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P62806

- H4_MOUSE

UniProt

P62806 - H4_MOUSE

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Protein

Histone H4

Gene

Hist1h4a

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi17 – 215

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. DNA replication-dependent nucleosome assembly Source: Ensembl
  2. DNA replication-independent nucleosome assembly Source: Ensembl
  3. negative regulation of megakaryocyte differentiation Source: Ensembl
  4. nucleosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_196580. Condensation of Prophase Chromosomes.
REACT_198563. Amyloids.
REACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_198626. Meiotic synapsis.
REACT_198629. Meiotic recombination.
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_226125. Packaging Of Telomere Ends.
REACT_226917. HATs acetylate histones.
REACT_244207. RMTs methylate histone arginines.
REACT_256030. HDMs demethylate histones.
REACT_256157. RNA Polymerase I Promoter Opening.
REACT_257106. HDACs deacetylate histones.
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 H4
Gene namesi
Name:Hist1h4a
AND
Name:Hist1h4b
Synonyms:H4-53
AND
Name:Hist1h4c
Synonyms:H4-12
AND
Name:Hist1h4d
AND
Name:Hist1h4f
AND
Name:Hist1h4h
AND
Name:Hist1h4i
AND
Name:Hist1h4j
AND
Name:Hist1h4k
AND
Name:Hist1h4m
AND
Name:Hist2h4a
Synonyms:Hist2h4
AND
Name:Hist4h4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13, UP000000589: Chromosome 3, UP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:2448419. Hist1h4a.
MGI:2448420. Hist1h4b.
MGI:2448421. Hist1h4c.
MGI:2448423. Hist1h4d.
MGI:2448425. Hist1h4f.
MGI:2448427. Hist1h4h.
MGI:2448432. Hist1h4i.
MGI:2448436. Hist1h4j.
MGI:2448439. Hist1h4k.
MGI:2448441. Hist1h4m.
MGI:2140113. Hist2h4.
MGI:2448443. Hist4h4.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. nuclear chromosome Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleosome Source: UniProtKB
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 – 103102Histone H4PRO_0000158329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei4 – 41Asymmetric dimethylarginine; by PRMT1; alternate1 Publication
Modified residuei4 – 41Citrulline; alternateBy similarity
Modified residuei4 – 41Omega-N-methylarginine; by PRMT1; alternateBy similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate1 Publication
Modified residuei6 – 61N6-acetyllysine; alternate2 Publications
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Modified residuei9 – 91N6-acetyllysine; alternate2 Publications
Modified residuei9 – 91N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternate2 Publications
Modified residuei13 – 131N6-crotonyllysine; alternateBy similarity
Modified residuei17 – 171N6-acetyllysine; alternate2 Publications
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei21 – 211N6,N6-dimethyllysine; alternateBy similarity
Modified residuei21 – 211N6-methyllysine; alternateBy similarity
Modified residuei32 – 321N6-acetyllysine1 Publication
Modified residuei48 – 481Phosphoserine; by PAK2By similarity
Modified residuei52 – 521Phosphotyrosine2 Publications
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
Modified residuei92 – 921N6-succinyllysine; alternate1 Publication
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

Post-translational modificationi

Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.2 Publications
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.2 Publications
Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity).By similarity
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and induces gene silencing (By similarity).By similarity
Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 (By similarity).By similarity
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. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) (By similarity).By similarity
Sumoylated, which is associated with transcriptional repression.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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62806.
PaxDbiP62806.
PRIDEiP62806.

PTM databases

PhosphoSiteiP62806.

Expressioni

Gene expression databases

BgeeiP62806.
CleanExiMM_HIST1H4A.
MM_HIST1H4B.
MM_HIST1H4C.
MM_HIST1H4D.
MM_HIST1H4F.
MM_HIST1H4H.
MM_HIST1H4I.
MM_HIST1H4J.
MM_HIST1H4K.
MM_HIST1H4M.
MM_HIST2H4.
MM_HIST4H4.
ExpressionAtlasiP62806. baseline and differential.
GenevestigatoriP62806.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Atad2Q8CDM12EBI-299632,EBI-2944582

