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P15865 (H14_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone H1.4
Alternative name(s):
H1d
Gene names
Name:Hist1h1e
Synonyms:H1f4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length219 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.

Post-translational modification

Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1 By similarity.

H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter By similarity.

Sequence similarities

Belongs to the histone H1/H5 family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 219218Histone H1.4
PRO_0000195924

Regions

Domain36 – 10974H15

Amino acid modifications

Modified residue21N-acetylserine Ref.3
Modified residue41Phosphothreonine By similarity
Modified residue181Phosphothreonine By similarity
Modified residue261N6-acetyllysine; alternate By similarity
Modified residue261N6-methyllysine; alternate By similarity
Modified residue361Phosphoserine By similarity
Modified residue1461Phosphothreonine By similarity
Modified residue1871Phosphoserine By similarity

Experimental info

Sequence conflict163 – 1642Missing in AAA41327. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15865 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8977726B816119CC

FASTA21921,987
        10         20         30         40         50         60 
MSETAPAAPA APAPAEKTPI KKKARKAAGG AKRKASGPPV SELITKAVAA SKERSGVSLA 

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

       130        140        150        160        170        180 
KKAGAAKAKK PAGAAKKPKK ATGTATPKKS TKKTPKKAKK PAAAAGAKKA KSPKKAKATK 

       190        200        210 
AKKAPKSPAK ARAVKPKAAK PKTSKPKAAK PKKTAAKKK 

« Hide

References

« Hide 'large scale' references
[1]"A rat histone H2B pseudogene is closely associated with the histone H1d gene."
Drabent B., Kunz C., Doenecke D.
Biochim. Biophys. Acta 1172:193-196(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"Isolation of a genomic clone encoding the rat histone variant, H1d."
Cole K.D., Kandala J.C., Kremer E., Kistler W.S.
Gene 89:265-269(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]Bienvenut W.V., von Kriegsheim A.F., Kolch W.
Submitted (AUG-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 34-46 AND 55-75, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
Tissue: Pheochromocytoma.
[4]"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.
[5]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Renal collecting duct.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67320 Genomic DNA. Translation: CAA47734.1.
M31229 Genomic DNA. Translation: AAA41327.1.
IPIIPI00231650.
PIRJH0159.
RefSeqNP_579819.1. NM_133285.1.
UniGeneRn.196361.

3D structure databases

DisProtDP00136.
ProteinModelPortalP15865.
SMRP15865. Positions 36-109.
ModBaseSearch...

Protein-protein interaction databases

IntActP15865. 1 interaction.

PTM databases

PhosphoSiteP15865.

Proteomic databases

PRIDEP15865.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000072564; ENSRNOP00000066786; ENSRNOG00000047459.
GeneID201097.
KEGGrno:201097.

Organism-specific databases

CTD3007.

Phylogenomic databases

GeneTreeENSGT00670000097781.
HOVERGENHBG009035.
KOK11275.

Gene expression databases

GenevestigatorP15865.

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

NextBio623093.

Entry information

Entry nameH14_RAT
AccessionPrimary (citable) accession number: P15865
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 92 of the entry and version 3 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