H3 3A | ENSG00000163041 | NCBI 3020

Details for: H3 3A

Gene ID: 3020

Symbol: H3 3A

Ensembl ID: ENSG00000163041

Description: H3.3 histone A

Associated with

Activated pkn1 stimulates transcription of ar (androgen receptor) regulated genes klk2 and klk3
(R-HSA-5625886)
Activation of anterior hox genes in hindbrain development during early embryogenesis
(R-HSA-5617472)
Activation of hox genes during differentiation
(R-HSA-5619507)
Amyloid fiber formation
(R-HSA-977225)
Assembly of the orc complex at the origin of replication
(R-HSA-68616)
Assembly of the pre-replicative complex
(R-HSA-68867)
B-wich complex positively regulates rrna expression
(R-HSA-5250924)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular senescence
(R-HSA-2559583)
Chromatin modifications during the maternal to zygotic transition (mzt)
(R-HSA-9821002)
Chromosome maintenance
(R-HSA-73886)
Condensation of prophase chromosomes
(R-HSA-2299718)
Defective pyroptosis
(R-HSA-9710421)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of programmed cell death
(R-HSA-9645723)
Dna methylation
(R-HSA-5334118)
Dna replication
(R-HSA-69306)
Dna replication pre-initiation
(R-HSA-69002)
Epigenetic regulation by wdr5-containing histone modifying complexes
(R-HSA-9917777)
Epigenetic regulation of adipogenesis genes by mll3 and mll4 complexes
(R-HSA-9851695)
Epigenetic regulation of gene expression
(R-HSA-212165)
Epigenetic regulation of gene expression by mll3 and mll4 complexes
(R-HSA-9818564)
Ercc6 (csb) and ehmt2 (g9a) positively regulate rrna expression
(R-HSA-427389)
Esr-mediated signaling
(R-HSA-8939211)
Estrogen-dependent gene expression
(R-HSA-9018519)
Factors involved in megakaryocyte development and platelet production
(R-HSA-983231)
Formation of the beta-catenin:tcf transactivating complex
(R-HSA-201722)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Gene silencing by rna
(R-HSA-211000)
Hemostasis
(R-HSA-109582)
Inhibition of dna recombination at telomere
(R-HSA-9670095)
Maternal to zygotic transition (mzt)
(R-HSA-9816359)
Meiosis
(R-HSA-1500620)
Meiotic recombination
(R-HSA-912446)
Metabolism of proteins
(R-HSA-392499)
Mitotic prophase
(R-HSA-68875)
Mll4 and mll3 complexes regulate expression of pparg target genes in adipogenesis and hepatic steatosis
(R-HSA-9841922)
M phase
(R-HSA-68886)
Negative epigenetic regulation of rrna expression
(R-HSA-5250941)
Norc negatively regulates rrna expression
(R-HSA-427413)
Oxidative stress induced senescence
(R-HSA-2559580)
Positive epigenetic regulation of rrna expression
(R-HSA-5250913)
Prc2 methylates histones and dna
(R-HSA-212300)
Pre-notch expression and processing
(R-HSA-1912422)
Pre-notch transcription and translation
(R-HSA-1912408)
Regulation of endogenous retroelements
(R-HSA-9842860)
Regulation of endogenous retroelements by krab-zfp proteins
(R-HSA-9843940)
Regulation of endogenous retroelements by piwi-interacting rnas (pirnas)
(R-HSA-9845323)
Regulation of endogenous retroelements by the human silencing hub (hush) complex
(R-HSA-9843970)
Replacement of protamines by nucleosomes in the male pronucleus
(R-HSA-9821993)
Reproduction
(R-HSA-1474165)
Rho gtpase effectors
(R-HSA-195258)
Rho gtpases activate pkns
(R-HSA-5625740)
Rna polymerase ii transcription
(R-HSA-73857)
Rna polymerase i promoter clearance
(R-HSA-73854)
Rna polymerase i promoter escape
(R-HSA-73772)
Rna polymerase i promoter opening
(R-HSA-73728)
Rna polymerase i transcription
(R-HSA-73864)
Runx1 regulates genes involved in megakaryocyte differentiation and platelet function
(R-HSA-8936459)
Runx1 regulates transcription of genes involved in differentiation of hscs
(R-HSA-8939236)
Senescence-associated secretory phenotype (sasp)
(R-HSA-2559582)
Signaling by notch
(R-HSA-157118)
Signaling by nuclear receptors
(R-HSA-9006931)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signaling by wnt
(R-HSA-195721)
Signal transduction
(R-HSA-162582)
Sirt1 negatively regulates rrna expression
(R-HSA-427359)
Tcf dependent signaling in response to wnt
(R-HSA-201681)
Telomere maintenance
(R-HSA-157579)
Transcriptional regulation by runx1
(R-HSA-8878171)
Transcriptional regulation by small rnas
(R-HSA-5578749)
Transcriptional regulation of granulopoiesis
(R-HSA-9616222)
Cell population proliferation
(GO:0008283)
Embryo implantation
(GO:0007566)
Male gonad development
(GO:0008584)
Multicellular organism growth
(GO:0035264)
Muscle cell differentiation
(GO:0042692)
Nucleosomal dna binding
(GO:0031492)
Nucleosome assembly
(GO:0006334)
Nucleus organization
(GO:0006997)
Oocyte maturation
(GO:0001556)
Osteoblast differentiation
(GO:0001649)
Pericentric heterochromatin formation
(GO:0031508)
Positive regulation of cell growth
(GO:0030307)
Protein binding
(GO:0005515)
Protein heterodimerization activity
(GO:0046982)
Rna polymerase ii cis-regulatory region sequence-specific dna binding
(GO:0000978)
Rna polymerase ii core promoter sequence-specific dna binding
(GO:0000979)
Single fertilization
(GO:0007338)
Spermatid development
(GO:0007286)
Structural constituent of chromatin
(GO:0030527)
Subtelomeric heterochromatin formation
(GO:0031509)
Telomere organization
(GO:0032200)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 671.7017
Cell Significance Index: -104.4800
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 500.6241
Cell Significance Index: -126.9800
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 464.3794
Cell Significance Index: -191.3000
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 410.5713
Cell Significance Index: -193.8400
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 386.9279
Cell Significance Index: -199.0300
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 290.5865
Cell Significance Index: -194.9900
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 122.8917
