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Q6ZWY9 (H2B1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2B type 1-C/E/G
Gene names
Name:Hist1h2bc
AND
Name:Hist1h2be
AND
Name:Hist1h2bg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length126 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons 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.7

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.8

Sequence similarities

Belongs to the histone H2B family.

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Glycoprotein
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 126125Histone H2B type 1-C/E/G
PRO_0000244831

Amino acid modifications

Modified residue21N-acetylproline By similarity
Modified residue61N6-acetyllysine; alternate By similarity
Modified residue61N6-crotonyllysine; alternate Ref.8
Modified residue121N6-acetyllysine; alternate By similarity
Modified residue121N6-crotonyllysine; alternate Ref.8
Modified residue131N6-acetyllysine; alternate By similarity
Modified residue131N6-crotonyllysine; alternate Ref.8
Modified residue151Phosphoserine; by STK4/MST1 Ref.5 Ref.6
Modified residue161N6-acetyllysine; alternate By similarity
Modified residue161N6-crotonyllysine; alternate Ref.8
Modified residue171N6-acetyllysine; alternate By similarity
Modified residue171N6-crotonyllysine; alternate Ref.8
Modified residue211N6-acetyllysine; alternate By similarity
Modified residue211N6-crotonyllysine; alternate Ref.8
Modified residue241N6-acetyllysine; alternate By similarity
Modified residue241N6-crotonyllysine; alternate Ref.8
Modified residue351N6-crotonyllysine; alternate Ref.8
Modified residue371Phosphoserine; by AMPK Ref.7
Modified residue471N6-methyllysine By similarity
Modified residue581N6,N6-dimethyllysine By similarity
Modified residue801Dimethylated arginine By similarity
Modified residue861N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue861N6-acetyllysine; alternate By similarity
Modified residue871Omega-N-methylarginine By similarity
Modified residue931Omega-N-methylarginine By similarity
Modified residue1091N6-methyllysine By similarity
Modified residue1161Phosphothreonine By similarity
Modified residue1171N6-methylated lysine By similarity
Glycosylation1131O-linked (GlcNAc) By similarity
Cross-link35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ZWY9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FAE1479F44BE703D

FASTA12613,906
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[8]"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-21; 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.
CCDSCCDS26349.1.
CCDS26354.1.
CCDS26357.1.
RefSeqNP_001171124.1. NM_001177653.1.
NP_001277309.1. NM_001290380.1.
NP_001277459.1. NM_001290530.1.
NP_075911.2. NM_023422.3.
NP_835501.1. NM_178194.4.
NP_835503.1. NM_178196.4.
UniGeneMm.261673.
Mm.261676.
Mm.440391.

3D structure databases

ProteinModelPortalQ6ZWY9.
SMRQ6ZWY9. Positions 5-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212605. 9 interactions.
235098. 8 interactions.
235100. 8 interactions.

PTM databases

PhosphoSiteQ6ZWY9.

Proteomic databases

PaxDbQ6ZWY9.
PRIDEQ6ZWY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018246; ENSMUSP00000018246; ENSMUSG00000018102.
ENSMUST00000051091; ENSMUSP00000061247; ENSMUSG00000047246.
ENSMUST00000079251; ENSMUSP00000078239; ENSMUSG00000058385.
ENSMUST00000091704; ENSMUSP00000089296; ENSMUSG00000047246.
GeneID319179.
319181.
68024.
KEGGmmu:319179.
mmu:319181.
mmu:68024.
UCSCuc007pue.2. mouse.

Organism-specific databases

CTD8339.
8344.
8347.
MGIMGI:1915274. Hist1h2bc.
MGI:2448380. Hist1h2be.
MGI:2448386. Hist1h2bg.

Phylogenomic databases

eggNOGNOG289161.
GeneTreeENSGT00690000101835.
HOGENOMHOG000231213.
HOVERGENHBG007774.
InParanoidQ6ZWY9.
KOK11252.
OMAILQGMTA.
OrthoDBEOG72VH8J.
PhylomeDBQ6ZWY9.
TreeFamTF300212.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.
REACT_218274. Chromatin organization.

Gene expression databases

BgeeQ6ZWY9.
CleanExMM_HIST1H2BC.
MM_HIST1H2BE.
GenevestigatorQ6ZWY9.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERPTHR23428. PTHR23428. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00621. HISTONEH2B.
SMARTSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio326230.
SOURCESearch...

Entry information

Entry nameH2B1C_MOUSE
AccessionPrimary (citable) accession number: Q6ZWY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot