Skip Header

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

Histone H3.2

Gene

HIST2H3A

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

  • DNA binding Source: UniProtKB-KW
  • histone binding Source: UniProtKB

GO - Biological processi

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_2204. RNA Polymerase I Chain Elongation.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_263923. HDACs deacetylate histones.
REACT_263961. HDMs demethylate histones.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264245. HATs acetylate histones.
REACT_264303. Condensation of Prophase Chromosomes.
REACT_264352. PRC2 methylates histones and DNA.
REACT_264541. SIRT1 negatively regulates rRNA Expression.
REACT_264545. RMTs methylate histone arginines.
REACT_268237. DNA methylation.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_268728. PKMTs methylate histone lysines.
REACT_27271. Meiotic recombination.
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
REACT_75925. Amyloids.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.2
Alternative name(s):
Histone H3/m
Histone H3/o
Gene namesi
AND
Name:HIST2H3C
Synonyms:H3F2, H3FM
AND
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20505. HIST2H3A.
HGNC:20503. HIST2H3C.
HGNC:25311. HIST2H3D.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148728.

Polymorphism and mutation databases

BioMutaiHIST2H3A.
DMDMi74758899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 136135Histone H3.2PRO_0000250357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternate3 Publications
Modified residuei3 – 31Citrulline; alternate1 Publication
Modified residuei4 – 41Phosphothreonine; by GSG22 Publications
Modified residuei5 – 51Allysine; alternate
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate2 Publications
Modified residuei5 – 51N6,N6-dimethyllysine; alternate2 Publications
Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
Modified residuei5 – 51N6-crotonyllysine; alternate1 Publication
Modified residuei5 – 51N6-methyllysine; alternate2 Publications
Modified residuei7 – 71Phosphothreonine; by PKC1 Publication
Modified residuei9 – 91Citrulline; alternate2 Publications
Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternateBy similarity
Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate4 Publications
Modified residuei10 – 101N6,N6-dimethyllysine; alternate4 Publications
Modified residuei10 – 101N6-acetyllysine; alternate5 Publications
Modified residuei10 – 101N6-crotonyllysine; alternate1 Publication
Modified residuei10 – 101N6-methyllysine; alternate4 Publications
Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA55 Publications
Modified residuei12 – 121Phosphothreonine; by PKC2 Publications
Modified residuei15 – 151N6-acetyllysine5 Publications
Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternate3 Publications
Modified residuei18 – 181Citrulline; alternate3 Publications
Modified residuei19 – 191N6-acetyllysine; alternate3 Publications
Modified residuei19 – 191N6-crotonyllysine; alternate1 Publication
Modified residuei19 – 191N6-methyllysine; alternate2 Publications
Modified residuei24 – 241N6-acetyllysine; alternate3 Publications
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-methyllysine; alternate1 Publication
Modified residuei27 – 271Citrulline1 Publication
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate4 Publications
Modified residuei28 – 281N6,N6-dimethyllysine; alternate4 Publications
Modified residuei28 – 281N6-acetyllysine; alternate3 Publications
Modified residuei28 – 281N6-crotonyllysine; alternate1 Publication
Modified residuei28 – 281N6-methyllysine; alternate4 Publications
Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA55 Publications
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate4 Publications
Modified residuei37 – 371N6,N6-dimethyllysine; alternate4 Publications
Modified residuei37 – 371N6-acetyllysine; alternate2 Publications
Modified residuei37 – 371N6-methyllysine; alternate4 Publications
Modified residuei38 – 381N6-methyllysineBy similarity
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; alternateBy 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 residuei87 – 871PhosphoserineBy similarity
Modified residuei108 – 1081Phosphothreonine1 Publication
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.10 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.8 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.13 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 Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.14 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

MaxQBiQ71DI3.
PaxDbiQ71DI3.
PRIDEiQ71DI3.

PTM databases

PhosphoSiteiQ71DI3.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiQ71DI3.
CleanExiHS_HIST2H3A.
HS_HIST2H3C.
HS_HIST2H3D.

Organism-specific databases

HPAiHPA042570.

