UniProtKB - P10412 (H14_HUMAN)
Protein
Histone H1.4
Gene
H1-4
Organism
Homo sapiens (Human)
Status
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: GO_Central
- GTP binding Source: Ensembl
- nucleosomal DNA binding Source: GO_Central
- RNA binding Source: UniProtKB
GO - Biological processi
- chromosome condensation Source: GO_Central
- histone H3-K27 trimethylation Source: Ensembl
- histone H3-K4 trimethylation Source: Ensembl
- negative regulation of chromatin silencing Source: GO_Central
- negative regulation of DNA recombination Source: GO_Central
- negative regulation of transcription by RNA polymerase II Source: Ensembl
- nucleosome assembly Source: InterPro
- nucleosome positioning Source: GO_Central
- regulation of transcription, DNA-templated Source: GO_Central
Keywordsi
Molecular function | DNA-binding |
Enzyme and pathway databases
Reactomei | R-HSA-140342 Apoptosis induced DNA fragmentation R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF) |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H1.4Alternative name(s): Histone H1b Histone H1s-4 |
Gene namesi | Name:H1-4Imported Synonyms:H1F4Imported, HIST1H1EImported |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:4718 HIST1H1E |
MIMi | 142220 gene |
neXtProti | NX_P10412 |
Subcellular locationi
Nucleus
Other locations
Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
Nucleus
- nuclear chromatin Source: GO_Central
- nuclear euchromatin Source: GO_Central
- nuclear heterochromatin Source: UniProtKB
- nuclear nucleosome Source: Ensembl
- nucleus Source: UniProtKB
Keywords - Cellular componenti
Chromosome, NucleusPathology & 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.
Related information in OMIMKeywords - Diseasei
Mental retardationOrganism-specific databases
DisGeNETi | 3008 |
MalaCardsi | HIST1H1E |
MIMi | 617537 phenotype |
OpenTargetsi | ENSG00000168298 |
PharmGKBi | PA29096 |
Miscellaneous databases
Pharosi | P10412 |
Chemistry databases
DrugBanki | DB09130 Copper |
Polymorphism and mutation databases
BioMutai | HIST1H1E |
DMDMi | 121919 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources1 Publication | |||
ChainiPRO_0000195908 | 2 – 219 | Histone H1.4Add BLAST | 218 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 17 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 18 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 26 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 26 | N6-methyllysine; alternate1 Publication | 1 | |
Modified residuei | 34 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 34 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 36 | PhosphoserineBy similarity | 1 | |
Modified residuei | 52 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 54 | CitrullineBy similarity | 1 | |
Modified residuei | 64 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 85 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 90 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 106 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 146 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 150 | ADP-ribosylserine1 Publication | 1 | |
Modified residuei | 187 | PhosphoserineCombined sources | 1 |
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, PhosphoproteinProteomic databases
EPDi | P10412 |
jPOSTi | P10412 |
MassIVEi | P10412 |
MaxQBi | P10412 |
PaxDbi | P10412 |
PeptideAtlasi | P10412 |
PRIDEi | P10412 |
ProteomicsDBi | 52602 |
TopDownProteomicsi | P10412 |
PTM databases
iPTMneti | P10412 |
PhosphoSitePlusi | P10412 |
SwissPalmi | P10412 |
Expressioni
Gene expression databases
Bgeei | ENSG00000168298 Expressed in 89 organ(s), highest expression level in stomach |
ExpressionAtlasi | P10412 baseline and differential |
Genevisiblei | P10412 HS |
Organism-specific databases
HPAi | CAB011506 HPA055907 |
Interactioni
Binary interactionsi
Protein-protein interaction databases
BioGridi | 109263, 149 interactors |
IntActi | P10412, 185 interactors |
MINTi | P10412 |
STRINGi | 9606.ENSP00000307705 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P10412 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 36 – 109 | H15PROSITE-ProRule annotationAdd BLAST | 74 |
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
eggNOGi | KOG4012 Eukaryota ENOG4112541 LUCA |
GeneTreei | ENSGT00940000155501 |
HOGENOMi | HOG000251627 |
InParanoidi | P10412 |
KOi | K11275 |
