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Protein

Histone H1.5

Gene

HIST1H1B

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

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • 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)
SIGNORiP16401

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.5
Alternative name(s):
Histone H1a
Histone H1b
Histone H1s-3
Gene namesi
Name:HIST1H1B
Synonyms:H1F5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000184357.4
HGNCiHGNC:4719 HIST1H1B
MIMi142711 gene
neXtProtiNX_P16401

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

DisGeNETi3009
OpenTargetsiENSG00000184357
PharmGKBiPA29097

Polymorphism and mutation databases

BioMutaiHIST1H1B
DMDMi19856407

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001959092 – 226Histone H1.5Add BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine; partialCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei11Phosphothreonine; by GSK3Combined sources2 Publications1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei18PhosphoserineCombined sources1 Publication1
Modified residuei27N6-methyllysine1 Publication1
Modified residuei37N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei37N6-succinyllysine; alternateBy similarity1
Modified residuei39PhosphothreonineCombined sources1
Modified residuei49N6-acetyllysineBy similarity1
Modified residuei55N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei57CitrullineBy similarity1
Modified residuei67N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei78N6-acetyllysineBy similarity1
Modified residuei88N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei93N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei109N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei138PhosphothreonineCombined sources1 Publication1
Modified residuei155Phosphothreonine1 Publication1
Modified residuei168N6-acetyllysineCombined sources1
Modified residuei173Phosphoserine1 Publication1
Modified residuei189Phosphoserine1 Publication1

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). Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase.By similarity2 Publications
Citrullination at Arg-57 (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, Hydroxylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP16401
MaxQBiP16401
PaxDbiP16401
PeptideAtlasiP16401
PRIDEiP16401
ProteomicsDBi53351
TopDownProteomicsiP16401

PTM databases

iPTMnetiP16401
PhosphoSitePlusiP16401
SwissPalmiP16401

Expressioni

Tissue specificityi

Ubiquitous. Expressed in the majority of the cell lines tested and in testis.1 Publication

Gene expression databases

BgeeiENSG00000184357 Expressed in 48 organ(s), highest expression level in lung
CleanExiHS_HIST1H1B
GenevisibleiP16401 HS

Organism-specific databases

HPAiCAB012241
HPA055907

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109264, 67 interactors
IntActiP16401, 15 interactors
MINTiP16401
STRINGi9606.ENSP00000330074

Structurei

3D structure databases

ProteinModelPortaliP16401
SMRiP16401
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16401

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 112H15PROSITE-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
InParanoidiP16401
KOiK11275
OMAiECITAHP
OrthoDBiEOG091G0XGD
PhylomeDBiP16401
TreeFamiTF313664

Family and domain databases

CDDicd00073 H15, 1 hit
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.

P16401-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA
60 70 80 90 100
VAASKERNGL SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK
110 120 130 140 150
GTGASGSFKL NKKAASGEAK PKAKKAGAAK AKKPAGATPK KAKKAAGAKK
160 170 180 190 200
AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA AKPKKATKSP AKPKAVKPKA
210 220
AKPKAAKPKA AKPKAAKAKK AAAKKK
Length:226
Mass (Da):22,580
Last modified:January 23, 2007 - v3
Checksum:i0BA1402101766FDF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti216 – 218Missing AA sequence (PubMed:2613692).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03620486G → D in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_049308144K → R. Corresponds to variant dbSNP:rs11970638Ensembl.1
Natural variantiVAR_049309211A → T. Corresponds to variant dbSNP:rs34144478Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83509 Genomic DNA Translation: CAA58498.1
AF531304 Genomic DNA Translation: AAN06704.1
Z98744 Genomic DNA No translation available.
BC069101 mRNA Translation: AAH69101.1
BC101581 mRNA Translation: AAI01582.1
BC101583 mRNA Translation: AAI01584.1
CCDSiCCDS4635.1
PIRiS51660
RefSeqiNP_005313.1, NM_005322.2
UniGeneiHs.131956

Genome annotation databases

EnsembliENST00000331442; ENSP00000330074; ENSG00000184357
GeneIDi3009
KEGGihsa:3009
UCSCiuc003njx.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83509 Genomic DNA Translation: CAA58498.1
AF531304 Genomic DNA Translation: AAN06704.1
Z98744 Genomic DNA No translation available.
BC069101 mRNA Translation: AAH69101.1
BC101581 mRNA Translation: AAI01582.1
BC101583 mRNA Translation: AAI01584.1
CCDSiCCDS4635.1
PIRiS51660
RefSeqiNP_005313.1, NM_005322.2
UniGeneiHs.131956

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FE2model-A2-226[»]
2RHIX-ray1.66B23-27[»]
ProteinModelPortaliP16401
SMRiP16401
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109264, 67 interactors
IntActiP16401, 15 interactors
MINTiP16401
STRINGi9606.ENSP00000330074

PTM databases

iPTMnetiP16401
PhosphoSitePlusiP16401
SwissPalmiP16401

Polymorphism and mutation databases

BioMutaiHIST1H1B
DMDMi19856407

Proteomic databases

EPDiP16401
MaxQBiP16401
PaxDbiP16401
PeptideAtlasiP16401
PRIDEiP16401
ProteomicsDBi53351
TopDownProteomicsiP16401

Protocols and materials databases

DNASUi3009
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331442; ENSP00000330074; ENSG00000184357
GeneIDi3009
KEGGihsa:3009
UCSCiuc003njx.4 human

Organism-specific databases

CTDi3009
DisGeNETi3009
EuPathDBiHostDB:ENSG00000184357.4
GeneCardsiHIST1H1B
HGNCiHGNC:4719 HIST1H1B
HPAiCAB012241
HPA055907
MIMi142711 gene
neXtProtiNX_P16401
OpenTargetsiENSG00000184357
PharmGKBiPA29097
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4012 Eukaryota
ENOG4112541 LUCA
GeneTreeiENSGT00670000097781
HOGENOMiHOG000251627
HOVERGENiHBG009035
InParanoidiP16401
KOiK11275
OMAiECITAHP
OrthoDBiEOG091G0XGD
PhylomeDBiP16401
TreeFamiTF313664

Enzyme and pathway databases

ReactomeiR-HSA-211227 Activation of DNA fragmentation factor
R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
SIGNORiP16401

Miscellaneous databases

EvolutionaryTraceiP16401
GeneWikiiHIST1H1B
GenomeRNAii3009
PROiPR:P16401
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184357 Expressed in 48 organ(s), highest expression level in lung
CleanExiHS_HIST1H1B
GenevisibleiP16401 HS

Family and domain databases

CDDicd00073 H15, 1 hit
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
ProtoNetiSearch...

Entry informationi

Entry nameiH15_HUMAN
AccessioniPrimary (citable) accession number: P16401
Secondary accession number(s): Q14529, Q3MJ42
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 172 of the entry and version 3 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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