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Protein

Histone H3.1

Gene

HIST1H3A

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • histone binding Source: UniProtKB
  • nucleosomal DNA binding Source: GO_Central

GO - Biological processi

  • blood coagulation Source: Reactome
  • cellular protein metabolic process Source: Reactome
  • chromatin silencing at rDNA Source: Reactome
  • DNA replication-dependent 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 gene expression, epigenetic Source: Reactome
  • protein heterotetramerization Source: UniProtKB
  • regulation of gene silencing Source: BHF-UCL
  • telomere organization Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112727-MONOMER.
ZFISH:ENSG00000124642-MONOMER.
ZFISH:ENSG00000124687-MONOMER.
ZFISH:ENSG00000124693-MONOMER.
ZFISH:ENSG00000158597-MONOMER.
ZFISH:ENSG00000178458-MONOMER.
ReactomeiR-HSA-1266695. Interleukin-7 signaling.
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-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

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.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • membrane Source: UniProtKB
  • 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

DisGeNETi8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.
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 GSG22 Publications1
Modified residuei5Allysine; alternate1
Modified residuei5N6,N6,N6-trimethyllysine; alternate3 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate3 Publications1
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-acetyllysine; alternate6 Publications1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate5 Publications1
Modified residuei11Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications1
Modified residuei12Phosphothreonine; by PKC and CHEK13 Publications1
Modified residuei15N6-acetyllysine6 Publications1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate3 Publications1
Modified residuei18Citrulline; alternate3 Publications1
Modified residuei19N6-acetyllysine; alternate3 Publications1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate2 Publications1
Modified residuei24N6-acetyllysine; alternate4 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; alternate4 Publications1
Modified residuei28N6-acetyllysine; alternate2 Publications1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate4 Publications1
Modified residuei29Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternate5 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate5 Publications1
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-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; alternate4 Publications1
Modified residuei80N6-acetyllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate4 Publications1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineBy similarity1
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.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 GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.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 (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

EPDiP68431.
MaxQBiP68431.
PaxDbiP68431.
PeptideAtlasiP68431.
PRIDEiP68431.
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

BgeeiENSG00000124693.
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

WithEntry#Exp.IntActNotes
AIREO4391820EBI-79722,EBI-1753081
CBX1P839169EBI-79722,EBI-78129
CBX3Q131855EBI-79722,EBI-78176
CBX5P459739EBI-79722,EBI-78219
CDYLQ9Y2325EBI-79722,EBI-1387386
FBLIM1Q8WUP27EBI-79722,EBI-3864120
HIST2H4BP628053EBI-79722,EBI-302023
HTTP428582EBI-79722,EBI-466029
ING4Q9UNL43EBI-79722,EBI-2866661
IPL1P389912EBI-79722,EBI-9319From a different organism.
KDM4AO751647EBI-79722,EBI-936709
KMT2AQ0316411EBI-79722,EBI-591370
L3MBTL1Q9Y4682EBI-79722,EBI-1265089
MPHOSPH8Q995495EBI-79722,EBI-2653928
NASPP49321-28EBI-79722,EBI-7038920
PHF20Q9BVI06EBI-79722,EBI-2560802
PHF20L1A8MW922EBI-79722,EBI-2560834
PKMP14618-13EBI-79722,EBI-4304679
SETD7Q8WTS64EBI-79722,EBI-1268586
SGF29P2555411EBI-79722,EBI-21678From a different organism.
SGF29Q96ES725EBI-79722,EBI-743117
TP53BP1Q128885EBI-79722,EBI-396540
WDR5P6196411EBI-79722,EBI-540834
YWHAZP631043EBI-79722,EBI-347088

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113946. 282 interactors.
113947. 5 interactors.
113948. 10 interactors.
113949. 200 interactors.
113950. 5 interactors.
113951. 6 interactors.
113952. 4 interactors.
113953. 8 interactors.
113954. 23 interactors.
114458. 7 interactors.
DIPiDIP-29371N.
IntActiP68431. 73 interactors.
MINTiMINT-256465.
STRINGi9606.ENSP00000444823.

