Q16778 (H2B2E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B type 2-E

Alternative name(s):
Histone H2B-GL105
Histone H2B.q
Short name=H2B/q

Gene names

Name:	HIST2H2BE
Synonyms:	H2BFQ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. Chromosome.
Post-translational modification	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. 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. Ref.14 GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes 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. Ref.19
Sequence similarities	Belongs to the histone H2B family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
Molecular function	Antibiotic Antimicrobial
PTM	Acetylation Glycoprotein Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	nucleosome Non-traceable author statement Ref.1. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Non-traceable author statement Ref.1. Source: UniProtKB
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.9 Ref.10 Ref.11
	Chain	2 – 126	125	Histone H2B type 2-E		PRO_0000071835
Amino acid modifications
	Modified residue	2	1	N-acetylproline By similarity
	Modified residue	6	1	N6-acetyllysine; alternate Ref.12 Ref.16
	Modified residue	6	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	7	1	Phosphoserine By similarity
	Modified residue	12	1	N6-acetyllysine; alternate Ref.12
	Modified residue	12	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	13	1	N6-acetyllysine; alternate Ref.12 Ref.16
	Modified residue	13	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	15	1	Phosphoserine; by STK4/MST1 Ref.14
	Modified residue	16	1	N6-acetyllysine; alternate Ref.12 Ref.16
	Modified residue	16	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	17	1	N6-acetyllysine; alternate Ref.12
	Modified residue	17	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	21	1	N6-acetyllysine; alternate Ref.12 Ref.16
	Modified residue	21	1	N6-crotonyl-L-lysine; alternate
	Modified residue	24	1	N6-acetyllysine; alternate By similarity
	Modified residue	24	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	35	1	N6-acetyllysine; alternate By similarity
	Modified residue	35	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	37	1	Phosphoserine; by AMPK By similarity
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	47	1	N6-acetyllysine; alternate By similarity
	Modified residue	47	1	N6-methyllysine; alternate Ref.12
	Modified residue	58	1	N6,N6-dimethyllysine Ref.12
	Modified residue	79	1	Phosphoserine By similarity
	Modified residue	86	1	N6-acetyllysine By similarity
	Modified residue	109	1	N6-acetyllysine; alternate By similarity
	Modified residue	109	1	N6-methyllysine; alternate Ref.12
	Modified residue	113	1	Phosphoserine; alternate By similarity
	Modified residue	117	1	N6-acetyllysine By similarity
	Modified residue	121	1	N6-acetyllysine; alternate By similarity
	Glycosylation	113	1	O-linked (GlcNAc...); alternate By similarity
	Cross-link	35		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.20
	Cross-link	121		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate 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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[19]	"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification." Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y. Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-24 AND LYS-35.
[20]	"The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation." Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y. Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-35.
+	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. NM_003528.2.
UniGene	Hs.2178.
3D structure databases
ProteinModelPortal	Q16778.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39324N.
IntAct	Q16778. 10 interactions.
MINT	MINT-1461208.
STRING	9606.ENSP00000358151.
PTM databases
PhosphoSite	Q16778.
Polymorphism databases
DMDM	7387736.
Proteomic databases
PaxDb	Q16778.
PRIDE	Q16778.
Protocols and materials databases
DNASU	8349.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369155; ENSP00000358151; ENSG00000184678. ENST00000583061; ENSP00000464485; ENSG00000264719.
GeneID	8349.
KEGG	hsa:8349.
UCSC	uc001etc.3. human.
Organism-specific databases
CTD	8349.
GeneCards	GC01M149856.
H-InvDB	HIX0029389.
HGNC	HGNC:4760. HIST2H2BE.
MIM	601831. gene.
neXtProt	NX_Q16778.
PharmGKB	PA29135.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG315146.
HOGENOM	HOG000231213.
HOVERGEN	HBG007774.
InParanoid	Q16778.
KO	K11252.
OMA	AKTHKEA.
OrthoDB	EOG46DM4D.
PhylomeDB	Q16778.
Enzyme and pathway databases
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_116125. Disease.
Gene expression databases
Bgee	Q16778.
CleanEx	HS_HIST2H2BE.
Genevestigator	Q16778.
GermOnline	ENSG00000184678. Homo sapiens.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view]
PANTHER	PTHR23428. PTHR23428. 1 hit.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00621. HISTONEH2B.
SMART	SM00427. H2B. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00357. HISTONE_H2B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HIST2H2BE. human.
GenomeRNAi	8349.
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:	May 1, 2013
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.