Q6ZWY9 (H2B1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B type 1-C/E/G

Gene names

Name:	Hist1h2bc
AND
Name:	Hist1h2be
AND
Name:	Hist1h2bg

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
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 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. Ref.5 Ref.6 Ref.8 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.9
Sequence similarities	Belongs to the histone H2B family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Glycoprotein Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 126	125	Histone H2B type 1-C/E/G		PRO_0000244831
Amino acid modifications
	Modified residue	2	1	N-acetylproline By similarity
	Modified residue	6	1	N6-acetyllysine; alternate By similarity
	Modified residue	6	1	N6-crotonyl-L-lysine; alternate Ref.9
	Modified residue	12	1	N6-acetyllysine; alternate Ref.7
	Modified residue	12	1	N6-crotonyl-L-lysine; alternate Ref.9
	Modified residue	13	1	N6-acetyllysine; alternate Ref.7
	Modified residue	13	1	N6-crotonyl-L-lysine; alternate Ref.9
	Modified residue	15	1	Phosphoserine; by STK4/MST1 Ref.5 Ref.6
	Modified residue	16	1	N6-acetyllysine; alternate Ref.7
	Modified residue	16	1	N6-crotonyl-L-lysine; alternate Ref.9
	Modified residue	17	1	N6-acetyllysine; alternate Ref.7
	Modified residue	17	1	N6-crotonyl-L-lysine; alternate Ref.9
	Modified residue	21	1	N6-acetyllysine; alternate Ref.7
	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.9
	Modified residue	35	1	N6-acetyllysine; alternate By similarity
	Modified residue	35	1	N6-crotonyl-L-lysine; alternate Ref.9
	Modified residue	37	1	Phosphoserine; by AMPK Ref.8
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	47	1	N6-acetyllysine; alternate By similarity
	Modified residue	47	1	N6-methyllysine; alternate By similarity
	Modified residue	58	1	N6,N6-dimethyllysine By similarity
	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 By similarity
	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 By similarity
	Cross-link	121		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6ZWY9 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FAE1479F44BE703D	FASTA	126	13,906
	10 20 30 40 50 60 MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM 70 80 90 100 110 120 GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (HIST1H2BC; HIST1H2BE AND HIST1H2BG)).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Hippocampus, Pituitary and Placenta.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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]. Strain: Czech II and FVB/N. Tissue: Colon and Mammary tumor.
[5]	"Phosphorylation of histone H2B at DNA double-strand breaks." Fernandez-Capetillo O., Allis C.D., Nussenzweig A. J. Exp. Med. 199:1671-1677(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15.
[6]	"Histone modifications associated with somatic hypermutation." Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., Schatz D.G. Immunity 23:101-110(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15.
[7]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12; LYS-13; LYS-16; LYS-17 AND LYS-21, MASS SPECTROMETRY.
[8]	"Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation." Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B., Carling D., Thompson C.B., Jones R.G., Berger S.L. Science 329:1201-1205(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-37.
[9]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY158934 Genomic DNA. Translation: AAO06244.1. AY158936 Genomic DNA. Translation: AAO06246.1. AY158937 Genomic DNA. Translation: AAO06247.1. AK005407 mRNA. Translation: BAB24007.1. AK011516 mRNA. Translation: BAB27670.1. AK030546 mRNA. Translation: BAC27014.1. AK049948 mRNA. Translation: BAC34000.1. AL592149 Genomic DNA. Translation: CAI24894.1. BC019673 mRNA. Translation: AAH19673.1. BC060304 mRNA. Translation: AAH60304.1. BC069889 mRNA. Translation: AAH69889.1.
IPI	IPI00282266.
RefSeq	NP_001171124.1. NM_001177653.1. NP_075911.2. NM_023422.3. NP_835501.1. NM_178194.4. NP_835503.1. NM_178196.3.
UniGene	Mm.261673. Mm.261676. Mm.440391.
3D structure databases
ProteinModelPortal	Q6ZWY9.
SMR	Q6ZWY9. Positions 5-126.
ModBase	Search...
PTM databases
PhosphoSite	Q6ZWY9.
Proteomic databases
PaxDb	Q6ZWY9.
PRIDE	Q6ZWY9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000018246; ENSMUSP00000018246; ENSMUSG00000018102. ENSMUST00000051091; ENSMUSP00000061247; ENSMUSG00000047246. ENSMUST00000079251; ENSMUSP00000078239; ENSMUSG00000058385. ENSMUST00000091704; ENSMUSP00000089296; ENSMUSG00000047246.
GeneID	319179. 319181. 68024.
KEGG	mmu:319179. mmu:319181. mmu:68024.
UCSC	uc007pue.2. mouse.
Organism-specific databases
CTD	8339. 8344. 8347.
MGI	MGI:1915274. Hist1h2bc. MGI:2448380. Hist1h2be. MGI:2448386. Hist1h2bg.
Phylogenomic databases
eggNOG	NOG289161.
GeneTree	ENSGT00690000101835.
HOGENOM	HOG000231213.
HOVERGEN	HBG007774.
InParanoid	Q6ZWY9.
KO	K11252.
OMA	HAILQGM.
OrthoDB	EOG4FN4K9.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse). REACT_75800. Meiotic Synapsis (mouse).
Gene expression databases
Bgee	Q6ZWY9.
CleanEx	MM_HIST1H2BC. MM_HIST1H2BE.
Genevestigator	Q6ZWY9.
GermOnline	ENSMUSG00000018102. Mus musculus. ENSMUSG00000047246. Mus musculus. ENSMUSG00000058385. Mus musculus.
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
NextBio	326230.
SOURCE	Search...

Entry information

Entry name

H2B1C_MOUSE

Accession

Primary (citable) accession number: Q6ZWY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program