Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H1.4

Gene

Hist1h1e

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • ADP binding Source: CAFA
  • AMP binding Source: CAFA
  • ATP binding Source: CAFA
  • calcium ion binding Source: CAFA
  • chromatin DNA binding Source: Ensembl
  • dATP binding Source: CAFA
  • double-stranded DNA binding Source: CAFA
  • GTP binding Source: CAFA
  • nucleotide binding Source: CAFA
  • RNA binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionDNA-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001959242 – 219Histone H1.4Add BLAST218

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei18PhosphothreonineCombined sources1
Modified residuei26N6-acetyllysine; alternateBy similarity1
Modified residuei26N6-methyllysine; alternateBy similarity1
Modified residuei34N6-succinyllysineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei54CitrullineBy similarity1
Modified residuei104PhosphoserineBy similarity1
Modified residuei146PhosphothreonineBy similarity1
Modified residuei150ADP-ribosylserineBy similarity1
Modified residuei187PhosphoserineBy similarity1

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
ADP-ribosylated on Ser-55, Ser-113 and Ser-150 in response to DNA damage.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP15865.
PRIDEiP15865.

PTM databases

iPTMnetiP15865.
PhosphoSitePlusiP15865.

Expressioni

Gene expression databases

BgeeiENSRNOG00000047459.
GenevisibleiP15865. RN.

Interactioni

Protein-protein interaction databases

BioGridi251423. 2 interactors.
IntActiP15865. 1 interactor.
STRINGi10116.ENSRNOP00000066786.

Structurei

3D structure databases

DisProtiDP00136.
ProteinModelPortaliP15865.
SMRiP15865.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 109H15PROSITE-ProRule annotationAdd BLAST74

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

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOVERGENiHBG009035.
InParanoidiP15865.
KOiK11275.
OMAiFVESKYH.
OrthoDBiEOG091G0XGD.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
PfamiView protein in Pfam
PF00538. Linker_histone. 1 hit.
PRINTSiPR00624. HISTONEH5.
SMARTiView protein in SMART
SM00526. H15. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiView protein in PROSITE
PS51504. H15. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti163 – 164Missing in AAA41327 (PubMed:2373370).Curated2

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.

Similar proteinsi

Entry informationi

Entry nameiH14_RAT
AccessioniPrimary (citable) accession number: P15865
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 126 of the entry and version 3 of the sequence. See 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