Skip Header

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

UniProtKB - P70696 (H2B1A_MOUSE)

UniProt

P70696 - H2B1A_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-A

Gene

Hist1h2ba

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. 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.1 Publication

GO - Molecular functioni

GO - Biological processi

  • chromatin organization Source: MGI
  • inflammatory response Source: MGI
  • mononuclear cell migration Source: MGI
  • nucleosome assembly Source: UniProtKB
  • nucleosome disassembly Source: UniProtKB
  • plasminogen activation Source: MGI
  • positive regulation of binding Source: MGI
  • spermatogenesis, exchange of chromosomal proteins Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-3214847. HATs acetylate histones.
R-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 1-A
Alternative name(s):
Histone H2B, testis
Testis-specific histone H2B
Gene namesi
Name:Hist1h2ba
Synonyms:Th2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2448375. Hist1h2ba.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of plasma membrane Source: MGI
  • nuclear chromosome, telomeric region Source: MGI
  • nuclear nucleosome Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleosome Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 127126Histone H2B type 1-APRO_0000071843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei7 – 71N6-acetyllysine; alternateBy similarity
Modified residuei7 – 71N6-crotonyllysine; alternate1 Publication
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei14 – 141N6-acetyllysine; alternateBy similarity
Modified residuei14 – 141N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei18 – 181N6-acetyllysine; alternateBy similarity
Modified residuei18 – 181N6-crotonyllysine; alternate1 Publication
Modified residuei22 – 221N6-acetyllysine; alternateBy similarity
Modified residuei22 – 221N6-crotonyllysine; alternate1 Publication
Modified residuei25 – 251N6-acetyllysine; alternateBy similarity
Modified residuei25 – 251N6-crotonyllysine; alternate1 Publication
Modified residuei36 – 361N6-crotonyllysine; alternate1 Publication
Cross-linki36 – 36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei48 – 481N6-methyllysineBy similarity
Modified residuei59 – 591N6,N6-dimethyllysineBy similarity
Modified residuei81 – 811Dimethylated arginineBy similarity
Modified residuei87 – 871N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei87 – 871N6-acetyllysine; alternateBy similarity
Modified residuei88 – 881Omega-N-methylarginineBy similarity
Modified residuei94 – 941Omega-N-methylarginineBy similarity
Modified residuei110 – 1101N6-methyllysineBy similarity
Modified residuei117 – 1171PhosphothreonineBy similarity
Modified residuei118 – 1181N6-methylated lysineBy similarity
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Monoubiquitination at Lys-36 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 of Lys-122 (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
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
Acetylated during spermatogenesis. Acetylated form is most abundant in spermatogonia compared to spermatocytes and round spermatids (By similarity).By similarity
Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids.By similarity
Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP70696.
PaxDbiP70696.
PeptideAtlasiP70696.
PRIDEiP70696.
TopDownProteomicsiP70696.

PTM databases

iPTMnetiP70696.
PhosphoSiteiP70696.

Expressioni

Tissue specificityi

Mainly expressed in testis, and the corresponding protein is also present in mature sperm. Also present in metaphase oocytes (at protein level).2 Publications

Developmental stagei

Accumulates at 10 day postpartum (dpp), when pre-leptotene/leptotene spermatocytes first appear and when H2B expression shows a drastic decrease. Replaces H2B by 18 dpp in spermatocytes. Also present in metaphase oocytes and in the female pronucleus at fertilization and is also rapidly incorporated into the male pronucleus.1 Publication

Gene expression databases

BgeeiENSMUSG00000050799.
CleanExiMM_HIST1H2BA.

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.1 Publication

Protein-protein interaction databases

BioGridi235096. 1 interaction.
IntActiP70696. 1 interaction.
STRINGi10090.ENSMUSP00000056604.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5011Combined sources
Helixi58 – 8528Combined sources
Beta strandi89 – 913Combined sources
Helixi93 – 10311Combined sources
Helixi106 – 12419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3X1TX-ray2.81D/H2-127[»]
3X1VX-ray2.92D/H2-127[»]
ProteinModelPortaliP70696.
SMRiP70696. Positions 7-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiP70696.
KOiK11252.
OMAiHPRMSIM.
OrthoDBiEOG091G0XGD.
PhylomeDBiP70696.
TreeFamiTF300212.

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.

P70696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEVAVKGAT ISKKGFKKAV TKTQKKEGRK RKRCRKESYS IYIYKVLKQV 
        60         70         80         90        100
HPDTGISSKA MSIMNSFVTD IFERIASEAS RLAHYNKRST ITSREIQTAV 
       110        120 
RLLLPGELAK HAVSEGTKAV TKYTSSK
Length:127
Mass (Da):14,237
Last modified:January 23, 2007 - v3
Checksum:iF9A6180E4D005AF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90778 Genomic DNA. Translation: CAA62299.1.
AY158939 Genomic DNA. Translation: AAO06249.1.
AL606464 Genomic DNA. Translation: CAI35973.1.
CCDSiCCDS26373.1.
RefSeqiNP_783594.1. NM_175663.2.
UniGeneiMm.377879.

Genome annotation databases

EnsembliENSMUST00000052776; ENSMUSP00000056604; ENSMUSG00000050799.
GeneIDi319177.
KEGGimmu:319177.
UCSCiuc007pvi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90778 Genomic DNA. Translation: CAA62299.1.
AY158939 Genomic DNA. Translation: AAO06249.1.
AL606464 Genomic DNA. Translation: CAI35973.1.
CCDSiCCDS26373.1.
RefSeqiNP_783594.1. NM_175663.2.
UniGeneiMm.377879.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3X1TX-ray2.81D/H2-127[»]
3X1VX-ray2.92D/H2-127[»]
ProteinModelPortaliP70696.
SMRiP70696. Positions 7-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi235096. 1 interaction.
IntActiP70696. 1 interaction.
STRINGi10090.ENSMUSP00000056604.

PTM databases

iPTMnetiP70696.
PhosphoSiteiP70696.

Proteomic databases

EPDiP70696.
PaxDbiP70696.
PeptideAtlasiP70696.
PRIDEiP70696.
TopDownProteomicsiP70696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052776; ENSMUSP00000056604; ENSMUSG00000050799.
GeneIDi319177.
KEGGimmu:319177.
UCSCiuc007pvi.2. mouse.

Organism-specific databases

CTDi255626.
MGIiMGI:2448375. Hist1h2ba.

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiP70696.
KOiK11252.
OMAiHPRMSIM.
OrthoDBiEOG091G0XGD.
PhylomeDBiP70696.
TreeFamiTF300212.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-3214847. HATs acetylate histones.
R-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

PROiP70696.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000050799.
CleanExiMM_HIST1H2BA.

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 nameiH2B1A_MOUSE
AccessioniPrimary (citable) accession number: P70696
Secondary accession number(s): Q5NCL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 129 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.