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Protein

Histone H1.4

Gene

HIST1H1E

Organism
Homo sapiens (Human)
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

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.

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

Organism-specific databases

DisGeNETi3008.
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-succinyllysineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei54CitrullineBy similarity1
Modified residuei104PhosphoserineBy 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, Methylation, Phosphoprotein

Proteomic databases

EPDiP10412.
MaxQBiP10412.
PaxDbiP10412.
PeptideAtlasiP10412.
PRIDEiP10412.
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. 130 interactors.
IntActiP10412. 20 interactors.
MINTiMINT-1136873.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TZDX-ray1.81T19-36[»]
5JJZX-ray2.00B21-32[»]
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.
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.

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: September 27, 2017
This is version 174 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