Protein-protein interaction databases

BioGridi213404. 1 interaction.
220610. 5 interactions.
235074. 1 interaction.
235079. 1 interaction.
235942. 8 interactions.
236472. 2 interactions.
236473. 1 interaction.
DIPiDIP-45837N.
IntActiP62806. 9 interactions.
MINTiMINT-1866189.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 233Combined sources
Helixi26 – 294Combined sources
Helixi32 – 4110Combined sources
Helixi51 – 7626Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 9310Combined sources
Beta strandi98 – 1014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60B/F1-103[»]
1U35X-ray3.00B/F1-103[»]
2WP2X-ray2.37P/Q2-21[»]
4AU7X-ray2.07C18-25[»]
4DOWX-ray1.95C/D15-26[»]
ProteinModelPortaliP62806.
SMRiP62806. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62806.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000119019.
HOVERGENiHBG051878.
InParanoidiP62806.
KOiK11254.
OMAiYEEVRVV.
OrthoDBiEOG77T174.
PhylomeDBiP62806.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00047. HISTONE_H4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62806-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL
60 70 80 90 100
IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG

FGG
Length:103
Mass (Da):11,367
Last modified:January 23, 2007 - v2
Checksum:iA9E5DFD3F8B97598
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341A → V in BAB26692. (PubMed:16141072)Curated
Sequence conflicti80 – 801K → E in BAB27698. (PubMed:16141072)Curated
Sequence conflicti90 – 901A → R in CAA31622. (PubMed:2915930)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00753 Genomic DNA. Translation: CAA24130.1.
X13235 Genomic DNA. Translation: CAA31621.1.
X13236 Genomic DNA. Translation: CAA31622.1.
U62672 Genomic DNA. Translation: AAB04766.1.
Y12290 Genomic DNA. Translation: CAA72967.1.
AY158956 Genomic DNA. Translation: AAO06266.1.
AY158957 Genomic DNA. Translation: AAO06267.1.
AY158958 Genomic DNA. Translation: AAO06268.1.
AY158959 Genomic DNA. Translation: AAO06269.1.
AY158960 Genomic DNA. Translation: AAO06270.1.
AY158961 Genomic DNA. Translation: AAO06271.1.
AY158962 Genomic DNA. Translation: AAO06272.1.
AY158963 Genomic DNA. Translation: AAO06273.1.
AY158964 Genomic DNA. Translation: AAO06274.1.
AY158965 Genomic DNA. Translation: AAO06275.1.
AY158966 Genomic DNA. Translation: AAO06276.1.
AY158967 Genomic DNA. Translation: AAO06277.1.
AK007642 mRNA. Translation: BAB25157.1.
AK010085 mRNA. Translation: BAB26692.1.
AK011560 mRNA. Translation: BAB27698.1.
AK139521 mRNA. Translation: BAE24047.1.
AL589651 Genomic DNA. Translation: CAI24108.1.
AL589651 Genomic DNA. Translation: CAI24109.1.
AL590388 Genomic DNA. Translation: CAI25838.1.
AL590388 Genomic DNA. Translation: CAI25839.1.
AL590614 Genomic DNA. Translation: CAI26128.1.
BC028550 mRNA. Translation: AAH28550.3.
BC052219 mRNA. No translation available.
BC057955 mRNA. Translation: AAH57955.1.
BC058529 mRNA. Translation: AAH58529.2.
BC087952 mRNA. Translation: AAH87952.1.
BC092144 mRNA. Translation: AAH92144.1.
BC115446 mRNA. Translation: AAI15447.1.
BC115447 mRNA. Translation: AAI15448.1.
BC115451 mRNA. Translation: AAI15452.1.
BC115448 mRNA. Translation: AAI15449.1.
BC115449 mRNA. Translation: AAI15450.1.
BC115450 mRNA. Translation: AAI15451.1.
BC117010 mRNA. Translation: AAI17011.1.
BC117012 mRNA. Translation: AAI17013.1.
BC111813 mRNA. Translation: AAI11814.1.
BC119241 mRNA. Translation: AAI19242.1.
BC119243 mRNA. Translation: AAI19244.1.
BC119611 mRNA. Translation: AAI19612.1.
BC119612 mRNA. Translation: AAI19613.1.
BC125598 mRNA. Translation: AAI25599.1.
BC125600 mRNA. Translation: AAI25601.1.
BC132186 mRNA. Translation: AAI32187.1.
BC132212 mRNA. Translation: AAI32213.1.
BC139809 mRNA. Translation: AAI39810.1.
BC152397 mRNA. Translation: AAI52398.1.
CCDSiCCDS26291.1.
CCDS26292.1.
CCDS26300.1.
CCDS26306.1.
CCDS26340.1.
CCDS26345.1.
CCDS26353.1.
CCDS26359.1.
CCDS26366.1.
CCDS26367.1.
CCDS39684.1.
CCDS51002.1.
PIRiS03426.
S03427.
RefSeqiNP_001182350.1. NM_001195421.1.
NP_291074.1. NM_033596.3.
NP_694813.1. NM_153173.4.
NP_783583.1. NM_175652.3.
NP_783585.1. NM_175654.2.
NP_783586.1. NM_175655.2.
NP_783587.1. NM_175656.3.
NP_783588.1. NM_175657.2.
NP_835499.1. NM_178192.2.
NP_835500.1. NM_178193.2.
NP_835515.1. NM_178208.2.
NP_835582.1. NM_178210.1.
NP_835583.1. NM_178211.2.
XP_006544162.1. XM_006544099.1.
UniGeneiMm.14775.
Mm.158272.
Mm.227295.
Mm.228709.
Mm.246720.
Mm.255646.
Mm.260530.
Mm.261642.
Mm.261662.
Mm.261664.
Mm.442307.
Mm.486099.