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. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BPTFQ12830-42EBI-750650,EBI-4288838
LMNAP025456EBI-750650,EBI-351935
LMNAP02545-63EBI-750650,EBI-9034379

Protein-protein interaction databases

BioGridi126025. 92 interactions.
130616. 21 interactions.
575920. 4 interactions.
DIPiDIP-48606N.
IntActiQ71DI3. 10 interactions.
MINTiMINT-4828325.
STRINGi9606.ENSP00000385479.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi26 – 294Combined sources
Turni39 – 413Combined sources
Helixi46 – 5712Combined sources
Helixi65 – 7713Combined sources
Helixi87 – 11428Combined sources
Beta strandi118 – 1203Combined sources
Helixi122 – 13110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIJNMR-B121-136[»]
2X4WX-ray1.50B23-43[»]
2X4XX-ray1.85B/D/F/H23-43[»]
2X4YX-ray1.70B/D/F/H/J/L/N/P23-43[»]
3AV1X-ray2.50A/E1-136[»]
3DB3X-ray2.40B7-12[»]
3MO8X-ray1.69B31-42[»]
3QO2X-ray2.49P/Q/R/S2-16[»]
3R93X-ray2.06E/F/G/H2-16[»]
4MZFX-ray2.10A2-8[»]
4MZGX-ray1.70A/C2-21[»]
4MZHX-ray2.20B2-10[»]
4OUCX-ray1.90B2-12[»]
ProteinModelPortaliQ71DI3.
SMRiQ71DI3. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ71DI3.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiQ71DI3.
KOiK11253.
OMAiSSATHQK.
OrthoDBiEOG7HB5C2.
PhylomeDBiQ71DI3.
TreeFamiTF314241.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
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.

Q71DI3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,388
Last modified:January 23, 2007 - v3
Checksum:i6FD8508EA50A0EEC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911M → T.
Corresponds to variant rs2664732 [ dbSNP | Ensembl ].
VAR_059313
Natural varianti128 – 1281A → V.
Corresponds to variant rs2664731 [ dbSNP | Ensembl ].
VAR_059314

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF531305 Genomic DNA. No translation available.
AF531307 Genomic DNA. Translation: AAN39283.1.
AY648851 Genomic DNA. Translation: AAT68254.1.
AL591493 Genomic DNA. Translation: CAI12559.1.
AL591493 Genomic DNA. Translation: CAI12561.1.
AL591493 Genomic DNA. Translation: CAI12566.1.
BC074969 mRNA. Translation: AAH74969.2.
BC130635 mRNA. Translation: AAI30636.1.
BC130637 mRNA. Translation: AAI30638.1.
CCDSiCCDS30848.1.
CCDS30850.1.
CCDS41388.1.
RefSeqiNP_001005464.1. NM_001005464.2.
NP_001116847.1. NM_001123375.2.
NP_066403.2. NM_021059.2.
UniGeneiHs.647745.
Hs.706618.
Hs.712062.

Genome annotation databases

EnsembliENST00000331491; ENSP00000333277; ENSG00000183598.
ENST00000369158; ENSP00000358154; ENSG00000203811.
ENST00000403683; ENSP00000385479; ENSG00000203852.
GeneIDi126961.
333932.
653604.
KEGGihsa:126961.
hsa:333932.
hsa:653604.
UCSCiuc001esv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF531305 Genomic DNA. No translation available.
AF531307 Genomic DNA. Translation: AAN39283.1.
AY648851 Genomic DNA. Translation: AAT68254.1.
AL591493 Genomic DNA. Translation: CAI12559.1.
AL591493 Genomic DNA. Translation: CAI12561.1.
AL591493 Genomic DNA. Translation: CAI12566.1.
BC074969 mRNA. Translation: AAH74969.2.
BC130635 mRNA. Translation: AAI30636.1.
BC130637 mRNA. Translation: AAI30638.1.
CCDSiCCDS30848.1.
CCDS30850.1.
CCDS41388.1.
RefSeqiNP_001005464.1. NM_001005464.2.
NP_001116847.1. NM_001123375.2.
NP_066403.2. NM_021059.2.
UniGeneiHs.647745.
Hs.706618.
Hs.712062.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIJNMR-B121-136[»]
2X4WX-ray1.50B23-43[»]
2X4XX-ray1.85B/D/F/H23-43[»]
2X4YX-ray1.70B/D/F/H/J/L/N/P23-43[»]
3AV1X-ray2.50A/E1-136[»]
3DB3X-ray2.40B7-12[»]
3MO8X-ray1.69B31-42[»]
3QO2X-ray2.49P/Q/R/S2-16[»]
3R93X-ray2.06E/F/G/H2-16[»]
4MZFX-ray2.10A2-8[»]
4MZGX-ray1.70A/C2-21[»]
4MZHX-ray2.20B2-10[»]
4OUCX-ray1.90B2-12[»]
ProteinModelPortaliQ71DI3.
SMRiQ71DI3. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126025. 92 interactions.
130616. 21 interactions.
575920. 4 interactions.
DIPiDIP-48606N.
IntActiQ71DI3. 10 interactions.
MINTiMINT-4828325.
STRINGi9606.ENSP00000385479.

