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Protein

Histone H3.1

Gene

HIST1H3A

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

Miscellaneous

This histone is only present in mammals and is enriched in acetylation of Lys-15 and dimethylation of Lys-10 (H3K9me2).

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The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148).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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1266695 Interleukin-7 signaling
R-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-3214815 HDACs deacetylate histones
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-3214842 HDMs demethylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-3247509 Chromatin modifying enzymes
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
SIGNORiP68431

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.1
Alternative name(s):
Histone H3/a
Histone H3/b
Histone H3/c
Histone H3/d
Histone H3/f
Histone H3/h
Histone H3/i
Histone H3/j
Histone H3/k
Histone H3/l
Gene namesi
Name:HIST1H3A
Synonyms:H3FA
AND
Name:HIST1H3B
Synonyms:H3FL
AND
Name:HIST1H3C
Synonyms:H3FC
AND
Name:HIST1H3D
Synonyms:H3FB
AND
Name:HIST1H3E
Synonyms:H3FD
AND
Name:HIST1H3F
Synonyms:H3FI
AND
Name:HIST1H3G
Synonyms:H3FH
AND
Name:HIST1H3H
Synonyms:H3FK
AND
Name:HIST1H3I
Synonyms:H3FF
AND
Name:HIST1H3J
Synonyms:H3FJ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000197153.4
HostDB:ENSG00000197409.7
HostDB:ENSG00000273983.1
HostDB:ENSG00000274267.1
HostDB:ENSG00000274750.2
HostDB:ENSG00000275379.1
HostDB:ENSG00000275714.1
HostDB:ENSG00000277775.1
HostDB:ENSG00000278272.1
HostDB:ENSG00000278828.1
HGNCiHGNC:4766 HIST1H3A
HGNC:4776 HIST1H3B
HGNC:4768 HIST1H3C
HGNC:4767 HIST1H3D
HGNC:4769 HIST1H3E
HGNC:4773 HIST1H3F
HGNC:4772 HIST1H3G
HGNC:4775 HIST1H3H
HGNC:4771 HIST1H3I
HGNC:4774 HIST1H3J
MIMi602810 gene
602811 gene
602812 gene
602813 gene
602814 gene
602815 gene
602816 gene
602817 gene
602818 gene
602819 gene
neXtProtiNX_P68431

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)1 Publication
The gene represented in this entry is involved in disease pathogenesis. HIST1H3B mutations affecting residue Lys-28 involved in post-translational modifications of histone H3.1 are recurrent in malignant, aggressive gliomas including pediatric non-brain stem glioblastoma and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286216). The mechanism through which mutations lead to tumorigenesis involves altered histone methylation, impaired regulation of Polycomb repressive complex 2 (PRC2) activity, and aberrant epigenetic regulation of gene expression (PubMed:23603901).2 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_07901828K → M in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels. 2 PublicationsCorresponds to variant dbSNP:rs1057519904Ensembl.1
HIST1H3B or HIST1H3C mutations affecting residue Lys-37 of histone H3.1 are involved in the pathogenesis of pediatric undifferentiated soft tissue sarcomas. The mechanism through which mutations lead to tumorigenesis involves altered histones methylation with gain of global H3K27 methylation, altered Polycomb repressive complex 1 (PRC1) activity, aberrant epigenetic regulation of gene expression and impaired differentiation of mesenchimal progenitor cells.1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
MalaCardsiHIST1H3A
MIMi137800 phenotype
OpenTargetsiENSG00000197153
ENSG00000197409
ENSG00000273983
ENSG00000274267
ENSG00000274750
ENSG00000275379
ENSG00000275714
ENSG00000277775
ENSG00000278272
ENSG00000278828
PharmGKBiPA29148

