Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H3.3

Gene

H3f3a

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

Functioni

Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 321Interaction with ZMYND11By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. brain development Source: Ensembl
  2. chromatin silencing at rDNA Source: Reactome
  3. response to hormone Source: Ensembl
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_256157. RNA Polymerase I Promoter Opening.
REACT_259097. RNA Polymerase I Chain Elongation.
REACT_268475. DNA methylation.
REACT_270446. Transcriptional regulation by small RNAs.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.3
Gene namesi
Name:H3f3a
Synonyms:H3.3a
AND
Name:H3f3b
Synonyms:H3.3b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1, UP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1097686. H3f3a.
MGI:1101768. H3f3b.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. 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 H3.3PRO_0000221251Add
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; alternate1 Publication
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 residuei32 – 321PhosphoserineBy similarity
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 residuei87 – 871PhosphoserineBy 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
Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. 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), which are linked to gene repression, are underrepresented. 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. Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes. metaphase chromosomes.10 Publications
Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (By similarity).By similarity
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

MaxQBiP84244.
PaxDbiP84244.
PRIDEiP84244.

Expressioni

Developmental stagei

Expressed throughout the cell cycle independently of DNA synthesis.1 Publication

Gene expression databases

BgeeiP84244.
CleanExiMM_H3F3A.
MM_H3F3B.
ExpressionAtlasiP84244. baseline and differential.
GenevestigatoriP84244.

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. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes. Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).

Protein-protein interaction databases

BioGridi200196. 26 interactions.
200199. 2 interactions.
IntActiP84244. 39 interactions.
MINTiMINT-4097105.

Structurei

3D structure databases

ProteinModelPortaliP84244.
SMRiP84244. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Specific interaction of trimethylated form at 'Lys-36' (H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-32 residue with a composite pocket formed by the tandem bromo-PWWP domains (By similarity). Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).By similarity

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP84244.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG7HB5C2.
PhylomeDBiP84244.
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.

P84244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,328
Last modified:January 23, 2007 - v2
Checksum:i5158ED279E6F9E1C
GO

Sequence cautioni

The sequence AAH92300.1 differs from that shown. Reason: Frameshift at position 127. Curated
The sequence BAB27616.1 differs from that shown. Reason: Frameshift at position 99. Curated
The sequence BAE35387.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751I → T in AAH21768 (PubMed:15489334).Curated
Sequence conflicti99 – 991A → E in BAE31789 (PubMed:16141072).Curated
Sequence conflicti99 – 991A → E in BAE30411 (PubMed:16141072).Curated
Sequence conflicti129 – 1291R → C in X91866 (PubMed:9174168).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13605 mRNA. Translation: CAA31940.1.
Z85979 mRNA. Translation: CAB06625.1.
X91866 mRNA. No translation available.
AK002928 mRNA. Translation: BAB22464.1.
AK011431 mRNA. Translation: BAB27616.1. Frameshift.
AK037900 mRNA. Translation: BAC29895.1.
AK088075 mRNA. Translation: BAC40130.1.
AK135839 mRNA. Translation: BAE22687.1.
AK150467 mRNA. Translation: BAE29584.1.
AK150468 mRNA. Translation: BAE29585.1.
AK150591 mRNA. Translation: BAE29685.1.
AK150928 mRNA. Translation: BAE29966.1.
AK151274 mRNA. Translation: BAE30261.1.
AK151336 mRNA. Translation: BAE30314.1.
AK151451 mRNA. Translation: BAE30411.1.
AK151634 mRNA. Translation: BAE30566.1.
AK151658 mRNA. Translation: BAE30586.1.
AK151661 mRNA. Translation: BAE30589.1.
AK151869 mRNA. Translation: BAE30757.1.
AK152293 mRNA. Translation: BAE31102.1.
AK152453 mRNA. Translation: BAE31231.1.
AK152455 mRNA. Translation: BAE31233.1.
AK152623 mRNA. Translation: BAE31366.1.
AK152911 mRNA. Translation: BAE31590.1.
AK153034 mRNA. Translation: BAE31666.1.
AK153189 mRNA. Translation: BAE31789.1.
AK153239 mRNA. Translation: BAE31831.1.
AK153294 mRNA. Translation: BAE31877.1.
AK153371 mRNA. Translation: BAE31939.1.
AK153530 mRNA. Translation: BAE32069.1.
AK159615 mRNA. Translation: BAE35232.1.
AK159807 mRNA. Translation: BAE35387.1. Frameshift.
AK159850 mRNA. Translation: BAE35427.1.
AK160677 mRNA. Translation: BAE35953.1.
AK161675 mRNA. Translation: BAE36524.1.
AK162040 mRNA. Translation: BAE36694.1.
AK163244 mRNA. Translation: BAE37253.1.
AK167828 mRNA. Translation: BAE39850.1.
AK167879 mRNA. Translation: BAE39892.1.
AK168197 mRNA. Translation: BAE40157.1.
AK168698 mRNA. Translation: BAE40542.1.
AK169042 mRNA. Translation: BAE40831.1.
AK169226 mRNA. Translation: BAE40995.1.
BC002268 mRNA. Translation: AAH02268.1.
BC012687 mRNA. Translation: AAH12687.1.
BC021768 mRNA. Translation: AAH21768.1.
BC037730 mRNA. Translation: AAH37730.1.
BC083353 mRNA. Translation: AAH83353.1.
BC088835 mRNA. Translation: AAH88835.1.
BC092043 mRNA. Translation: AAH92043.1.
BC092300 mRNA. Translation: AAH92300.1. Frameshift.
BC106177 mRNA. Translation: AAI06178.1.
AY383567 Genomic DNA. Translation: AAQ96274.1.
CCDSiCCDS15573.1.
CCDS36377.1.
PIRiS04186.
RefSeqiNP_032236.1. NM_008210.4.
NP_032237.1. NM_008211.3.
XP_006532311.1. XM_006532248.1.
UniGeneiMm.138832.
Mm.18516.
Mm.315189.
Mm.316825.
Mm.322735.
Mm.371563.
Mm.389332.
Mm.442502.
Mm.471842.

