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P68431

- H31_HUMAN

UniProt

P68431 - H31_HUMAN

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Protein
Histone H3.1
Gene
HIST1H3A, H3FA
HIST1H3B, H3FL
HIST1H3C, H3FC
HIST1H3D, H3FB
HIST1H3E, H3FD
HIST1H3F, H3FI
more..
HIST1H3G, H3FH
HIST1H3H, H3FK
HIST1H3I, H3FF
HIST1H3J, H3FJ less..
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. DNA replication-dependent nucleosome assembly Source: UniProt
  2. blood coagulation Source: Reactome
  3. chromatin organization Source: Reactome
  4. regulation of gene silencing Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_27271. Meiotic recombination.
REACT_75925. Amyloids.

Names & Taxonomyi

Organism-specific databases

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
Synonyms:H3FA
AND
Synonyms:H3FL
AND
Synonyms:H3FC
AND
Synonyms:H3FB
AND
Synonyms:H3FD
AND
Synonyms:H3FI
AND
Synonyms:H3FH
AND
Synonyms:H3FK
AND
Synonyms:H3FF
AND
Synonyms:H3FJ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6
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

  1. extracellular region Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nuclear chromosome Source: UniProt
  4. nucleoplasm Source: Reactome
  5. nucleosome Source: UniProtKB-KW
  6. nucleus Source: UniProt
  7. protein complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29148.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 136135Histone H3.1
PRO_0000221245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternate3 Publications
Modified residuei3 – 31Citrulline; alternate
Modified residuei4 – 41Phosphothreonine; by GSG22 Publications
Modified residuei5 – 51Allysine; alternate
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate3 Publications
Modified residuei5 – 51N6,N6-dimethyllysine; alternate3 Publications
Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
Modified residuei5 – 51N6-crotonyllysine; alternate1 Publication
Modified residuei5 – 51N6-methyllysine; alternate3 Publications
Modified residuei7 – 71Phosphothreonine; by PKC1 Publication
Modified residuei9 – 91Citrulline; alternate
Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate5 Publications
Modified residuei10 – 101N6,N6-dimethyllysine; alternate5 Publications
Modified residuei10 – 101N6-acetyllysine; alternate6 Publications
Modified residuei10 – 101N6-crotonyllysine; alternate1 Publication
Modified residuei10 – 101N6-methyllysine; alternate5 Publications
Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications
Modified residuei12 – 121Phosphothreonine; by PKC and CHEK13 Publications
Modified residuei15 – 151N6-acetyllysine6 Publications
Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternate3 Publications
Modified residuei18 – 181Citrulline; alternate
Modified residuei19 – 191N6-acetyllysine; alternate3 Publications
Modified residuei19 – 191N6-crotonyllysine; alternate1 Publication
Modified residuei19 – 191N6-methyllysine; alternate2 Publications
Modified residuei24 – 241N6-acetyllysine; alternate4 Publications
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-methyllysine; alternate1 Publication
Modified residuei27 – 271Citrulline
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate4 Publications
Modified residuei28 – 281N6,N6-dimethyllysine; alternate4 Publications
Modified residuei28 – 281N6-acetyllysine; alternate2 Publications
Modified residuei28 – 281N6-crotonyllysine; alternate1 Publication
Modified residuei28 – 281N6-methyllysine; alternate4 Publications
Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate5 Publications
Modified residuei37 – 371N6,N6-dimethyllysine; alternate5 Publications
Modified residuei37 – 371N6-acetyllysine; alternate2 Publications
Modified residuei37 – 371N6-methyllysine; alternate5 Publications
Modified residuei38 – 381N6-methyllysine1 Publication
Modified residuei42 – 421Phosphotyrosine1 Publication
Modified residuei57 – 571N6,N6,N6-trimethyllysine; alternate2 Publications
Modified residuei57 – 571N6-acetyllysine; alternate1 Publication
Modified residuei57 – 571N6-crotonyllysine; alternate1 Publication
Modified residuei57 – 571N6-methyllysine; by EHMT2; alternate2 Publications
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei65 – 651N6-methyllysine2 Publications
Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei80 – 801N6,N6-dimethyllysine; alternate4 Publications
Modified residuei80 – 801N6-acetyllysine; alternate1 Publication
Modified residuei80 – 801N6-methyllysine; alternate4 Publications
Modified residuei81 – 811Phosphothreonine1 Publication
Modified residuei108 – 1081Phosphothreonine By similarity
Modified residuei116 – 1161N6-acetyllysine1 Publication
Modified residuei123 – 1231N6-acetyllysine; alternate2 Publications
Modified residuei123 – 1231N6-methyllysine; alternate2 Publications

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.9 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.
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.
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.12 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.1 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

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP68431.
PaxDbiP68431.
PRIDEiP68431.