Polymorphism and mutation databases

BioMutaiHIST1H3A
DMDMi55977055

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002212452 – 136Histone H3.1Add 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; alternate3 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate3 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; alternate3 Publications1
Modified residuei7Phosphothreonine; by PKC1 Publication1
Modified residuei9Citrulline; alternate2 Publications1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei10N6,N6,N6-trimethyllysine; alternate5 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate5 Publications1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate6 Publications1
Modified residuei10N6-butyryllysine; alternate1 Publication1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate5 Publications1
Modified residuei11ADP-ribosylserine; alternate1 Publication1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications1
Modified residuei12Phosphothreonine; by PKC and CHEK13 Publications1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate6 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; alternate3 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; alternate4 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; alternate4 Publications1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei28N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternate2 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 residuei37N6,N6,N6-trimethyllysine; alternate5 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate5 Publications1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate2 Publications1
Modified residuei37N6-methyllysine; alternate5 Publications1
Modified residuei38N6-methyllysine1 Publication1
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; alternate4 Publications1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei80N6-acetyllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate4 Publications1
Modified residuei80N6-succinyllysine; alternate2 Publications1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineBy similarity1
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.9 Publications
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.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 Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.17 Publications
Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (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.By similarity1 Publication
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression.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

EPDiP68431
MaxQBiP68431
PaxDbiP68431
PeptideAtlasiP68431
PRIDEiP68431
ProteomicsDBi57541
TopDownProteomicsiP68431

PTM databases

iPTMnetiP68431
PhosphoSitePlusiP68431
SwissPalmiP68431

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiENSG00000197153 Expressed in 43 organ(s), highest expression level in stomach
CleanExiHS_HIST1H3A
HS_HIST1H3B
HS_HIST1H3C
HS_HIST1H3D
HS_HIST1H3E
HS_HIST1H3F
HS_HIST1H3G
HS_HIST1H3H
HS_HIST1H3I
GenevisibleiP68431 HS

Organism-specific databases

HPAiCAB070190
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.2 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113946, 310 interactors
113947, 6 interactors
113948, 12 interactors
113949, 201 interactors
113950, 6 interactors
113951, 7 interactors
113952, 5 interactors
113953, 9 interactors
113954, 24 interactors
114458, 9 interactors
CORUMiP68431
DIPiDIP-29371N
ELMiP68431
IntActiP68431, 430 interactors
MINTiP68431
STRINGi9606.ENSP00000444823

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP68431
SMRiP68431
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68431

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00760000118967
HOVERGENiHBG001172
InParanoidiP68431
KOiK11253
OMAiASEAYYL
OrthoDBiEOG09370ZG5
PhylomeDBiP68431
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

Sequencei

Sequence statusi: Complete.

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

P68431-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,404
Last modified:January 23, 2007 - v2
Checksum:i9B89008EA50A0EF6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70R → C in AAH67493 (PubMed:15489334).Curated1
Sequence conflicti100Y → T in CAB02546 (PubMed:9119399).Curated1
Sequence conflicti122P → L in AAH66884 (PubMed:15489334).Curated1
Sequence conflicti135Missing in AAA52651 (PubMed:3013246).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07901828K → M in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels. 2 PublicationsCorresponds to variant dbSNP:rs1057519904Ensembl.1
Natural variantiVAR_07901937K → I Probable disease-associated mutation found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels. 1 Publication1
Natural variantiVAR_07902037K → M Probable disease-associated mutation found in pediatric undifferentiated soft tissue sarcoma samples; 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. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00090 Genomic DNA Translation: CAA24952.1
M26150 Genomic DNA Translation: AAA52651.1
M60746 Genomic DNA Translation: AAA63185.1
X57128 Genomic DNA Translation: CAA40407.1
Z46261 Genomic DNA Translation: CAA86403.1
X83550 Genomic DNA Translation: CAA58540.1
Z80784 Genomic DNA Translation: CAB02546.1
Z80785 Genomic DNA Translation: CAB02547.1
Z80786 Genomic DNA Translation: CAB02548.1
Z83735 Genomic DNA Translation: CAB06030.1
Z83737 Genomic DNA Translation: CAB06032.1
AF531274 Genomic DNA Translation: AAN10051.1
AF531275 Genomic DNA Translation: AAN10052.1
AF531276 Genomic DNA Translation: AAN10053.1
AF531277 Genomic DNA Translation: AAN10054.1
AF531278 Genomic DNA Translation: AAN10055.1
AF531279 Genomic DNA Translation: AAN10056.1
AF531280 Genomic DNA Translation: AAN10057.1
AF531281 Genomic DNA Translation: AAN10058.1
AF531282 Genomic DNA Translation: AAN10059.1
AF531283 Genomic DNA Translation: AAN10060.1
AK311991 mRNA Translation: BAG34929.1
AK313905 mRNA Translation: BAG36628.1
AK314142 mRNA Translation: BAG36832.1
AK316611 mRNA Translation: BAG38198.1
CR542014 mRNA Translation: CAG46811.1
CR542011 mRNA Translation: CAG46808.1
CR541983 mRNA Translation: CAG46780.1
CR541858 mRNA Translation: CAG46656.1
Z98744 Genomic DNA No translation available.
AL009179 Genomic DNA No translation available.
AL031777 Genomic DNA No translation available.
BC031333 mRNA Translation: AAH31333.1
BC066245 mRNA Translation: AAH66245.1
BC066246 mRNA Translation: AAH66246.1
BC066247 mRNA Translation: AAH66247.1
BC066884 mRNA Translation: AAH66884.1
BC067490 mRNA Translation: AAH67490.1
BC067491 mRNA Translation: AAH67491.1
BC067492 mRNA Translation: AAH67492.1
BC067493 mRNA Translation: AAH67493.1
BC069133 mRNA Translation: AAH69133.1
BC069303 mRNA Translation: AAH69303.1
BC069305 mRNA Translation: AAH69305.2
BC069818 mRNA Translation: AAH69818.1
BC096128 mRNA Translation: AAH96128.1
BC096129 mRNA Translation: AAH96129.1
BC096130 mRNA Translation: AAH96130.1
BC096131 mRNA Translation: AAH96131.1
BC096132 mRNA Translation: AAH96132.1
BC096133 mRNA Translation: AAH96133.1
BC096134 mRNA Translation: AAH96134.1
BC099630 mRNA Translation: AAH99630.1
BC127610 mRNA Translation: AAI27611.1
BC143046 mRNA Translation: AAI43047.1
BC148243 mRNA Translation: AAI48244.1
BC148250 mRNA Translation: AAI48251.1
CCDSiCCDS4570.1
CCDS4573.1
CCDS4576.1
CCDS4590.1
CCDS4596.1
CCDS4600.1
CCDS4602.1
CCDS4627.1
CCDS4636.1
CCDS4638.1
PIRiI37446 HSHU3
RefSeqiNP_003520.1, NM_003529.2
NP_003521.2, NM_003530.4
NP_003522.1, NM_003531.2
NP_003523.1, NM_003532.2
NP_003524.1, NM_003533.2
NP_003525.1, NM_003534.2
NP_003526.1, NM_003535.2
NP_003527.1, NM_003536.2
NP_003528.1, NM_003537.3
NP_066298.1, NM_021018.2
UniGeneiHs.132854
Hs.247813
Hs.247814
Hs.248176
Hs.443021
Hs.484990
Hs.532144
Hs.533292
Hs.546315
Hs.586261
Hs.591778
Hs.626666

Genome annotation databases

EnsembliENST00000356476; ENSP00000366999; ENSG00000197409
ENST00000359303; ENSP00000352252; ENSG00000197153
ENST00000369163; ENSP00000358160; ENSG00000278828
ENST00000612966; ENSP00000484658; ENSG00000278272
ENST00000613854; ENSP00000480826; ENSG00000275714
ENST00000614378; ENSP00000484638; ENSG00000273983
ENST00000614911; ENSP00000482271; ENSG00000274750
ENST00000616365; ENSP00000483283; ENSG00000275379
ENST00000618052; ENSP00000484095; ENSG00000277775
ENST00000621411; ENSP00000484841; ENSG00000274267
ENST00000634733; ENSP00000489282; ENSG00000274750
GeneIDi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
KEGGihsa:8350
hsa:8351
hsa:8352
hsa:8353
hsa:8354
hsa:8355
hsa:8356
hsa:8357
hsa:8358
hsa:8968
UCSCiuc003nfp.2 human

