Skip Header

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

UniProtKB - P84243 (H33_HUMAN)

Protein

Histone H3.3

Gene

H3F3A

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Caution

The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this modification was confirmed in a subsequent publication (PubMed:27735137).2 Publications1 Publication

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1912408 Pre-NOTCH Transcription and Translation
R-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-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componentsi: Chromosome 1, Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000132475.8
HostDB:ENSG00000163041.9
HGNCiHGNC:4764 H3F3A
HGNC:4765 H3F3B
MIMi601058 gene
601128 gene
neXtProtiNX_P84243

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Involvement in diseasei

Glioma (GLM)3 Publications
The gene represented in this entry is involved in disease pathogenesis. H3F3A mutations affecting residues involved in post-translational modifications of histone H3.3 are recurrent in malignant, aggressive gliomas including glioblastoma multiforme (GBM) and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286061, PubMed:22286216). The mechanism through which mutations lead to tumorigenesis involves altered histones methylation, impaired regulation of Polycomb repressive complex 2 (PRC2) activity, and aberrant epigenetic regulation of gene expression (PubMed:23539269, PubMed:23539183, PubMed:23603901).5 Publications
Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
See also OMIM:137800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07902128K → M in GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels. 3 PublicationsCorresponds to variant dbSNP:rs1057519903Ensembl.1
Natural variantiVAR_07902235G → R in GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 2 Publications1
Natural variantiVAR_07902335G → V in GLM; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 3 Publications1
H3F3A and H3F3B mutations affecting residues involved in post-translational modifications of histone H3.3 are implicated in the pathogenesis of some bone and cartilage neoplasms. Mutations have been found with high prevalence in chondroblastoma and giant cell tumors of bone, and with low frequency in osteosarcoma, conventional chondrosarcoma and clear cell chondrosarcoma. Chondroblastoma samples frequently carry a H3F3B mutation affecting residue Lys-37 (H3K36), although H3F3A is mutated in some cases. Most giant cell tumors of bone harbor H3F3A mutations affecting residue Gly-35 (H3G34).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43R → K: Reduced binding of histone H1 to histone H3.3-containing nucleosomes. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3020
3021
MalaCardsiH3F3A
MIMi137800 phenotype
OpenTargetsiENSG00000132475
ENSG00000163041
PharmGKBiPA29140

Polymorphism and mutation databases

BioMutaiH3F3A
DMDMi55977062

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
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 HASPIN2 Publications1
Modified residuei5Allysine; alternate1 Publication1
Modified residuei5N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei5N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei5N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
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-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate5 Publications1
Modified residuei10N6-butyryllysine; alternate1 Publication1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate6 Publications1
Modified residuei11ADP-ribosylserine; alternate1 Publication1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications1
Modified residuei12Phosphothreonine; by PKC2 Publications1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate5 Publications1
Modified residuei15N6-succinyllysine; alternate1 Publication1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate3 Publications1
Modified residuei18Citrulline; alternate3 Publications1
Modified residuei19N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei19N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei19N6-acetyllysine; alternate2 Publications1
Modified residuei19N6-butyryllysine; alternate1 Publication1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate2 Publications1
Modified residuei24N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei24N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternate3 Publications1
Modified residuei24N6-butyryllysine; alternate1 Publication1
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-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei28N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternateCombined sources2 Publications1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate4 Publications1
Modified residuei29ADP-ribosylserine; alternate1 Publication1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei32Phosphoserine2 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
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-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei57N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei57N6-acetyllysine; alternate1 Publication1
Modified residuei57N6-crotonyllysine; alternate1 Publication1
Modified residuei57N6-methyllysine; by EHMT2; alternate2 Publications1
Modified residuei57N6-succinyllysine; alternate1 Publication1
Modified residuei58Phosphoserine1 Publication1
Modified residuei65N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei65N6-methyllysine; alternate2 Publications1
Modified residuei80N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei80N6,N6-dimethyllysine; alternate3 Publications1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei80N6-acetyllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate3 Publications1
Modified residuei80N6-succinyllysine; alternate2 Publications1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineCombined sources1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysine1 Publication1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei123N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei123N6-acetyllysine; alternate2 Publications1
Modified residuei123N6-methyllysine; alternate2 Publications1
Modified residuei123N6-succinyllysine; alternate1 Publication1

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 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 MAP3K20 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.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
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.By similarity
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes (PubMed:29211711). It gives a specific tag for epigenetic transcription activation (PubMed:29211711).1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP84243
MaxQBiP84243
PaxDbiP84243
PeptideAtlasiP84243
PRIDEiP84243
ProteomicsDBi57757
TopDownProteomicsiP84243

PTM databases

iPTMnetiP84243
PhosphoSitePlusiP84243
SwissPalmiP84243

Expressioni

Developmental stagei

Expressed throughout the cell cycle independently of DNA synthesis.

