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Q92133 (Q92133_XENLA) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone H3 RuleBase RU004471
Gene names
Name:H3l EMBL CAA51455.1
OrganismXenopus laevis (African clawed frog) EMBL CAA51455.1
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity. RuleBase RU004471

Sequence similarities

Belongs to the histone H3 family. RuleBase RU004471

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core RuleBase RU004471
Nucleus RuleBase RU004471 SAAS SAAS000164
   LigandDNA-binding
   Technical term3D-structure PDB 4HSU PDB 2L11 PDB 3GL6 PDB 2L12 PDB 2L1B PDB 3O7A
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue51N6,N6,N6-trimethyllysine
Modified residue101N6,N6,N6-trimethyllysine PDB 2L11 PDB 2L12
Modified residue281N6,N6,N6-trimethyllysine PDB 2L1B

Sequences

Sequence LengthMass (Da)Tools
Q92133 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 69B8368EA50A0EEC

FASTA13615,374
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CGIHAKRVTI 

       130 
MPKDIQLARR IRGERA

« Hide

References

[1]"Evolutionary relations between histone gene clusters in the genome of Xenopus laevis."
Schilthuis J.G., Hagenaar M., Destree O.H.J.
Submitted (MAR-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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-10, METHYLATION AT LYS-5.
[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 (JUL-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 2-12, METHYLATION AT LYS-5.
[4]"Recognition and specificity determinants of the human cbx chromodomains."
Kaustov L., Ouyang H., Amaya M., Lemak A., Nady N., Duan S., Wasney G.A., Li Z., Vedadi M., Schapira M., Min J., Arrowsmith C.H.
J. Biol. Chem. 286:521-529(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 20-34, METHYLATION AT LYS-10 AND LYS-28.
[5]"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(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 2-31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X72950 Genomic DNA. Translation: CAA51455.1.
PIRS32638.
RefSeqNP_001091119.1. NM_001097650.1.
UniGeneXl.79618.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L11NMR-B2-16[»]
2L12NMR-B2-16[»]
2L1BNMR-B20-34[»]
3GL6X-ray1.90B2-10[»]
3O7AX-ray1.67B2-12[»]
4HSUX-ray1.99C2-31[»]
ProteinModelPortalQ92133.
SMRQ92133. Positions 2-136.
ModBaseSearch...

Protein-protein interaction databases

IntActQ92133. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399088.
KEGGxla:399088.

Organism-specific databases

CTD8355.

Phylogenomic databases

HOVERGENHBG001172.
KOK11253.

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. Histone-fold. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ92133.

Entry information

Entry nameQ92133_XENLA
AccessionPrimary (citable) accession number: Q92133
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: May 29, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info