Reviewed,
UniProtKB/Swiss-Prot Q16778 (H2B2E_HUMAN)
Last modified
February 9, 2010.
Version 99.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Histone H2B type 2-E Alternative name(s): Histone H2B.q Short name=H2B/q Histone H2B-GL105 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 126 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. Ref.8 Ref.10 Ref.11 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. Ref.8 Ref.10 Ref.11 |
| Subunit structure | 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. |
| Subcellular location | |
| Post-translational modification | Monoubiquitination of Lys-121 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. Phosphorylated on Ser-15 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. Ref.14 |
| Sequence similarities | Belongs to the histone H2B family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosomal protein Nucleosome core Nucleus |
| Ligand | DNA-binding |
| Molecular function | Antibiotic Antimicrobial |
| PTM | Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Ref.1Non-traceable author statement. Source: UniProtKB |
| Cellular component | nucleosome Ref.1 Non-traceable author statement. Source: UniProtKB nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Ref.1 Non-traceable author statement. Source: UniProtKB protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.8 Ref.10 Ref.11 Ref.9 | ||||||
| Chain | 2 – 126 | 125 | Histone H2B type 2-E | PRO_0000071835 | |||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | N6-acetyllysine Ref.12 Ref.16 Ref.19 | ||||||
| Modified residue | 12 | 1 | N6-acetyllysine Ref.12 Ref.19 | ||||||
| Modified residue | 13 | 1 | N6-acetyllysine Ref.12 Ref.16 Ref.19 | ||||||
| Modified residue | 15 | 1 | Phosphoserine; by STK4 Ref.14 | ||||||
| Modified residue | 16 | 1 | N6-acetyllysine Ref.12 Ref.16 Ref.19 | ||||||
| Modified residue | 17 | 1 | N6-acetyllysine Ref.12 Ref.19 | ||||||
| Modified residue | 21 | 1 | N6-acetyllysine Ref.12 Ref.16 Ref.19 | ||||||
| Modified residue | 24 | 1 | N6-acetyllysine Ref.19 | ||||||
| Modified residue | 47 | 1 | N6-methyllysine Ref.12 | ||||||
| Modified residue | 58 | 1 | N6,N6-dimethyllysine Ref.12 | ||||||
| Modified residue | 109 | 1 | N6-acetyllysine; alternate Ref.19 | ||||||
| Modified residue | 109 | 1 | N6-methyllysine; alternate Ref.12 | ||||||
| Cross-link | 121 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 Ref.15 Ref.17 | |||||||
Experimental info | |||||||||
| Sequence conflict | 5 | 1 | A → S in AAH98112. Ref.7 | ||||||
| Sequence conflict | 5 | 1 | A → S in AAH98289. Ref.7 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing." Collart D., Romain P.L., Huebner K., Pockwinse S., Pilapil S., Cannizzaro L.A., Lian J.B., Croce C.M., Stein J.L., Stein G.S. J. Cell. Biochem. 50:374-385(1992) [PubMed: 1469070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lymphocyte. |
| [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: 12408966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [5] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [7] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Ovary. |
| [8] | "Endotoxin-neutralizing antimicrobial proteins of the human placenta." Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C. J. Immunol. 168:2356-2364(2002) [PubMed: 11859126] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION. |
| [9] | "Biochemical and antibacterial analysis of human wound and blister fluid." Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A., Liden S., Joernvall H., Boman H.G. Eur. J. Biochem. 237:86-92(1996) [PubMed: 8620898] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. |
| [10] | "Antimicrobial peptides in the first line defence of human colon mucosa." Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H., Agerberth B. Peptides 24:523-530(2003) [PubMed: 12860195] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION. |
| [11] | "Antimicrobial polypeptides of the human colonic epithelium." Howell S.J., Wilk D., Yadav S.P., Bevins C.L. Peptides 24:1763-1770(2003) [PubMed: 15019208] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION. |
| [12] | "Quantitative proteomic analysis of post-translational modifications of human histones." Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N. Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed: 16627869] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109, UBIQUITINATION AT LYS-121, MASS SPECTROMETRY. |
| [13] | "Isolation and characterization of a cDNA from a human histone H2B gene which is reciprocally expressed in relation to replication-dependent H2B histone genes during HL60 cell differentiation." Collart D., Ramsey-Ewing A., Bortell R., Lian J., Stein J., Stein G. Biochemistry 30:1610-1617(1991) [PubMed: 1993178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-126. Tissue: Liver. |
| [14] | "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase." Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D. Cell 113:507-517(2003) [PubMed: 12757711] [Abstract] Cited for: PHOSPHORYLATION AT SER-15. |
| [15] | "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation." Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Mol. Cell 20:601-611(2005) [PubMed: 16307923] [Abstract] Cited for: UBIQUITINATION AT LYS-121. |
| [16] | "Inhibition of core histones acetylation by carcinogenic nickel(II)." Golebiowski F., Kasprzak K.S. Mol. Cell. Biochem. 279:133-139(2005) [PubMed: 16283522] [Abstract] Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21. |
| [17] | "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II." Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Cell 125:703-717(2006) [PubMed: 16713563] [Abstract] Cited for: UBIQUITINATION AT LYS-121. |
| [18] | "Gene-specific characterization of human histone H2B by electron capture dissociation." Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J. J. Proteome Res. 5:233-239(2006) [PubMed: 16457587] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. |
| [19] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-109, MASS SPECTROMETRY. Tissue: Epithelium. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00003935. |
| PIR | I37467. S65409. |
| RefSeq | NP_003519.1. |
| UniGene | Hs.2178 |
3D structure databases | |
| SMR | Q16778. Positions 5-126. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q16778. 3 interactions. |
| STRING | Q16778. |
PTM databases | |
| PhosphoSite | Q16778. |
Proteomic databases | |
| PRIDE | Q16778. |
Genome annotation databases | |
| Ensembl | ENST00000369155; ENSP00000358151; ENSG00000184678; Homo sapiens. [Genome view] |
| GeneID | 8349. |
| KEGG | hsa:8349. |
| UCSC | uc001etc.1. human. |
Organism-specific databases | |
| CTD | 8349. |
| GeneCards | GC01M148082. |
| H-InvDB | HIX0001004. |
| HGNC | HGNC:4760. HIST2H2BE. |
| MIM | 601831. gene. |
| PharmGKB | PA29135. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | maNOG20177. |
| HOGENOM | HBG715487. |
| HOVERGEN | Q16778. |
| InParanoid | Q16778. |
| OMA | NRTHRAD. |
| OrthoDB | EOG9W9MP7. |
| PhylomeDB | Q16778. |
Enzyme and pathway databases | |
| Reactome | REACT_7970. Telomere Maintenance. |
Gene expression databases | |
| ArrayExpress | Q16778. |
| Bgee | Q16778. |
| CleanEx | HS_HIST2H2BE. |
| Genevestigator | Q16778. |
| GermOnline | ENSG00000184678. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view] |
| Gene3D | G3DSA:1.10.20.10. Histone-fold. 1 hit. |
| PANTHER | PTHR23428. Histone_H2B. 1 hit. |
| Pfam | PF00125. Histone. 1 hit. [Graphical view] |
| PRINTS | PR00621. HISTONEH2B. |
| SMART | SM00427. H2B. 1 hit. [Graphical view] |
| PROSITE | PS00357. HISTONE_H2B. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 31268. |
| SOURCE | Search... |
Entry information
| Entry name | H2B2E_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q16778 Secondary accession number(s): A3KMC7 Q9UE88 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