Gene expression databases

BgeeiENSG00000132475 Expressed in 238 organ(s), highest expression level in secondary oocyte
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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109272, 113 interactors
109273, 20 interactors
CORUMiP84243
DIPiDIP-40046N
IntActiP84243, 56 interactors
MINTiP84243
STRINGi9606.ENSP00000355778

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiRIEPEYR
OrthoDBiEOG091G0XGD
PhylomeDBiP84243
TreeFamiTF314241

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR007125 Histone_H2A/H2B/H3
IPR000164 Histone_H3/CENP-A
PANTHERiPTHR11426 PTHR11426, 1 hit
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PRINTSiPR00622 HISTONEH3
SMARTiView protein in SMART
SM00428 H3, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00322 HISTONE_H3_1, 1 hit
PS00959 HISTONE_H3_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EMV3K7EMV3_HUMAN
Histone H3
H3F3B
92Annotation score:
K7EK07K7EK07_HUMAN
Histone H3
H3F3B
132Annotation score:
B4DEB1B4DEB1_HUMAN
Histone H3
H3F3A
123Annotation score:
K7ES00K7ES00_HUMAN
Histone H3.3
H3F3B
151Annotation score:
K7EP01K7EP01_HUMAN
Histone H3.3
H3F3B
113Annotation score:

Experimental Info

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07902128K → M in GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels. 3 PublicationsCorresponds to variant dbSNP:rs1057519903Ensembl.1
Natural variantiVAR_07902235G → R in GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 2 Publications1
Natural variantiVAR_07902335G → V in GLM; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 3 Publications1
Natural variantiVAR_07902435G → W Probable disease-associated mutation found in giant cell tumors of bone; somatic mutation. 1 Publication1
Natural variantiVAR_07902537K → M Probable disease-associated mutation found in chondroblastoma and clear cell chondrosarcoma; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels. 3 Publications1

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 No translation available.
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

Similar proteinsi

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 No translation available.
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[»]
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[»]
5JJYX-ray2.05B30-43[»]
5JLBX-ray1.50B30-43[»]
5KDMX-ray3.50A2-136[»]
5X7XX-ray2.18A/E1-136[»]
6HBONMR-B2-10[»]
ProteinModelPortaliP84243
SMRiP84243
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109272, 113 interactors
109273, 20 interactors
CORUMiP84243
DIPiDIP-40046N
IntActiP84243, 56 interactors
MINTiP84243
STRINGi9606.ENSP00000355778

PTM databases

iPTMnetiP84243
PhosphoSitePlusiP84243
SwissPalmiP84243

Polymorphism and mutation databases

BioMutaiH3F3A
DMDMi55977062

Proteomic databases

EPDiP84243
MaxQBiP84243
PaxDbiP84243
PeptideAtlasiP84243
PRIDEiP84243
ProteomicsDBi57757
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
EuPathDBiHostDB:ENSG00000132475.8
HostDB:ENSG00000163041.9
GeneCardsiH3F3A
H3F3B
H-InvDBiHIX0135637
HGNCiHGNC:4764 H3F3A
HGNC:4765 H3F3B
HPAiCAB011481
CAB037166
CAB037178
CAB037187
CAB037221
HPA042570
MalaCardsiH3F3A
MIMi137800 phenotype
601058 gene
601128 gene
neXtProtiNX_P84243
OpenTargetsiENSG00000132475
ENSG00000163041
PharmGKBiPA29140
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00760000118967
HOVERGENiHBG001172
InParanoidiP84243
KOiK11253
OMAiRIEPEYR
OrthoDBiEOG091G0XGD
PhylomeDBiP84243
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-HSA-1912408 Pre-NOTCH Transcription and Translation
R-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-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
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
PROiPR:P84243
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132475 Expressed in 238 organ(s), highest expression level in secondary oocyte
CleanExiHS_H3F3A
HS_H3F3B
ExpressionAtlasiP84243 baseline and differential
GenevisibleiP84243 HS

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR007125 Histone_H2A/H2B/H3
IPR000164 Histone_H3/CENP-A
PANTHERiPTHR11426 PTHR11426, 1 hit
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PRINTSiPR00622 HISTONEH3
SMARTiView protein in SMART
SM00428 H3, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00322 HISTONE_H3_1, 1 hit
PS00959 HISTONE_H3_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH33_HUMAN
AccessioniPrimary (citable) accession number: P84243
Secondary accession number(s): P06351
, P33155, Q5VV55, Q5VV56, Q66I33, Q9V3W4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 160 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again