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Protein

Histone H2B type 2-E

Gene

HIST2H2BE

Organism
Homo sapiens (Human)
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.
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.

GO - Molecular functioni

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • innate immune response in mucosa Source: UniProtKB
  • nucleosome assembly Source: GO_Central

Keywordsi

Molecular functionAntibiotic, Antimicrobial, DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214847. HATs acetylate histones.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 2-E
Alternative name(s):
Histone H2B-GL105
Histone H2B.q
Short name:
H2B/q
Gene namesi
Name:HIST2H2BE
Synonyms:H2BFQ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4760. HIST2H2BE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: HPA
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleosome Source: UniProtKB
  • nucleus Source: UniProtKB

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000184678.
PharmGKBiPA29135.

Polymorphism and mutation databases

BioMutaiHIST2H2BE.
DMDMi7387736.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity4 Publications
ChainiPRO_00000718352 – 126Histone H2B type 2-EAdd BLAST125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylprolineBy similarity1
Modified residuei6N6-acetyllysine; alternate2 Publications1
Modified residuei6N6-crotonyllysine; alternate1 Publication1
Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei12N6-acetyllysine; alternate1 Publication1
Modified residuei12N6-crotonyllysine; alternate1 Publication1
Modified residuei13N6-acetyllysine; alternate2 Publications1
Modified residuei13N6-crotonyllysine; alternate1 Publication1
Modified residuei15Phosphoserine; by STK4/MST11 Publication1
Modified residuei16N6-acetyllysine; alternate2 Publications1
Modified residuei16N6-crotonyllysine; alternate1 Publication1
Modified residuei17N6-acetyllysine; alternate1 Publication1
Modified residuei17N6-crotonyllysine; alternate1 Publication1
Modified residuei21N6-acetyllysine; alternate2 Publications1
Modified residuei21N6-crotonyllysine; alternate1 Publication1
Cross-linki21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei24N6-acetyllysine; alternateBy similarity1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei35N6-crotonyllysine; alternate1 Publication1
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei37Phosphoserine; by AMPKBy similarity1
Modified residuei47N6-methyllysine1 Publication1
Modified residuei58N6,N6-dimethyllysine1 Publication1
Modified residuei80Dimethylated arginineBy similarity1
Modified residuei86N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei86N6-acetyllysine; alternateBy similarity1
Modified residuei87Omega-N-methylarginineBy similarity1
Modified residuei93Omega-N-methylarginineBy similarity1
Modified residuei109N6-methyllysine1 Publication1
Glycosylationi113O-linked (GlcNAc) serineBy similarity1
Modified residuei116PhosphothreonineBy similarity1
Modified residuei117N6-methylated lysineBy similarity1
Cross-linki121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications

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.1 Publication
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (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.By similarity1 Publication
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

EPDiQ16778.
MaxQBiQ16778.
PaxDbiQ16778.
PeptideAtlasiQ16778.
PRIDEiQ16778.
TopDownProteomicsiQ16778.

PTM databases

iPTMnetiQ16778.
PhosphoSitePlusiQ16778.
SwissPalmiQ16778.

Expressioni

Gene expression databases

BgeeiENSG00000184678.
CleanExiHS_HIST2H2BE.
GenevisibleiQ16778. HS.

Organism-specific databases

HPAiHPA042205.
HPA043013.
HPA048671.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
AP2M1Q96CW14EBI-1056125,EBI-297683

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113945. 125 interactors.
DIPiDIP-39324N.
IntActiQ16778. 16 interactors.
MINTiMINT-1461208.
STRINGi9606.ENSP00000358151.

Structurei

Secondary structure

1126
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 49Combined sources11
Helixi57 – 82Combined sources26
Helixi92 – 102Combined sources11
Helixi105 – 123Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NFTX-ray2.61A/B/C/D34-126[»]
ProteinModelPortaliQ16778.
SMRiQ16778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiQ16778.
KOiK11252.
OMAiDIFDRMA.
OrthoDBiEOG091G0XGD.
PhylomeDBiQ16778.
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.

Q16778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSSK
Length:126
Mass (Da):13,920
Last modified:January 23, 2007 - v3
Checksum:i0410A881ABBE6647
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5A → S in AAH98112 (PubMed:15489334).Curated1
Sequence conflicti5A → S in AAH98289 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57985 Genomic DNA. Translation: CAA41051.1.
AY131979 Genomic DNA. Translation: AAN59961.1.
CR541895 mRNA. Translation: CAG46693.1.
AK289725 mRNA. Translation: BAF82414.1.
AL591493 Genomic DNA. Translation: CAI12568.1.
CH471121 Genomic DNA. Translation: EAW53605.1.
BC005827 mRNA. Translation: AAH05827.1.
BC069193 mRNA. Translation: AAH69193.1.
BC096121 mRNA. Translation: AAH96121.1.
BC098112 mRNA. Translation: AAH98112.1.
BC098289 mRNA. Translation: AAH98289.1.
BC107084 mRNA. Translation: AAI07085.1.
BC107085 mRNA. Translation: AAI07086.1.
M60756 mRNA. Translation: AAA63192.1.
CCDSiCCDS936.1.
PIRiI37467.
S65409.
RefSeqiNP_003519.1. NM_003528.2.
UniGeneiHs.2178.

Genome annotation databases

EnsembliENST00000369155; ENSP00000358151; ENSG00000184678.
GeneIDi8349.
KEGGihsa:8349.
UCSCiuc001etc.4. human.

Similar proteinsi

Entry informationi

Entry nameiH2B2E_HUMAN
AccessioniPrimary (citable) accession number: Q16778
Secondary accession number(s): A3KMC7
, A8K110, Q4KMY1, Q5QNX0, Q9UE88
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 172 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families