Cell Significance Index: -151.5200
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 46.1449
Cell Significance Index: -182.0900
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 36.8685
Cell Significance Index: -113.2400
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 26.8484
Cell Significance Index: -58.7600
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 14.8615
Cell Significance Index: 274.6800
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 14.2514
Cell Significance Index: 495.2300
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: 13.6670
Cell Significance Index: 114.8000
Cell Name: peg cell (CL4033014)
Fold Change: 11.6256
Cell Significance Index: 268.5900
Cell Name: kidney cell (CL1000497)
Fold Change: 11.5252
Cell Significance Index: 92.0200
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 11.2805
Cell Significance Index: 236.1200
Cell Name: granulosa cell (CL0000501)
Fold Change: 10.5800
Cell Significance Index: 278.2000
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 10.3778
Cell Significance Index: 132.9100
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 9.9804
Cell Significance Index: 108.5000
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 7.7909
Cell Significance Index: 918.7800
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 7.7162
Cell Significance Index: 87.6600
Cell Name: early pro-B cell (CL0002046)
Fold Change: 6.8778
Cell Significance Index: 443.7200
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 6.4134
Cell Significance Index: 880.7400
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 6.3543
Cell Significance Index: 781.3200
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 6.3177
Cell Significance Index: 1138.8900
Cell Name: cell in vitro (CL0001034)
Fold Change: 5.9444
Cell Significance Index: 3246.3800
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 5.6901
Cell Significance Index: 424.0800
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 5.6431
Cell Significance Index: 2494.9700
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 5.5253
Cell Significance Index: 390.7800
Cell Name: odontoblast (CL0000060)
Fold Change: 5.3654
Cell Significance Index: 687.8200
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 5.2062
Cell Significance Index: 47.9400
Cell Name: lactocyte (CL0002325)
Fold Change: 5.1001
Cell Significance Index: 658.8900
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 4.9163
Cell Significance Index: 229.2200
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: 4.6868
Cell Significance Index: 33.6600
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 4.6183
Cell Significance Index: 217.0600
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 4.5957
Cell Significance Index: 241.2900
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 4.4408
Cell Significance Index: 130.4200
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 4.4038
Cell Significance Index: 77.8200
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 4.0787
Cell Significance Index: 111.0200
Cell Name: theca cell (CL0000503)
Fold Change: 2.7659
Cell Significance Index: 16.2500
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 2.5423
Cell Significance Index: 142.6600
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 2.2921
Cell Significance Index: 65.7100
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.4210
Cell Significance Index: 140.5700
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 1.3426
Cell Significance Index: 153.8200
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.3034
Cell Significance Index: 67.7100
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.8387
Cell Significance Index: 143.2200
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.6980
Cell Significance Index: 132.8400
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.6880
Cell Significance Index: 504.4700
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.6292
Cell Significance Index: 476.2400
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.2304
Cell Significance Index: 82.6300
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.2091
Cell Significance Index: 3.5000
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.2026
Cell Significance Index: 12.7700
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.1754
Cell Significance Index: 5.0600
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: 0.1073
Cell Significance Index: 8.5000
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0294
Cell Significance Index: -3.0000
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0691
Cell Significance Index: -130.1000
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: -0.0701
Cell Significance Index: -0.5400
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: -0.0829
Cell Significance Index: -16.6200
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.1139
Cell Significance Index: -210.1200
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.1296
Cell Significance Index: -199.5400
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.1300
Cell Significance Index: -6.5700
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.1516
Cell Significance Index: -206.0900
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.1682
Cell Significance Index: -124.6000
Cell Name: neoplastic cell (CL0001063)
Fold Change: -0.1925
Cell Significance Index: -38.2000
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.2615
Cell Significance Index: -166.0700
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.2674
Cell Significance Index: -150.8300
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.3688
Cell Significance Index: -230.2900
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.3899
Cell Significance Index: -176.9800
