P15796 · H12_CAEEL

Function

function

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

Miscellaneous

H1.2 is a minor form.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleosome
Cellular Componentnucleus
Molecular Functiondouble-stranded DNA binding
Molecular Functionnucleosomal DNA binding
Molecular Functionstructural constituent of chromatin
Biological Processchromosome condensation
Biological Processnegative regulation of DNA recombination
Biological Processnucleosome assembly

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Histone H1.2
  • Alternative names
    • Histone H1-like protein 2

Gene names

    • Name
      hil-2
    • ORF names
      Y73B6BL.9

Organism names

  • Taxonomic identifier
  • Strains
    • Bristol N2
    • him-8
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    P15796
  • Secondary accessions
    • O18649
    • Q8IU03
    • Q8MXR7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00001959822-191Histone H1.2

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-35Disordered
Domain37-113H15
Region116-191Disordered
Compositional bias129-150Basic and acidic residues
Compositional bias151-181Basic residues

Sequence similarities

Belongs to the histone H1/H5 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P15796-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    191
  • Mass (Da)
    19,779
  • Last updated
    2007-01-23 v3
  • Checksum
    927F7C2BD4C70864
MSDVTVAETPAVKTPTKAPKAPKSKTTKEPKAKVAAAHPPFINMVTAAISSLKERKGSSKIAILKYITANYKVGDQLTKINSRLRAALNKGVASKALVQSVGNGASGRFRVAEKAAATKKPVAKKPVAKKAATGEKKAKKTTVAKKTGDKVKKAKSPKKIAKPAAKKVAKSPAKKAAPKKAPAKKAAAPKA

P15796-2

  • Name
    b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict28in Ref. 3; AA sequence
Sequence conflict31-32in Ref. 3; AA sequence
Sequence conflict45-51in Ref. 3; AA sequence
Alternative sequenceVSP_01175949-116in isoform b
Sequence conflict79in Ref. 3; AA sequence
Sequence conflict112in Ref. 3; AA sequence
Compositional bias129-150Basic and acidic residues
Compositional bias151-181Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF017812
EMBL· GenBank· DDBJ
AAB70559.1
EMBL· GenBank· DDBJ
Genomic DNA
AF017811
EMBL· GenBank· DDBJ
AAB70666.1
EMBL· GenBank· DDBJ
mRNA
FO081731
EMBL· GenBank· DDBJ
CCD74158.2
EMBL· GenBank· DDBJ
Genomic DNA
FO081731
EMBL· GenBank· DDBJ
CCD74159.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp