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Protein

Histone H2B type 1

Gene
N/A
Organism
Bos taurus (Bovine)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componentsi: Chromosome 23, Chromosome 3

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 similarity3 Publications
Chaini2 – 126125Histone H2B type 1PRO_0000071825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei6 – 61N6-acetyllysine; alternateBy similarity
Modified residuei6 – 61N6-crotonyllysine; alternateBy similarity
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei12 – 121N6-acetyllysine; alternateBy similarity
Modified residuei12 – 121N6-crotonyllysine; alternateBy similarity
Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
Modified residuei13 – 131N6-crotonyllysine; alternateBy similarity
Modified residuei15 – 151Phosphoserine; by STK4/MST1By similarity
Modified residuei16 – 161N6-acetyllysine; alternateBy similarity
Modified residuei16 – 161N6-crotonyllysine; alternateBy similarity
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-crotonyllysine; alternateBy similarity
Modified residuei21 – 211N6-acetyllysine; alternateBy similarity
Modified residuei21 – 211N6-crotonyllysine; alternateBy similarity
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-crotonyllysine; alternateBy similarity
Modified residuei35 – 351N6-crotonyllysine; alternateBy similarity
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei37 – 371Phosphoserine; by AMPKBy similarity
Modified residuei47 – 471N6-methyllysineBy similarity
Modified residuei58 – 581N6,N6-dimethyllysineBy similarity
Modified residuei80 – 801Dimethylated arginineBy similarity
Modified residuei86 – 861N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei86 – 861N6-acetyllysine; alternateBy similarity
Modified residuei87 – 871Omega-N-methylarginineBy similarity
Modified residuei93 – 931Omega-N-methylarginineBy similarity
Modified residuei109 – 1091N6-methyllysineBy similarity
Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
Modified residuei116 – 1161PhosphothreonineBy similarity
Modified residuei117 – 1171N6-methylated lysineBy similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity).By similarity
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity).By similarity
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
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP62808.
PeptideAtlasiP62808.
PRIDEiP62808.

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.

Protein-protein interaction databases

BioGridi542671. 1 interaction.
MINTiMINT-1519773.
STRINGi9913.ENSBTAP00000055514.

Structurei

3D structure databases

ProteinModelPortaliP62808.
SMRiP62808. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00760000118976.
ENSGT00840000129751.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiP62808.
KOiK11252.
OMAiIGPILWK.
OrthoDBiEOG72VH8J.
TreeFamiTF300212.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
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.

P62808-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSSK
Length:126
Mass (Da):13,906
Last modified:January 23, 2007 - v2
Checksum:iFAE1479F44BE703D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211K → T AA sequence (PubMed:6320184).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT029886 mRNA. Translation: ABM06136.1.
BC108143 mRNA. Translation: AAI08144.1.
BC142102 mRNA. Translation: AAI42103.1.
PIRiA02605. HSBO22.
RefSeqiNP_001032546.1. NM_001037469.2.
XP_002686101.1. XM_002686055.5.
XP_002697553.1. XM_002697507.4.
XP_002697561.1. XM_002697515.4.
XP_002702931.1. XM_002702885.4.
XP_003583950.1. XM_003583902.4.
XP_003587771.1. XM_003587723.4.
XP_010816749.1. XM_010818447.2.
XP_010816750.1. XM_010818448.1.
XP_010816751.1. XM_010818449.2.
XP_010816752.1. XM_010818450.1.
XP_010816754.1. XM_010818452.2.
XP_010816755.1. XM_010818453.1.
XP_010816756.1. XM_010818454.2.
XP_010816757.1. XM_010818455.1.
XP_010816759.1. XM_010818457.2.
XP_010816816.1. XM_010818514.1.
XP_010823688.1. XM_010825386.2.
XP_010823689.1. XM_010825387.1.
XP_010823690.1. XM_010825388.2.
XP_010823691.1. XM_010825389.1.
XP_010823693.1. XM_010825391.2.
XP_010823694.1. XM_010825392.2.
XP_010823695.1. XM_010825393.2.
XP_010823697.1. XM_010825395.2.
XP_010823715.1. XM_010825413.2.
XP_010825135.2. XM_010826833.2.
XP_015315427.1. XM_015459941.1.
XP_015324467.1. XM_015468981.1.
XP_581429.3. XM_581429.7.
XP_599845.2. XM_599845.8.
UniGeneiBt.43773.
Bt.61174.