PTM databases

PhosphoSiteiP68431.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiP68431.
CleanExiHS_HIST1H3A.
HS_HIST1H3B.
HS_HIST1H3C.
HS_HIST1H3D.
HS_HIST1H3E.
HS_HIST1H3F.
HS_HIST1H3G.
HS_HIST1H3H.
HS_HIST1H3I.
GenevestigatoriP68431.

Organism-specific databases

HPAiCAB037166.
CAB037178.
CAB037187.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
AIREO4391820EBI-79722,EBI-1753081
CBX1P839169EBI-79722,EBI-78129
CBX3Q131855EBI-79722,EBI-78176
CBX5P459739EBI-79722,EBI-78219
CCDC101Q96ES725EBI-79722,EBI-743117
CDYLQ9Y2325EBI-79722,EBI-1387386
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
PHF20Q9BVI06EBI-79722,EBI-2560802
PHF20L1A8MW922EBI-79722,EBI-2560834
SETD7Q8WTS64EBI-79722,EBI-1268586
SGF29P2555411EBI-79722,EBI-21678From a different organism.
TP53BP1Q128885EBI-79722,EBI-396540
WDR5P619649EBI-79722,EBI-540834
YWHAZP631043EBI-79722,EBI-347088

Protein-protein interaction databases

BioGridi113946. 164 interactions.
113947. 5 interactions.
113948. 10 interactions.
113949. 31 interactions.
113950. 5 interactions.
113951. 6 interactions.
113952. 4 interactions.
113953. 7 interactions.
113954. 22 interactions.
114458. 6 interactions.
DIPiDIP-29371N.
IntActiP68431. 55 interactions.
MINTiMINT-256465.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73
Beta strandi14 – 163
Helixi46 – 5712
Helixi65 – 7713
Beta strandi80 – 823
Helixi87 – 11428
Beta strandi118 – 1203
Helixi122 – 13110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
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[»]
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[»]
4N4HX-ray2.30B22-43[»]
ProteinModelPortaliP68431.
SMRiP68431. Positions 17-136.

Miscellaneous databases

EvolutionaryTraceiP68431.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.

Phylogenomic databases

eggNOGiCOG2036.
HOVERGENiHBG001172.
InParanoidiP68431.
KOiK11253.
OMAiTEFANEM.
OrthoDBiEOG7HB5C2.
PhylomeDBiP68431.
TreeFamiTF314241.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[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

MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR    50
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY 100
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA 136
Length:136
Mass (Da):15,404
Last modified:January 23, 2007 - v2
Checksum:i9B89008EA50A0EF6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701R → C in AAH67493. 1 Publication
Sequence conflicti100 – 1001Y → T in CAB02546. 1 Publication
Sequence conflicti122 – 1221P → L in AAH66884. 1 Publication
Sequence conflicti135 – 1351Missing in AAA52651. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000244661; ENSP00000244661; ENSG00000124693.
ENST00000305910; ENSP00000439660; ENSG00000256018.
ENST00000328488; ENSP00000329554; ENSG00000182572.
ENST00000356476; ENSP00000366999; ENSG00000197409.
ENST00000357647; ENSP00000350275; ENSG00000198366.
ENST00000359303; ENSP00000352252; ENSG00000197153.
ENST00000360408; ENSP00000353581; ENSG00000196966.
ENST00000369163; ENSP00000358160; ENSG00000203813.
ENST00000377831; ENSP00000367062; ENSG00000197409.
ENST00000446824; ENSP00000444823; ENSG00000256316.
ENST00000540144; ENSP00000439493; ENSG00000196532.
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.1. human.

