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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

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168298-MONOMER.
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

HGNCiHGNC:4718. HIST1H1E.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear heterochromatin Source: UniProtKB
  • nucleosome Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

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-acetyllysine; alternateBy similarity1
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei18PhosphothreonineCombined sources1
Modified residuei26N6-acetyllysine; alternate1 Publication1
Modified residuei26N6-methyllysine; alternate1 Publication1
Modified residuei34N6-methyllysine; alternateBy similarity1
Modified residuei34N6-succinyllysine; alternateBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei46N6-acetyllysineBy similarity1
Modified residuei54CitrullineBy similarity1
Modified residuei75N6-acetyllysineBy similarity1
Modified residuei90N6-acetyllysineBy similarity1
Modified residuei97N6-succinyllysineBy similarity1
Modified residuei104PhosphoserineBy similarity1
Modified residuei146PhosphothreonineCombined sources1
Modified residuei154PhosphothreonineBy similarity1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei172PhosphoserineBy similarity1
Modified residuei186N6-methyllysineBy similarity1
Modified residuei187PhosphoserineCombined sources1
Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

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

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

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

WithEntry#Exp.IntActNotes
L3MBTL1Q9Y4687EBI-358163,EBI-1265089
NCK1P163332EBI-358163,EBI-389883

Protein-protein interaction databases

BioGridi109263. 112 interactors.
IntActiP10412. 19 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
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

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

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.

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 rs768731472dbSNPEnsembl.1
Natural variantiVAR_049307152K → R.Corresponds to variant rs2298090dbSNPEnsembl.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. Translation: CAC04132.1.
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

Cross-referencesi

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. Translation: CAC04132.1.
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.

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...

Protein-protein interaction databases

BioGridi109263. 112 interactors.
IntActiP10412. 19 interactors.
MINTiMINT-1136873.
STRINGi9606.ENSP00000307705.

PTM databases

iPTMnetiP10412.
PhosphoSitePlusiP10412.
SwissPalmiP10412.

Polymorphism and mutation databases

BioMutaiHIST1H1E.
DMDMi121919.

Proteomic databases

EPDiP10412.
MaxQBiP10412.
PaxDbiP10412.
PeptideAtlasiP10412.
PRIDEiP10412.
TopDownProteomicsiP10412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3008.
DisGeNETi3008.
GeneCardsiHIST1H1E.
HGNCiHGNC:4718. HIST1H1E.
HPAiCAB011506.
HPA055907.
MIMi142220. gene.
neXtProtiNX_P10412.
OpenTargetsiENSG00000168298.
PharmGKBiPA29096.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168298-MONOMER.
ReactomeiR-HSA-211227. Activation of DNA fragmentation factor.
R-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

ChiTaRSiHIST1H1E. human.
GeneWikiiHIST1H1E.
GenomeRNAii3008.
PROiP10412.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168298.
CleanExiHS_HIST1H1E.
ExpressionAtlasiP10412. baseline and differential.
GenevisibleiP10412. HS.

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...

Entry informationi

Entry nameiH14_HUMAN
AccessioniPrimary (citable) accession number: P10412
Secondary accession number(s): Q4VB25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 166 of the entry and version 2 of the sequence. [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

Miscellaneous

This variant accounts for 60% of histone H1.

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

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.