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Protein

Histone H1.4

Gene

HIST1H1E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

This variant accounts for 60% of histone H1.

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-211227 Activation of DNA fragmentation factor
R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.4
Alternative name(s):
Histone H1b
Histone H1s-4
Gene namesi
Name:HIST1H1E
Synonyms:H1F4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000168298.6
HGNCiHGNC:4718 HIST1H1E
MIMi142220 gene
neXtProtiNX_P10412

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

Pathology & Biotechi

Involvement in diseasei

Rahman syndrome (RMNS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant syndrome characterized by intellectual disability and overgrowth manifesting as increased birth length, height, weight, and/or head circumference.
See also OMIM:617537

Keywords - Diseasei

Mental retardation

Organism-specific databases

DisGeNETi3008
MalaCardsiHIST1H1E
MIMi617537 phenotype
OpenTargetsiENSG00000168298
PharmGKBiPA29096

Polymorphism and mutation databases

BioMutaiHIST1H1E
DMDMi121919

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001959082 – 219Histone H1.4Add BLAST218

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei18PhosphothreonineCombined sources1
Modified residuei26N6-acetyllysine; alternate1 Publication1
Modified residuei26N6-methyllysine; alternate1 Publication1
Modified residuei34N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei34N6-succinyllysine; alternateBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei52N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei54CitrullineBy similarity1
Modified residuei64N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei85N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei90N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei106N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei146PhosphothreonineCombined sources1
Modified residuei150ADP-ribosylserine1 Publication1
Modified residuei187PhosphoserineCombined sources1

Post-translational modificationi

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
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.1 Publication
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-150 in response to DNA damage.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP10412
MaxQBiP10412
PaxDbiP10412
PeptideAtlasiP10412
PRIDEiP10412
ProteomicsDBi52602
TopDownProteomicsiP10412

PTM databases

iPTMnetiP10412
PhosphoSitePlusiP10412
SwissPalmiP10412

Expressioni

Gene expression databases

BgeeiENSG00000168298
CleanExiHS_HIST1H1E
ExpressionAtlasiP10412 baseline and differential
GenevisibleiP10412 HS

Organism-specific databases

HPAiCAB011506
HPA055907

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi109263, 133 interactors
IntActiP10412, 23 interactors
MINTiP10412
STRINGi9606.ENSP00000307705

Structurei

Secondary structure

1219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 25Combined sources6

3D structure databases

ProteinModelPortaliP10412
SMRiP10412
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.By similarity

Sequence similaritiesi

Belongs to the histone H1/H5 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4012 Eukaryota
ENOG4112541 LUCA
GeneTreeiENSGT00670000097781
HOGENOMiHOG000251627
HOVERGENiHBG009035
InParanoidiP10412
KOiK11275
OMAiFVESKYH
OrthoDBiEOG091G0XGD
PhylomeDBiP10412
TreeFamiTF313664

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR005818 Histone_H1/H5_H15
IPR005819 Histone_H5
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
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.

P10412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA
60 70 80 90 100
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG
110 120 130 140 150
ASGSFKLNKK AASGEAKPKA KKAGAAKAKK PAGAAKKPKK ATGAATPKKS
160 170 180 190 200
AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK PKKAPKSPAK AKAVKPKAAK
210
PKTAKPKAAK PKKAAAKKK
Length:219
Mass (Da):21,865
Last modified:January 23, 2007 - v2
Checksum:i1720FECCCBEBCC7F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036203128A → V in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs768731472Ensembl.1
Natural variantiVAR_049307152K → R. Corresponds to variant dbSNP:rs2298090Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60748 Genomic DNA Translation: AAA63187.1
AF531302 Genomic DNA Translation: AAN06702.1
AL353759 Genomic DNA No translation available.
BC096168 mRNA Translation: AAH96168.1
BC096169 mRNA Translation: AAH96169.1
BC099632 mRNA Translation: AAH99632.1
CCDSiCCDS4586.1
PIRiC40335 HSHU1B
RefSeqiNP_005312.1, NM_005321.2
UniGeneiHs.248133

Genome annotation databases

EnsembliENST00000304218; ENSP00000307705; ENSG00000168298
GeneIDi3008
KEGGihsa:3008
UCSCiuc003ngq.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiH14_HUMAN
AccessioniPrimary (citable) accession number: P10412
Secondary accession number(s): Q4VB25
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 182 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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