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Protein

Histone H1.1

Gene

HIST1H1A

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
  • heparin binding Source: Ensembl

GO - Biological processi

  • nucleosome assembly Source: InterPro
  • positive regulation of receptor-mediated endocytosis Source: Ensembl
  • spermatogenesis Source: ProtInc

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).
SIGNORiQ02539.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.1
Alternative name(s):
Histone H1a
Gene namesi
Name:HIST1H1A
Synonyms:H1F1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000124610.4.
HGNCiHGNC:4715. HIST1H1A.

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi152T → E: Significant destabilization of binding to chromatin. 1 Publication1
Mutagenesisi183S → E: Significant destabilization of binding to chromatin. 1 Publication1

Organism-specific databases

DisGeNETi3024.
OpenTargetsiENSG00000124610.
PharmGKBiPA29093.

Polymorphism and mutation databases

BioMutaiHIST1H1A.
DMDMi18202479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001959052 – 215Histone H1.1Add BLAST214

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei12PhosphoserineBy similarity1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei37N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei44PhosphoserineBy 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 residuei93N6-acetyllysineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei109N6-(beta-hydroxybutyryl)lysineBy similarity1
Modified residuei125N6-acetyllysineBy similarity1
Modified residuei204PhosphothreonineBy similarity1

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
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, Phosphoprotein

Proteomic databases

EPDiQ02539.
MaxQBiQ02539.
PaxDbiQ02539.
PeptideAtlasiQ02539.
PRIDEiQ02539.

PTM databases

iPTMnetiQ02539.
PhosphoSitePlusiQ02539.
SwissPalmiQ02539.

Expressioni

Gene expression databases

BgeeiENSG00000124610.
CleanExiHS_HIST1H1A.
GenevisibleiQ02539. HS.

Organism-specific databases

HPAiHPA043753.

Interactioni

Subunit structurei

Interacts with DFFB.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SIR2rp1Q57V412EBI-932603,EBI-7579996From Trypanosoma brucei brucei (strain 927/4 GUTat10.1).

Protein-protein interaction databases

BioGridi109275. 193 interactors.
CORUMiQ02539.
IntActiQ02539. 32 interactors.
STRINGi9606.ENSP00000244573.

Structurei

3D structure databases

ProteinModelPortaliQ02539.
SMRiQ02539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 112H15Add BLAST74

Domaini

The C-terminal domain is required for high-affinity binding to chromatin.1 Publication

Sequence similaritiesi

Belongs to the histone H1/H5 family.

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiQ02539.
KOiK11275.
OMAiKPRSHPP.
OrthoDBiEOG091G0XGD.
PhylomeDBiQ02539.
TreeFamiTF313664.

Family and domain databases

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.

Q02539-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETVPPAPA ASAAPEKPLA GKKAKKPAKA AAASKKKPAG PSVSELIVQA
60 70 80 90 100
ASSSKERGGV SLAALKKALA AAGYDVEKNN SRIKLGIKSL VSKGTLVQTK
110 120 130 140 150
GTGASGSFKL NKKASSVETK PGASKVATKT KATGASKKLK KATGASKKSV
160 170 180 190 200
KTPKKAKKPA ATRKSSKNPK KPKTVKPKKV AKSPAKAKAV KPKAAKARVT
210
KPKTAKPKKA APKKK
Length:215
Mass (Da):21,842
Last modified:January 23, 2007 - v3
Checksum:i854B03622D78774A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04930199T → I. Corresponds to variant dbSNP:rs417751Ensembl.1
Natural variantiVAR_049302115S → F. Corresponds to variant dbSNP:rs34541321Ensembl.1
Natural variantiVAR_049303140K → R. Corresponds to variant dbSNP:rs16891235Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57130 Genomic DNA. Translation: CAA40409.1.
AF531299 Genomic DNA. Translation: AAN06699.1.
U91328 Genomic DNA. No translation available.
BC069492 mRNA. Translation: AAH69492.1.
BC101593 mRNA. Translation: AAI01594.1.
BC112140 mRNA. Translation: AAI12141.1.
CCDSiCCDS4569.1.
PIRiS26363.
RefSeqiNP_005316.1. NM_005325.3.
UniGeneiHs.150206.

Genome annotation databases

EnsembliENST00000244573; ENSP00000244573; ENSG00000124610.
GeneIDi3024.
KEGGihsa:3024.
UCSCiuc003nfo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiH11_HUMAN
AccessioniPrimary (citable) accession number: Q02539
Secondary accession number(s): Q3MJ34
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 146 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

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families