Polymorphism databases

DMDMi55977055.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4570.1.
CCDS4573.1.
CCDS4576.1.
CCDS4590.1.
CCDS4596.1.
CCDS4600.1.
CCDS4602.1.
CCDS4627.1.
CCDS4636.1.
CCDS4638.1.
PIRi I37446. HSHU3.
RefSeqi NP_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.
UniGenei Hs.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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CS9 NMR - A 131-136 [» ]
1CT6 NMR - A 131-136 [» ]
1O9S X-ray 1.75 K/L 2-10 [» ]
1Q3L X-ray 1.64 P 2-16 [» ]
2B2T X-ray 2.45 D 2-20 [» ]
2B2U X-ray 2.95 D 2-16 [» ]
2B2V X-ray 2.65 D 2-16 [» ]
2B2W X-ray 2.40 D 2-20 [» ]
2C1J X-ray 2.60 C/D 8-15 [» ]
2C1N X-ray 2.00 C/E 8-15 [» ]
2CV5 X-ray 2.50 A/E 1-136 [» ]
2KWJ NMR - B 2-21 [» ]
2KWK NMR - B 2-21 [» ]
2L75 NMR - B 2-14 [» ]
2LBM NMR - C 2-16 [» ]
2M0O NMR - B 32-42 [» ]
2OQ6 X-ray 2.00 C/D 8-15 [» ]
2OT7 X-ray 2.14 C/D 8-15 [» ]
2OX0 X-ray 1.95 C/D 8-15 [» ]
2RI7 X-ray 1.45 P 2-10 [» ]
2UXN X-ray 2.72 E 2-22 [» ]
2VPG X-ray 1.60 P/R 2-19 [» ]
3A1B X-ray 2.29 A 2-21 [» ]
3AFA X-ray 2.50 A/E 1-136 [» ]
3AVR X-ray 1.80 B 18-39 [» ]
3AYW X-ray 2.90 A/E 1-136 [» ]
3AZE X-ray 3.00 A/E 1-136 [» ]
3AZF X-ray 2.70 A/E 1-136 [» ]
3AZG X-ray 2.40 A/E 1-136 [» ]
3AZH X-ray 3.49 A/E 1-136 [» ]
3AZI X-ray 2.70 A/E 1-136 [» ]
3AZJ X-ray 2.89 A/E 1-136 [» ]
3AZK X-ray 3.20 A/E 1-136 [» ]
3AZL X-ray 2.70 A/E 1-136 [» ]
3AZM X-ray 2.89 A/E 1-136 [» ]
3AZN X-ray 3.00 A/E 1-136 [» ]
3B95 X-ray 2.99 P 2-16 [» ]
3KMT X-ray 1.78 G/H/I 26-33 [» ]
3KQI X-ray 1.78 B 2-13 [» ]
3LQI X-ray 1.92 R/S/T 2-10 [» ]
3LQJ X-ray 1.90 Q/T 2-10 [» ]
3O34 X-ray 1.90 B 14-33 [» ]
3O35 X-ray 1.76 D/E 24-32 [» ]
3O37 X-ray 2.00 E/F/G/H 2-11 [» ]
3QJ6 X-ray 2.30 T 74-84 [» ]
3RIG X-ray 2.00 C/D 5-16 [» ]
3RIY X-ray 1.55 C/D 5-16 [» ]
3SOU X-ray 1.80 D/E 2-10 [» ]
3SOW X-ray 1.95 C/D 2-10 [» ]
3U31 X-ray 2.20 B 5-14 [» ]
3U3D X-ray 2.40 B 5-14 [» ]
3U4S X-ray 2.15 C/D 8-15 [» ]
3U5N X-ray 1.95 C/D 2-21 [» ]
3U5O X-ray 2.70 I/J/K/L/M/N/O/P 2-23 [» ]
3U5P X-ray 2.80 I/J/K/L/M/N/O/P 2-29 [» ]
3UEE X-ray 2.61 B/D 2-13 [» ]
3UEF X-ray 2.45 B/D 2-13 [» ]
3UIG X-ray 2.40 P/Q 2-16 [» ]
3UII X-ray 2.60 P/Q 2-11 [» ]
3UIK X-ray 2.70 P/Q 2-11 [» ]
3V43 X-ray 1.47 Q 2-19 [» ]
3W96 X-ray 3.00 A/E 1-136 [» ]
3W97 X-ray 3.20 A/E 1-136 [» ]
3W98 X-ray 3.42 A/E 29-136 [» ]
3W99 X-ray 3.00 A/E 1-136 [» ]
3WA9 X-ray 3.07 A/E 1-136 [» ]
3WAA X-ray 3.20 A/E 1-136 [» ]
3WKJ X-ray 2.80 A/E 1-136 [» ]
3ZG6 X-ray 2.20 F 5-14 [» ]
3ZVY X-ray 1.95 C/D 2-9 [» ]
4A0J X-ray 2.80 C/D 2-7 [» ]
4A0N X-ray 2.74 C 2-7 [» ]
4A7J X-ray 1.90 B 1-16 [» ]
4BD3 NMR - B 32-42 [» ]
4C1Q X-ray 2.30 C 2-10 [» ]
4F4U X-ray 2.00 C/D 5-16 [» ]
4F56 X-ray 1.70 C/D 5-16 [» ]
4FWF X-ray 2.70 E 2-21 [» ]
4HON X-ray 1.80 F/G 7-16 [» ]
4I51 X-ray 1.90 C/D 4-12 [» ]
4L7X X-ray 1.35 U 2-13 [» ]
4LK9 X-ray 1.60 B 2-22 [» ]
4LKA X-ray 1.61 B 2-22 [» ]
4LLB X-ray 2.50 C/D 2-22 [» ]
4N4H X-ray 2.30 B 22-43 [» ]
ProteinModelPortali P68431.
SMRi P68431. Positions 17-136.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113946. 164 interactions.
113947. 5 interactions.
113948. 10 interactions.
113949. 31 interactions.
113950. 5 interactions.
113951. 6 interactions.
113952. 4 interactions.
113953. 7 interactions.
113954. 22 interactions.
114458. 6 interactions.
DIPi DIP-29371N.
IntActi P68431. 55 interactions.
MINTi MINT-256465.

