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P84228

- H32_MOUSE

UniProt

P84228 - H32_MOUSE

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Protein

Histone H3.2

Gene

Hist1h3b

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. regulation of gene silencing Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
REACT_196580. Condensation of Prophase Chromosomes.
REACT_198563. Amyloids.
REACT_198626. Meiotic synapsis.
REACT_198629. Meiotic recombination.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_222475. PRC2 methylates histones and DNA.
REACT_224328. SIRT1 negatively regulates rRNA Expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.2
Gene namesi
Name:Hist1h3b
Synonyms:H3-53, H3.2, H3b
AND
Name:Hist1h3c
Synonyms:H3-143
AND
Name:Hist1h3d
Synonyms:H3-B
AND
Name:Hist1h3e
Synonyms:H3-F
AND
Name:Hist1h3f
Synonyms:H3.2-221, H3f
AND
Name:Hist2h3b
Synonyms:H3.2-616
AND
Name:Hist2h3c1
Synonyms:H3.2-615, Hist2h3ca1
AND
Name:Hist2h3c2
Synonyms:H3.2-614, Hist2h3ca2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13, UP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:2448319. Hist1h3b.
MGI:2448320. Hist1h3c.
MGI:2448322. Hist1h3d.
MGI:2448326. Hist1h3e.
MGI:2448329. Hist1h3f.
MGI:2448351. Hist2h3b.
MGI:2448355. Hist2h3c1.
MGI:2448357. Hist2h3c2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. nucleoplasm Source: BHF-UCL
  3. 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 – 136135Histone H3.2PRO_0000221250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
Modified residuei3 – 31Citrulline; alternateBy similarity
Modified residuei4 – 41Phosphothreonine; by GSG21 Publication
Modified residuei5 – 51Allysine; alternateBy similarity
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei5 – 51N6,N6-dimethyllysine; alternate1 Publication
Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
Modified residuei5 – 51N6-crotonyllysine; alternate1 Publication
Modified residuei5 – 51N6-methyllysine; alternate1 Publication
Modified residuei7 – 71Phosphothreonine; by PKCBy similarity
Modified residuei9 – 91Citrulline; alternate1 Publication
Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternate1 Publication
Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate2 Publications
Modified residuei10 – 101N6,N6-dimethyllysine; alternate2 Publications
Modified residuei10 – 101N6-acetyllysine; alternate2 Publications
Modified residuei10 – 101N6-crotonyllysine; alternate1 Publication
Modified residuei10 – 101N6-methyllysine; alternate2 Publications
Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA55 Publications
Modified residuei12 – 121Phosphothreonine; by PKCBy similarity
Modified residuei15 – 151N6-acetyllysine3 Publications
Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternate3 Publications
Modified residuei18 – 181Citrulline; alternateBy similarity
Modified residuei19 – 191N6-acetyllysine; alternate3 Publications
Modified residuei19 – 191N6-crotonyllysine; alternate1 Publication
Modified residuei19 – 191N6-methyllysine; alternate1 Publication
Modified residuei24 – 241N6-acetyllysine; alternate3 Publications
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-methyllysine; alternate1 Publication
Modified residuei27 – 271CitrullineBy similarity
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate2 Publications
Modified residuei28 – 281N6,N6-dimethyllysine; alternate2 Publications
Modified residuei28 – 281N6-acetyllysine; alternate1 Publication
Modified residuei28 – 281N6-crotonyllysine; alternate1 Publication
Modified residuei28 – 281N6-methyllysine; alternate2 Publications
Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei37 – 371N6,N6-dimethyllysine; alternate2 Publications
Modified residuei37 – 371N6-acetyllysine; alternate1 Publication
Modified residuei37 – 371N6-methyllysine; alternate2 Publications
Modified residuei38 – 381N6-methyllysineBy similarity
Modified residuei42 – 421PhosphotyrosineBy similarity
Modified residuei57 – 571N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei57 – 571N6-acetyllysine; alternateBy similarity
Modified residuei57 – 571N6-crotonyllysine; alternate1 Publication
Modified residuei57 – 571N6-methyllysine; by EHMT2; alternateBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei65 – 651N6-methyllysineBy similarity
Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternate2 Publications
Modified residuei80 – 801N6,N6-dimethyllysine; alternate2 Publications
Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
Modified residuei80 – 801N6-methyllysine; alternate2 Publications
Modified residuei81 – 811PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei123 – 1231N6-acetyllysine; alternateBy similarity
Modified residuei123 – 1231N6-methyllysine; alternate1 Publication

