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P02253 (H11_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 75. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.1
Alternative name(s):
CTL-1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length104 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histones H1 are necessary for the condensation of nucleosome chains into higher order structures.

Subcellular location

Nucleus. Chromosome.

Sequence similarities

Belongs to the histone H1/H5 family.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleosome

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›104›104Histone H1.1
PRO_0000195903

Regions

Domain35 – 10470H15

Amino acid modifications

Modified residue11N-acetylserine Ref.1
Modified residue351Phosphoserine Potential
Modified residue841N6-acetyllysine By similarity
Modified residue1031Phosphoserine; by PKC Ref.3

Experimental info

Non-terminal residue1041

Sequences

Sequence LengthMass (Da)Tools
P02253 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 801BF289751E41B2

FASTA10410,365
        10         20         30         40         50         60 
SETAPAAPAA APPAEKTPVK KKAAKKPAGA RRKASGPPVS ELITKAVAAS KERSGVSLAA 

        70         80         90        100 
LKKALAAAGY DVEKNNSRIK LGLKSLVSKG TLVQTKGTGA SGSF 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

IPIIPI00699808.
PIRHSBO11. A92316.
UniGeneBt.2728.

3D structure databases

ProteinModelPortalP02253.
SMRP02253. Positions 35-104.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1519695.

Proteomic databases

PRIDEP02253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG21104.
GeneTreeENSGT00550000074201.
HOVERGENHBG009035.
InParanoidP02253.

Family and domain databases

InterProIPR005818. Histone_H1/H5.
IPR005819. Histone_H5.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 1 hit.
[Graphical view]
PROSITEPS51504. H15. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH11_BOVIN
AccessionPrimary (citable) accession number: P02253
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 21, 2011
This is version 75 of the entry and version 1 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