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00090 Genomic DNA Translation: CAA24952.1
M26150 Genomic DNA Translation: AAA52651.1
M60746 Genomic DNA Translation: AAA63185.1
X57128 Genomic DNA Translation: CAA40407.1
Z46261 Genomic DNA Translation: CAA86403.1
X83550 Genomic DNA Translation: CAA58540.1
Z80784 Genomic DNA Translation: CAB02546.1
Z80785 Genomic DNA Translation: CAB02547.1
Z80786 Genomic DNA Translation: CAB02548.1
Z83735 Genomic DNA Translation: CAB06030.1
Z83737 Genomic DNA Translation: CAB06032.1
AF531274 Genomic DNA Translation: AAN10051.1
AF531275 Genomic DNA Translation: AAN10052.1
AF531276 Genomic DNA Translation: AAN10053.1
AF531277 Genomic DNA Translation: AAN10054.1
AF531278 Genomic DNA Translation: AAN10055.1
AF531279 Genomic DNA Translation: AAN10056.1
AF531280 Genomic DNA Translation: AAN10057.1
AF531281 Genomic DNA Translation: AAN10058.1
AF531282 Genomic DNA Translation: AAN10059.1
AF531283 Genomic DNA Translation: AAN10060.1
AK311991 mRNA Translation: BAG34929.1
AK313905 mRNA Translation: BAG36628.1
AK314142 mRNA Translation: BAG36832.1
AK316611 mRNA Translation: BAG38198.1
CR542014 mRNA Translation: CAG46811.1
CR542011 mRNA Translation: CAG46808.1
CR541983 mRNA Translation: CAG46780.1
CR541858 mRNA Translation: CAG46656.1
Z98744 Genomic DNA No translation available.
AL009179 Genomic DNA No translation available.
AL031777 Genomic DNA No translation available.
BC031333 mRNA Translation: AAH31333.1
BC066245 mRNA Translation: AAH66245.1
BC066246 mRNA Translation: AAH66246.1
BC066247 mRNA Translation: AAH66247.1
BC066884 mRNA Translation: AAH66884.1
BC067490 mRNA Translation: AAH67490.1
BC067491 mRNA Translation: AAH67491.1
BC067492 mRNA Translation: AAH67492.1
BC067493 mRNA Translation: AAH67493.1
BC069133 mRNA Translation: AAH69133.1
BC069303 mRNA Translation: AAH69303.1
BC069305 mRNA Translation: AAH69305.2
BC069818 mRNA Translation: AAH69818.1
BC096128 mRNA Translation: AAH96128.1
BC096129 mRNA Translation: AAH96129.1
BC096130 mRNA Translation: AAH96130.1
BC096131 mRNA Translation: AAH96131.1
BC096132 mRNA Translation: AAH96132.1
BC096133 mRNA Translation: AAH96133.1
BC096134 mRNA Translation: AAH96134.1
BC099630 mRNA Translation: AAH99630.1
BC127610 mRNA Translation: AAI27611.1
BC143046 mRNA Translation: AAI43047.1
BC148243 mRNA Translation: AAI48244.1
BC148250 mRNA Translation: AAI48251.1
CCDSiCCDS4570.1
CCDS4573.1
CCDS4576.1
CCDS4590.1
CCDS4596.1
CCDS4600.1
CCDS4602.1
CCDS4627.1
CCDS4636.1
CCDS4638.1
PIRiI37446 HSHU3
RefSeqiNP_003520.1, NM_003529.2
NP_003521.2, NM_003530.4
NP_003522.1, NM_003531.2
NP_003523.1, NM_003532.2
NP_003524.1, NM_003533.2
NP_003525.1, NM_003534.2
NP_003526.1, NM_003535.2
NP_003527.1, NM_003536.2
NP_003528.1, NM_003537.3
NP_066298.1, NM_021018.2
UniGeneiHs.132854
Hs.247813
Hs.247814
Hs.248176
Hs.443021
Hs.484990
Hs.532144
Hs.533292
Hs.546315
Hs.586261
Hs.591778
Hs.626666