OMAi | WIDMIKE |
OrthoDBi | 1565299at2759 |
PhylomeDBi | P10412 |
TreeFami | TF313664 |
Family and domain databases
CDDi | cd00073 H15, 1 hit |
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR005818 Histone_H1/H5_H15 IPR005819 Histone_H5 IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf |
Pfami | View protein in Pfam PF00538 Linker_histone, 1 hit |
PRINTSi | PR00624 HISTONEH5 |
SMARTi | View protein in SMART SM00526 H15, 1 hit |
SUPFAMi | SSF46785 SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS51504 H15, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P10412-1 [UniParc]FASTAAdd to basket
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
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_036203 | 128 | A → V in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs768731472Ensembl. | 1 | |
Natural variantiVAR_049307 | 152 | K → 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 |
CCDSi | CCDS4586.1 |
PIRi | C40335 HSHU1B |
RefSeqi | NP_005312.1, NM_005321.2 |
Genome annotation databases
Ensembli | ENST00000304218; ENSP00000307705; ENSG00000168298 |
GeneIDi | 3008 |
KEGGi | hsa:3008 |
UCSCi | uc003ngq.4 human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
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 No translation available. BC096168 mRNA Translation: AAH96168.1 BC096169 mRNA Translation: AAH96169.1 BC099632 mRNA Translation: AAH99632.1 |
CCDSi | CCDS4586.1 |
PIRi | C40335 HSHU1B |
RefSeqi | NP_005312.1, NM_005321.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3TZD | X-ray | 1.81 | T | 19-36 | [»] | |
5JJZ | X-ray | 2.00 | B | 21-32 | [»] | |
6H8P | X-ray | 1.98 | C/D | 18-32 | [»] | |
SMRi | P10412 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 109263, 149 interactors |
IntActi | P10412, 185 interactors |
MINTi | P10412 |
STRINGi | 9606.ENSP00000307705 |
Chemistry databases
DrugBanki | DB09130 Copper |
PTM databases
iPTMneti | P10412 |
PhosphoSitePlusi | P10412 |
SwissPalmi | P10412 |
Polymorphism and mutation databases
BioMutai | HIST1H1E |
DMDMi | 121919 |
Proteomic databases
EPDi | P10412 |
jPOSTi | P10412 |
MassIVEi | P10412 |
MaxQBi | P10412 |
PaxDbi | P10412 |
PeptideAtlasi | P10412 |
PRIDEi | P10412 |
ProteomicsDBi | 52602 |
TopDownProteomicsi | P10412 |
Genome annotation databases
Ensembli | ENST00000304218; ENSP00000307705; ENSG00000168298 |
GeneIDi | 3008 |
KEGGi | hsa:3008 |
UCSCi | uc003ngq.4 human |
Organism-specific databases
CTDi | 3008 |
DisGeNETi | 3008 |
GeneCardsi | HIST1H1E |
HGNCi | HGNC:4718 HIST1H1E |
HPAi | CAB011506 HPA055907 |
MalaCardsi | HIST1H1E |
MIMi | 142220 gene 617537 phenotype |
neXtProti | NX_P10412 |
OpenTargetsi | ENSG00000168298 |
PharmGKBi | PA29096 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG4012 Eukaryota ENOG4112541 LUCA |
GeneTreei | ENSGT00940000155501 |
HOGENOMi | HOG000251627 |
InParanoidi | P10412 |
KOi | K11275 |
OMAi | WIDMIKE |
OrthoDBi | 1565299at2759 |
PhylomeDBi | P10412 |
TreeFami | TF313664 |
Enzyme and pathway databases
Reactomei | R-HSA-140342 Apoptosis induced DNA fragmentation R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF) |
Miscellaneous databases
ChiTaRSi | HIST1H1E human |
GeneWikii | HIST1H1E |
GenomeRNAii | 3008 |
Pharosi | P10412 |
PROi | PR:P10412 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000168298 Expressed in 89 organ(s), highest expression level in stomach |
ExpressionAtlasi | P10412 baseline and differential |
Genevisiblei | P10412 HS |
Family and domain databases
CDDi | cd00073 H15, 1 hit |
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR005818 Histone_H1/H5_H15 IPR005819 Histone_H5 IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf |
Pfami | View protein in Pfam PF00538 Linker_histone, 1 hit |
PRINTSi | PR00624 HISTONEH5 |
SMARTi | View protein in SMART SM00526 H15, 1 hit |
SUPFAMi | SSF46785 SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS51504 H15, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | H14_HUMAN | |
Accessioni | P10412Primary (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 13, 2019 | |
This is version 194 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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 proteomeDocuments
- Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - SIMILARITY comments
Index of protein domains and families - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references