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.4118
Cell Significance Index: -14.4700
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.4232
Cell Significance Index: -121.7800
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.5223
Cell Significance Index: -21.4000
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.7040
Cell Significance Index: -17.9900
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.9571
Cell Significance Index: -201.6000
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -0.9637
Cell Significance Index: -156.7300
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -1.1147
Cell Significance Index: -162.0400
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: -1.3900
Cell Significance Index: -151.2000
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -1.5886
Cell Significance Index: -50.8800
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -1.5894
Cell Significance Index: -27.4000
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: -1.6781
Cell Significance Index: -14.4200
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -1.7136
Cell Significance Index: -47.8900
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -1.7239
Cell Significance Index: -132.2900
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -1.7489
Cell Significance Index: -182.1000
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -1.7972
Cell Significance Index: -38.9400
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -1.7981
Cell Significance Index: -81.5000
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: -1.8337
Cell Significance Index: -11.2900
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -1.9527
Cell Significance Index: -29.2600
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -2.2620
Cell Significance Index: -156.4300
Cell Name: retinal rod cell (CL0000604)
Fold Change: -2.3434
Cell Significance Index: -27.9400
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -2.9695
Cell Significance Index: -79.2900
Cell Name: sensory neuron (CL0000101)
Fold Change: -3.0392
Cell Significance Index: -17.2800
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -3.1842
Cell Significance Index: -195.2200
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -3.2335
Cell Significance Index: -95.2400
Cell Name: BEST4+ enteroycte (CL4030026)
Fold Change: -3.4228
Cell Significance Index: -51.5800
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -3.8354
Cell Significance Index: -102.6000
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -3.8795
Cell Significance Index: -52.9300
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -3.9566
Cell Significance Index: -175.0100
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -4.1526
Cell Significance Index: -106.7400
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -4.2301
Cell Significance Index: -90.0900
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -4.2605
Cell Significance Index: -156.4000
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -4.5626
Cell Significance Index: -149.3800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** H3.3 histone A is a member of the histone H3 family, which is essential for chromatin structure and gene regulation. This gene is characterized by its ability to regulate gene expression through various mechanisms, including histone modification, chromatin assembly, and DNA replication. Notably, H3.3 histone A is involved in the assembly of the pre-replicative complex and the origin of replication, highlighting its critical role in DNA replication and cell cycle progression. **Pathways and Functions:** H3.3 histone A is implicated in numerous cellular processes, including: 1. **Gene Expression Regulation**: H3.3 histone A regulates gene expression through histone modification, chromatin assembly, and DNA replication. 2. **DNA Replication**: H3.3 histone A is involved in the assembly of the pre-replicative complex and the origin of replication, ensuring accurate DNA replication. 3. **Cell Cycle Regulation**: H3.3 histone A regulates cell cycle progression, including mitotic prophase and the G2/M checkpoint. 4. **Immune Cell Development and Differentiation**: H3.3 histone A is expressed in follicular B cells, skeletal muscle satellite cells, and effector memory CD4-positive T cells, highlighting its role in immune cell development and differentiation. 5. **Epigenetic Regulation**: H3.3 histone A is involved in epigenetic regulation, including DNA methylation and histone modification, which shape gene expression and cellular behavior. **Clinical Significance:** The dysregulation of H3.3 histone A has been implicated in various immunological disorders, including: 1. **Autoimmune Diseases**: H3.3 histone A dysfunction has been linked to autoimmune diseases, such as rheumatoid arthritis and lupus, where chromatin structure and gene regulation are disrupted. 2. **Cancer**: H3.3 histone A alterations have been observed in various cancers, including leukemia and lymphoma, where chromatin structure and gene expression are dysregulated. 3. **Immunodeficiency Disorders**: H3.3 histone A dysfunction has been associated with immunodeficiency disorders, such as severe combined immunodeficiency (SCID), where chromatin structure and gene regulation are impaired. In conclusion, H3.3 histone A is a multifaceted gene that plays a critical role in various cellular processes, including gene expression regulation, DNA replication, and immune cell development and differentiation. Its dysregulation has been implicated in various immunological disorders, highlighting the importance of understanding its mechanisms and functions in the context of immunology and disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Histone H3.3