Genome annotation databases

EnsembliENSMUST00000087714; ENSMUSP00000085006; ENSMUSG00000067455.
ENSMUST00000102964; ENSMUSP00000100029; ENSMUSG00000060093.
ENSMUST00000102965; ENSMUSP00000100030; ENSMUSG00000069266.
ENSMUST00000102967; ENSMUSP00000100032; ENSMUSG00000060678.
ENSMUST00000102968; ENSMUSP00000100033; ENSMUSG00000061482.
ENSMUST00000102971; ENSMUSP00000100036; ENSMUSG00000069274.
ENSMUST00000102972; ENSMUSP00000100037; ENSMUSG00000060981.
ENSMUST00000102977; ENSMUSP00000100042; ENSMUSG00000060639.
ENSMUST00000102979; ENSMUSP00000100044; ENSMUSG00000069305.
ENSMUST00000102983; ENSMUSP00000100048; ENSMUSG00000064288.
ENSMUST00000104941; ENSMUSP00000100546; ENSMUSG00000069306.
ENSMUST00000171473; ENSMUSP00000129930; ENSMUSG00000091405.
ENSMUST00000179285; ENSMUSP00000136357; ENSMUSG00000096010.
GeneIDi100041230.
102641229.
319155.
319156.
319157.
319158.
319159.
319160.
319161.
320332.
326619.
326620.
69386.
97122.
KEGGimmu:100041230.
mmu:102641229.
mmu:319155.
mmu:319156.
mmu:319157.
mmu:319158.
mmu:319159.
mmu:319160.
mmu:319161.
mmu:320332.
mmu:326619.
mmu:326620.
mmu:69386.
mmu:97122.
UCSCiuc007pre.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00753 Genomic DNA. Translation: CAA24130.1 .
X13235 Genomic DNA. Translation: CAA31621.1 .
X13236 Genomic DNA. Translation: CAA31622.1 .
U62672 Genomic DNA. Translation: AAB04766.1 .
Y12290 Genomic DNA. Translation: CAA72967.1 .
AY158956 Genomic DNA. Translation: AAO06266.1 .
AY158957 Genomic DNA. Translation: AAO06267.1 .
AY158958 Genomic DNA. Translation: AAO06268.1 .
AY158959 Genomic DNA. Translation: AAO06269.1 .
AY158960 Genomic DNA. Translation: AAO06270.1 .
AY158961 Genomic DNA. Translation: AAO06271.1 .
AY158962 Genomic DNA. Translation: AAO06272.1 .
AY158963 Genomic DNA. Translation: AAO06273.1 .
AY158964 Genomic DNA. Translation: AAO06274.1 .
AY158965 Genomic DNA. Translation: AAO06275.1 .
AY158966 Genomic DNA. Translation: AAO06276.1 .
AY158967 Genomic DNA. Translation: AAO06277.1 .
AK007642 mRNA. Translation: BAB25157.1 .
AK010085 mRNA. Translation: BAB26692.1 .
AK011560 mRNA. Translation: BAB27698.1 .
AK139521 mRNA. Translation: BAE24047.1 .
AL589651 Genomic DNA. Translation: CAI24108.1 .
AL589651 Genomic DNA. Translation: CAI24109.1 .
AL590388 Genomic DNA. Translation: CAI25838.1 .
AL590388 Genomic DNA. Translation: CAI25839.1 .
AL590614 Genomic DNA. Translation: CAI26128.1 .
BC028550 mRNA. Translation: AAH28550.3 .
BC052219 mRNA. No translation available.
BC057955 mRNA. Translation: AAH57955.1 .
BC058529 mRNA. Translation: AAH58529.2 .
BC087952 mRNA. Translation: AAH87952.1 .
BC092144 mRNA. Translation: AAH92144.1 .
BC115446 mRNA. Translation: AAI15447.1 .
BC115447 mRNA. Translation: AAI15448.1 .
BC115451 mRNA. Translation: AAI15452.1 .
BC115448 mRNA. Translation: AAI15449.1 .
BC115449 mRNA. Translation: AAI15450.1 .
BC115450 mRNA. Translation: AAI15451.1 .
BC117010 mRNA. Translation: AAI17011.1 .
BC117012 mRNA. Translation: AAI17013.1 .
BC111813 mRNA. Translation: AAI11814.1 .
BC119241 mRNA. Translation: AAI19242.1 .
BC119243 mRNA. Translation: AAI19244.1 .
BC119611 mRNA. Translation: AAI19612.1 .
BC119612 mRNA. Translation: AAI19613.1 .
BC125598 mRNA. Translation: AAI25599.1 .
BC125600 mRNA. Translation: AAI25601.1 .
BC132186 mRNA. Translation: AAI32187.1 .
BC132212 mRNA. Translation: AAI32213.1 .
BC139809 mRNA. Translation: AAI39810.1 .
BC152397 mRNA. Translation: AAI52398.1 .
CCDSi CCDS26291.1.
CCDS26292.1.
CCDS26300.1.
CCDS26306.1.
CCDS26340.1.
CCDS26345.1.
CCDS26353.1.
CCDS26359.1.
CCDS26366.1.
CCDS26367.1.
CCDS39684.1.
CCDS51002.1.
PIRi S03426.
S03427.
RefSeqi NP_001182350.1. NM_001195421.1.
NP_291074.1. NM_033596.3.
NP_694813.1. NM_153173.4.
NP_783583.1. NM_175652.3.
NP_783585.1. NM_175654.2.
NP_783586.1. NM_175655.2.
NP_783587.1. NM_175656.3.
NP_783588.1. NM_175657.2.
NP_835499.1. NM_178192.2.
NP_835500.1. NM_178193.2.
NP_835515.1. NM_178208.2.
NP_835582.1. NM_178210.1.
NP_835583.1. NM_178211.2.
XP_006544162.1. XM_006544099.1.
UniGenei Mm.14775.
Mm.158272.
Mm.227295.
Mm.228709.
Mm.246720.
Mm.255646.
Mm.260530.
Mm.261642.
Mm.261662.
Mm.261664.
Mm.442307.
Mm.486099.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F66 X-ray 2.60 B/F 1-103 [» ]
1U35 X-ray 3.00 B/F 1-103 [» ]
2WP2 X-ray 2.37 P/Q 2-21 [» ]
4AU7 X-ray 2.07 C 18-25 [» ]
4DOW X-ray 1.95 C/D 15-26 [» ]
ProteinModelPortali P62806.
SMRi P62806. Positions 21-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 213404. 1 interaction.
220610. 5 interactions.
235074. 1 interaction.
235079. 1 interaction.
235942. 8 interactions.
236472. 2 interactions.
236473. 1 interaction.
DIPi DIP-45837N.
IntActi P62806. 9 interactions.
MINTi MINT-1866189.