PTM databases

PhosphoSitei P68431.

Polymorphism databases

DMDMi 55977055.

Proteomic databases

MaxQBi P68431.
PaxDbi P68431.
PRIDEi P68431.

Protocols and materials databases

DNASUi 8350.
8352.
8353.
8355.
8356.
8357.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244661 ; ENSP00000244661 ; ENSG00000124693 .
ENST00000305910 ; ENSP00000439660 ; ENSG00000256018 .
ENST00000328488 ; ENSP00000329554 ; ENSG00000182572 .
ENST00000356476 ; ENSP00000366999 ; ENSG00000197409 .
ENST00000357647 ; ENSP00000350275 ; ENSG00000198366 .
ENST00000359303 ; ENSP00000352252 ; ENSG00000197153 .
ENST00000360408 ; ENSP00000353581 ; ENSG00000196966 .
ENST00000369163 ; ENSP00000358160 ; ENSG00000203813 .
ENST00000377831 ; ENSP00000367062 ; ENSG00000197409 .
ENST00000446824 ; ENSP00000444823 ; ENSG00000256316 .
ENST00000540144 ; ENSP00000439493 ; ENSG00000196532 .
GeneIDi 8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.
KEGGi hsa:8350.
hsa:8351.
hsa:8352.
hsa:8353.
hsa:8354.
hsa:8355.
hsa:8356.
hsa:8357.
hsa:8358.
hsa:8968.
UCSCi uc003nfp.1. human.

Organism-specific databases

CTDi 8350.
8351.
8352.
8353.
8354.
8355.
8356.
8357.
8358.
8968.
GeneCardsi GC06M026031.
GC06M026197.
GC06M026250.
GC06M026271.
GC06M027914.
GC06M027920.
GC06P026020.
GC06P026065.
GC06P026225.
GC06P027777.
HGNCi HGNC: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.
HPAi CAB037166.
CAB037178.
CAB037187.
MIMi 602810. gene.
602811. gene.
602812. gene.
602813. gene.
602814. gene.
602815. gene.
602816. gene.
602817. gene.
602818. gene.
602819. gene.
neXtProti NX_P68431.
PharmGKBi PA29148.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2036.
HOVERGENi HBG001172.
InParanoidi P68431.
KOi K11253.
OMAi TEFANEM.
OrthoDBi EOG7HB5C2.
PhylomeDBi P68431.
TreeFami TF314241.

Enzyme and pathway databases

Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_27271. Meiotic recombination.
REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSi HIST1H3F. human.
EvolutionaryTracei P68431.
GeneWikii HIST1H3A.
HIST1H3B.
HIST1H3C.
HIST1H3D.
HIST1H3E.
HIST1H3F.
HIST1H3G.
HIST1H3H.
HIST1H3I.
HIST1H3J.
NextBioi 31272.
SOURCEi Search...