PTM databases

PhosphoSiteiQ71DI3.

Polymorphism and mutation databases

BioMutaiHIST2H3A.
DMDMi74758899.

Proteomic databases

MaxQBiQ71DI3.
PaxDbiQ71DI3.
PRIDEiQ71DI3.

Protocols and materials databases

DNASUi126961.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331491; ENSP00000333277; ENSG00000183598.
ENST00000369158; ENSP00000358154; ENSG00000203811.
ENST00000403683; ENSP00000385479; ENSG00000203852.
GeneIDi126961.
333932.
653604.
KEGGihsa:126961.
hsa:333932.
hsa:653604.
UCSCiuc001esv.3. human.

Organism-specific databases

CTDi126961.
333932.
653604.
GeneCardsiGC01M149784.
GC01M149812.
GC01P149824.
HGNCiHGNC:20505. HIST2H3A.
HGNC:20503. HIST2H3C.
HGNC:25311. HIST2H3D.
HPAiHPA042570.
MIMi142780. gene.
neXtProtiNX_Q71DI3.
PharmGKBiPA145148728.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiQ71DI3.
KOiK11253.
OMAiSSATHQK.
OrthoDBiEOG7HB5C2.
PhylomeDBiQ71DI3.
TreeFamiTF314241.

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169436. Oxidative Stress Induced Senescence.
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_263923. HDACs deacetylate histones.
REACT_263961. HDMs demethylate histones.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264245. HATs acetylate histones.
REACT_264303. Condensation of Prophase Chromosomes.
REACT_264352. PRC2 methylates histones and DNA.
REACT_264541. SIRT1 negatively regulates rRNA Expression.
REACT_264545. RMTs methylate histone arginines.
REACT_268237. DNA methylation.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_268728. PKMTs methylate histone lysines.
REACT_27271. Meiotic recombination.
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSiHIST2H3C. human.
EvolutionaryTraceiQ71DI3.
GeneWikiiHIST2H3C.
NextBioi81962.
PROiQ71DI3.
SOURCEiSearch...

Gene expression databases

BgeeiQ71DI3.
CleanExiHS_HIST2H3A.
HS_HIST2H3C.
HS_HIST2H3D.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
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...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "Functional characterization of a human histone gene cluster duplication."
    Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.
    Gene 342:35-40(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. Cited for: PROTEIN SEQUENCE OF 28-41, 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.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. Cited for: METHYLATION AT LYS-80.
  13. Cited for: CITRULLINATION AT ARG-9 AND ARG-18, METHYLATION AT ARG-18.
  14. "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.
  15. "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.
  16. "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; LYS-24 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. Cited for: ACETYLATION AT LYS-116 AND LYS-123.
  28. "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.
  29. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  30. "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.
  31. Cited for: PHOSPHORYLATION AT THR-7.
  32. "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.
  33. "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.
  34. Cited for: ALLYSINE AT LYS-5.
  35. "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.
  36. "Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights."
    Agez M., Chen J., Guerois R., van Heijenoort C., Thuret J.-Y., Mann C., Ochsenbein F.
    Structure 15:191-199(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 121-136 IN COMPLEX WITH ASF1.

Entry informationi

Entry nameiH32_HUMAN
AccessioniPrimary (citable) accession number: Q71DI3
Secondary accession number(s): A2BDF6, A6NFS4, Q6B053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 133 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.