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P68432

- H31_BOVIN

UniProt

P68432 - H31_BOVIN

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Protein
Histone H3.1
Gene
N/A
Organism
Bos taurus (Bovine)
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

GO - Biological processi

  1. nucleosome assembly Source: InterPro
  2. regulation of gene silencing Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_203215. Senescence-Associated Secretory Phenotype (SASP).
REACT_206540. Amyloids.
REACT_207393. PRC2 methylates histones and DNA.
REACT_207666. Condensation of Prophase Chromosomes.
REACT_209769. Meiotic recombination.
REACT_211838. RNA Polymerase I Promoter Opening.
REACT_214253. NoRC negatively regulates rRNA expression.
REACT_215067. Factors involved in megakaryocyte development and platelet production.
REACT_217942. SIRT1 negatively regulates rRNA Expression.
REACT_219482. HATs acetylate histones.
REACT_222355. formation of the beta-catenin:TCF transactivating complex.
REACT_225163. RNA Polymerase I Chain Elongation.
REACT_225657. Oxidative Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 23

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 136135Histone H3.1
PRO_0000221256Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residuei3 – 31Citrulline; alternate By similarity
Modified residuei4 – 41Phosphothreonine By similarity
Modified residuei5 – 51Allysine; alternate By similarity
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei5 – 51N6,N6-dimethyllysine; alternate By similarity
Modified residuei5 – 51N6-acetyllysine; alternate By similarity
Modified residuei5 – 51N6-crotonyllysine; alternate By similarity
Modified residuei5 – 51N6-methyllysine; alternate By similarity
Modified residuei7 – 71Phosphothreonine; by PKC By similarity
Modified residuei9 – 91Citrulline; alternate By similarity
Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei10 – 101N6,N6-dimethyllysine; alternate1 Publication
Modified residuei10 – 101N6-acetyllysine; alternate By similarity
Modified residuei10 – 101N6-crotonyllysine; alternate By similarity
Modified residuei10 – 101N6-methyllysine; alternate1 Publication
Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA51 Publication
Modified residuei12 – 121Phosphothreonine; by PKC and CHEK1 By similarity
Modified residuei15 – 151N6-acetyllysine1 Publication
Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternate By similarity
Modified residuei18 – 181Citrulline; alternate By similarity
Modified residuei19 – 191N6-acetyllysine; alternate By similarity
Modified residuei19 – 191N6-crotonyllysine; alternate By similarity
Modified residuei19 – 191N6-methyllysine; alternate By similarity
Modified residuei24 – 241N6-acetyllysine; alternate1 Publication
Modified residuei24 – 241N6-crotonyllysine; alternate By similarity
Modified residuei24 – 241N6-methyllysine; alternate By similarity
Modified residuei27 – 271Citrulline By similarity
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei28 – 281N6,N6-dimethyllysine; alternate1 Publication
Modified residuei28 – 281N6-acetyllysine; alternate By similarity
Modified residuei28 – 281N6-crotonyllysine; alternate By similarity
Modified residuei28 – 281N6-methyllysine; alternate1 Publication
Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA51 Publication
Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei37 – 371N6,N6-dimethyllysine; alternate By similarity
Modified residuei37 – 371N6-acetyllysine; alternate By similarity
Modified residuei37 – 371N6-methyllysine; alternate By similarity
Modified residuei38 – 381N6-methyllysine By similarity
Modified residuei42 – 421Phosphotyrosine By similarity
Modified residuei57 – 571N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei57 – 571N6-acetyllysine; alternate By similarity
Modified residuei57 – 571N6-crotonyllysine; alternate By similarity
Modified residuei57 – 571N6-methyllysine; by EHMT2; alternate By similarity
Modified residuei58 – 581Phosphoserine By similarity
Modified residuei65 – 651N6-methyllysine By similarity
Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residuei80 – 801N6,N6-dimethyllysine; alternate By similarity
Modified residuei80 – 801N6-acetyllysine; alternate By similarity
Modified residuei80 – 801N6-methyllysine; alternate By similarity
Modified residuei81 – 811Phosphothreonine By similarity
Modified residuei108 – 1081Phosphothreonine By similarity
Modified residuei116 – 1161N6-acetyllysine By similarity
Modified residuei123 – 1231N6-acetyllysine; alternate By similarity
Modified residuei123 – 1231N6-methyllysine; alternate By similarity