Chemistry

BindingDBi P62806.

PTM databases

PhosphoSitei P62806.

Proteomic databases

MaxQBi P62806.
PaxDbi P62806.
PRIDEi P62806.

Protocols and materials databases

DNASUi 319156.
319157.
319159.
320332.
326620.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000087714 ; ENSMUSP00000085006 ; ENSMUSG00000067455 .
ENSMUST00000102964 ; ENSMUSP00000100029 ; ENSMUSG00000060093 .
ENSMUST00000102965 ; ENSMUSP00000100030 ; ENSMUSG00000069266 .
ENSMUST00000102967 ; ENSMUSP00000100032 ; ENSMUSG00000060678 .
ENSMUST00000102968 ; ENSMUSP00000100033 ; ENSMUSG00000061482 .
ENSMUST00000102971 ; ENSMUSP00000100036 ; ENSMUSG00000069274 .
ENSMUST00000102972 ; ENSMUSP00000100037 ; ENSMUSG00000060981 .
ENSMUST00000102977 ; ENSMUSP00000100042 ; ENSMUSG00000060639 .
ENSMUST00000102979 ; ENSMUSP00000100044 ; ENSMUSG00000069305 .
ENSMUST00000102983 ; ENSMUSP00000100048 ; ENSMUSG00000064288 .
ENSMUST00000104941 ; ENSMUSP00000100546 ; ENSMUSG00000069306 .
ENSMUST00000171473 ; ENSMUSP00000129930 ; ENSMUSG00000091405 .
ENSMUST00000179285 ; ENSMUSP00000136357 ; ENSMUSG00000096010 .
GeneIDi 100041230.
102641229.
319155.
319156.
319157.
319158.
319159.
319160.
319161.
320332.
326619.
326620.
69386.
97122.
KEGGi mmu:100041230.
mmu:102641229.
mmu:319155.
mmu:319156.
mmu:319157.
mmu:319158.
mmu:319159.
mmu:319160.
mmu:319161.
mmu:320332.
mmu:326619.
mmu:326620.
mmu:69386.
mmu:97122.
UCSCi uc007pre.1. mouse.

