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Protein

Histone H1.4

Gene

Hist1h1e

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.4
Alternative name(s):
H1d
Gene namesi
Name:Hist1h1e
Synonyms:H1f4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 219218Histone H1.4PRO_0000195924Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei18 – 181PhosphothreonineCombined sources
Modified residuei26 – 261N6-acetyllysine; alternateBy similarity
Modified residuei26 – 261N6-methyllysine; alternateBy similarity
Modified residuei34 – 341N6-succinyllysineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei54 – 541CitrullineBy similarity
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei146 – 1461PhosphothreonineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity

Post-translational modificationi

Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1 (By similarity).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
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.By similarity

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP15865.
PRIDEiP15865.

PTM databases

iPTMnetiP15865.
PhosphoSiteiP15865.

Expressioni

Gene expression databases

GenevisibleiP15865. RN.

Interactioni

Protein-protein interaction databases

BioGridi251423. 2 interactions.
IntActiP15865. 1 interaction.
STRINGi10116.ENSRNOP00000066786.

Structurei

3D structure databases

DisProtiDP00136.
ProteinModelPortaliP15865.
SMRiP15865. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15PROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the histone H1/H5 family.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOVERGENiHBG009035.
InParanoidiP15865.
KOiK11275.
OrthoDBiEOG74TX2T.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15865-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAPAAPA APAPAEKTPI KKKARKAAGG AKRKASGPPV SELITKAVAA
60 70 80 90 100
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG
110 120 130 140 150
ASGSFKLNKK AASGEAKPKA KKAGAAKAKK PAGAAKKPKK ATGTATPKKS
160 170 180 190 200
TKKTPKKAKK PAAAAGAKKA KSPKKAKATK AKKAPKSPAK ARAVKPKAAK
210
PKTSKPKAAK PKKTAAKKK
Length:219
Mass (Da):21,987
Last modified:January 23, 2007 - v3
Checksum:i8977726B816119CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1642Missing in AAA41327 (PubMed:2373370).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67320 Genomic DNA. Translation: CAA47734.1.
M31229 Genomic DNA. Translation: AAA41327.1.
PIRiJH0159.
RefSeqiNP_579819.1. NM_133285.1.
UniGeneiRn.196361.

Genome annotation databases

EnsembliENSRNOT00000072564; ENSRNOP00000066786; ENSRNOG00000047459.
GeneIDi201097.
KEGGirno:201097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67320 Genomic DNA. Translation: CAA47734.1.
M31229 Genomic DNA. Translation: AAA41327.1.
PIRiJH0159.
RefSeqiNP_579819.1. NM_133285.1.
UniGeneiRn.196361.

3D structure databases

DisProtiDP00136.
ProteinModelPortaliP15865.
SMRiP15865. Positions 36-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251423. 2 interactions.
IntActiP15865. 1 interaction.
STRINGi10116.ENSRNOP00000066786.

PTM databases

iPTMnetiP15865.
PhosphoSiteiP15865.

Proteomic databases

PaxDbiP15865.
PRIDEiP15865.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000072564; ENSRNOP00000066786; ENSRNOG00000047459.
GeneIDi201097.
KEGGirno:201097.

Organism-specific databases

CTDi3007.

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOVERGENiHBG009035.
InParanoidiP15865.
KOiK11275.
OrthoDBiEOG74TX2T.

Miscellaneous databases

PROiP15865.

Gene expression databases

GenevisibleiP15865. RN.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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 maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiH14_RAT
AccessioniPrimary (citable) accession number: P15865
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.