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P16401 (H15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.5
Alternative name(s):
Histone H1a
Histone H1b
Histone H1s-3
Gene names
Name:HIST1H1B
Synonyms:H1F5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Nucleus. Chromosome. Note: According to Ref.9 more commonly found in heterochromatin. According to Ref.7 associates with actively transcribed chromatin and not heterochromatin. Ref.7 Ref.8 Ref.9

Tissue specificity

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

Domain

The C-terminal domain is required for high-affinity binding to chromatin By similarity.

Post-translational modification

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. Ref.11 Ref.14

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.

Sequence similarities

Belongs to the histone H1/H5 family.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   PTMAcetylation
Citrullination
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Inferred from mutant phenotype PubMed 22956909. Source: UniProt

establishment of protein localization to chromatin

Inferred from mutant phenotype PubMed 22956909. Source: UniProt

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22956909. Source: UniProt

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

positive regulation of cell growth

Inferred from mutant phenotype PubMed 22956909. Source: UniProt

positive regulation of histone H3-K9 methylation

Inferred from mutant phenotype PubMed 22956909. Source: UniProt

protein stabilization

Inferred from mutant phenotype PubMed 22956909. Source: UniProt

   Cellular_componentnuclear chromatin

Inferred from direct assay PubMed 19882353. Source: UniProtKB

nuclear heterochromatin

Inferred from direct assay Ref.9. Source: UniProt

nucleosome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionchromatin DNA binding

Inferred from mutant phenotype Ref.9PubMed 22956909. Source: UniProt

histone deacetylase binding

Inferred from physical interaction PubMed 22956909. Source: UniProt

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 226225Histone H1.5
PRO_0000195909

Regions

Domain39 – 11274H15

Amino acid modifications

Modified residue21N-acetylserine; partial Ref.6 Ref.13 Ref.18 Ref.20 Ref.21 Ref.22
Modified residue21Phosphoserine Ref.20
Modified residue111Phosphothreonine; by GSK3 Ref.11 Ref.12 Ref.14
Modified residue171N6-acetyllysine By similarity
Modified residue181Phosphoserine Ref.11 Ref.12 Ref.16 Ref.18 Ref.20
Modified residue271N6-methyllysine Ref.15
Modified residue371N6-succinyllysine By similarity
Modified residue391Phosphothreonine Ref.12
Modified residue491N6-acetyllysine By similarity
Modified residue571Citrulline By similarity
Modified residue781N6-acetyllysine By similarity
Modified residue1381Phosphothreonine Ref.11 Ref.18 Ref.20
Modified residue1551Phosphothreonine Ref.11
Modified residue1681N6-acetyllysine Ref.17
Modified residue1731Phosphoserine Ref.11
Modified residue1891Phosphoserine Ref.11

Natural variations

Natural variant861G → D in a colorectal cancer sample; somatic mutation. Ref.23
VAR_036204
Natural variant1441K → R.
Corresponds to variant rs11970638 [ dbSNP | Ensembl ].
VAR_049308
Natural variant2111A → T.
Corresponds to variant rs34144478 [ dbSNP | Ensembl ].
VAR_049309

Experimental info

Sequence conflict216 – 2183Missing AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P16401 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0BA1402101766FDF

FASTA22622,580
        10         20         30         40         50         60 
MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL 

        70         80         90        100        110        120 
SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK 

       130        140        150        160        170        180 
PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA 

       190        200        210        220 
AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the H1.5 gene completes the set of human H1 subtype genes."
Albig W., Meergans T., Doenecke D.
Gene 184:141-148(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[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. expand/collapse author list , 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: Liver.
[5]"Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d."
Ohe Y., Hayashi H., Iwai K.
J. Biochem. 106:844-857(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-226.
Tissue: Spleen.
[6]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]"The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: distribution in human fetal fibroblasts."
Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.
Chromosome Res. 8:405-424(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin II: distribution in human adult fibroblasts."
Parseghian M.H., Newcomb R.L., Hamkalo B.A.
J. Cell. Biochem. 83:643-659(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"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.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1."
Sarg B., Helliger W., Talasz H., Forg B., Lindner H.H.
J. Biol. Chem. 281:6573-6580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-11; SER-18; THR-138; THR-155; SER-173 AND SER-189.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"M phase-specific phosphorylation of histone H1.5 at threonine 10 by GSK-3."
Happel N., Stoldt S., Schmidt B., Doenecke D.
J. Mol. Biol. 386:339-350(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-11 BY GSK3B.
[15]"Mapping of lysine monomethylation of linker histones in human breast and its cancer."
Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M., Wisniewski J.R.
J. Proteome Res. 8:4207-4215(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-27.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-18 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-86.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4635.1.
PIRS51660.
RefSeqNP_005313.1. NM_005322.2.
UniGeneHs.131956.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FE2model-A2-226[»]
2RHIX-ray1.66B23-27[»]
ProteinModelPortalP16401.
SMRP16401. Positions 40-112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109264. 46 interactions.
IntActP16401. 4 interactions.
MINTMINT-3008567.
STRING9606.ENSP00000330074.

PTM databases

PhosphoSiteP16401.

Polymorphism databases

DMDM19856407.

Proteomic databases

MaxQBP16401.
PaxDbP16401.
PeptideAtlasP16401.
PRIDEP16401.

Protocols and materials databases

DNASU3009.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331442; ENSP00000330074; ENSG00000184357.
GeneID3009.
KEGGhsa:3009.
UCSCuc003njx.3. human.

Organism-specific databases

CTD3009.
GeneCardsGC06M027835.
HGNCHGNC:4719. HIST1H1B.
HPACAB012241.
MIM142711. gene.
neXtProtNX_P16401.
PharmGKBPA29097.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258621.
HOGENOMHOG000251627.
HOVERGENHBG009035.
InParanoidP16401.
KOK11275.
OMATRVAKAK.
OrthoDBEOG74TX2T.
PhylomeDBP16401.
TreeFamTF313664.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_578. Apoptosis.

Gene expression databases

BgeeP16401.
CleanExHS_HIST1H1B.
GenevestigatorP16401.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 1 hit.
[Graphical view]
PROSITEPS51504. H15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16401.
GeneWikiHIST1H1B.
GenomeRNAi3009.
NextBio11932.
PROP16401.
SOURCESearch...

Entry information

Entry nameH15_HUMAN
AccessionPrimary (citable) accession number: P16401
Secondary accession number(s): Q14529, Q3MJ42
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM