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Protein

Histone H3.3

Gene

H3F3A

more
Organism
Homo sapiens (Human)
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.3 Publications

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • nucleosomal DNA binding Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: Reactome
  • cellular protein metabolic process Source: Reactome
  • chromatin silencing at rDNA Source: Reactome
  • DNA replication-independent nucleosome assembly Source: UniProtKB
  • gene silencing by RNA Source: Reactome
  • negative regulation of gene expression, epigenetic Source: Reactome
  • nucleosome assembly Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of gene expression, epigenetic Source: Reactome
  • telomere organization Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000132475-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiP84243.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.3
Gene namesi
Name:H3F3A
Synonyms:H3.3A, H3F3
ORF Names:PP781
AND
Name:H3F3B
Synonyms:H3.3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componentsi: Chromosome 1, Chromosome 17

Organism-specific databases

HGNCiHGNC:4764. H3F3A.
HGNC:4765. H3F3B.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • nuclear chromosome Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear nucleosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleosome Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi3020.
3021.
OpenTargetsiENSG00000132475.
ENSG00000163041.
PharmGKBiPA29140.

Polymorphism and mutation databases

BioMutaiH3F3A.
DMDMi55977062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002212472 – 136Histone H3.3Add BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3Asymmetric dimethylarginine; by PRMT6; alternate3 Publications1
Modified residuei3Citrulline; alternate1 Publication1
Modified residuei4Phosphothreonine; by GSG22 Publications1
Modified residuei5Allysine; alternate1
Modified residuei5N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei5N6-acetyllysine; alternate1 Publication1
Modified residuei5N6-crotonyllysine; alternate1 Publication1
Modified residuei5N6-methyllysine; alternate4 Publications1
Modified residuei7Phosphothreonine; by PKC1 Publication1
Modified residuei9Citrulline; alternate2 Publications1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei10N6,N6,N6-trimethyllysine; alternate6 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate6 Publications1
Modified residuei10N6-acetyllysine; alternate5 Publications1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate6 Publications1
Modified residuei11Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications1
Modified residuei12Phosphothreonine; by PKC2 Publications1
Modified residuei15N6-acetyllysine5 Publications1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate3 Publications1
Modified residuei18Citrulline; alternate3 Publications1
Modified residuei19N6-acetyllysine; alternate2 Publications1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate2 Publications1
Modified residuei24N6-acetyllysine; alternate3 Publications1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei24N6-methyllysine; alternate1 Publication1
Modified residuei27Citrulline1 Publication1
Modified residuei28N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei28N6,N6-dimethyllysine; alternateCombined sources4 Publications1
Modified residuei28N6-acetyllysine; alternateCombined sources2 Publications1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate4 Publications1
Modified residuei29Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei32Phosphoserine2 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei37N6-acetyllysine; alternate2 Publications1
Modified residuei37N6-methyllysine; alternate4 Publications1
Modified residuei38N6-methyllysineBy similarity1
Modified residuei42Phosphotyrosine1 Publication1
Modified residuei57N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei57N6-acetyllysine; alternate1 Publication1
Modified residuei57N6-crotonyllysine; alternate1 Publication1
Modified residuei57N6-methyllysine; by EHMT2; alternate2 Publications1
Modified residuei58Phosphoserine1 Publication1
Modified residuei65N6-methyllysine2 Publications1
Modified residuei80N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei80N6,N6-dimethyllysine; alternate3 Publications1
Modified residuei80N6-acetyllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate3 Publications1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineCombined sources1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysine1 Publication1
Modified residuei123N6-acetyllysine; alternate2 Publications1
Modified residuei123N6-methyllysine; alternate2 Publications1

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.11 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.4 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.10 Publications
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.15 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.17 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 (PubMed:22483618).1 Publication
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

EPDiP84243.
MaxQBiP84243.
PaxDbiP84243.
PeptideAtlasiP84243.
PRIDEiP84243.
TopDownProteomicsiP84243.

PTM databases

iPTMnetiP84243.
PhosphoSitePlusiP84243.
SwissPalmiP84243.

