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Protein

Histone H2B.2

Gene

HTB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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.7 Publications

GO - Molecular functioni

  • DNA binding Source: SGD

GO - Biological processi

  • chromatin assembly or disassembly Source: SGD
  • nucleosome assembly Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28908-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B.2
Gene namesi
Name:HTB2
Synonyms:H2B2
Ordered Locus Names:YBL002W
ORF Names:YBL0104
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL002W.
SGDiS000000098. HTB2.

Subcellular locationi

GO - Cellular componenti

  • nuclear nucleosome Source: SGD
  • replication fork protection complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 82KK → AA: Reduces sumoylation. 1 Publication
Mutagenesisi11 – 111S → A: Desensitizes cells to H(2)O(2) treatment. 1 Publication
Mutagenesisi11 – 111S → E: Induces apoptotic-like features including chromatin condensation. 1 Publication
Mutagenesisi17 – 182KK → AA: Reduces sumoylation. 1 Publication
Mutagenesisi124 – 1241K → R: Impairs ubiquitin conjugation, DNA double-strand breaks formation during meiosis and histone H3-K79 methylation. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCurated
Chaini2 – 131130Histone H2B.2PRO_0000071939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71N6-acetyllysine; alternate1 Publication
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei8 – 81N6-acetyllysine; alternate1 Publication
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei11 – 111Phosphoserine2 Publications
Modified residuei12 – 121N6-acetyllysine2 Publications
Modified residuei17 – 171N6-acetyllysine; alternate3 Publications
Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Cross-linki124 – 124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)5 Publications

Post-translational modificationi

Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.
Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H2O2 treatment, and is a step leading to apoptosis.2 Publications
Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription.4 Publications
Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP02294.
PRIDEiP02294.

PTM databases

iPTMnetiP02294.

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 NAP1.2 Publications

Protein-protein interaction databases

BioGridi32700. 211 interactions.
DIPiDIP-3897N.
IntActiP02294. 83 interactions.
MINTiMINT-482371.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 498Combined sources
Turni50 – 523Combined sources
Helixi60 – 8728Combined sources
Beta strandi91 – 933Combined sources
Helixi95 – 10511Combined sources
Helixi109 – 12820Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ID3X-ray3.10D/H2-131[»]
2FSBmodel-D/H1-131[»]
4JJNX-ray3.09D/H2-131[»]
ProteinModelPortaliP02294.
SMRiP02294. Positions 10-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02294.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

GeneTreeiENSGT00840000129751.
HOGENOMiHOG000231213.
InParanoidiP02294.
KOiK11252.
OMAiRICDEAS.
OrthoDBiEOG092C5QTV.

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.

P02294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAAEKKPA SKAPAEKKPA AKKTSTSVDG KKRSKVRKET YSSYIYKVLK
60 70 80 90 100
QTHPDTGISQ KSMSILNSFV NDIFERIATE ASKLAAYNKK STISAREIQT
110 120 130
AVRLILPGEL AKHAVSEGTR AVTKYSSSTQ A
Length:131
Mass (Da):14,237
Last modified:January 23, 2007 - v2
Checksum:i3DCC26FF124D71E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01308 Genomic DNA. Translation: CAA24615.1.
Z26494 Genomic DNA. Translation: CAA81268.1.
Z35763 Genomic DNA. Translation: CAA84817.1.
AY693063 Genomic DNA. Translation: AAT93082.1.
BK006936 Genomic DNA. Translation: DAA07120.1.
PIRiS44558. HSBYB2.
RefSeqiNP_009553.1. NM_001178242.1.

Genome annotation databases

EnsemblFungiiYBL002W; YBL002W; YBL002W.
GeneIDi852284.
KEGGisce:YBL002W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01308 Genomic DNA. Translation: CAA24615.1.
Z26494 Genomic DNA. Translation: CAA81268.1.
Z35763 Genomic DNA. Translation: CAA84817.1.
AY693063 Genomic DNA. Translation: AAT93082.1.
BK006936 Genomic DNA. Translation: DAA07120.1.
PIRiS44558. HSBYB2.
RefSeqiNP_009553.1. NM_001178242.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ID3X-ray3.10D/H2-131[»]
2FSBmodel-D/H1-131[»]
4JJNX-ray3.09D/H2-131[»]
ProteinModelPortaliP02294.
SMRiP02294. Positions 10-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32700. 211 interactions.
DIPiDIP-3897N.
IntActiP02294. 83 interactions.
MINTiMINT-482371.

PTM databases

iPTMnetiP02294.

Proteomic databases

MaxQBiP02294.
PRIDEiP02294.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL002W; YBL002W; YBL002W.
GeneIDi852284.
KEGGisce:YBL002W.

Organism-specific databases

EuPathDBiFungiDB:YBL002W.
SGDiS000000098. HTB2.

Phylogenomic databases

GeneTreeiENSGT00840000129751.
HOGENOMiHOG000231213.
InParanoidiP02294.
KOiK11252.
OMAiRICDEAS.
OrthoDBiEOG092C5QTV.

Enzyme and pathway databases

BioCyciYEAST:G3O-28908-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02294.
PROiP02294.

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 nameiH2B2_YEAST
AccessioniPrimary (citable) accession number: P02294
Secondary accession number(s): D6VQ00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 443000 molecules/cell in log phase SD medium.1 Publication

Caution

To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = monoubiquitinated Lys-124.Curated

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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.