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CS9NMR-A131-136[»]
1CT6NMR-A131-136[»]
1O9SX-ray1.75K/L2-10[»]
1Q3LX-ray1.64P2-16[»]
2B2TX-ray2.45D2-20[»]
2B2UX-ray2.95D2-16[»]
2B2VX-ray2.65D2-16[»]
2B2WX-ray2.40D2-20[»]
2C1JX-ray2.60C/D8-15[»]
2C1NX-ray2.00C/E8-15[»]
2CO0X-ray2.25B/D2-16[»]
2CV5X-ray2.50A/E1-136[»]
2KWJNMR-B2-21[»]
2KWKNMR-B2-21[»]
2L75NMR-B2-14[»]
2LBMNMR-C2-16[»]
2M0ONMR-B32-42[»]
2NDFNMR-B13-25[»]
2NDGNMR-B13-25[»]
2OQ6X-ray2.00C/D8-15[»]
2OT7X-ray2.14C/D8-15[»]
2OX0X-ray1.95C/D8-15[»]
2RI7X-ray1.45P2-10[»]
2UXNX-ray2.72E2-22[»]
2V85X-ray2.00D/E2-13[»]
2V89X-ray1.10D/E2-10[»]
2VNFX-ray1.76B/D2-11[»]
2VPGX-ray1.60P/R2-19[»]
2X0LX-ray3.00C6-17[»]
3A1BX-ray2.29A2-21[»]
3AFAX-ray2.50A/E1-136[»]
3AVRX-ray1.80B18-39[»]
3AYWX-ray2.90A/E1-136[»]
3AZEX-ray3.00A/E1-136[»]
3AZFX-ray2.70A/E1-136[»]
3AZGX-ray2.40A/E1-136[»]
3AZHX-ray3.49A/E1-136[»]
3AZIX-ray2.70A/E1-136[»]
3AZJX-ray2.89A/E1-136[»]
3AZKX-ray3.20A/E1-136[»]
3AZLX-ray2.70A/E1-136[»]
3AZMX-ray2.89A/E1-136[»]
3AZNX-ray3.00A/E1-136[»]
3B95X-ray2.99P2-16[»]
3KMTX-ray1.78G/H/I26-33[»]
3KQIX-ray1.78B2-13[»]
3LQIX-ray1.92R/S/T2-10[»]
3LQJX-ray1.90Q/T2-10[»]
3MP1X-ray2.60P2-6[»]
3O34X-ray1.90B14-33[»]
3O35X-ray1.76D/E24-32[»]
3O37X-ray2.00E/F/G/H2-11[»]
3QJ6X-ray2.30T74-84[»]
3RIGX-ray2.00C/D5-16[»]
3RIYX-ray1.55C/D5-16[»]
3SOUX-ray1.80D/E2-10[»]
3SOWX-ray1.95C/D2-10[»]
3U31X-ray2.20B5-14[»]
3U3DX-ray2.40B5-14[»]
3U4SX-ray2.15C/D8-15[»]
3U5NX-ray1.95C/D2-21[»]
3U5OX-ray2.70I/J/K/L/M/N/O/P2-23[»]
3U5PX-ray2.80I/J/K/L/M/N/O/P2-29[»]
3UEEX-ray2.61B/D2-13[»]
3UEFX-ray2.45B/D2-13[»]
3UIGX-ray2.40P/Q2-16[»]
3UIIX-ray2.60P/Q2-11[»]
3UIKX-ray2.70P/Q2-11[»]
3V43X-ray1.47Q2-19[»]
3W96X-ray3.00A/E1-136[»]
3W97X-ray3.20A/E1-136[»]
3W98X-ray3.42A/E29-136[»]
3W99X-ray3.00A/E1-136[»]
