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 H3.1

Gene

Hist1h3a

more
Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-1266695. Interleukin-7 signaling.
R-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3214842. HDMs demethylate histones.
R-MMU-3214847. HATs acetylate histones.
R-MMU-3214858. RMTs methylate histone arginines.
R-MMU-3247509. Chromatin modifying enzymes.
R-MMU-427359. SIRT1 negatively regulates rRNA Expression.
R-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-73777. RNA Polymerase I Chain Elongation.
R-MMU-912497. Meiotic Recombination.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.1
Gene namesi
Name:Hist1h3a
Synonyms:H3a
AND
Name:Hist1h3g
Synonyms:H3.1-221, H3g
AND
Name:Hist1h3h
Synonyms:H3.1-291, H3h
AND
Name:Hist1h3i
Synonyms:H3.1-I, H3i
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2668828. Hist1h3a.
MGI:2145541. Hist1h3g.
MGI:2448349. Hist1h3h.
MGI:2448350. Hist1h3i.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002212492 – 136Histone H3.1Add BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3Asymmetric dimethylarginine; by PRMT6; alternateBy similarity1
Modified residuei3Citrulline; alternateBy similarity1
Modified residuei3Phosphoarginine; alternateCurated1
Modified residuei4Phosphothreonine; by GSG21 Publication1
Modified residuei5Allysine; alternateBy similarity1
Modified residuei5N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei5N6-acetyllysine; alternate1 Publication1
Modified residuei5N6-crotonyllysine; alternate1 Publication1
Modified residuei5N6-methyllysine; alternate2 Publications1
Modified residuei7Phosphothreonine; by PKCBy similarity1
Modified residuei9Citrulline; alternate1 Publication1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternate1 Publication1
Modified residuei10N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei10N6-acetyllysine; alternate2 Publications1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate2 Publications1
Modified residuei11Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA55 Publications1
Modified residuei12Phosphothreonine; by PKC and CHEK1By similarity1
Modified residuei15N6-acetyllysine3 Publications1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate4 Publications1
Modified residuei18Citrulline; alternate1 Publication1
Modified residuei19N6-acetyllysine; alternate3 Publications1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternate3 Publications1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei24N6-methyllysine; alternate1 Publication1
Modified residuei27CitrullineBy similarity1
Modified residuei28N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei28N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei28N6-acetyllysine; alternate1 Publication1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate2 Publications1
Modified residuei29Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei37N6-acetyllysine; alternate1 Publication1
Modified residuei37N6-methyllysine; alternate2 Publications1
Modified residuei38N6-methyllysineBy similarity1
Modified residuei42PhosphotyrosineBy similarity1
Modified residuei57N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-crotonyllysine; alternate1 Publication1
Modified residuei57N6-methyllysine; by EHMT2; alternateBy similarity1
Modified residuei58PhosphoserineBy similarity1
Modified residuei65N6-methyllysineBy similarity1
Modified residuei80N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei80N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei80N6-acetyllysine; alternateBy similarity1
Modified residuei80N6-methyllysine; alternate2 Publications1
Modified residuei81PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-methyllysine; alternate1 Publication1
Modified residuei129PhosphoarginineCurated1
Modified residuei130PhosphoarginineCurated1
Modified residuei132PhosphoarginineSequence analysis1

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.7 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.6 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.10 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 Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.12 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

EPDiP68433.
MaxQBiP68433.
PaxDbiP68433.
PRIDEiP68433.
TopDownProteomicsiP68433.

PTM databases

iPTMnetiP68433.
PhosphoSitePlusiP68433.

Expressioni

Developmental stagei

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.1 Publication

Gene expression databases

BgeeiENSMUSG00000062417.
CleanExiMM_HIST1H3A.
MM_HIST1H3G.
MM_HIST1H3H.
MM_HIST1H3I.
GenevisibleiP68433. MM.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
Cbx1P839176EBI-79743,EBI-78119
SETD7Q8WTS62EBI-79743,EBI-1268586From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi237523. 1 interactor.
IntActiP68433. 26 interactors.
MINTiMINT-191105.
STRINGi10090.ENSMUSP00000097295.

