Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10854

- H2B1M_MOUSE

UniProt

P10854 - H2B1M_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone H2B type 1-M

Gene

Hist1h2bm

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_198626. Meiotic synapsis.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 1-M
Alternative name(s):
H2B 291B
Gene namesi
Name:Hist1h2bm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:2448404. Hist1h2bm.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 126125Histone H2B type 1-MPRO_0000071840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei6 – 61N6-acetyllysine; alternate1 Publication
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Modified residuei12 – 121N6-acetyllysine; alternate1 Publication
Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei15 – 151Phosphoserine; by STK4/MST12 Publications
Modified residuei16 – 161N6-acetyllysine; alternateBy similarity
Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei21 – 211N6-acetyllysine; alternateBy similarity
Modified residuei21 – 211N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei35 – 351N6-crotonyllysine; alternate1 Publication
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei37 – 371Phosphoserine; by AMPK1 Publication
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)By similarity

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.3 Publications
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.1 Publication

Keywords - PTMi

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

Proteomic databases

MaxQBiP10854.
PaxDbiP10854.
PRIDEiP10854.

PTM databases

PhosphoSiteiP10854.

Expressioni

Gene expression databases

BgeeiP10854.
CleanExiMM_HIST1H2BM.
ExpressionAtlasiP10854. baseline and differential.
GenevestigatoriP10854.

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

BioGridi235105. 1 interaction.
IntActiP10854. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP10854.
SMRiP10854. Positions 6-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiNOG289161.
GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiP10854.
KOiK11252.
OMAiPLVCHIS.
OrthoDBiEOG72VH8J.
PhylomeDBiP10854.
TreeFamiTF300212.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
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.

P10854 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEPTKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSSK
Length:126
Mass (Da):13,936
Last modified:January 23, 2007 - v2
Checksum:iFAE8378A44BE7028
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05863 Genomic DNA. Translation: CAA29292.1.
AY158928 Genomic DNA. Translation: AAO06238.1.
AL589651 Genomic DNA. Translation: CAI24107.1.
CCDSiCCDS26290.1.
PIRiS04153.
RefSeqiNP_835507.1. NM_178200.2.
XP_006516751.1. XM_006516688.1.
XP_006516752.1. XM_006516689.1.
UniGeneiMm.277425.

Genome annotation databases

EnsembliENSMUST00000110476; ENSMUSP00000106102; ENSMUSG00000096807.
GeneIDi319186.
KEGGimmu:319186.
UCSCiuc007prd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05863 Genomic DNA. Translation: CAA29292.1 .
AY158928 Genomic DNA. Translation: AAO06238.1 .
AL589651 Genomic DNA. Translation: CAI24107.1 .
CCDSi CCDS26290.1.
PIRi S04153.
RefSeqi NP_835507.1. NM_178200.2.
XP_006516751.1. XM_006516688.1.
XP_006516752.1. XM_006516689.1.
UniGenei Mm.277425.

3D structure databases

ProteinModelPortali P10854.
SMRi P10854. Positions 6-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 235105. 1 interaction.
IntActi P10854. 3 interactions.

PTM databases

PhosphoSitei P10854.

Proteomic databases

MaxQBi P10854.
PaxDbi P10854.
PRIDEi P10854.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000110476 ; ENSMUSP00000106102 ; ENSMUSG00000096807 .
GeneIDi 319186.
KEGGi mmu:319186.
UCSCi uc007prd.1. mouse.

Organism-specific databases

CTDi 8342.
MGIi MGI:2448404. Hist1h2bm.

Phylogenomic databases

eggNOGi NOG289161.
GeneTreei ENSGT00760000118976.
HOGENOMi HOG000231213.
HOVERGENi HBG007774.
InParanoidi P10854.
KOi K11252.
OMAi PLVCHIS.
OrthoDBi EOG72VH8J.
PhylomeDBi P10854.
TreeFami TF300212.

Enzyme and pathway databases

Reactomei REACT_198626. Meiotic synapsis.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

NextBioi 394326.
PROi P10854.
SOURCEi Search...

Gene expression databases

Bgeei P10854.
CleanExi MM_HIST1H2BM.
ExpressionAtlasi P10854. baseline and differential.
Genevestigatori P10854.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view ]
PANTHERi PTHR23428. PTHR23428. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00621. HISTONEH2B.
SMARTi SM00427. H2B. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00357. HISTONE_H2B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse histone H2A and H2B genes: four functional genes and a pseudogene undergoing gene conversion with a closely linked functional gene."
    Liu T.-J., Liu L., Marzluff W.F.
    Nucleic Acids Res. 15:3023-3039(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The human and mouse replication-dependent histone genes."
    Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
    Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BG AND HIST1H2BI).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Phosphorylation of histone H2B at DNA double-strand breaks."
    Fernandez-Capetillo O., Allis C.D., Nussenzweig A.
    J. Exp. Med. 199:1671-1677(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15.
  5. "Histone modifications associated with somatic hypermutation."
    Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., Schatz D.G.
    Immunity 23:101-110(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15.
  6. "Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation."
    Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B., Carling D., Thompson C.B., Jones R.G., Berger S.L.
    Science 329:1201-1205(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-37.
  7. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
    Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
    Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiH2B1M_MOUSE
AccessioniPrimary (citable) accession number: P10854
Secondary accession number(s): Q5T008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 123 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3