3WA9X-ray3.07A/E1-136[»]
3WAAX-ray3.20A/E1-136[»]
3WKJX-ray2.80A/E1-136[»]
3X1SX-ray2.81A/E2-136[»]
3X1TX-ray2.81A/E2-136[»]
3X1UX-ray3.25A/E2-136[»]
3X1VX-ray2.92A/E2-136[»]
3ZG6X-ray2.20F5-14[»]
3ZVYX-ray1.95C/D2-9[»]
4A0JX-ray2.80C/D2-7[»]
4A0NX-ray2.74C2-7[»]
4A7JX-ray1.90B1-16[»]
4BD3NMR-B32-42[»]
4C1QX-ray2.30C2-10[»]
4F4UX-ray2.00C/D5-16[»]
4F56X-ray1.70C/D5-16[»]
4FWFX-ray2.70E2-21[»]
4HONX-ray1.80F/G7-16[»]
4I51X-ray1.90C/D4-12[»]
4L7XX-ray1.35U2-13[»]
4LK9X-ray1.60B2-22[»]
4LKAX-ray1.61B2-22[»]
4LLBX-ray2.50C/D2-22[»]
4LXLX-ray1.87D8-15[»]
4N4HX-ray2.30B22-43[»]
4QBQX-ray2.41P2-9[»]
4QBRX-ray1.90E/P2-8[»]
4QBSX-ray1.80P2-8[»]
4TN7X-ray2.20E/F30-44[»]
4U68X-ray1.80D/E/F5-15[»]
4UP0X-ray1.28F2-16[»]
4UY4X-ray1.86C/D2-7[»]
4X3KX-ray1.45C/D24-30[»]
4Y6LX-ray1.60C/D7-13[»]
4YHPX-ray2.53P/Q2-17[»]
4YHZX-ray2.30P2-13[»]
4YM5X-ray4.00A/E1-136[»]
4YM6X-ray3.51A/E1-136[»]
4Z0RX-ray1.75D2-16[»]
4Z2MX-ray2.98G/I35-136[»]
5AV5X-ray2.40A/E1-136[»]
5AV6X-ray2.20A/E1-136[»]
5AV8X-ray2.20A/E1-136[»]
5AV9X-ray2.20A/E1-136[»]
5AVBX-ray2.40A/E1-136[»]
5AVCX-ray2.40A/E1-136[»]
5B24X-ray3.60A/E1-136[»]
5B2IX-ray3.00A/E1-136[»]
5B2JX-ray2.60A/E1-136[»]
5B31X-ray2.20A/E1-136[»]
5C11X-ray2.80B2-11[»]
5C13X-ray2.10D/F/H/P2-11[»]
5C3IX-ray3.50B/F/J/N/R/V1-136[»]
5CPIX-ray2.90A/E1-136[»]
5CPJX-ray3.15A/E1-136[»]
5CPKX-ray2.63A/E1-136[»]
5D6YX-ray2.29a/b/c/d20-29[»]
5DAHX-ray2.61C/D20-30[»]
5FB0X-ray2.70D/F2-16[»]
5FB1X-ray2.10C2-16[»]
5FFVX-ray1.30C/D10-20[»]
5GH9X-ray1.45B45-58[»]
5GSEX-ray3.14A/E/K/O1-136[»]
5GSUX-ray3.10A/E2-136[»]
5GT0X-ray2.82A/E2-136[»]
5GT3X-ray2.91A/E2-136[»]
5GTCX-ray2.70A/E1-136[»]
5H6QX-ray2.53C2-21[»]
5H6RX-ray2.60C2-21[»]
5HJBX-ray2.70B4-9[»]
5HJCX-ray2.60B16-24[»]
5HJDX-ray2.81B/D/F/H/I/J/L/M15-21[»]
5HYNX-ray2.95D/I/O/T22-34[»]
5IQLX-ray2.10B25-32[»]
5J3VX-ray3.05C/D12-28[»]
5J9SX-ray2.70B16-40[»]
5JHNX-ray1.67F/G4-14[»]
5JINX-ray1.85F/G4-14[»]
5JIYX-ray1.48F/G4-14[»]
5JJ0X-ray1.72F/G4-14[»]
5JRGX-ray2.50A/E1-136[»]
5KJHX-ray2.27D23-33[»]
E19-38[»]
5KJIX-ray2.71E19-38[»]
5KKLX-ray2.94B23-27[»]
5LUGX-ray1.70E/F/G/H2-11[»]
5M5GX-ray2.27D23-33[»]
5MR8X-ray1.74C2-10[»]
5OY3X-ray2.14B18-34[»]
5SVXX-ray1.56B2-12[»]
5SVYX-ray1.05B2-12[»]
5SZBX-ray1.20H2-19[»]
5SZCX-ray1.19H2-19[»]
5T0KX-ray1.70P/Q2-16[»]
5T0MX-ray1.90C/P2-16[»]
5T1GX-ray1.90B39-53[»]
5T1IX-ray1.60C39-53[»]
5T8RX-ray2.40E/G2-11[»]
5TBNNMR-C2-12[»]
5TDRX-ray1.42B2-12[»]
5TDWX-ray1.70B2-12[»]
5U2JX-ray1.60C/D2-17[»]
5V21X-ray2.42B30-44[»]
5V22X-ray2.40B30-44[»]
5VA6X-ray2.40C/D20-37[»]
5VABX-ray1.70F2-11[»]
5VGEX-ray2.60C41-49[»]
5WFCX-ray2.28D23-33[»]
5WLEX-ray1.95C2-13[»]
5WVOX-ray2.00D2-37[»]
5WXGX-ray1.70P2-8[»]
5WXHX-ray1.30D/P2-8[»]
5WYIX-ray2.00E120-127[»]
5X60X-ray2.69C2-21[»]
5XF3X-ray2.60A/E1-136[»]
5XF4X-ray2.87A/E1-136[»]
5XF5X-ray2.82A/E1-136[»]
5XFQX-ray2.40E/F30-42[»]
5XFRX-ray2.25C/D34-41[»]
5XNVX-ray2.70B25-32[»]
5Y0CX-ray2.09A/E1-136[»]
5Y0DX-ray1.99A/E1-136[»]
5Y20X-ray2.41P2-8[»]
5Z30X-ray2.45A/E1-136[»]
6AXJX-ray2.38E/F/G/H22-32[»]
6BHDX-ray1.25B4-20[»]
6BHEX-ray1.35B4-20[»]
6BHGX-ray1.45B4-20[»]
6BHHX-ray1.85B4-20[»]
6BHIX-ray1.40B5-20[»]
6ETXelectron microscopy4.80I/M1-136[»]
ProteinModelPortaliP68431
SMRiP68431
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113946, 310 interactors
113947, 6 interactors
113948, 12 interactors
113949, 201 interactors
113950, 6 interactors
113951, 7 interactors
113952, 5 interactors
113953, 9 interactors
113954, 24 interactors
114458, 9 interactors
CORUMiP68431
DIPiDIP-29371N
ELMiP68431
IntActiP68431, 430 interactors
MINTiP68431
STRINGi9606.ENSP00000444823