Genular Protein ID: 3685484018

Symbol: H33_HUMAN

Name: Histone H3.3

UniProtKB Accession Codes:

P84243 P06351 P33155 Q5VV55 Q5VV56 Q66I33 Q9V3W4

Database IDs:

Citations:

PubMed ID: 2859593

Title: Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs.

PubMed ID: 2859593

DOI: 10.1073/pnas.82.9.2834

PubMed ID: 3031613

Title: Unusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family.

PubMed ID: 3031613

DOI: 10.1093/nar/15.7.2871

PubMed ID: 8586426

Title: The human replacement histone H3.3B gene (H3F3B).

PubMed ID: 8586426

DOI: 10.1006/geno.1995.9878

PubMed ID: 15498874

Title: Large-scale cDNA transfection screening for genes related to cancer development and progression.

PubMed ID: 15498874

DOI: 10.1073/pnas.0404089101

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7309716

Title: Human spleen histone H3. Isolation and amino acid sequence.

PubMed ID: 7309716

DOI: 10.1093/oxfordjournals.jbchem.a133573

PubMed ID: 16185088

Title: Modifications of human histone H3 variants during mitosis.

PubMed ID: 16185088

DOI: 10.1021/bi050906n

PubMed ID: 10464286

Title: Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation.

PubMed ID: 10464286

DOI: 10.1074/jbc.274.36.25543

PubMed ID: 11242053

Title: Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.

PubMed ID: 11242053

DOI: 10.1038/35065132

PubMed ID: 11856369

Title: Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation.

PubMed ID: 11856369

DOI: 10.1046/j.1356-9597.2001.00498.x

PubMed ID: 12560483

Title: Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase.

PubMed ID: 12560483

DOI: 10.1093/nar/gkg176

PubMed ID: 14718166

Title: Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis.

PubMed ID: 14718166

DOI: 10.1016/s0092-8674(03)01064-x

PubMed ID: 15471871

Title: Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1.

PubMed ID: 15471871

DOI: 10.1074/jbc.m410021200

PubMed ID: 15525939

Title: Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks.