Expressioni

Developmental stagei

Expressed throughout the cell cycle independently of DNA synthesis.

Gene expression databases

BgeeiENSG00000132475.
CleanExiHS_H3F3A.
HS_H3F3B.
ExpressionAtlasiP84243. baseline and differential.
GenevisibleiP84243. HS.

Organism-specific databases

HPAiCAB011481.
CAB037166.
CAB037178.
CAB037187.
CAB037221.
HPA042570.

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).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei32Interaction with ZMYND111 Publication1

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX5P459732EBI-120658,EBI-78219
DNMT3AQ9Y6K17EBI-120658,EBI-923653
HIST2H4BP628053EBI-120658,EBI-302023
NASPP49321-23EBI-120658,EBI-7038920
PELP1Q8IZL811EBI-120658,EBI-716449
SfmbtQ9VK3315EBI-120658,EBI-117801From a different organism.
TAF3Q5VWG93EBI-120658,EBI-1560087

GO - Molecular functioni

  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109272. 108 interactors.
109273. 17 interactors.
DIPiDIP-40046N.
IntActiP84243. 41 interactors.
MINTiMINT-4825076.
STRINGi9606.ENSP00000355778.

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi8 – 10Combined sources3
Beta strandi16 – 18Combined sources3
Beta strandi45 – 47Combined sources3
Helixi49 – 59Combined sources11
Helixi65 – 79Combined sources15
Beta strandi80 – 82Combined sources3
Beta strandi84 – 86Combined sources3
Helixi87 – 110Combined sources24
Beta strandi118 – 120Combined sources3
Helixi122 – 132Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L43NMR-A2-13[»]
3ASKX-ray2.90P/Q/R2-14[»]
3ASLX-ray1.41B2-12[»]
3AV2X-ray2.80A/E1-136[»]
3JVKX-ray1.80C13-20[»]
3MUKX-ray1.75D22-29[»]
3MULX-ray1.65D13-20[»]
3QL9X-ray0.93C2-16[»]
3QLAX-ray1.60C/F2-16[»]
3QLCX-ray2.50C/D2-16[»]
3WTPX-ray2.67E1-136[»]
4GNEX-ray1.47B2-8[»]
4GNFX-ray1.55C2-16[»]
4GNGX-ray1.73B/F2-16[»]
4GU0X-ray3.10E/F2-27[»]
4GURX-ray2.51C2-22[»]
4GUSX-ray2.23C2-22[»]
4GY5X-ray2.96E/F2-18[»]
4H9NX-ray1.95A2-136[»]
4H9OX-ray2.05A2-136[»]
4H9PX-ray2.20A2-136[»]
4H9QX-ray1.95A2-136[»]
4H9RX-ray2.20A2-136[»]
4H9SX-ray2.60A/B2-136[»]
4HGAX-ray2.80B1-136[»]
4L58X-ray1.48B2-13[»]
4N4IX-ray2.00B20-43[»]
4O62X-ray1.78D2-12[»]
4QQ4X-ray1.75C/D2-16[»]
4TMPX-ray2.30B/D2-12[»]
4U7TX-ray2.90F/G2-13[»]
4W5AX-ray2.60C/D/F2-16[»]
5AY8X-ray2.80A/E1-134[»]
5B32X-ray2.35A/E1-136[»]
5B33X-ray2.92A/E1-136[»]
5BNVX-ray2.79A/D58-136[»]
5BNXX-ray2.31A58-136[»]
5DWQX-ray2.36F/G14-31[»]
5DX0X-ray2.05F/G/H/I14-31[»]
5JA4X-ray2.42A58-136[»]
5KDMX-ray3.50A2-136[»]
ProteinModelPortaliP84243.
SMRiP84243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84243.

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.1 Publication

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP84243.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP84243.
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.

