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Protein

Histone H1.5

Gene

HIST1H1B

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
  • histone deacetylase binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • chromatin organization Source: UniProtKB
  • establishment of protein localization to chromatin Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • nucleosome assembly Source: InterPro
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of histone H3-K9 methylation Source: UniProtKB
  • protein stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:G66-30683-MONOMER.
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

HGNCiHGNC:4719. HIST1H1B.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: According to PubMed:15911621 more commonly found in heterochromatin. According to PubMed:10997781 associates with actively transcribed chromatin and not heterochromatin.

GO - Cellular componenti

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

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-acetyllysine; alternateBy similarity1
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei18PhosphoserineCombined sources1 Publication1
Modified residuei26N6-acetyllysine; alternateBy similarity1
Modified residuei26N6-methyllysine; alternateBy similarity1
Modified residuei27N6-methyllysine1 Publication1
Modified residuei37N6-methyllysine; alternateBy similarity1
Modified residuei37N6-succinyllysine; alternateBy similarity1
Modified residuei39PhosphothreonineCombined sources1
Modified residuei44PhosphoserineBy similarity1
Modified residuei49N6-acetyllysineBy similarity1
Modified residuei57CitrullineBy similarity1
Modified residuei78N6-acetyllysineBy similarity1
Modified residuei93N6-acetyllysineBy similarity1
Modified residuei100N6-succinyllysineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei138PhosphothreonineCombined sources1 Publication1
Modified residuei155Phosphothreonine1 Publication1
Modified residuei168N6-acetyllysineCombined sources1
Modified residuei173Phosphoserine1 Publication1
Modified residuei188N6-methyllysineBy similarity1
Modified residuei189Phosphoserine1 Publication1
Cross-linki219Glycyl 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). 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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP16401.
MaxQBiP16401.
PaxDbiP16401.
PeptideAtlasiP16401.
PRIDEiP16401.
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.
CleanExiHS_HIST1H1B.
GenevisibleiP16401. HS.

Organism-specific databases

HPAiCAB012241.
HPA055907.

Interactioni

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109264. 59 interactors.
IntActiP16401. 14 interactors.
MINTiMINT-3008567.
STRINGi9606.ENSP00000330074.

Structurei

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...

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
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP16401.
KOiK11275.
OrthoDBiEOG091G0XGD.
PhylomeDBiP16401.
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.

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 rs11970638dbSNPEnsembl.1
Natural variantiVAR_049309211A → T.Corresponds to variant rs34144478dbSNPEnsembl.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. Translation: CAB11421.1.
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

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. Translation: CAB11421.1.
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. 59 interactors.
IntActiP16401. 14 interactors.
MINTiMINT-3008567.
STRINGi9606.ENSP00000330074.

PTM databases

iPTMnetiP16401.
PhosphoSitePlusiP16401.
SwissPalmiP16401.

Polymorphism and mutation databases

BioMutaiHIST1H1B.
DMDMi19856407.

Proteomic databases

EPDiP16401.
MaxQBiP16401.
PaxDbiP16401.
PeptideAtlasiP16401.
PRIDEiP16401.
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.
GeneCardsiHIST1H1B.
HGNCiHGNC:4719. HIST1H1B.
HPAiCAB012241.
HPA055907.
MIMi142711. gene.
neXtProtiNX_P16401.
OpenTargetsiENSG00000184357.
PharmGKBiPA29097.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:G66-30683-MONOMER.
ReactomeiR-HSA-211227. Activation of DNA fragmentation factor.
R-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
SIGNORiP16401.

Miscellaneous databases

EvolutionaryTraceiP16401.
GeneWikiiHIST1H1B.
GenomeRNAii3009.
PROiP16401.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184357.
CleanExiHS_HIST1H1B.
GenevisibleiP16401. 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 nameiH15_HUMAN
AccessioniPrimary (citable) accession number: P16401
Secondary accession number(s): Q14529, Q3MJ42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 158 of the entry and version 3 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

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.