Gene expression databases

Bgeei P68431.
CleanExi HS_HIST1H3A.
HS_HIST1H3B.
HS_HIST1H3C.
HS_HIST1H3D.
HS_HIST1H3E.
HS_HIST1H3F.
HS_HIST1H3G.
HS_HIST1H3H.
HS_HIST1H3I.
Genevestigatori P68431.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view ]
PANTHERi PTHR11426. PTHR11426. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00622. HISTONEH3.
SMARTi SM00428. H3. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure and expression of four cloned human histone genes."
    Zhong R., Roeder R.G., Heintz N.
    Nucleic Acids Res. 11:7409-7425(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
  2. "Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5' regulatory sequences."
    Marashi F., Helms S., Shiels A., Silverstein S., Greenspan D.S., Stein G., Stein J.
    Biochem. Cell Biol. 64:277-289(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
    Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
    Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3FD).
  4. "Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones."
    Kardalinou E., Eick S., Albig W., Doenecke D.
    J. Cell. Biochem. 52:375-383(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Expression of human histone h1.1 and the nearby core histones."
    Runge D., Eick S., Doenecke D.
    Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  6. "Characterization of the H1.5 gene completes the set of human H1 subtype genes."
    Albig W., Meergans T., Doenecke D.
    Gene 184:141-148(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
  7. "Human histone gene organization: nonregular arrangement within a large cluster."
    Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.
    Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3F AND HIST1H3G).
  8. "The human histone gene cluster at the D6S105 locus."
    Albig W., Doenecke D.
    Hum. Genet. 101:284-294(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3H AND HIST1H3J).
  9. "The human and mouse replication-dependent histone genes."
    Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
    Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J).
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Caudate nucleus, Stomach and Thymus.
  11. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  12. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  14. "Human spleen histone H3. Isolation and amino acid sequence."
    Ohe Y., Iwai K.
    J. Biochem. 90:1205-1211(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Spleen.
  15. Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37, PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY.
  16. "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation."
    Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.
    J. Biol. Chem. 274:25543-25549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, PHOSPHORYLATION AT SER-11 AND SER-29.
  17. "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins."
    Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.
    Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-10.
  18. "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
    Goto H., Yasui Y., Nigg E.A., Inagaki M.
    Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
  19. "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase."
    Preuss U., Landsberg G., Scheidtmann K.H.
    Nucleic Acids Res. 31:878-885(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.
  20. "Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1."
    Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.
    J. Biol. Chem. 279:54348-54357(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-18.
  21. Cited for: METHYLATION AT LYS-80.
  22. Cited for: CITRULLINATION AT ARG-9 AND ARG-18, METHYLATION AT ARG-18.
  23. "The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment."
    Dai J., Sultan S., Taylor S.S., Higgins J.M.G.
    Genes Dev. 19:472-488(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
  24. "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
    Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
    J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-29.
  25. "Protein identification using sequential ion/ion reactions and tandem mass spectrometry."
    Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J., Shabanowitz J., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-37 AND LYS-38, IDENTIFICATION BY MASS SPECTROMETRY.
  26. "Expression patterns and post-translational modifications associated with mammalian histone H3 variants."
    Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G., Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.
    J. Biol. Chem. 281:559-568(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
  27. "Mass spectrometric characterization of human histone H3: a bird's eye view."
    Thomas C.E., Kelleher N.L., Mizzen C.A.
    J. Proteome Res. 5:240-247(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 AND LYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY.
  28. "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
    Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
    Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  29. "Quantitative proteomic analysis of post-translational modifications of human histones."
    Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N.
    Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
  30. "Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17."
    Miao F., Li S., Chavez V., Lanting L., Natarajan R.
    Mol. Endocrinol. 20:1562-1573(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, CITRULLINATION AT ARG-18.
  31. "Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
    Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
    Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
  32. "PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation."
    Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y., Hsieh J., Bauer U.M.
    Genes Dev. 21:3369-3380(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-3 BY PRMT6.
  33. "Organismal differences in post-translational modifications in histones H3 and H4."
    Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
    J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
  34. "Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
    Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
    J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-37.
  35. "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive."
    Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M., Schuchlautz H., Luescher B., Amati B.
    Nature 449:933-937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-3 BY PRMT6.
  36. "Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression."
    Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H., Nakanishi M.
    Cell 132:221-232(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
  37. "Arginine methylation of the histone H3 tail impedes effector binding."
    Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J., Richard S., Bedford M.T.
    J. Biol. Chem. 283:3006-3010(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-3 BY PRMT6.
  38. "Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation."
    Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R.
    Nat. Cell Biol. 10:53-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-12.
  39. Cited for: ACETYLATION AT LYS-116 AND LYS-123.
  40. "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin."
    Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.
    Nature 461:819-822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-42.
  41. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
    Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
    Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
  42. Cited for: PHOSPHORYLATION AT THR-7.
  43. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
    Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
    Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
  44. "Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA."
    Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M.
    Mol. Cell 46:7-17(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-57.
  45. Cited for: ALLYSINE AT LYS-5.
  46. "Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer."
    Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.
    Cell 152:859-872(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-123.
  47. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-15 IN COMPLEX WITH YWHAZ.
  48. "Double chromodomains cooperate to recognize the methylated histone H3 tail."
    Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., Minor W., Rastinejad F., Khorasanizadeh S.
    Nature 438:1181-1185(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-20 IN COMPLEX WITH CHD1.
  49. "Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle."
    Tsunaka Y., Kajimura N., Tate S., Morikawa K.
    Nucleic Acids Res. 33:3424-3434(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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: September 3, 2014
This is version 119 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

External Data

Dasty 3

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