P84243-1 [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 CAH73371 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9R → L in AAH81561 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11354 mRNA. Translation: AAA52653.1.
M11353 mRNA. Translation: AAA52654.1.
Z48950 Genomic DNA. Translation: CAA88778.1.
X05855, X05856, X05857 Genomic DNA. Translation: CAA29288.1. Sequence problems.
AF218029 mRNA. Translation: AAG17271.1.
BX537379 mRNA. Translation: CAD97621.1.
AL512343 Genomic DNA. Translation: CAH73371.1. Sequence problems.
AL512343 Genomic DNA. Translation: CAH73372.1.
BC001124 mRNA. Translation: AAH01124.1.
BC006497 mRNA. Translation: AAH06497.1.
BC012813 mRNA. Translation: AAH12813.1.
BC017558 mRNA. Translation: AAH17558.1.
BC029405 mRNA. Translation: AAH29405.1.
BC038989 mRNA. Translation: AAH38989.1.
BC066901 mRNA. No translation available.
BC067757 mRNA. No translation available.
BC081560 mRNA. Translation: AAH81560.1.
BC081561 mRNA. Translation: AAH81561.1.
BC095447 mRNA. Translation: AAH95447.1.
BC108701 mRNA. Translation: AAI08702.1.
CCDSiCCDS11729.1.
CCDS1550.1.
PIRiA27501. HSHU33.
RefSeqiNP_002098.1. NM_002107.4.
NP_005315.1. NM_005324.4.
UniGeneiHs.180877.
Hs.533624.
Hs.726012.

Genome annotation databases

EnsembliENST00000254810; ENSP00000254810; ENSG00000132475.
ENST00000366813; ENSP00000355778; ENSG00000163041.
ENST00000366815; ENSP00000355780; ENSG00000163041.
ENST00000366816; ENSP00000355781; ENSG00000163041.
ENST00000586607; ENSP00000466020; ENSG00000132475.
ENST00000587560; ENSP00000468714; ENSG00000132475.
ENST00000589599; ENSP00000465813; ENSG00000132475.
GeneIDi3020.
3021.
KEGGihsa:3020.
hsa:3021.
UCSCiuc001hpw.4. human.

Cross-referencesi

Web resourcesi

Wikipedia

Histone H3 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11354 mRNA. Translation: AAA52653.1.
M11353 mRNA. Translation: AAA52654.1.
Z48950 Genomic DNA. Translation: CAA88778.1.
X05855, X05856, X05857 Genomic DNA. Translation: CAA29288.1. Sequence problems.
AF218029 mRNA. Translation: AAG17271.1.
BX537379 mRNA. Translation: CAD97621.1.
AL512343 Genomic DNA. Translation: CAH73371.1. Sequence problems.
AL512343 Genomic DNA. Translation: CAH73372.1.
BC001124 mRNA. Translation: AAH01124.1.
BC006497 mRNA. Translation: AAH06497.1.
BC012813 mRNA. Translation: AAH12813.1.
BC017558 mRNA. Translation: AAH17558.1.
BC029405 mRNA. Translation: AAH29405.1.
BC038989 mRNA. Translation: AAH38989.1.
BC066901 mRNA. No translation available.
BC067757 mRNA. No translation available.
BC081560 mRNA. Translation: AAH81560.1.
BC081561 mRNA. Translation: AAH81561.1.
BC095447 mRNA. Translation: AAH95447.1.
BC108701 mRNA. Translation: AAI08702.1.
CCDSiCCDS11729.1.
CCDS1550.1.
PIRiA27501. HSHU33.
RefSeqiNP_002098.1. NM_002107.4.
NP_005315.1. NM_005324.4.
UniGeneiHs.180877.
Hs.533624.
Hs.726012.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L43NMR-A2-13[»]
3ASKX-ray2.90P/Q/R2-14[»]
3ASLX-ray1.41B2-12[»]
3AV2X-ray2.80A/E1-136[»]
3JVKX-ray1.80C13-20[»]
3MUKX-ray1.75D22-29[»]
3MULX-ray1.65D13-20[»]
3QL9X-ray0.93C2-16[»]
3QLAX-ray1.60C/F2-16[»]
3QLCX-ray2.50C/D2-16[»]
3WTPX-ray2.67E1-136[»]
4GNEX-ray1.47B2-8[»]
4GNFX-ray1.55C2-16[»]
4GNGX-ray1.73B/F2-16[»]
4GU0X-ray3.10E/F2-27[»]
4GURX-ray2.51C2-22[»]
4GUSX-ray2.23C2-22[»]
4GY5X-ray2.96E/F2-18[»]
4H9NX-ray1.95A2-136[»]
4H9OX-ray2.05A2-136[»]
4H9PX-ray2.20A2-136[»]
4H9QX-ray1.95A2-136[»]
4H9RX-ray2.20A2-136[»]
4H9SX-ray2.60A/B2-136[»]
4HGAX-ray2.80B1-136[»]
4L58X-ray1.48B2-13[»]
4N4IX-ray2.00B20-43[»]
4O62X-ray1.78D2-12[»]
4QQ4X-ray1.75C/D2-16[»]
4TMPX-ray2.30B/D2-12[»]
4U7TX-ray2.90F/G2-13[»]
4W5AX-ray2.60C/D/F2-16[»]
5AY8X-ray2.80A/E1-134[»]
5B32X-ray2.35A/E1-136[»]
5B33X-ray2.92A/E1-136[»]
5BNVX-ray2.79A/D58-136[»]
5BNXX-ray2.31A58-136[»]
5DWQX-ray2.36F/G14-31[»]
5DX0X-ray2.05F/G/H/I14-31[»]
5JA4X-ray2.42A58-136[»]
5KDMX-ray3.50A2-136[»]
ProteinModelPortaliP84243.
SMRiP84243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109272. 108 interactors.
109273. 17 interactors.
DIPiDIP-40046N.
IntActiP84243. 41 interactors.
MINTiMINT-4825076.
STRINGi9606.ENSP00000355778.