Post-translational modificationi

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.6 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.5 Publications
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).By similarity
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.9 Publications
Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.10 Publications
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination.By similarity1 Publication
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (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, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP84228.
PaxDbiP84228.
PRIDEiP84228.

PTM databases

PhosphoSiteiP84228.

Expressioni

Developmental stagei

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

Gene expression databases

BgeeiP84228.
CleanExiMM_HIST1H3B.
MM_HIST1H3C.
MM_HIST1H3D.
MM_HIST1H3E.
MM_HIST1H3F.
MM_HIST2H3C1.
MM_HIST2H3C2.
ExpressionAtlasiP84228. baseline and differential.
GenevestigatoriP84228.

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. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer (By similarity).By similarity

Protein-protein interaction databases

BioGridi234451. 6 interactions.
235070. 1 interaction.
DIPiDIP-49015N.
IntActiP84228. 27 interactions.
MINTiMINT-1848003.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V86X-ray2.05D/E2-9[»]
2V87X-ray1.80D/E2-14[»]
2V88X-ray2.00D/F2-8[»]
ProteinModelPortaliP84228.
SMRiP84228. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP84228.
KOiK11253.
OrthoDBiEOG7HB5C2.
PhylomeDBiP84228.
TreeFamiTF314241.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P84228-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,388
Last modified:January 23, 2007 - v2
Checksum:i6FD8508EA50A0EEC
GO

Sequence cautioni

The sequence AAH94041.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAO06264.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01685 Genomic DNA. Translation: CAA25840.1.
M32459 Genomic DNA. Translation: AAA37810.1.
M32461 Genomic DNA. Translation: AAA37812.1.
X16148 Genomic DNA. Translation: CAA34274.1.
M33989 Genomic DNA. Translation: AAA37764.1.
X80328 Genomic DNA. Translation: CAA56577.1.
U62669 Genomic DNA. Translation: AAB04760.1.
U62671 Genomic DNA. Translation: AAB04764.1.
U62674 Genomic DNA. Translation: AAB04771.1.
U62675 Genomic DNA. Translation: AAB04772.1.
AY158941 Genomic DNA. Translation: AAO06251.1.
AY158947 Genomic DNA. Translation: AAO06257.1.
AY158948 Genomic DNA. Translation: AAO06258.1.
AY158949 Genomic DNA. Translation: AAO06259.1.
AY158950 Genomic DNA. Translation: AAO06260.1.
AY158951 Genomic DNA. Translation: AAO06261.1.
AY158954 Genomic DNA. Translation: AAO06264.1. Different initiation.
AY158955 Genomic DNA. Translation: AAO06265.1.
AK010121 mRNA. Translation: BAB26714.1.
AK020421 mRNA. Translation: BAB32097.1.
AL590388 Genomic DNA. Translation: CAI25840.1.
AL590388 Genomic DNA. Translation: CAI25844.1.
BC015270 mRNA. Translation: AAH15270.1.
BC094041 mRNA. Translation: AAH94041.1. Different initiation.
BC101954 mRNA. Translation: AAI01955.1.
BC101955 mRNA. Translation: AAI01956.1.
BC101956 mRNA. Translation: AAI01957.1.
BC103549 mRNA. Translation: AAI03550.1.
BC120800 mRNA. Translation: AAI20801.1.
BC120802 mRNA. Translation: AAI20803.1.
BC132488 mRNA. Translation: AAI32489.1.
BC132490 mRNA. Translation: AAI32491.1.
Z30939 mRNA. Translation: CAA83209.1.
CCDSiCCDS17638.1.
CCDS26344.1.
CCDS26347.1.
CCDS26352.1.
CCDS26362.1.
CCDS26365.1.
CCDS38554.2.
CCDS57240.1.
PIRiA39525.
JH0304.
S06743.
S48060. S45111.
RefSeqiNP_038576.1. NM_013548.4.
NP_473386.1. NM_054045.4.
NP_783584.1. NM_175653.2.
NP_835510.1. NM_178203.2.
NP_835511.1. NM_178204.2.
NP_835512.1. NM_178205.2.
NP_835587.1. NM_178215.2.
NP_835734.2. NM_178216.3.
UniGeneiMm.221389.
Mm.261658.
Mm.262517.
Mm.347699.
Mm.358797.
Mm.383293.
Mm.422680.