PubMed ID: 15525939

DOI: 10.1038/nature03114

PubMed ID: 15345777

Title: Human PAD4 regulates histone arginine methylation levels via demethylimination.

PubMed ID: 15345777

DOI: 10.1126/science.1101400

PubMed ID: 15776021

Title: Variant histone H3.3 marks promoters of transcriptionally active genes during mammalian cell division.

PubMed ID: 15776021

DOI: 10.1038/sj.embor.7400366

PubMed ID: 15681610

Title: The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment.

PubMed ID: 15681610

DOI: 10.1101/gad.1267105

PubMed ID: 15684425

Title: Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha.

PubMed ID: 15684425

DOI: 10.1074/jbc.m410521200

PubMed ID: 15851689

Title: Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes.

PubMed ID: 15851689

DOI: 10.1073/pnas.0502413102

PubMed ID: 16258499

Title: Histone H3.3 deposition at E2F-regulated genes is linked to transcription.

PubMed ID: 16258499

DOI: 10.1038/sj.embor.7400561

PubMed ID: 16267050

Title: Expression patterns and post-translational modifications associated with mammalian histone H3 variants.

PubMed ID: 16267050

DOI: 10.1074/jbc.m509266200

PubMed ID: 16457588

Title: Mass spectrometric characterization of human histone H3: a bird's eye view.

PubMed ID: 16457588

DOI: 10.1021/pr050266a

PubMed ID: 16497732

Title: Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17.

PubMed ID: 16497732

DOI: 10.1210/me.2005-0365

PubMed ID: 18079182

Title: PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation.

PubMed ID: 18079182

DOI: 10.1101/gad.447007

PubMed ID: 16567635

Title: Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4.

PubMed ID: 16567635

DOI: 10.1073/pnas.0509639103

PubMed ID: 17194708

Title: Organismal differences in post-translational modifications in histones H3 and H4.

PubMed ID: 17194708

DOI: 10.1074/jbc.m607900200

PubMed ID: 17189264

Title: Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification.

PubMed ID: 17189264

DOI: 10.1074/jbc.m607909200

PubMed ID: 17898714

Title: Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive.

PubMed ID: 17898714

DOI: 10.1038/nature06166

PubMed ID: 18077460

Title: Arginine methylation of the histone H3 tail impedes effector binding.

PubMed ID: 18077460

DOI: 10.1074/jbc.c700192200

PubMed ID: 18066052

Title: Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation.

PubMed ID: 18066052

DOI: 10.1038/ncb1668

PubMed ID: 19520870

Title: Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

PubMed ID: 19520870

DOI: 10.1074/jbc.m109.003202

PubMed ID: 19783980

Title: JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin.

PubMed ID: 19783980

DOI: 10.1038/nature08448

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20850016

Title: Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers.

PubMed ID: 20850016

DOI: 10.1016/j.cell.2010.08.020

PubMed ID: 20504901

Title: The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.

PubMed ID: 20504901

DOI: 10.1101/gad.566910

PubMed ID: 20228790

Title: Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4.

PubMed ID: 20228790

DOI: 10.1038/nature08839

PubMed ID: 21925322

Title: Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.

PubMed ID: 21925322

DOI: 10.1016/j.cell.2011.08.008

PubMed ID: 22195965

Title: A specific function for the histone chaperone NASP to fine-tune a reservoir of soluble H3-H4 in the histone supply chain.

PubMed ID: 22195965

DOI: 10.1016/j.molcel.2011.11.021

PubMed ID: 22901803

Title: PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis.

PubMed ID: 22901803

DOI: 10.1016/j.cell.2012.07.018

PubMed ID: 22387026

Title: Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA.

PubMed ID: 22387026

DOI: 10.1016/j.molcel.2012.01.019

PubMed ID: 22483618

Title: Lysyl oxidase-like 2 deaminates lysine 4 in histone H3.

PubMed ID: 22483618

DOI: 10.1016/j.molcel.2012.03.002

PubMed ID: 27392148

Title:

PubMed ID: 27392148

DOI: 10.1016/j.molcel.2016.06.013

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 22389435

Title: Lysine succinylation and lysine malonylation in histones.

