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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

GO - Biological processi

  • nucleosome assembly Source: InterPro
  • spermatogenesis Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

DNA-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

HGNCiHGNC:4715. HIST1H1A.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication
  • Chromosome PROSITE-ProRule annotation1 Publication

  • Note: Mainly localizes in euchromatin.

GO - Cellular componenti

  • nuclear chromatin Source: UniProtKB
  • nuclear euchromatin Source: UniProtKB
  • nucleosome Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521T → E: Significant destabilization of binding to chromatin. 1 Publication
Mutagenesisi183 – 1831S → E: Significant destabilization of binding to chromatin. 1 Publication

Organism-specific databases

PharmGKBiPA29093.

Polymorphism and mutation databases

BioMutaiHIST1H1A.
DMDMi18202479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 215214Histone H1.1PRO_0000195905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei57 – 571CitrullineBy similarity
Modified residuei78 – 781N6-acetyllysineBy similarity
Modified residuei93 – 931N6-acetyllysineBy similarity
Modified residuei107 – 1071PhosphoserineBy similarity
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei204 – 2041PhosphothreonineBy 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
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, Phosphoprotein

Proteomic databases

EPDiQ02539.
MaxQBiQ02539.
PaxDbiQ02539.
PeptideAtlasiQ02539.
PRIDEiQ02539.

PTM databases

iPTMnetiQ02539.
PhosphoSiteiQ02539.
SwissPalmiQ02539.

Expressioni

Gene expression databases

BgeeiQ02539.
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 a different organism.

Protein-protein interaction databases

BioGridi109275. 179 interactions.
IntActiQ02539. 26 interactions.
STRINGi9606.ENSP00000244573.

Structurei

3D structure databases

ProteinModelPortaliQ02539.
SMRiQ02539. Positions 39-112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 11274H15PROSITE-ProRule annotationAdd
BLAST

Domaini

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

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.
InParanoidiQ02539.
KOiK11275.
OMAiKKNVKTP.
OrthoDBiEOG74TX2T.
PhylomeDBiQ02539.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991T → I.
Corresponds to variant rs417751 [ dbSNP | Ensembl ].
VAR_049301
Natural varianti115 – 1151S → F.
Corresponds to variant rs34541321 [ dbSNP | Ensembl ].
VAR_049302
Natural varianti140 – 1401K → R.
Corresponds to variant rs16891235 [ dbSNP | Ensembl ].
VAR_049303

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ02539.
SMRiQ02539. Positions 39-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109275. 179 interactions.
IntActiQ02539. 26 interactions.
STRINGi9606.ENSP00000244573.

PTM databases

iPTMnetiQ02539.
PhosphoSiteiQ02539.
SwissPalmiQ02539.

Polymorphism and mutation databases

BioMutaiHIST1H1A.
DMDMi18202479.

Proteomic databases

EPDiQ02539.
MaxQBiQ02539.
PaxDbiQ02539.
PeptideAtlasiQ02539.
PRIDEiQ02539.

Protocols and materials databases

DNASUi3024.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3024.
GeneCardsiHIST1H1A.
HGNCiHGNC:4715. HIST1H1A.
HPAiHPA043753.
MIMi142709. gene.
neXtProtiNX_Q02539.
PharmGKBiPA29093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiQ02539.
KOiK11275.
OMAiKKNVKTP.
OrthoDBiEOG74TX2T.
PhylomeDBiQ02539.
TreeFamiTF313664.

Enzyme and pathway databases

ReactomeiR-HSA-211227. Activation of DNA fragmentation factor.
R-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
SIGNORiQ02539.

Miscellaneous databases

GeneWikiiHIST1H1A.
GenomeRNAii3024.
PROiQ02539.
SOURCEiSearch...

Gene expression databases

BgeeiQ02539.
CleanExiHS_HIST1H1A.
GenevisibleiQ02539. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Human H1 histones: conserved and varied sequence elements in two H1 subtype genes."
    Eick S., Nicolai M., Mumberg D., Doenecke D.
    Eur. J. Cell Biol. 49:110-115(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  2. "The human and mouse replication-dependent histone genes."
    Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
    Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. "A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences."
    Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.
    Protein Sci. 3:575-587(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  6. "The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo."
    Hendzel M.J., Lever M.A., Crawford E., Th'ng J.P.
    J. Biol. Chem. 279:20028-20034(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF THR-152 AND SER-183.
  7. "H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain."
    Th'ng J.P., Sung R., Ye M., Hendzel M.J.
    J. Biol. Chem. 280:27809-27814(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Histone H1 subtype preferences of DFF40 and possible nuclear localization of DFF40/45 in normal and trichostatin A-treated NB4 leukemic cells."
    Ninios Y.P., Sekeri-Pataryas K.E., Sourlingas T.G.
    Apoptosis 15:128-138(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DFFB.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiH11_HUMAN
AccessioniPrimary (citable) accession number: Q02539
Secondary accession number(s): Q3MJ34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 133 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

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

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.