Genome annotation databases

EnsembliENSMUST00000075558; ENSMUSP00000074994; ENSMUSG00000100210.
ENSMUST00000091703; ENSMUSP00000089295; ENSMUSG00000069267.
ENSMUST00000091752; ENSMUSP00000089346; ENSMUSG00000069310.
ENSMUST00000098843; ENSMUSP00000096442; ENSMUSG00000074403.
ENSMUST00000105105; ENSMUSP00000100737; ENSMUSG00000099583.
ENSMUST00000105107; ENSMUSP00000100739; ENSMUSG00000069273.
ENSMUST00000167403; ENSMUSP00000135215; ENSMUSG00000081058.
ENSMUST00000176059; ENSMUSP00000134751; ENSMUSG00000093769.
GeneIDi15077.
260423.
319148.
319149.
319150.
319151.
319154.
97114.
KEGGimmu:15077.
mmu:260423.
mmu:319148.
mmu:319149.
mmu:319150.
mmu:319151.
mmu:319154.
mmu:97114.
UCSCiuc007ptz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01685 Genomic DNA. Translation: CAA25840.1 .
M32459 Genomic DNA. Translation: AAA37810.1 .
M32461 Genomic DNA. Translation: AAA37812.1 .
X16148 Genomic DNA. Translation: CAA34274.1 .
M33989 Genomic DNA. Translation: AAA37764.1 .
X80328 Genomic DNA. Translation: CAA56577.1 .
U62669 Genomic DNA. Translation: AAB04760.1 .
U62671 Genomic DNA. Translation: AAB04764.1 .
U62674 Genomic DNA. Translation: AAB04771.1 .
U62675 Genomic DNA. Translation: AAB04772.1 .
AY158941 Genomic DNA. Translation: AAO06251.1 .
AY158947 Genomic DNA. Translation: AAO06257.1 .
AY158948 Genomic DNA. Translation: AAO06258.1 .
AY158949 Genomic DNA. Translation: AAO06259.1 .
AY158950 Genomic DNA. Translation: AAO06260.1 .
AY158951 Genomic DNA. Translation: AAO06261.1 .
AY158954 Genomic DNA. Translation: AAO06264.1 . Different initiation.
AY158955 Genomic DNA. Translation: AAO06265.1 .
AK010121 mRNA. Translation: BAB26714.1 .
AK020421 mRNA. Translation: BAB32097.1 .
AL590388 Genomic DNA. Translation: CAI25840.1 .
AL590388 Genomic DNA. Translation: CAI25844.1 .
BC015270 mRNA. Translation: AAH15270.1 .
BC094041 mRNA. Translation: AAH94041.1 . Different initiation.
BC101954 mRNA. Translation: AAI01955.1 .
BC101955 mRNA. Translation: AAI01956.1 .
BC101956 mRNA. Translation: AAI01957.1 .
BC103549 mRNA. Translation: AAI03550.1 .
BC120800 mRNA. Translation: AAI20801.1 .
BC120802 mRNA. Translation: AAI20803.1 .
BC132488 mRNA. Translation: AAI32489.1 .
BC132490 mRNA. Translation: AAI32491.1 .
Z30939 mRNA. Translation: CAA83209.1 .
CCDSi CCDS17638.1.
CCDS26344.1.
CCDS26347.1.
CCDS26352.1.
CCDS26362.1.
CCDS26365.1.
CCDS38554.2.
CCDS57240.1.
PIRi A39525.
JH0304.
S06743.
S48060. S45111.
RefSeqi NP_038576.1. NM_013548.4.
NP_473386.1. NM_054045.4.
NP_783584.1. NM_175653.2.
NP_835510.1. NM_178203.2.
NP_835511.1. NM_178204.2.
NP_835512.1. NM_178205.2.
NP_835587.1. NM_178215.2.
NP_835734.2. NM_178216.3.
UniGenei Mm.221389.
Mm.261658.
Mm.262517.
Mm.347699.
Mm.358797.
Mm.383293.
Mm.422680.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V86 X-ray 2.05 D/E 2-9 [» ]
2V87 X-ray 1.80 D/E 2-14 [» ]
2V88 X-ray 2.00 D/F 2-8 [» ]
ProteinModelPortali P84228.
SMRi P84228. Positions 17-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 234451. 6 interactions.
235070. 1 interaction.
DIPi DIP-49015N.
IntActi P84228. 27 interactions.
MINTi MINT-1848003.