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi46 – 55Combined sources10
Helixi65 – 77Combined sources13
Beta strandi80 – 82Combined sources3
Helixi87 – 114Combined sources28
Beta strandi118 – 120Combined sources3
Helixi122 – 132Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GUWNMR-B2-17[»]
1U35X-ray3.00A/E1-136[»]
2V83X-ray2.40D/E2-10[»]
2W5ZX-ray2.20C2-9[»]
2WP1X-ray2.10P/Q15-24[»]
2XL3X-ray2.70D/F2-9[»]
4EZHX-ray2.52C/D25-35[»]
5IX1X-ray2.60P/Q2-16[»]
5IX2X-ray2.90P/Q2-33[»]
ProteinModelPortaliP68433.
SMRiP68433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68433.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP68433.
KOiK11253.
OMAiRISKMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP68433.
TreeFamiTF314241.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
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.

P68433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,404
Last modified:January 23, 2007 - v2
Checksum:i9B89008EA50A0EF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01684 Genomic DNA. Translation: CAA25839.1.
M32460 Genomic DNA. Translation: AAA37811.1.
M32462 Genomic DNA. Translation: AAA37813.1.
X16496 Genomic DNA. Translation: CAA34512.1.
U62670 Genomic DNA. Translation: AAB04763.1.
U62672 Genomic DNA. Translation: AAB04765.1.
AY158944 Genomic DNA. Translation: AAO06254.1.
AY158945 Genomic DNA. Translation: AAO06255.1.
AY158946 Genomic DNA. Translation: AAO06256.1.
AY158952 Genomic DNA. Translation: AAO06262.1.
Y12290 Genomic DNA. Translation: CAA72968.1.
AK006742 mRNA. Translation: BAB24722.1.
AK018952 mRNA. Translation: BAB31493.1.
AK155722 mRNA. Translation: BAE33402.1.
AL590388 Genomic DNA. Translation: CAI25837.1.
AL589651 Genomic DNA. Translation: CAI24113.1.
AL589651 Genomic DNA. Translation: CAI24105.1.
BC107285 mRNA. Translation: AAI07286.1.
BC107287 mRNA. Translation: AAI07288.1.
BC115816 mRNA. Translation: AAI15817.1.
BC116383 mRNA. Translation: AAI16384.1.
BC125355 mRNA. Translation: AAI25356.1.
BC125357 mRNA. Translation: AAI25358.1.
CCDSiCCDS26289.1.
CCDS26296.1.
CCDS26342.1.
CCDS26368.1.
PIRiA39525.
S06755.
RefSeqiNP_038578.2. NM_013550.5.
NP_659539.1. NM_145073.2.
NP_835513.1. NM_178206.2.
NP_835514.1. NM_178207.2.
UniGeneiMm.221301.
Mm.261657.
Mm.377874.
Mm.390558.
Mm.397328.

Genome annotation databases

EnsembliENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000099517.
ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
ENSMUST00000188775; ENSMUSP00000140394; ENSMUSG00000101355.
ENSMUST00000189457; ENSMUSP00000139663; ENSMUSG00000101972.
GeneIDi319152.
319153.
360198.
97908.
KEGGimmu:319152.
mmu:319153.
mmu:360198.
mmu:97908.
UCSCiuc007prc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01684 Genomic DNA. Translation: CAA25839.1.
M32460 Genomic DNA. Translation: AAA37811.1.
M32462 Genomic DNA. Translation: AAA37813.1.
X16496 Genomic DNA. Translation: CAA34512.1.
U62670 Genomic DNA. Translation: AAB04763.1.
U62672 Genomic DNA. Translation: AAB04765.1.
AY158944 Genomic DNA. Translation: AAO06254.1.
AY158945 Genomic DNA. Translation: AAO06255.1.
AY158946 Genomic DNA. Translation: AAO06256.1.
AY158952 Genomic DNA. Translation: AAO06262.1.
Y12290 Genomic DNA. Translation: CAA72968.1.
AK006742 mRNA. Translation: BAB24722.1.
AK018952 mRNA. Translation: BAB31493.1.
AK155722 mRNA. Translation: BAE33402.1.
AL590388 Genomic DNA. Translation: CAI25837.1.
AL589651 Genomic DNA. Translation: CAI24113.1.
AL589651 Genomic DNA. Translation: CAI24105.1.
BC107285 mRNA. Translation: AAI07286.1.
BC107287 mRNA. Translation: AAI07288.1.
BC115816 mRNA. Translation: AAI15817.1.
BC116383 mRNA. Translation: AAI16384.1.
BC125355 mRNA. Translation: AAI25356.1.
BC125357 mRNA. Translation: AAI25358.1.
CCDSiCCDS26289.1.
CCDS26296.1.
CCDS26342.1.
CCDS26368.1.
PIRiA39525.
S06755.
RefSeqiNP_038578.2. NM_013550.5.
NP_659539.1. NM_145073.2.
NP_835513.1. NM_178206.2.
NP_835514.1. NM_178207.2.
UniGeneiMm.221301.
Mm.261657.
Mm.377874.
Mm.390558.
Mm.397328.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GUWNMR-B2-17[»]
1U35X-ray3.00A/E1-136[»]
2V83X-ray2.40D/E2-10[»]
2W5ZX-ray2.20C2-9[»]
2WP1X-ray2.10P/Q15-24[»]
2XL3X-ray2.70D/F2-9[»]
4EZHX-ray2.52C/D25-35[»]
5IX1X-ray2.60P/Q2-16[»]
5IX2X-ray2.90P/Q2-33[»]
ProteinModelPortaliP68433.
SMRiP68433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237523. 1 interactor.
IntActiP68433. 26 interactors.
MINTiMINT-191105.
STRINGi10090.ENSMUSP00000097295.

PTM databases

iPTMnetiP68433.
PhosphoSitePlusiP68433.

Proteomic databases

EPDiP68433.
MaxQBiP68433.
PaxDbiP68433.
PRIDEiP68433.
TopDownProteomicsiP68433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000099517.
ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
ENSMUST00000188775; ENSMUSP00000140394; ENSMUSG00000101355.
ENSMUST00000189457; ENSMUSP00000139663; ENSMUSG00000101972.
GeneIDi319152.
319153.
360198.
97908.
KEGGimmu:319152.
mmu:319153.
mmu:360198.
mmu:97908.
UCSCiuc007prc.1. mouse.

Organism-specific databases

CTDi8350.
8354.
8355.
8357.
MGIiMGI:2668828. Hist1h3a.
MGI:2145541. Hist1h3g.
MGI:2448349. Hist1h3h.
MGI:2448350. Hist1h3i.

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP68433.
KOiK11253.
OMAiRISKMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP68433.
TreeFamiTF314241.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-1266695. Interleukin-7 signaling.
R-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-MMU-3214841. PKMTs methylate histone lysines.
R-MMU-3214842. HDMs demethylate histones.
R-MMU-3214847. HATs acetylate histones.
R-MMU-3214858. RMTs methylate histone arginines.
R-MMU-3247509. Chromatin modifying enzymes.
R-MMU-427359. SIRT1 negatively regulates rRNA Expression.
R-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5250924. B-WICH complex positively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-5578749. Transcriptional regulation by small RNAs.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-73777. RNA Polymerase I Chain Elongation.
R-MMU-912497. Meiotic Recombination.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP68433.
PROiP68433.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000062417.
CleanExiMM_HIST1H3A.
MM_HIST1H3G.
MM_HIST1H3H.
MM_HIST1H3I.
GenevisibleiP68433. MM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
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...

Entry informationi

Entry nameiH31_MOUSE
AccessioniPrimary (citable) accession number: P68433
Secondary accession number(s): P02295
, P02296, P16106, Q05A97, Q3B7Z8, Q3B7Z9, Q5T009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This histone is only present in mammals.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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 one 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.