Genome annotation databases

EnsembliENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559.
ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559.
ENSMUST00000161308; ENSMUSP00000124509; ENSMUSG00000060743.
ENSMUST00000162814; ENSMUSP00000125104; ENSMUSG00000060743.
GeneIDi15078.
15081.
KEGGimmu:15078.
mmu:15081.
UCSCiuc007dwr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13605 mRNA. Translation: CAA31940.1.
Z85979 mRNA. Translation: CAB06625.1.
X91866 mRNA. No translation available.
AK002928 mRNA. Translation: BAB22464.1.
AK011431 mRNA. Translation: BAB27616.1. Frameshift.
AK037900 mRNA. Translation: BAC29895.1.
AK088075 mRNA. Translation: BAC40130.1.
AK135839 mRNA. Translation: BAE22687.1.
AK150467 mRNA. Translation: BAE29584.1.
AK150468 mRNA. Translation: BAE29585.1.
AK150591 mRNA. Translation: BAE29685.1.
AK150928 mRNA. Translation: BAE29966.1.
AK151274 mRNA. Translation: BAE30261.1.
AK151336 mRNA. Translation: BAE30314.1.
AK151451 mRNA. Translation: BAE30411.1.
AK151634 mRNA. Translation: BAE30566.1.
AK151658 mRNA. Translation: BAE30586.1.
AK151661 mRNA. Translation: BAE30589.1.
AK151869 mRNA. Translation: BAE30757.1.
AK152293 mRNA. Translation: BAE31102.1.
AK152453 mRNA. Translation: BAE31231.1.
AK152455 mRNA. Translation: BAE31233.1.
AK152623 mRNA. Translation: BAE31366.1.
AK152911 mRNA. Translation: BAE31590.1.
AK153034 mRNA. Translation: BAE31666.1.
AK153189 mRNA. Translation: BAE31789.1.
AK153239 mRNA. Translation: BAE31831.1.
AK153294 mRNA. Translation: BAE31877.1.
AK153371 mRNA. Translation: BAE31939.1.
AK153530 mRNA. Translation: BAE32069.1.
AK159615 mRNA. Translation: BAE35232.1.
AK159807 mRNA. Translation: BAE35387.1. Frameshift.
AK159850 mRNA. Translation: BAE35427.1.
AK160677 mRNA. Translation: BAE35953.1.
AK161675 mRNA. Translation: BAE36524.1.
AK162040 mRNA. Translation: BAE36694.1.
AK163244 mRNA. Translation: BAE37253.1.
AK167828 mRNA. Translation: BAE39850.1.
AK167879 mRNA. Translation: BAE39892.1.
AK168197 mRNA. Translation: BAE40157.1.
AK168698 mRNA. Translation: BAE40542.1.
AK169042 mRNA. Translation: BAE40831.1.
AK169226 mRNA. Translation: BAE40995.1.
BC002268 mRNA. Translation: AAH02268.1.
BC012687 mRNA. Translation: AAH12687.1.
BC021768 mRNA. Translation: AAH21768.1.
BC037730 mRNA. Translation: AAH37730.1.
BC083353 mRNA. Translation: AAH83353.1.
BC088835 mRNA. Translation: AAH88835.1.
BC092043 mRNA. Translation: AAH92043.1.
BC092300 mRNA. Translation: AAH92300.1. Frameshift.
BC106177 mRNA. Translation: AAI06178.1.
AY383567 Genomic DNA. Translation: AAQ96274.1.
CCDSiCCDS15573.1.
CCDS36377.1.
PIRiS04186.
RefSeqiNP_032236.1. NM_008210.4.
NP_032237.1. NM_008211.3.
XP_006532311.1. XM_006532248.1.
UniGeneiMm.138832.
Mm.18516.
Mm.315189.
Mm.316825.
Mm.322735.
Mm.371563.
Mm.389332.
Mm.442502.
Mm.471842.