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 7Combined sources3
Helixi13 – 15Combined sources3
Beta strandi25 – 27Combined sources3
Beta strandi45 – 49Combined sources5
Helixi50 – 58Combined sources9
Helixi65 – 77Combined sources13
Beta strandi80 – 82Combined sources3
Helixi87 – 114Combined sources28
Beta strandi118 – 120Combined sources3
Helixi122 – 132Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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[»]
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[»]
2VPGX-ray1.60P/R2-19[»]
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[»]
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[»]
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[»]
5CH1X-ray2.27D23-33[»]
E19-38[»]
5CH2X-ray2.71E19-38[»]
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[»]
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[»]
5JHNX-ray1.67F/G4-14[»]
5JINX-ray1.85F/G4-14[»]
5JIYX-ray1.48F/G4-14[»]
5JJ0X-ray1.72F/G4-14[»]
5T1GX-ray1.90B39-53[»]
5T1IX-ray1.60C39-53[»]
5TBNNMR-C2-12[»]
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.
OMAiRTKQMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP68431.
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.

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

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. Translation: CAD24076.1.
Z98744 Genomic DNA. Translation: CAB11424.1.
AL009179 Genomic DNA. Translation: CAA15670.1.
AL031777 Genomic DNA. Translation: CAC03412.1.
AL031777 Genomic DNA. Translation: CAC03413.1.
AL031777 Genomic DNA. Translation: CAC03416.1.
AL031777 Genomic DNA. Translation: CAC03421.1.
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.

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. Translation: CAD24076.1.
Z98744 Genomic DNA. Translation: CAB11424.1.
AL009179 Genomic DNA. Translation: CAA15670.1.
AL031777 Genomic DNA. Translation: CAC03412.1.
AL031777 Genomic DNA. Translation: CAC03413.1.
AL031777 Genomic DNA. Translation: CAC03416.1.
AL031777 Genomic DNA. Translation: CAC03421.1.
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[»]
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[»]
2VPGX-ray1.60P/R2-19[»]
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[»]
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[»]
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[»]
5CH1X-ray2.27D23-33[»]
E19-38[»]
5CH2X-ray2.71E19-38[»]
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[»]
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[»]
5JHNX-ray1.67F/G4-14[»]
5JINX-ray1.85F/G4-14[»]
5JIYX-ray1.48F/G4-14[»]
5JJ0X-ray1.72F/G4-14[»]
5T1GX-ray1.90B39-53[»]
5T1IX-ray1.60C39-53[»]
5TBNNMR-C2-12[»]
ProteinModelPortaliP68431.
SMRiP68431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113946. 282 interactors.
113947. 5 interactors.
113948. 10 interactors.
113949. 200 interactors.
113950. 5 interactors.
113951. 6 interactors.
113952. 4 interactors.
113953. 8 interactors.
113954. 23 interactors.
114458. 7 interactors.
DIPiDIP-29371N.
IntActiP68431. 73 interactors.
MINTiMINT-256465.
STRINGi9606.ENSP00000444823.

PTM databases

iPTMnetiP68431.
PhosphoSitePlusiP68431.
SwissPalmiP68431.

Polymorphism and mutation databases

BioMutaiHIST1H3A.
DMDMi55977055.

Proteomic databases

EPDiP68431.
MaxQBiP68431.
PaxDbiP68431.
PeptideAtlasiP68431.
PRIDEiP68431.
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.
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.
MIMi602810. 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.
OMAiRTKQMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP68431.
TreeFamiTF314241.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112727-MONOMER.
ZFISH:ENSG00000124642-MONOMER.
ZFISH:ENSG00000124687-MONOMER.
ZFISH:ENSG00000124693-MONOMER.
ZFISH:ENSG00000158597-MONOMER.
ZFISH:ENSG00000178458-MONOMER.
ReactomeiR-HSA-1266695. Interleukin-7 signaling.
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-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.
PROiP68431.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124693.
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.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH31_HUMAN
AccessioniPrimary (citable) accession number: P68431
Secondary accession number(s): A0PJT7
, A5PLR1, P02295, P02296, P16106, Q6ISV8, Q6NWP8, Q6NWP9, Q6NXU4, Q71DJ3, Q93081
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 145 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

Miscellaneous

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

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.