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 By similarity.1 Publication
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription By similarity.
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 By similarity.
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 By similarity.1 Publication
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 By similarity.1 Publication
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. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity.
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 By similarity.
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 By similarity.

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP68432.
PRIDEiP68432.

Expressioni

Developmental stagei

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

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
SUV39H1O434632EBI-79764,EBI-349968From a different organism.

Protein-protein interaction databases

BioGridi619877. 1 interaction.
IntActiP68432. 9 interactions.
STRINGi9913.ENSBTAP00000050291.

Structurei

3D structure databases

ProteinModelPortaliP68432.
SMRiP68432. Positions 17-136.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00740000114849.
HOGENOMiHOG000155290.
HOVERGENiHBG001172.
InParanoidiP68432.
KOiK11253.
OMAiQKEMART.
OrthoDBiEOG7HB5C2.
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.

P68432-1 [UniParc]FASTAAdd to Basket

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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 databases

PIRiA02624. HSBO3.
RefSeqiXP_002697506.1. XM_002697460.2.
XP_002697557.1. XM_002697511.2.
XP_002697575.1. XM_002697529.2.
XP_005196701.1. XM_005196644.1.
XP_005196705.1. XM_005196648.1.
XP_005196706.1. XM_005196649.1.
XP_005223855.1. XM_005223798.1.
XP_005223856.1. XM_005223799.1.
XP_595303.1. XM_595303.2.
XP_874006.1. XM_868913.2.

Genome annotation databases

EnsembliENSBTAT00000033364; ENSBTAP00000051709; ENSBTAG00000024175.
ENSBTAT00000033374; ENSBTAP00000047915; ENSBTAG00000024184.
ENSBTAT00000033376; ENSBTAP00000053020; ENSBTAG00000024186.
ENSBTAT00000044972; ENSBTAP00000048362; ENSBTAG00000031717.
ENSBTAT00000044975; ENSBTAP00000052244; ENSBTAG00000031721.
ENSBTAT00000045036; ENSBTAP00000051924; ENSBTAG00000031759.
ENSBTAT00000045041; ENSBTAP00000048719; ENSBTAG00000031761.
ENSBTAT00000045045; ENSBTAP00000049208; ENSBTAG00000031766.
ENSBTAT00000045050; ENSBTAP00000051492; ENSBTAG00000031773.
ENSBTAT00000047042; ENSBTAP00000044281; ENSBTAG00000033117.
GeneIDi101908845.
517139.
523214.
525511.
616800.
788250.
KEGGibta:101908845.
bta:517139.
bta:523214.
bta:525511.
bta:616800.
bta:788250.

Cross-referencesi

Sequence databases

PIRi A02624. HSBO3.
RefSeqi XP_002697506.1. XM_002697460.2.
XP_002697557.1. XM_002697511.2.
XP_002697575.1. XM_002697529.2.
XP_005196701.1. XM_005196644.1.
XP_005196705.1. XM_005196648.1.
XP_005196706.1. XM_005196649.1.
XP_005223855.1. XM_005223798.1.
XP_005223856.1. XM_005223799.1.
XP_595303.1. XM_595303.2.
XP_874006.1. XM_868913.2.

3D structure databases

ProteinModelPortali P68432.
SMRi P68432. Positions 17-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 619877. 1 interaction.
IntActi P68432. 9 interactions.
STRINGi 9913.ENSBTAP00000050291.