PubMed ID: 22389435

DOI: 10.1074/mcp.m111.015875

PubMed ID: 23415232

Title: Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer.

PubMed ID: 23415232

DOI: 10.1016/j.cell.2013.01.032

PubMed ID: 24681537

Title: Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark.

PubMed ID: 24681537

DOI: 10.1038/nchembio.1497

PubMed ID: 27735137

Title: Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3.

PubMed ID: 27735137

DOI: 10.1111/febs.13922

PubMed ID: 27105113

Title: Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters.

PubMed ID: 27105113

DOI: 10.1016/j.molcel.2016.03.014

PubMed ID: 27105115

Title: Metabolic regulation of gene expression by histone lysine beta-hydroxybutyrylation.

PubMed ID: 27105115

DOI: 10.1016/j.molcel.2016.03.036

PubMed ID: 27436229

Title: SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability.

PubMed ID: 27436229

DOI: 10.1038/ncomms12235

PubMed ID: 27016736

Title: Structure and function of human histone H3.Y nucleosome.

PubMed ID: 27016736

DOI: 10.1093/nar/gkw202

PubMed ID: 28497810

Title: Class I histone deacetylases are major histone decrotonylases: evidence for critical and broad function of histone crotonylation in transcription.

PubMed ID: 28497810

DOI: 10.1038/cr.2017.68

PubMed ID: 28190768

Title: Serine ADP-ribosylation depends on HPF1.

PubMed ID: 28190768

DOI: 10.1016/j.molcel.2017.01.003

PubMed ID: 29211711

Title: KAT2A coupled with the alpha-KGDH complex acts as a histone H3 succinyltransferase.

PubMed ID: 29211711

DOI: 10.1038/nature25003

PubMed ID: 30257210

Title: Interplay of histone marks with serine ADP-ribosylation.

PubMed ID: 30257210

DOI: 10.1016/j.celrep.2018.08.092

PubMed ID: 29480802

Title: Serine is the major residue for ADP-ribosylation upon DNA damage.

PubMed ID: 29480802

DOI: 10.7554/elife.34334

PubMed ID: 31542297

Title: Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.

PubMed ID: 31542297

DOI: 10.1016/j.molcel.2019.08.018

PubMed ID: 30867594

Title: Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3.

PubMed ID: 30867594

DOI: 10.1038/s41586-019-1024-7

PubMed ID: 31645732

Title: Metabolic regulation of gene expression by histone lactylation.

PubMed ID: 31645732

DOI: 10.1038/s41586-019-1678-1

PubMed ID: 31527692

Title: VRK1 functional insufficiency due to alterations in protein stability or kinase activity of human VRK1 pathogenic variants implicated in neuromotor syndromes.

PubMed ID: 31527692

DOI: 10.1038/s41598-019-49821-7

PubMed ID: 32273471

Title: Dopaminylation of histone H3 in ventral tegmental area regulates cocaine seeking.

PubMed ID: 32273471

DOI: 10.1126/science.aaw8806

PubMed ID: 34874266

Title: Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling.

PubMed ID: 34874266

DOI: 10.7554/elife.71502

PubMed ID: 35939806

Title: Potent Activation of NAD+-Dependent Deacetylase Sirt7 by Nucleosome Binding.

PubMed ID: 35939806

DOI: 10.1021/acschembio.2c00348

PubMed ID: 24590075

Title: ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression.

PubMed ID: 24590075

DOI: 10.1038/nature13045

PubMed ID: 33857403

Title: DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.

PubMed ID: 33857403

DOI: 10.1016/j.molcel.2021.03.041

PubMed ID: 32911480

Title: Structural basis for sequestration and autoinhibition of cGAS by chromatin.

PubMed ID: 32911480

DOI: 10.1038/s41586-020-2748-0

PubMed ID: 22286216

Title: Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas.

PubMed ID: 22286216

DOI: 10.1038/ng.1102

PubMed ID: 22286061

Title: Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma.

PubMed ID: 22286061

DOI: 10.1038/nature10833

PubMed ID: 23539269

Title: Histone H3.3. mutations drive pediatric glioblastoma through upregulation of MYCN.

PubMed ID: 23539269

DOI: 10.1158/2159-8290.cd-12-0426

PubMed ID: 23603901

Title: The histone H3.3K27M mutation in pediatric glioma reprograms H3K27 methylation and gene expression.

PubMed ID: 23603901

DOI: 10.1101/gad.217778.113

PubMed ID: 24162739

Title: Distinct H3F3A and H3F3B driver mutations define chondroblastoma and giant cell tumor of bone.

PubMed ID: 24162739

DOI: 10.1038/ng.2814

PubMed ID: 23539183

Title: Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma.

PubMed ID: 23539183

DOI: 10.1126/science.1232245

PubMed ID: 27174990

Title: Histone H3K36 mutations promote sarcomagenesis through altered histone methylation landscape.

PubMed ID: 27174990

DOI: 10.1126/science.aac7272

PubMed ID: 28067913

Title: Impaired H3K36 methylation defines a subset of head and neck squamous cell carcinomas.

PubMed ID: 28067913

DOI: 10.1038/ng.3757

PubMed ID: 33268356

Title: Histone H3.3 beyond cancer: Germline mutations in Histone 3 Family 3A and 3B cause a previously unidentified neurodegenerative disorder in 46 patients.

PubMed ID: 33268356

DOI: 10.1126/sciadv.abc9207

PubMed ID: 34876591

Title: De novo variants in H3-3A and H3-3B are associated with neurodevelopmental delay, dysmorphic features, and structural brain abnormalities.

PubMed ID: 34876591

DOI: 10.1038/s41525-021-00268-8

Sequence Information:

Length: 136
Mass: 15328
Checksum: 5158ED279E6F9E1C
Sequence:

MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE 
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI 
MPKDIQLARR IRGERA

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: H3 3A

Associated with

Cells (max top 100)

Other Information

Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs. PubMed ID: 2859593

Unusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family. PubMed ID: 3031613

The human replacement histone H3.3B gene (H3F3B). PubMed ID: 8586426

Large-scale cDNA transfection screening for genes related to cancer development and progression. PubMed ID: 15498874

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

The DNA sequence and biological annotation of human chromosome 1. PubMed ID: 16710414

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Human spleen histone H3. Isolation and amino acid sequence. PubMed ID: 7309716

Modifications of human histone H3 variants during mitosis. PubMed ID: 16185088

Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. PubMed ID: 10464286

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. PubMed ID: 11242053

Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. PubMed ID: 11856369

Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. PubMed ID: 12560483

Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. PubMed ID: 14718166

Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1. PubMed ID: 15471871

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. PubMed ID: 15525939

Human PAD4 regulates histone arginine methylation levels via demethylimination. PubMed ID: 15345777

Variant histone H3.3 marks promoters of transcriptionally active genes during mammalian cell division. PubMed ID: 15776021

The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. PubMed ID: 15681610

Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha. PubMed ID: 15684425

Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes. PubMed ID: 15851689

Histone H3.3 deposition at E2F-regulated genes is linked to transcription. PubMed ID: 16258499

Expression patterns and post-translational modifications associated with mammalian histone H3 variants. PubMed ID: 16267050

Mass spectrometric characterization of human histone H3: a bird's eye view. PubMed ID: 16457588

Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17. PubMed ID: 16497732

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. PubMed ID: 18079182

Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4. PubMed ID: 16567635

Organismal differences in post-translational modifications in histones H3 and H4. PubMed ID: 17194708

Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification. PubMed ID: 17189264

Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. PubMed ID: 17898714

Arginine methylation of the histone H3 tail impedes effector binding. PubMed ID: 18077460

Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. PubMed ID: 18066052

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding. PubMed ID: 19520870

JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. PubMed ID: 19783980

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. PubMed ID: 20850016

The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. PubMed ID: 20504901

Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. PubMed ID: 20228790

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. PubMed ID: 21925322

A specific function for the histone chaperone NASP to fine-tune a reservoir of soluble H3-H4 in the histone supply chain. PubMed ID: 22195965

PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis. PubMed ID: 22901803

Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA. PubMed ID: 22387026

Lysyl oxidase-like 2 deaminates lysine 4 in histone H3. PubMed ID: 22483618