Reviewed,
UniProtKB/Swiss-Prot P02253 (H11_BOVIN)
Last modified
October 13, 2009.
Version 61.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Histone H1.1 Alternative name(s): CTL-1 |
| Organism | Bos taurus (Bovine) |
| Taxonomic identifier | 9913 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 104 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Histones H1 are necessary for the condensation of nucleosome chains into higher order structures. |
| Subcellular location | |
| Sequence similarities | Belongs to the histone H1/H5 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosomal protein Nucleus |
| Ligand | DNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | nucleosome assembly Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleosome Inferred from electronic annotation. Source: InterPro nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›104 | ›104 | Histone H1.1 | PRO_0000195903 | |||||
Regions | |||||||||
| Region | 35 – ›104 | ›70 | Globular | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylserine Ref.1 | ||||||
| Modified residue | 35 | 1 | Phosphoserine Potential | ||||||
| Modified residue | 84 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 103 | 1 | Phosphoserine; by PKC Ref.3 | ||||||
Experimental info | |||||||||
| Non-terminal residue | 104 | 1 | |||||||
Sequences
References
| [1] | "The amino acid sequence of residues 1-104 of CTL-1, a bovine H1 histone." Liao L.W., Cole R.D. J. Biol. Chem. 256:3024-3029(1981) [PubMed: 7204387] [Abstract] Cited for: PROTEIN SEQUENCE. |
| [2] | "Amino acid sequence and sequence variability of the amino-terminal regions of lysine-rich histones." Rall S.C., Cole R.D. J. Biol. Chem. 246:7175-7190(1971) [PubMed: 5167020] [Abstract] Cited for: AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES. |
| [3] | "Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C." Jakes S., Hastings T.G., Reimann E.M., Schlender K.K. FEBS Lett. 234:31-34(1988) [PubMed: 3134256] [Abstract] Cited for: PHOSPHORYLATION AT SER-103. |
Cross-references
Sequence databases | |
|---|---|
| IPI | IPI00699808. |
| PIR | HSBO11. A92316. |
| UniGene | Bt.85301 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GHC based on UniProtKB P08287. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000015499; ENSBTAP00000015499; ENSBTAG00000011677; Bos taurus. [Genome view] |
Phylogenomic databases | |
| HOVERGEN | P02253. |
Family and domain databases | |
| InterPro | IPR005818. Histone_H1/H5. IPR005819. Histone_H5. IPR011991. Wing_hlx_DNA_bd. [Graphical view] |
| Gene3D | G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. |
| Pfam | PF00538. Linker_histone. 1 hit. [Graphical view] |
| PRINTS | PR00624. HISTONEH5. |
| SMART | SM00526. H15. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | H11_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P02253 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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