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Q00715

- H2B1_RAT

UniProt

Q00715 - H2B1_RAT

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Protein
Histone H2B type 1
Gene
N/A
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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.
Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid By similarity.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 125124Histone H2B type 1
PRO_0000071841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylproline By similarity
Modified residuei6 – 61N6-acetyllysine; alternate1 Publication
Modified residuei6 – 61N6-crotonyllysine; alternate By similarity
Modified residuei12 – 121N6-acetyllysine; alternate By similarity
Modified residuei12 – 121N6-crotonyllysine; alternate By similarity
Modified residuei13 – 131N6-acetyllysine; alternate1 Publication
Modified residuei13 – 131N6-crotonyllysine; alternate By similarity
Modified residuei15 – 151Phosphoserine; by STK4/MST1 By similarity
Modified residuei16 – 161N6-acetyllysine; alternate1 Publication
Modified residuei16 – 161N6-crotonyllysine; alternate By similarity
Modified residuei17 – 171N6-acetyllysine; alternate By similarity
Modified residuei17 – 171N6-crotonyllysine; alternate By similarity
Modified residuei21 – 211N6-acetyllysine; alternate1 Publication
Modified residuei21 – 211N6-crotonyllysine; alternate By similarity
Modified residuei24 – 241N6-acetyllysine; alternate By similarity
Modified residuei24 – 241N6-crotonyllysine; alternate By similarity
Modified residuei35 – 351N6-crotonyllysine; alternate By similarity
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei37 – 371Phosphoserine; by AMPK By similarity
Modified residuei47 – 471N6-methyllysine By similarity
Modified residuei58 – 581N6,N6-dimethyllysine By similarity
Modified residuei79 – 791Dimethylated arginine By similarity
Modified residuei85 – 851N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei85 – 851N6-acetyllysine; alternate By similarity
Modified residuei86 – 861Omega-N-methylarginine By similarity
Modified residuei92 – 921Omega-N-methylarginine By similarity
Modified residuei108 – 1081N6-methyllysine By similarity
Modified residuei115 – 1151Phosphothreonine By similarity
Modified residuei116 – 1161N6-methylated lysine By similarity
Cross-linki120 – 120Glycyl 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-120 (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.
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.
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.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ00715.
PRIDEiQ00715.

PTM databases

PhosphoSiteiQ00715.

Expressioni

Gene expression databases

GenevestigatoriQ00715.

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

BioGridi249180. 2 interactions.
IntActiQ00715. 1 interaction.
STRINGi10116.ENSRNOP00000028779.

Structurei

3D structure databases

ProteinModelPortaliQ00715.
SMRiQ00715. Positions 5-125.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.

Phylogenomic databases

eggNOGiNOG289161.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiQ00715.
KOiK11252.
PhylomeDBiQ00715.

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.

Q00715-1 [UniParc]FASTAAdd to Basket

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MPEPAKSRPA PKKGSKKAVT KAQKKDGKER KRSRKESYSV YVYKVLKQVH    50
PDTGISSKAM GIMNSFVNDI FERIAGERRL AHYNKRSTIT SREIQTAVRL 100
LLPGELAKHA VSEGTKAVTK YTSSK 125
Length:125
Mass (Da):13,990
Last modified:January 23, 2007 - v2
Checksum:i43BF1F86A6DA221A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59961 Genomic DNA. Translation: CAA42585.1.
PIRiB45945.
S26185.
RefSeqiNP_072173.1. NM_022647.1.
UniGeneiRn.112590.

Genome annotation databases

GeneIDi64647.
KEGGirno:64647.
UCSCiRGD:621439. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59961 Genomic DNA. Translation: CAA42585.1 .
PIRi B45945.
S26185.
RefSeqi NP_072173.1. NM_022647.1.
UniGenei Rn.112590.

3D structure databases

ProteinModelPortali Q00715.
SMRi Q00715. Positions 5-125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249180. 2 interactions.
IntActi Q00715. 1 interaction.
STRINGi 10116.ENSRNOP00000028779.

PTM databases

PhosphoSitei Q00715.

Proteomic databases

PaxDbi Q00715.
PRIDEi Q00715.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 64647.
KEGGi rno:64647.
UCSCi RGD:621439. rat.

Organism-specific databases

CTDi 8340.

Phylogenomic databases

eggNOGi NOG289161.
HOGENOMi HOG000231213.
HOVERGENi HBG007774.
InParanoidi Q00715.
KOi K11252.
PhylomeDBi Q00715.

Miscellaneous databases

NextBioi 613637.

Gene expression databases

Genevestigatori Q00715.

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

  1. "Presence of a bi-directional S phase-specific transcription regulatory element in the promoter shared by testis-specific TH2A and TH2B histone genes."
    Huh N.E., Hwang I., Lim K., You K.H., Chae C.-B.
    Nucleic Acids Res. 19:93-98(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  2. "Molecular cloning and differential expression of somatic and testis-specific H2B histone genes during rat spermatogenesis."
    Kim Y.-J., Hwang I., Tres L.L., Kierszenbaum A.L., Chae C.-B.
    Dev. Biol. 124:23-34(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 36-44; 48-73 AND 100-108, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Inhibition of core histones acetylation by carcinogenic nickel(II)."
    Golebiowski F., Kasprzak K.S.
    Mol. Cell. Biochem. 279:133-139(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.

Entry informationi

Entry nameiH2B1_RAT
AccessioniPrimary (citable) accession number: Q00715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 108 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

External Data

Dasty 3

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