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P68432 (H31_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus. Chromosome.

Developmental stage

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

Post-translational modification

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. Ref.1

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. Ref.1

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. Ref.5

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.

Miscellaneous

This histone is only present in mammals.

Sequence similarities

Belongs to the histone H3 family.

Caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2
Chain2 – 136135Histone H3.1
PRO_0000221256

Amino acid modifications

Modified residue31Asymmetric dimethylarginine; by PRMT6; alternate By similarity
Modified residue31Citrulline; alternate By similarity
Modified residue41Phosphothreonine By similarity
Modified residue51Allysine; alternate By similarity
Modified residue51N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue51N6,N6-dimethyllysine; alternate By similarity
Modified residue51N6-acetyllysine; alternate By similarity
Modified residue51N6-crotonyllysine; alternate By similarity
Modified residue51N6-methyllysine; alternate By similarity
Modified residue71Phosphothreonine; by PKC By similarity
Modified residue91Citrulline; alternate By similarity
Modified residue91Symmetric dimethylarginine; by PRMT5; alternate By similarity
Modified residue101N6,N6,N6-trimethyllysine; alternate Ref.1
Modified residue101N6,N6-dimethyllysine; alternate Ref.1
Modified residue101N6-acetyllysine; alternate By similarity
Modified residue101N6-crotonyllysine; alternate By similarity
Modified residue101N6-methyllysine; alternate Ref.1
Modified residue111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 Ref.5
Modified residue121Phosphothreonine; by PKC and CHEK1 By similarity
Modified residue151N6-acetyllysine Ref.1
Modified residue181Asymmetric dimethylarginine; by CARM1; alternate By similarity
Modified residue181Citrulline; alternate By similarity
Modified residue191N6-acetyllysine; alternate By similarity
Modified residue191N6-crotonyllysine; alternate By similarity
Modified residue191N6-methyllysine; alternate By similarity
Modified residue241N6-acetyllysine; alternate Ref.1
Modified residue241N6-crotonyllysine; alternate By similarity
Modified residue241N6-methyllysine; alternate By similarity
Modified residue271Citrulline By similarity
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.1
Modified residue281N6,N6-dimethyllysine; alternate Ref.1
Modified residue281N6-acetyllysine; alternate By similarity
Modified residue281N6-crotonyllysine; alternate By similarity
Modified residue281N6-methyllysine; alternate Ref.1
Modified residue291Phosphoserine; by AURKB, AURKC and RPS6KA5 Ref.5
Modified residue371N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue371N6,N6-dimethyllysine; alternate By similarity
Modified residue371N6-acetyllysine; alternate By similarity
Modified residue371N6-methyllysine; alternate By similarity
Modified residue381N6-methyllysine By similarity
Modified residue421Phosphotyrosine By similarity
Modified residue571N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue571N6-acetyllysine; alternate By similarity
Modified residue571N6-crotonyllysine; alternate By similarity
Modified residue571N6-methyllysine; by EHMT2; alternate By similarity
Modified residue581Phosphoserine By similarity
Modified residue651N6-methyllysine By similarity
Modified residue801N6,N6,N6-trimethyllysine; alternate By similarity
Modified residue801N6,N6-dimethyllysine; alternate By similarity
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-methyllysine; alternate By similarity
Modified residue811Phosphothreonine By similarity
Modified residue1081Phosphothreonine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine; alternate By similarity
Modified residue1231N6-methyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P68432 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9B89008EA50A0EF6

FASTA13615,404
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

« Hide

References

[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.

Cross-references

Sequence databases

PIRHSBO3. A02624.
RefSeqXP_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

ProteinModelPortalP68432.
SMRP68432. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid619877. 1 interaction.
IntActP68432. 9 interactions.
STRING9913.ENSBTAP00000050291.

Proteomic databases

PaxDbP68432.
PRIDEP68432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000033364; 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.
GeneID101908845.
517139.
523214.
525511.
616800.
788250.
KEGGbta:101908845.
bta:517139.
bta:523214.
bta:525511.
bta:616800.
bta:788250.

Organism-specific databases

CTD8351.
8352.
8353.
8354.
8355.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00740000114849.
HOGENOMHOG000155290.
HOVERGENHBG001172.
InParanoidP68432.
KOK11253.
OMAQKEMART.
OrthoDBEOG7HB5C2.
TreeFamTF314241.

Enzyme and pathway databases

ReactomeREACT_214934. Cell Cycle.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20872386.

Entry information

Entry nameH31_BOVIN
AccessionPrimary (citable) accession number: P68432
Secondary accession number(s): P02295, P02296, P16106
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families