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P02253 (H12_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. 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 H1.2
Alternative name(s):
CTL-1
Gene names
Name:HIST1H1C
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation By similarity.

Subcellular location

Nucleus. Chromosome. Note: Mainly localizes in euchromatin By similarity.

Domain

The C-terminal domain is required for high-affinity binding to chromatin By similarity.

Post-translational modification

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.

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
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   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

Initiator methionine11Removed Ref.3
Chain2 – 213212Histone H1.2
PRO_0000195903

Regions

Domain36 – 10974H15

Amino acid modifications

Modified residue21N-acetylserine
Modified residue21N-acetylserine; partial By similarity
Modified residue21Phosphoserine By similarity
Modified residue341N6-crotonyl-L-lysine; alternate By similarity
Modified residue341N6-methyllysine; alternate By similarity
Modified residue641N6-crotonyl-L-lysine By similarity
Modified residue851N6-crotonyl-L-lysine By similarity
Modified residue901N6-crotonyl-L-lysine By similarity
Modified residue971N6-crotonyl-L-lysine By similarity
Modified residue1041Phosphoserine; by PKC Ref.5
Modified residue1461Phosphothreonine By similarity
Modified residue1591N6-crotonyl-L-lysine By similarity
Modified residue1681N6-crotonyl-L-lysine By similarity
Modified residue1871N6-methyllysine; by EHMT1 and EHMT2 By similarity
Cross-link17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P02253 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: B5D69F890B6FB5DD

FASTA21321,356
        10         20         30         40         50         60 
MSETAPAAPA AAPPAEKTPV KKKAAKKPAG ARRKASGPPV SELITKAVAA SKERSGVSLA 

        70         80         90        100        110        120 
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AATGEAKPKA 

       130        140        150        160        170        180 
KKAGAAKPKK AAGAAKKTKK ATGAATPKKT AKKTPKKAKK PAAAAVTKKV AKSPKKAKAA 

       190        200        210 
KPKKAAKSAA KAVKPKAAKP KVAKPKKAAP KKK 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of taurine cattle: a window to ruminant biology and evolution."
The bovine genome sequencing and analysis consortium
Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hereford.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal cerebellum.
[3]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-105.
[4]"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] [Europe PMC] [Abstract]
Cited for: AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
[5]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-104.
[6]"A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences."
Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.
Protein Sci. 3:575-587(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DAAA02055500 Genomic DNA. No translation available.
BC133454 mRNA. Translation: AAI33455.1.
IPIIPI00699808.
PIRHSBO11. A92316.
RefSeqNP_001076894.1. NM_001083425.1.
UniGeneBt.2728.

3D structure databases

ProteinModelPortalP02253.
SMRP02253. Positions 36-109.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1519695.
STRING9913.ENSBTAP00000015499.

Proteomic databases

PaxDbP02253.
PRIDEP02253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000015499; ENSBTAP00000015499; ENSBTAG00000011677.
GeneID513971.
KEGGbta:513971.

Organism-specific databases

CTD3006.

Phylogenomic databases

eggNOGNOG258621.
GeneTreeENSGT00670000097781.
HOVERGENHBG009035.
InParanoidP02253.
KOK11275.
OMAMSETAPX.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR005818. Histone_H1/H5.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 1 hit.
[Graphical view]
PROSITEPS51504. H15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20871120.

Entry information

Entry nameH12_BOVIN
AccessionPrimary (citable) accession number: P02253
Secondary accession number(s): A3KN02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 3, 2012
Last modified: May 1, 2013
This is version 85 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