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Q6ZWY9

- H2B1C_MOUSE

UniProt

Q6ZWY9 - H2B1C_MOUSE

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Protein

Histone H2B type 1-C/E/G

Gene

Hist1h2bc

more
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. antibacterial humoral response Source: Ensembl
  2. defense response to Gram-positive bacterium Source: Ensembl
  3. innate immune response in mucosa Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_198626. Meiotic synapsis.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 1-C/E/G
Gene namesi
Name:Hist1h2bc
AND
Name:Hist1h2be
AND
Name:Hist1h2bg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1915274. Hist1h2bc.
MGI:2448380. Hist1h2be.
MGI:2448386. Hist1h2bg.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 126125Histone H2B type 1-C/E/GPRO_0000244831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei6 – 61N6-acetyllysine; alternateBy similarity
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Modified residuei12 – 121N6-acetyllysine; alternateBy similarity
Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei15 – 151Phosphoserine; by STK4/MST12 Publications
Modified residuei16 – 161N6-acetyllysine; alternateBy similarity
Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei21 – 211N6-acetyllysine; alternateBy similarity
Modified residuei21 – 211N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei35 – 351N6-crotonyllysine; alternate1 Publication
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei37 – 371Phosphoserine; by AMPK1 Publication
Modified residuei47 – 471N6-methyllysineBy similarity
Modified residuei58 – 581N6,N6-dimethyllysineBy similarity
Modified residuei80 – 801Dimethylated arginineBy similarity
Modified residuei86 – 861N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei86 – 861N6-acetyllysine; alternateBy similarity
Modified residuei87 – 871Omega-N-methylarginineBy similarity
Modified residuei93 – 931Omega-N-methylarginineBy similarity
Modified residuei109 – 1091N6-methyllysineBy similarity
Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
Modified residuei116 – 1161PhosphothreonineBy similarity
Modified residuei117 – 1171N6-methylated lysineBy similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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).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.3 Publications
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).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.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6ZWY9.
PaxDbiQ6ZWY9.
PRIDEiQ6ZWY9.

PTM databases

PhosphoSiteiQ6ZWY9.

Expressioni

Gene expression databases

BgeeiQ6ZWY9.
CleanExiMM_HIST1H2BC.
MM_HIST1H2BE.
GenevestigatoriQ6ZWY9.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi212605. 9 interactions.
235098. 8 interactions.
235100. 8 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWY9.
SMRiQ6ZWY9. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiNOG289161.
GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiQ6ZWY9.
KOiK11252.
OMAiILQGMTA.
OrthoDBiEOG72VH8J.
PhylomeDBiQ6ZWY9.
TreeFamiTF300212.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6ZWY9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSSK
Length:126
Mass (Da):13,906
Last modified:January 23, 2007 - v3
Checksum:iFAE1479F44BE703D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26349.1.
CCDS26354.1.
CCDS26357.1.
RefSeqiNP_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.
UniGeneiMm.261673.
Mm.261676.
Mm.440391.

Genome annotation databases

EnsembliENSMUST00000018246; ENSMUSP00000018246; ENSMUSG00000018102.
ENSMUST00000051091; ENSMUSP00000061247; ENSMUSG00000047246.
ENSMUST00000079251; ENSMUSP00000078239; ENSMUSG00000058385.
ENSMUST00000091704; ENSMUSP00000089296; ENSMUSG00000047246.
GeneIDi319179.
319181.
68024.
KEGGimmu:319179.
mmu:319181.
mmu:68024.
UCSCiuc007pue.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26349.1.
CCDS26354.1.
CCDS26357.1.
RefSeqi NP_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.
UniGenei Mm.261673.
Mm.261676.
Mm.440391.

3D structure databases

ProteinModelPortali Q6ZWY9.
SMRi Q6ZWY9. Positions 5-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212605. 9 interactions.
235098. 8 interactions.
235100. 8 interactions.

PTM databases

PhosphoSitei Q6ZWY9.

Proteomic databases

MaxQBi Q6ZWY9.
PaxDbi Q6ZWY9.
PRIDEi Q6ZWY9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018246 ; ENSMUSP00000018246 ; ENSMUSG00000018102 .
ENSMUST00000051091 ; ENSMUSP00000061247 ; ENSMUSG00000047246 .
ENSMUST00000079251 ; ENSMUSP00000078239 ; ENSMUSG00000058385 .
ENSMUST00000091704 ; ENSMUSP00000089296 ; ENSMUSG00000047246 .
GeneIDi 319179.
319181.
68024.
KEGGi mmu:319179.
mmu:319181.
mmu:68024.
UCSCi uc007pue.2. mouse.

Organism-specific databases

CTDi 8339.
8344.
8347.
MGIi MGI:1915274. Hist1h2bc.
MGI:2448380. Hist1h2be.
MGI:2448386. Hist1h2bg.

Phylogenomic databases

eggNOGi NOG289161.
GeneTreei ENSGT00760000118976.
HOGENOMi HOG000231213.
HOVERGENi HBG007774.
InParanoidi Q6ZWY9.
KOi K11252.
OMAi ILQGMTA.
OrthoDBi EOG72VH8J.
PhylomeDBi Q6ZWY9.
TreeFami TF300212.

Enzyme and pathway databases

Reactomei REACT_198626. Meiotic synapsis.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

NextBioi 326230.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZWY9.
CleanExi MM_HIST1H2BC.
MM_HIST1H2BE.
Genevestigatori Q6ZWY9.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view ]
PANTHERi PTHR23428. PTHR23428. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00621. HISTONEH2B.
SMARTi SM00427. H2B. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00357. HISTONE_H2B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiH2B1C_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3