Organism-specific databases

CTDi 100041230.
121504.
319161.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
97122.
MGIi MGI:2448419. Hist1h4a.
MGI:2448420. Hist1h4b.
MGI:2448421. Hist1h4c.
MGI:2448423. Hist1h4d.
MGI:2448425. Hist1h4f.
MGI:2448427. Hist1h4h.
MGI:2448432. Hist1h4i.
MGI:2448436. Hist1h4j.
MGI:2448439. Hist1h4k.
MGI:2448441. Hist1h4m.
MGI:2140113. Hist2h4.
MGI:2448443. Hist4h4.

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00760000119019.
HOVERGENi HBG051878.
InParanoidi P62806.
KOi K11254.
OMAi YEEVRVV.
OrthoDBi EOG77T174.
PhylomeDBi P62806.

Enzyme and pathway databases

Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_196580. Condensation of Prophase Chromosomes.
REACT_198563. Amyloids.
REACT_198597. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_198626. Meiotic synapsis.
REACT_198629. Meiotic recombination.
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_226125. Packaging Of Telomere Ends.
REACT_226917. HATs acetylate histones.
REACT_244207. RMTs methylate histone arginines.
REACT_256030. HDMs demethylate histones.
REACT_256157. RNA Polymerase I Promoter Opening.
REACT_257106. HDACs deacetylate histones.
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

EvolutionaryTracei P62806.
NextBioi 329305.
PROi P62806.
SOURCEi Search...

Gene expression databases

Bgeei P62806.
CleanExi MM_HIST1H4A.
MM_HIST1H4B.
MM_HIST1H4C.
MM_HIST1H4D.
MM_HIST1H4F.
MM_HIST1H4H.
MM_HIST1H4I.
MM_HIST1H4J.
MM_HIST1H4K.
MM_HIST1H4M.
MM_HIST2H4.
MM_HIST4H4.
ExpressionAtlasi P62806. baseline and differential.
Genevestigatori P62806.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00623. HISTONEH4.
SMARTi SM00417. H4. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00047. HISTONE_H4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression in L-cells of a cloned H4 histone gene of the mouse."
    Seiler-Tuyns A., Birnstiel M.L.
    J. Mol. Biol. 151:607-625(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of two mouse histone H4 genes."
    Meier V.S., Boehni R., Schuemperli D.
    Nucleic Acids Res. 17:795-795(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4B AND HIST1H4C).
  3. "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] (HIST1H4A).
    Strain: C57BL/6.
  4. Franke K., Drabent B., Doenecke D.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  5. "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] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4F; HIST1H44; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4M; HIST2H4A AND HIST4H4).
  6. "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: Egg, Pancreas and Tongue.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  8. "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: C57BL/6J.
    Tissue: Brain, Embryo, Eye, Heart, Mammary gland and Testis.
  9. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
    Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
    Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-21.
  10. "Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is conserved in fly and mouse spermatogenesis."
    Krishnamoorthy T., Chen X., Govin J., Cheung W.L., Dorsey J., Schindler K., Winter E., Allis C.D., Guacci V., Khochbin S., Fuller M.T., Berger S.L.
    Genes Dev. 20:2580-2592(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2.
  11. "Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells."
    Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., Kouzarides T., Surani M.A.
    Nat. Cell Biol. 8:623-630(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-4.
  12. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  13. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  14. "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-9 AND LYS-17.
  15. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND LYS-32, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  16. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Crystal structure of a nucleosome core particle containing the variant histone H2A.Z."
    Suto R.K., Clarkson M.J., Tremethick D.J., Luger K.
    Nat. Struct. Biol. 7:1121-1124(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH H2A-Z; H2B AND H3.

Entry informationi

Entry nameiH4_MOUSE
AccessioniPrimary (citable) accession number: P62806
Secondary accession number(s): A0AUM5
, A4FUP8, A4QMY0, P02304, P02305, Q0VDL9, Q2M2Q5, Q5T006, Q6PDS7, Q811M0, Q9D0C9, Q9D6Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 123 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