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Protein

Histone H2B.1

Gene

HTB1

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.9 Publications

GO - Molecular functioni

  • DNA binding Source: SGD

GO - Biological processi

  • chromatin assembly or disassembly Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • nucleosome assembly Source: GO_Central
  • postreplication repair Source: SGD
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29804-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B.1
Alternative name(s):
Suppressor of Ty protein 12
Gene namesi
Name:HTB1
Synonyms:H2B1, SPT12
Ordered Locus Names:YDR224C
ORF Names:YD9934.09C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR224C.
SGDiS000002632. HTB1.

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)DescriptionActionsGraphical viewLength
Mutagenesisi7 – 8KK → AA: Reduces sumoylation. 1 Publication2
Mutagenesisi11S → A: Desensitizes cells to H(2)O(2) treatment. 1 Publication1
Mutagenesisi11S → E: Induces apoptotic-like features including chromatin condensation. 1 Publication1
Mutagenesisi17 – 18KK → AA: Reduces sumoylation. 1 Publication2
Mutagenesisi48V → F: Confers UV-radiation sensitivity; when associated with F-87 and S-88. 1 Publication1
Mutagenesisi87Y → F: Confers UV-radiation sensitivity; when associated with F-48 and S-88. 1 Publication1
Mutagenesisi88N → S: Confers UV-radiation sensitivity; when associated with F-48 and F-87. 1 Publication1
Mutagenesisi124K → R: Impairs ubiquitin conjugation, DNA double-strand brakes formation during meiosis and histone H3-K79 methylation. 5 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
ChainiPRO_00000719382 – 131Histone H2B.1Add BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7N6-acetyllysine; alternate1 Publication1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei8N6-acetyllysine; alternate1 Publication1
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei11Phosphoserine2 Publications1
Modified residuei12N6-acetyllysine2 Publications1
Modified residuei17N6-acetyllysine; alternate3 Publications1
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)6 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

MaxQBiP02293.
PRIDEiP02293.

PTM databases

iPTMnetiP02293.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
STH1P325973EBI-8088,EBI-18410
SWR1Q054712EBI-8088,EBI-22102

Protein-protein interaction databases

BioGridi32276. 393 interactors.
DIPiDIP-416N.
IntActiP02293. 226 interactors.
MINTiMINT-564492.

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 52Combined sources11
Beta strandi57 – 59Combined sources3
Helixi60 – 87Combined sources28
Beta strandi91 – 93Combined sources3
Helixi95 – 105Combined sources11
Helixi108 – 127Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JSSNMR-A37-131[»]
4KUDX-ray3.20D/H1-131[»]
4M6BX-ray1.78A/D37-131[»]
4WNNX-ray1.80B/D/F/H31-131[»]
ProteinModelPortaliP02293.
SMRiP02293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02293.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
InParanoidiP02293.
KOiK11252.
OMAiTMAANDI.
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.

P02293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKAEKKPA SKAPAEKKPA AKKTSTSTDG KKRSKARKET YSSYIYKVLK
60 70 80 90 100
QTHPDTGISQ KSMSILNSFV NDIFERIATE ASKLAAYNKK STISAREIQT
110 120 130
AVRLILPGEL AKHAVSEGTR AVTKYSSSTQ A
Length:131
Mass (Da):14,252
Last modified:January 23, 2007 - v2
Checksum:i9F5E9CFB341DB399
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01327 Genomic DNA. Translation: AAA88719.1.
U13239 Genomic DNA. Translation: AAC33141.1.
Z48612 Genomic DNA. Translation: CAA88504.1.
AY557724 Genomic DNA. Translation: AAS56050.1.
M37743 mRNA. Translation: AAA34694.2.
BK006938 Genomic DNA. Translation: DAA12066.1.
PIRiA02621. HSBY22.
RefSeqiNP_010510.3. NM_001180532.3.

Genome annotation databases

EnsemblFungiiYDR224C; YDR224C; YDR224C.
GeneIDi851810.
KEGGisce:YDR224C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01327 Genomic DNA. Translation: AAA88719.1.
U13239 Genomic DNA. Translation: AAC33141.1.
Z48612 Genomic DNA. Translation: CAA88504.1.
AY557724 Genomic DNA. Translation: AAS56050.1.
M37743 mRNA. Translation: AAA34694.2.
BK006938 Genomic DNA. Translation: DAA12066.1.
PIRiA02621. HSBY22.
RefSeqiNP_010510.3. NM_001180532.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JSSNMR-A37-131[»]
4KUDX-ray3.20D/H1-131[»]
4M6BX-ray1.78A/D37-131[»]
4WNNX-ray1.80B/D/F/H31-131[»]
ProteinModelPortaliP02293.
SMRiP02293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32276. 393 interactors.
DIPiDIP-416N.
IntActiP02293. 226 interactors.
MINTiMINT-564492.

PTM databases

iPTMnetiP02293.

Proteomic databases

MaxQBiP02293.
PRIDEiP02293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR224C; YDR224C; YDR224C.
GeneIDi851810.
KEGGisce:YDR224C.

Organism-specific databases

EuPathDBiFungiDB:YDR224C.
SGDiS000002632. HTB1.

Phylogenomic databases

GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
InParanoidiP02293.
KOiK11252.
OMAiTMAANDI.
OrthoDBiEOG092C5QTV.

Enzyme and pathway databases

BioCyciYEAST:G3O-29804-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02293.
PROiP02293.

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 nameiH2B1_YEAST
AccessioniPrimary (citable) accession number: P02293
Secondary accession number(s): D6VSK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.