PTM databases

PhosphoSitei P84228.

Proteomic databases

MaxQBi P84228.
PaxDbi P84228.
PRIDEi P84228.

Protocols and materials databases

DNASUi 319149.
319150.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075558 ; ENSMUSP00000074994 ; ENSMUSG00000100210 .
ENSMUST00000091703 ; ENSMUSP00000089295 ; ENSMUSG00000069267 .
ENSMUST00000091752 ; ENSMUSP00000089346 ; ENSMUSG00000069310 .
ENSMUST00000098843 ; ENSMUSP00000096442 ; ENSMUSG00000074403 .
ENSMUST00000105105 ; ENSMUSP00000100737 ; ENSMUSG00000099583 .
ENSMUST00000105107 ; ENSMUSP00000100739 ; ENSMUSG00000069273 .
ENSMUST00000167403 ; ENSMUSP00000135215 ; ENSMUSG00000081058 .
ENSMUST00000176059 ; ENSMUSP00000134751 ; ENSMUSG00000093769 .
GeneIDi 15077.
260423.
319148.
319149.
319150.
319151.
319154.
97114.
KEGGi mmu:15077.
mmu:260423.
mmu:319148.
mmu:319149.
mmu:319150.
mmu:319151.
mmu:319154.
mmu:97114.
UCSCi uc007ptz.2. mouse.

Organism-specific databases

CTDi 15077.
319154.
8351.
8352.
8353.
8358.
8968.
97114.
MGIi MGI:2448319. Hist1h3b.
MGI:2448320. Hist1h3c.
MGI:2448322. Hist1h3d.
MGI:2448326. Hist1h3e.
MGI:2448329. Hist1h3f.
MGI:2448351. Hist2h3b.
MGI:2448355. Hist2h3c1.
MGI:2448357. Hist2h3c2.

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00760000118967.
HOVERGENi HBG001172.
InParanoidi P84228.
KOi K11253.
OrthoDBi EOG7HB5C2.
PhylomeDBi P84228.
TreeFami TF314241.

Enzyme and pathway databases

Reactomei REACT_188970. Oxidative Stress Induced Senescence.
REACT_196580. Condensation of Prophase Chromosomes.
REACT_198563. Amyloids.
REACT_198626. Meiotic synapsis.
REACT_198629. Meiotic recombination.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_222475. PRC2 methylates histones and DNA.
REACT_224328. SIRT1 negatively regulates rRNA Expression.
REACT_226917. HATs acetylate histones.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

NextBioi 287476.
SOURCEi Search...