3D structure databases

ProteinModelPortaliP84244.
SMRiP84244. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200196. 26 interactions.
200199. 2 interactions.
IntActiP84244. 39 interactions.
MINTiMINT-4097105.

Proteomic databases

MaxQBiP84244.
PaxDbiP84244.
PRIDEiP84244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559.
ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559.
ENSMUST00000161308; ENSMUSP00000124509; ENSMUSG00000060743.
ENSMUST00000162814; ENSMUSP00000125104; ENSMUSG00000060743.
GeneIDi15078.
15081.
KEGGimmu:15078.
mmu:15081.
UCSCiuc007dwr.1. mouse.

Organism-specific databases

CTDi3020.
3021.
MGIiMGI:1097686. H3f3a.
MGI:1101768. H3f3b.

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP84244.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG7HB5C2.
PhylomeDBiP84244.
TreeFamiTF314241.

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_256157. RNA Polymerase I Promoter Opening.
REACT_259097. RNA Polymerase I Chain Elongation.
REACT_268475. DNA methylation.
REACT_270446. Transcriptional regulation by small RNAs.
REACT_27235. Meiotic Recombination.
REACT_75800. Meiotic Synapsis.

Miscellaneous databases

ChiTaRSiH3f3b. mouse.
NextBioi287482.
PROiP84244.
SOURCEiSearch...

Gene expression databases

BgeeiP84244.
CleanExiMM_H3F3A.
MM_H3F3B.
ExpressionAtlasiP84244. baseline and differential.
GenevestigatoriP84244.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of a mouse replacement histone H3.3 gene with a highly conserved 3' noncoding region during SV40- and polyoma-induced Go to S-phase transition."
    Hraba-Renevey S., Kress M.
    Nucleic Acids Res. 17:2449-2461(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3B).
  2. "Differential expression of the murine histone genes H3.3A and H3.3B."
    Bramlage B., Kosciessa U., Doenecke D.
    Differentiation 62:13-20(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A AND H3F3B), DEVELOPMENTAL STAGE.
    Tissue: Spermatid.
  3. "H3.3A variant histone mRNA containing an alpha-globin insertion: modulated expression during mouse gametogenesis correlates with meiotic onset."
    Lopez-Alanon D.M., Lopez-Fernandez L.A., Castaneda V., Krimer D.B., Del Mazo J.
    DNA Cell Biol. 16:639-644(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A).
    Strain: Swiss.
    Tissue: Ovary.
  4. "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] (H3F3A AND H3F3B).
    Strain: BALB/c, C57BL/6J, DBA/2 and NOD.
    Tissue: Bone marrow, Egg, Head, Kidney, Muellerian duct, Stomach and Thymus.
  5. "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] (H3F3A AND H3F3B).
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Colon, Mammary tumor and Retina.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-122.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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 nameiH33_MOUSE
AccessioniPrimary (citable) accession number: P84244
Secondary accession number(s): P06351
, P33155, Q3TW79, Q3U6D6, Q569U8, Q5HZY8, Q6TXQ5, Q8VDJ2, Q9D0H3, Q9V3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 110 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.