Reviewed, UniProtKB/Swiss-Prot Q16778 (H2B2E_HUMAN)

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

Name:	HIST2H2BE
Synonyms:	H2BFQ

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	Nucleus.
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.1 Non-traceable author statement. Source: UniProtKB
Cellular component	nucleosome Ref.1 Non-traceable author statement. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Ref.1 Non-traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PARP3	Q9Y6F1	1	EBI-1056125,EBI-1045281

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

	Sequence		Length	Mass (Da)
	Q16778-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0410A881ABBE6647	FASTA	126	13,920
	10 20 30 40 50 60 MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM 70 80 90 100 110 120 GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK

References

	« Hide 'large scale' referencesShow '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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., 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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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 , A8K110, Q4KMY1, Q5QNX0, Q9UE88

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 99 of the entry and version 3 of the sequence. [Complete 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.