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Protein

Histone H3

Gene

hist1h3g

Organism
Xenopus laevis (African clawed frog)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3UniRule annotation
Gene namesi
Name:hist1h3gImported
Synonyms:H3lImported
OrganismiXenopus laevis (African clawed frog)Imported
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5784387. hist1h3g.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleosome coreUniRule annotation, NucleusUniRule annotationSAAS annotation

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.UniRule annotation

Protein-protein interaction databases

DIPiDIP-60191N.
IntActiQ92133. 1 interaction.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L11NMR-B2-16[»]
2L12NMR-B2-16[»]
2L1BNMR-B20-34[»]
3GL6X-ray1.90B2-10[»]
3H91X-ray1.50C/D20-34[»]
3ME9X-ray1.37C/D2-12[»]
3MEAX-ray1.26B2-12[»]
3METX-ray2.00C/D2-12[»]
3MEUX-ray1.28C/D2-14[»]
3MEVX-ray1.83C/D2-9[»]
3O7AX-ray1.67B2-12[»]
4HSUX-ray1.99C2-31[»]
4QEOX-ray2.00P2-16[»]
ProteinModelPortaliQ92133.
SMRiQ92133. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92133.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG001172.
KOiK11253.

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.

Q92133-1 [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 CGIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,374
Last modified:November 1, 1996 - v1
Checksum:i69B8368EA50A0EEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72950 Genomic DNA. Translation: CAA51455.1.
PIRiS32638.
RefSeqiNP_001091119.1. NM_001097650.1.
UniGeneiXl.79618.

Genome annotation databases

GeneIDi399088.
KEGGixla:399088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72950 Genomic DNA. Translation: CAA51455.1.
PIRiS32638.
RefSeqiNP_001091119.1. NM_001097650.1.
UniGeneiXl.79618.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L11NMR-B2-16[»]
2L12NMR-B2-16[»]
2L1BNMR-B20-34[»]
3GL6X-ray1.90B2-10[»]
3H91X-ray1.50C/D20-34[»]
3ME9X-ray1.37C/D2-12[»]
3MEAX-ray1.26B2-12[»]
3METX-ray2.00C/D2-12[»]
3MEUX-ray1.28C/D2-14[»]
3MEVX-ray1.83C/D2-9[»]
3O7AX-ray1.67B2-12[»]
4HSUX-ray1.99C2-31[»]
4QEOX-ray2.00P2-16[»]
ProteinModelPortaliQ92133.
SMRiQ92133. Positions 2-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60191N.
IntActiQ92133. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399088.
KEGGixla:399088.

Organism-specific databases

CTDi8355.
XenbaseiXB-GENE-5784387. hist1h3g.

Phylogenomic databases

HOVERGENiHBG001172.
KOiK11253.

Miscellaneous databases

EvolutionaryTraceiQ92133.

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

  1. "Evolutionary relations between histone gene clusters in the genome of Xenopus laevis."
    Schilthuis J.G., Hagenaar M., Destree O.H.J.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger."
    Wang G.G., Song J., Wang Z., Dormann H.L., Casadio F., Li H., Luo J.L., Patel D.J., Allis C.D.
    Nature 459:847-851(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-10.
  3. "Crystal structure of PHF13 in complex with Tri-methylated histone H3K4."
    Bian C.B., Xu C., Lam R., Bountra C., Arrowsmith C.H., Weigelt J., Edwards A.M., Bochkarev A., Min J.
    Submitted (JUN-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 2-12.
  4. "Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation."
    Bian C., Xu C., Ruan J., Lee K.K., Burke T.L., Tempel W., Barsyte D., Li J., Wu M., Zhou B.O., Fleharty B.E., Paulson A., Allali-Hassani A., Zhou J.Q., Mer G., Grant P.A., Workman J.L., Zang J., Min J.
    EMBO J. 30:2829-2842(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 2-12.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 20-34.
  6. "Structural insight into substrate recognition by histone demethylase LSD2/KDM1b."
    Chen F., Yang H., Dong Z., Fang J., Wang P., Zhu T., Gong W., Fang R., Shi Y.G., Li Z., Xu Y.
    Cell Res. 23:306-309(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 2-31.
  7. "Mechanism of DNA methylation-directed histone methylation by KRYPTONITE."
    Du J., Johnson L.M., Groth M., Feng S., Hale C.J., Li S., Vashisht A.A., Gallego-Bartolome J., Wohlschlegel J.A., Patel D.J., Jacobsen S.E.
    Mol. Cell 55:495-504(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-16.

Entry informationi

Entry nameiQ92133_XENLA
AccessioniPrimary (citable) accession number: Q92133
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.