PTM databases

iPTMnetiP84243.
PhosphoSitePlusiP84243.
SwissPalmiP84243.

Polymorphism and mutation databases

BioMutaiH3F3A.
DMDMi55977062.

Proteomic databases

EPDiP84243.
MaxQBiP84243.
PaxDbiP84243.
PeptideAtlasiP84243.
PRIDEiP84243.
TopDownProteomicsiP84243.

Protocols and materials databases

DNASUi3020.
3021.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254810; ENSP00000254810; ENSG00000132475.
ENST00000366813; ENSP00000355778; ENSG00000163041.
ENST00000366815; ENSP00000355780; ENSG00000163041.
ENST00000366816; ENSP00000355781; ENSG00000163041.
ENST00000586607; ENSP00000466020; ENSG00000132475.
ENST00000587560; ENSP00000468714; ENSG00000132475.
ENST00000589599; ENSP00000465813; ENSG00000132475.
GeneIDi3020.
3021.
KEGGihsa:3020.
hsa:3021.
UCSCiuc001hpw.4. human.

Organism-specific databases

CTDi3020.
3021.
DisGeNETi3020.
3021.
GeneCardsiH3F3A.
H3F3B.
H-InvDBHIX0135637.
HGNCiHGNC:4764. H3F3A.
HGNC:4765. H3F3B.
HPAiCAB011481.
CAB037166.
CAB037178.
CAB037187.
CAB037221.
HPA042570.
MIMi601058. gene.
601128. gene.
neXtProtiNX_P84243.
OpenTargetsiENSG00000132475.
ENSG00000163041.
PharmGKBiPA29140.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
HOVERGENiHBG001172.
InParanoidiP84243.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP84243.
TreeFamiTF314241.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000132475-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiP84243.

Miscellaneous databases

ChiTaRSiH3F3B. human.
EvolutionaryTraceiP84243.
GeneWikiiH3F3A.
PROiP84243.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132475.
CleanExiHS_H3F3A.
HS_H3F3B.
ExpressionAtlasiP84243. baseline and differential.
GenevisibleiP84243. HS.

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 nameiH33_HUMAN
AccessioniPrimary (citable) accession number: P84243
Secondary accession number(s): P06351
, P33155, Q5VV55, Q5VV56, Q66I33, Q9V3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.