PTM databases

iPTMnetiP68431
PhosphoSitePlusiP68431
SwissPalmiP68431

Polymorphism and mutation databases

BioMutaiHIST1H3A
DMDMi55977055

Proteomic databases

EPDiP68431
MaxQBiP68431
PaxDbiP68431
PeptideAtlasiP68431
PRIDEiP68431
ProteomicsDBi57541
TopDownProteomicsiP68431

Protocols and materials databases

DNASUi8350
8352
8353
8355
8356
8357
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356476; ENSP00000366999; ENSG00000197409
ENST00000359303; ENSP00000352252; ENSG00000197153
ENST00000369163; ENSP00000358160; ENSG00000278828
ENST00000612966; ENSP00000484658; ENSG00000278272
ENST00000613854; ENSP00000480826; ENSG00000275714
ENST00000614378; ENSP00000484638; ENSG00000273983
ENST00000614911; ENSP00000482271; ENSG00000274750
ENST00000616365; ENSP00000483283; ENSG00000275379
ENST00000618052; ENSP00000484095; ENSG00000277775
ENST00000621411; ENSP00000484841; ENSG00000274267
ENST00000634733; ENSP00000489282; ENSG00000274750
GeneIDi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
KEGGihsa:8350
hsa:8351
hsa:8352
hsa:8353
hsa:8354
hsa:8355
hsa:8356
hsa:8357
hsa:8358
hsa:8968
UCSCiuc003nfp.2 human

Organism-specific databases

CTDi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
DisGeNETi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
EuPathDBiHostDB:ENSG00000197153.4
HostDB:ENSG00000197409.7
HostDB:ENSG00000273983.1
HostDB:ENSG00000274267.1
HostDB:ENSG00000274750.2
HostDB:ENSG00000275379.1
HostDB:ENSG00000275714.1
HostDB:ENSG00000277775.1
HostDB:ENSG00000278272.1
HostDB:ENSG00000278828.1
GeneCardsiHIST1H3A
HIST1H3B
HIST1H3C
HIST1H3D
HIST1H3E
HIST1H3F
HIST1H3G
HIST1H3H
HIST1H3I
HIST1H3J
HGNCiHGNC:4766 HIST1H3A
HGNC:4776 HIST1H3B
HGNC:4768 HIST1H3C
HGNC:4767 HIST1H3D
HGNC:4769 HIST1H3E
HGNC:4773 HIST1H3F
HGNC:4772 HIST1H3G
HGNC:4775 HIST1H3H
HGNC:4771 HIST1H3I
HGNC:4774 HIST1H3J
HPAiCAB070190
HPA042570
MalaCardsiHIST1H3A
MIMi137800 phenotype
602810 gene
602811 gene
602812 gene
602813 gene
602814 gene
602815 gene
602816 gene
602817 gene
602818 gene
602819 gene
neXtProtiNX_P68431
OpenTargetsiENSG00000197153
ENSG00000197409
ENSG00000273983
ENSG00000274267
ENSG00000274750
ENSG00000275379
ENSG00000275714
ENSG00000277775
ENSG00000278272
ENSG00000278828
PharmGKBiPA29148
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00760000118967
HOVERGENiHBG001172
InParanoidiP68431
KOiK11253
OMAiASEAYYL
OrthoDBiEOG09370ZG5
PhylomeDBiP68431
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-HSA-1266695 Interleukin-7 signaling
R-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-3214815 HDACs deacetylate histones
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-3214842 HDMs demethylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-3247509 Chromatin modifying enzymes
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
SIGNORiP68431

Miscellaneous databases

ChiTaRSiHIST1H3B human
HIST1H3F human
EvolutionaryTraceiP68431
GeneWikiiHIST1H3A
HIST1H3B
HIST1H3C
HIST1H3D
HIST1H3E
HIST1H3F
HIST1H3G
HIST1H3H
HIST1H3I
HIST1H3J
PROiPR:P68431
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197153 Expressed in 43 organ(s), highest expression level in stomach
CleanExiHS_HIST1H3A
HS_HIST1H3B
HS_HIST1H3C
HS_HIST1H3D
HS_HIST1H3E
HS_HIST1H3F
HS_HIST1H3G
HS_HIST1H3H
HS_HIST1H3I
GenevisibleiP68431 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 nameiH31_HUMAN
AccessioniPrimary (citable) accession number: P68431
Secondary accession number(s): A0PJT7
, A5PLR1, P02295, P02296, P16106, Q6ISV8, Q6NWP8, Q6NWP9, Q6NXU4, Q71DJ3, Q93081
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 166 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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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