]
1HIOX-ray3.10B37-126[»]
1HQ3X-ray2.15B/F1-126[»]
1TZYX-ray1.90B/F1-126[»]
2HIOX-ray3.10B2-126[»]
3C9Kelectron microscopy20.00B/F2-126[»]
ProteinModelPortaliP0C1H5.
SMRiP0C1H5. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C1H5.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
HOVERGENiHBG007774.
InParanoidiP0C1H5.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C1H5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KTQKKGDKKR KRARKESYSI YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM SIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSSK
Length:126
Mass (Da):13,964
Last modified:January 23, 2007 - v2
Checksum:iB14EC3822B5DAA97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05099 Genomic DNA. Translation: CAA28750.1.
U37575 Genomic DNA. Translation: AAC60000.1.
RefSeqiXP_015144978.1. XM_015289492.1.
UniGeneiGga.39843.

Genome annotation databases

GeneIDi107053803.
KEGGigga:107053803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05099 Genomic DNA. Translation: CAA28750.1.
U37575 Genomic DNA. Translation: AAC60000.1.
RefSeqiXP_015144978.1. XM_015289492.1.
UniGeneiGga.39843.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQZX-ray2.50B/F1-126[»]
1HIOX-ray3.10B37-126[»]
1HQ3X-ray2.15B/F1-126[»]
1TZYX-ray1.90B/F1-126[»]
2HIOX-ray3.10B2-126[»]
3C9Kelectron microscopy20.00B/F2-126[»]
ProteinModelPortaliP0C1H5.
SMRiP0C1H5. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C1H5. 1 interaction.
STRINGi9031.ENSGALP00000037260.

PTM databases

iPTMnetiP0C1H5.

Proteomic databases

PaxDbiP0C1H5.
PRIDEiP0C1H5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi107053803.
KEGGigga:107053803.

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
HOVERGENiHBG007774.
InParanoidiP0C1H5.

Miscellaneous databases

EvolutionaryTraceiP0C1H5.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH2B7_CHICK
AccessioniPrimary (citable) accession number: P0C1H5
Secondary accession number(s): P02279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 65 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.