Gene expression databases

Bgeei P84228.
CleanExi MM_HIST1H3B.
MM_HIST1H3C.
MM_HIST1H3D.
MM_HIST1H3E.
MM_HIST1H3F.
MM_HIST2H3C1.
MM_HIST2H3C2.
ExpressionAtlasi P84228. baseline and differential.
Genevestigatori P84228.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view ]
PANTHERi PTHR11426. PTHR11426. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00622. HISTONEH3.
SMARTi SM00428. H3. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
  2. "Sequences of four mouse histone H3 genes: implications for evolution of mouse histone genes."
    Taylor J.D., Wellman S.E., Marzluff W.F.
    J. Mol. Evol. 23:242-249(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST2H3C2 AND HIST1H3F).
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
    Tissue: Liver.
  4. "Structure of a mouse histone-encoding gene cluster."
    Gruber A., Streit A., Reist M., Benninger P., Boehni R., Schuemperli D.
    Gene 95:303-304(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
    Strain: BALB/c.
  5. "Selection on silent sites in the rodent histone H3 gene family."
    DeBry R.W., Marzluff W.F.
    Genetics 138:191-202(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3C).
  6. "Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb."
    Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F.
    Genome Res. 6:688-701(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3C).
    Strain: C57BL/6J.
  7. "Characterization of the 55-kb mouse histone gene cluster on chromosome 3."
    Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G., Marzluff W.F.
    Genome Res. 6:702-714(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3E; HIST2H3B AND HIST2H3CA1).
  8. "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] (HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST2H3B; HIST2H3C1 AND HIST2H3C2).
  9. "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: Embryo.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  11. "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] (HIST2H3C2).
    Strain: FVB/N.
    Tissue: Kidney.
  12. "An alternative pathway of histone mRNA 3' end formation in mouse round spermatids."
    Moss S.B., Ferry R.A., Groudine M.
    Nucleic Acids Res. 22:3160-3166(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 79-136.
    Strain: CD-1.
    Tissue: Testis.
  13. "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation."
    Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.
    J. Biol. Chem. 274:25543-25549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
  14. "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1."
    Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y., Dong Z.
    J. Biol. Chem. 276:33213-33219(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-29.
  15. "Crosstalk between CARM1 methylation and CBP acetylation on histone H3."
    Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.
    Curr. Biol. 12:2090-2097(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT ARG-18.
  16. "Methylation at arginine 17 of histone H3 is linked to gene activation."
    Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.
    EMBO Rep. 3:39-44(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-18.
  17. "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
    Goto H., Yasui Y., Nigg E.A., Inagaki M.
    Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
  18. "Identification of methylation and acetylation sites on mouse histone H3 using matrix-assisted laser desorption/ionization time-of-flight and nanoelectrospray ionization tandem mass spectrometry."
    Cocklin R.R., Wang M.
    J. Protein Chem. 22:327-334(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10; LYS-28; LYS-37; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
  19. Cited for: CITRULLINATION.
  20. "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes."
    Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.
    Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-9, ACETYLATION AT LYS-10.
  21. "Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression."
    Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O.
    EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-18.
  22. "The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment."
    Dai J., Sultan S., Taylor S.S., Higgins J.M.G.
    Genes Dev. 19:472-488(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-4 AND SER-11.
  23. "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
    Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
    J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-29.
  24. "MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2."
    Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K., Iborra F.J., Mahadevan L.C.
    J. Cell Sci. 118:2247-2259(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
  25. "Stimulation of the Ras-MAPK pathway leads to independent phosphorylation of histone H3 on serine 10 and 28."
    Dunn K.L., Davie J.R.
    Oncogene 24:3492-3502(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
  26. "Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
    Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
    J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-37.
  27. "Organismal differences in post-translational modifications in histones H3 and H4."
    Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
    J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
  28. "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in chromatin-mediated regulation of V(D)J joining."
    Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R., McBlane F.
    Mol. Cell 37:282-293(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  29. "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-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.

Entry informationi

Entry nameiH32_MOUSE
AccessioniPrimary (citable) accession number: P84228
Secondary accession number(s): A3KMN6
, P02295, P02297, P16105, P17269, P17320, Q60582, Q78E59, Q8CGN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3