Proteomic databases

PaxDbi P68432.
PRIDEi P68432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000033364 ; ENSBTAP00000051709 ; ENSBTAG00000024175 .
ENSBTAT00000033374 ; ENSBTAP00000047915 ; ENSBTAG00000024184 .
ENSBTAT00000033376 ; ENSBTAP00000053020 ; ENSBTAG00000024186 .
ENSBTAT00000044972 ; ENSBTAP00000048362 ; ENSBTAG00000031717 .
ENSBTAT00000044975 ; ENSBTAP00000052244 ; ENSBTAG00000031721 .
ENSBTAT00000045036 ; ENSBTAP00000051924 ; ENSBTAG00000031759 .
ENSBTAT00000045041 ; ENSBTAP00000048719 ; ENSBTAG00000031761 .
ENSBTAT00000045045 ; ENSBTAP00000049208 ; ENSBTAG00000031766 .
ENSBTAT00000045050 ; ENSBTAP00000051492 ; ENSBTAG00000031773 .
ENSBTAT00000047042 ; ENSBTAP00000044281 ; ENSBTAG00000033117 .
GeneIDi 101908845.
517139.
523214.
525511.
616800.
788250.
KEGGi bta:101908845.
bta:517139.
bta:523214.
bta:525511.
bta:616800.
bta:788250.

Organism-specific databases

CTDi 8351.
8352.
8353.
8354.
8355.

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00740000114849.
HOGENOMi HOG000155290.
HOVERGENi HBG001172.
InParanoidi P68432.
KOi K11253.
OMAi QKEMART.
OrthoDBi EOG7HB5C2.
TreeFami TF314241.

Enzyme and pathway databases

Reactomei REACT_203215. Senescence-Associated Secretory Phenotype (SASP).
REACT_206540. Amyloids.
REACT_207393. PRC2 methylates histones and DNA.
REACT_207666. Condensation of Prophase Chromosomes.
REACT_209769. Meiotic recombination.
REACT_211838. RNA Polymerase I Promoter Opening.
REACT_214253. NoRC negatively regulates rRNA expression.
REACT_215067. Factors involved in megakaryocyte development and platelet production.
REACT_217942. SIRT1 negatively regulates rRNA Expression.
REACT_219482. HATs acetylate histones.
REACT_222355. formation of the beta-catenin:TCF transactivating complex.
REACT_225163. RNA Polymerase I Chain Elongation.
REACT_225657. Oxidative Stress Induced Senescence.

Miscellaneous databases

NextBioi 20872386.

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

  1. "Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete amino acid sequence of calf thymus histone 3."
    Delange R.J., Hooper J.A., Smith E.L.
    J. Biol. Chem. 248:3261-3274(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-136, ACETYLATION AT LYS-15 AND LYS-24, METHYLATION AT LYS-10 AND LYS-28.
    Tissue: Thymus.
  2. "Histone III. VI. Two forms of calf thymus histone III."
    Patthy L., Smith E.L.
    J. Biol. Chem. 250:1919-1920(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-136.
    Tissue: Thymus.
  3. "Histone 3. I. Isolation and sequences of the tryptic peptides from the maleylated calf thymus protein."
    Delange R.J., Smith E.L.
    J. Biol. Chem. 248:3248-3254(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Thymus.
  4. "Histone 3. II. Isolation and sequences of chymotryptic peptides from calf thymus histone 3."
    Hooper J.A., Smith E.L.
    J. Biol. Chem. 248:3255-3260(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Thymus.
  5. "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: PHOSPHORYLATION AT SER-11 AND SER-29.

Entry informationi

Entry nameiH31_BOVIN
AccessioniPrimary (citable) accession number: P68432
Secondary accession number(s): P02295, P02296, P16106
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This histone is only present in mammals.

Caution

Disulfide bonds have been reported but this may not be physiologically relevant (1 Publication).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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