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UniProtKB - P70696 (H2B1A_MOUSE)

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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 (PubMed:23884607, PubMed:28366643). 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 (PubMed:23884607). In condensing spermatids, the heterodimer between H2AFB1 and HIST1H2BA/TH2B is loaded onto the nucleosomes and promotes loading of transition proteins (TNP1 and TNP2) onto the nucleosomes (PubMed:28366643). Inclusion of the H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and allowing the invasion of nucleosomes by transition proteins (TNP1 and TNP2) (PubMed:28366643). Then, transition proteins drive the recruitment and processing of protamines, which are responsible for histone eviction (PubMed:28366643). Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization (PubMed:23884607). 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.2 Publications

GO - Molecular functioni

Complete GO annotation...

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...

Keywordsi

Molecular functionDNA-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-8866654. E3 ubiquitin ligases ubiquitinate target proteins.
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 H2B1 Publication
Gene namesi
Name:Hist1h2baImported
Synonyms:Th2b1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › 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
  • 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000718432 – 127Histone H2B type 1-AAdd BLAST126

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylprolineBy similarity1
Modified residuei7N6-acetyllysine; alternateBy similarity1
Modified residuei7N6-crotonyllysine; alternate1 Publication1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei13N6-acetyllysine; alternateBy similarity1
Modified residuei13N6-crotonyllysine; alternate1 Publication1
Modified residuei14N6-acetyllysine; alternateBy similarity1
Modified residuei14N6-crotonyllysine; alternate1 Publication1
Modified residuei17N6-acetyllysine; alternateBy similarity1
Modified residuei17N6-crotonyllysine; alternate1 Publication1
Modified residuei18N6-acetyllysine; alternateBy similarity1
Modified residuei18N6-crotonyllysine; alternate1 Publication1
Modified residuei22N6-acetyllysine; alternateBy similarity1
Modified residuei22N6-crotonyllysine; alternate1 Publication1
Modified residuei25N6-acetyllysine; alternateBy similarity1
Modified residuei25N6-crotonyllysine; alternate1 Publication1
Modified residuei36N6-crotonyllysine; alternate1 Publication1
Cross-linki36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei38PhosphoserineBy similarity1
Modified residuei48N6-methyllysineBy similarity1
Modified residuei59N6,N6-dimethyllysineBy similarity1
Modified residuei81Dimethylated arginineBy similarity1
Modified residuei87N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei87N6-acetyllysine; alternateBy similarity1
Modified residuei88Omega-N-methylarginineBy similarity1
Modified residuei94Omega-N-methylarginineBy similarity1
Modified residuei110N6-methyllysineBy similarity1
Modified residuei117PhosphothreonineBy similarity1
Modified residuei118N6-methylated lysineBy similarity1
Cross-linki122Glycyl 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.
MaxQBiP70696.
PaxDbiP70696.
PeptideAtlasiP70696.
PRIDEiP70696.
TopDownProteomicsiP70696.

PTM databases

iPTMnetiP70696.
PhosphoSitePlusiP70696.

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 (PubMed:23884607). Interacts with H2AFB1; preferentially dimerizes with H2AFB1 to form nucleosomes (PubMed:28366643).2 Publications

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi235096. 1 interactor.
IntActiP70696. 1 interactor.
STRINGi10090.ENSMUSP00000056604.

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 50Combined sources11
Helixi58 – 85Combined sources28
Beta strandi89 – 91Combined sources3
Helixi93 – 103Combined sources11
Helixi106 – 124Combined sources19

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiView protein in Pfam
PF00125. Histone. 1 hit.
PRINTSiPR00621. HISTONEH2B.
SMARTiView protein in SMART
SM00427. H2B. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiView protein in PROSITE
PS00357. HISTONE_H2B. 1 hit.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3X1TX-ray2.81D/H2-127[»]
3X1VX-ray2.92D/H2-127[»]
ProteinModelPortaliP70696.
SMRiP70696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi235096. 1 interactor.
IntActiP70696. 1 interactor.
STRINGi10090.ENSMUSP00000056604.

PTM databases

iPTMnetiP70696.
PhosphoSitePlusiP70696.

Proteomic databases

EPDiP70696.
MaxQBiP70696.
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.
OMAiSKEMSIM.
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-8866654. E3 ubiquitin ligases ubiquitinate target proteins.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

PROiPR:P70696.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000050799.
CleanExiMM_HIST1H2BA.

Family and domain databases

InterProiView protein in InterPro
IPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiView protein in Pfam
PF00125. Histone. 1 hit.
PRINTSiPR00621. HISTONEH2B.
SMARTiView protein in SMART
SM00427. H2B. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiView protein in PROSITE
PS00357. HISTONE_H2B. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiH2B1A_MOUSE
AccessioniPrimary (citable) accession number: P70696
Secondary accession number(s): Q5NCL9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 135 of the entry and version 3 of the sequence. See 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.