Genome annotation databases

EnsembliENSBTAT00000024155; ENSBTAP00000024155; ENSBTAG00000038604.
ENSBTAT00000033366; ENSBTAP00000052160; ENSBTAG00000024177.
ENSBTAT00000033371; ENSBTAP00000048201; ENSBTAG00000024182.
ENSBTAT00000033378; ENSBTAP00000049889; ENSBTAG00000024188.
ENSBTAT00000039714; ENSBTAP00000039503; ENSBTAG00000031785.
ENSBTAT00000045039; ENSBTAP00000051376; ENSBTAG00000031760.
ENSBTAT00000045047; ENSBTAP00000051428; ENSBTAG00000031770.
ENSBTAT00000045053; ENSBTAP00000047687; ENSBTAG00000031776.
ENSBTAT00000045227; ENSBTAP00000052168; ENSBTAG00000031889.
ENSBTAT00000046026; ENSBTAP00000055514; ENSBTAG00000032455.
GeneIDi100295221.
104968456.
104975676.
505183.
506306.
615043.
616776.
616868.
787269.
787465.
KEGGibta:100295221.
bta:104968456.
bta:104975676.
bta:505183.
bta:506306.
bta:615043.
bta:616868.
bta:787269.
bta:787465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT029886 mRNA. Translation: ABM06136.1.
BC108143 mRNA. Translation: AAI08144.1.
BC142102 mRNA. Translation: AAI42103.1.
PIRiA02605. HSBO22.
RefSeqiNP_001032546.1. NM_001037469.2.
XP_002686101.1. XM_002686055.5.
XP_002697553.1. XM_002697507.4.
XP_002697561.1. XM_002697515.4.
XP_002702931.1. XM_002702885.4.
XP_003583950.1. XM_003583902.4.
XP_003587771.1. XM_003587723.4.
XP_010816749.1. XM_010818447.2.
XP_010816750.1. XM_010818448.1.
XP_010816751.1. XM_010818449.2.
XP_010816752.1. XM_010818450.1.
XP_010816754.1. XM_010818452.2.
XP_010816755.1. XM_010818453.1.
XP_010816756.1. XM_010818454.2.
XP_010816757.1. XM_010818455.1.
XP_010816759.1. XM_010818457.2.
XP_010816816.1. XM_010818514.1.
XP_010823688.1. XM_010825386.2.
XP_010823689.1. XM_010825387.1.
XP_010823690.1. XM_010825388.2.
XP_010823691.1. XM_010825389.1.
XP_010823693.1. XM_010825391.2.
XP_010823694.1. XM_010825392.2.
XP_010823695.1. XM_010825393.2.
XP_010823697.1. XM_010825395.2.
XP_010823715.1. XM_010825413.2.
XP_010825135.2. XM_010826833.2.
XP_015315427.1. XM_015459941.1.
XP_015324467.1. XM_015468981.1.
XP_581429.3. XM_581429.7.
XP_599845.2. XM_599845.8.
UniGeneiBt.43773.
Bt.61174.

3D structure databases

ProteinModelPortaliP62808.
SMRiP62808. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi542671. 1 interaction.
MINTiMINT-1519773.
STRINGi9913.ENSBTAP00000055514.

Proteomic databases

PaxDbiP62808.
PeptideAtlasiP62808.
PRIDEiP62808.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024155; ENSBTAP00000024155; ENSBTAG00000038604.
ENSBTAT00000033366; ENSBTAP00000052160; ENSBTAG00000024177.
ENSBTAT00000033371; ENSBTAP00000048201; ENSBTAG00000024182.
ENSBTAT00000033378; ENSBTAP00000049889; ENSBTAG00000024188.
ENSBTAT00000039714; ENSBTAP00000039503; ENSBTAG00000031785.
ENSBTAT00000045039; ENSBTAP00000051376; ENSBTAG00000031760.
ENSBTAT00000045047; ENSBTAP00000051428; ENSBTAG00000031770.
ENSBTAT00000045053; ENSBTAP00000047687; ENSBTAG00000031776.
ENSBTAT00000045227; ENSBTAP00000052168; ENSBTAG00000031889.
ENSBTAT00000046026; ENSBTAP00000055514; ENSBTAG00000032455.
GeneIDi100295221.
104968456.
104975676.
505183.
506306.
615043.
616776.
616868.
787269.
787465.
KEGGibta:100295221.
bta:104968456.
bta:104975676.
bta:505183.
bta:506306.
bta:615043.
bta:616868.
bta:787269.
bta:787465.

Organism-specific databases

CTDi8340.

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00760000118976.
ENSGT00840000129751.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiP62808.
KOiK11252.
OMAiIGPILWK.
OrthoDBiEOG72VH8J.
TreeFamiTF300212.

Enzyme and pathway databases

ReactomeiR-BTA-3214847. HATs acetylate histones.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus and Hereford.
    Tissue: Liver and Thymus.
  3. "Calf thymus lysine- and serine-rich histone. 3. Complete amino acid sequence and its implication for interactions of histones with DNA."
    Iwai K., Hayashi H., Ishikawa K.
    J. Biochem. 72:357-367(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-126.
  4. "Purification of bovine bone morphogenetic protein by hydroxyapatite chromatography."
    Urist M.R., Huo Y.K., Brownell A.G., Hohl W.M., Buyske J., Lietze A., Tempst P., Hunkapiller M., DeLange R.J.
    Proc. Natl. Acad. Sci. U.S.A. 81:371-375(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26.
  5. "Somatic histones are components of the perinuclear theca in bovine spermatozoa."
    Tovich P.R., Oko R.J.
    J. Biol. Chem. 278:32431-32438(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
  6. "Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin."
    Nickel B.E., Allis C.D., Davie J.R.
    Biochemistry 28:958-963(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.

Entry informationi

Entry nameiH2B1_BOVIN
AccessioniPrimary (citable) accession number: P62808
Secondary accession number(s): A1L599
, A5PJG5, P02278, Q32PE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 112 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.