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P10412 (H14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.4
Alternative name(s):
Histone H1b
Histone H1s-4
Gene names
Name:HIST1H1E
Synonyms:H1F4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 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: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus. Ref.6 Ref.8

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.

Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1. Ref.7

Citrullination at Arg-54 (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.

Miscellaneous

This variant accounts for 60% of histone H1.

Sequence similarities

Belongs to the histone H1/H5 family.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

L3MBTL1Q9Y4687EBI-358163,EBI-1265089
NCK1P163332EBI-358163,EBI-389883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.12
Chain2 – 219218Histone H1.4
PRO_0000195908

Regions

Domain36 – 10974H15

Amino acid modifications

Modified residue21N-acetylserine Ref.12 Ref.13 Ref.15 Ref.16 Ref.17
Modified residue171N6-acetyllysine By similarity
Modified residue181Phosphothreonine Ref.9 Ref.10 Ref.11 Ref.13 Ref.15
Modified residue261N6-acetyllysine; alternate Ref.7
Modified residue261N6-methyllysine; alternate
Modified residue341N6-succinyllysine By similarity
Modified residue361Phosphoserine By similarity
Modified residue541Citrulline By similarity
Modified residue1461Phosphothreonine Ref.13
Modified residue1871Phosphoserine Ref.9 Ref.13 Ref.15

Natural variations

Natural variant1281A → V in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036203
Natural variant1521K → R.
Corresponds to variant rs2298090 [ dbSNP | Ensembl ].
VAR_049307

Secondary structure

... 219
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10412 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1720FECCCBEBCC7F

FASTA21921,865
        10         20         30         40         50         60 
MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA SKERSGVSLA 

        70         80         90        100        110        120 
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA 

       130        140        150        160        170        180 
KKAGAAKAKK PAGAAKKPKK ATGAATPKKS AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK 

       190        200        210 
PKKAPKSPAK AKAVKPKAAK PKTAKPKAAK PKKAAAKKK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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].
[5]"Human spleen histone H1. Isolation and amino acid sequence of a main variant, H1b."
Ohe Y., Hayashi H., Iwai K.
J. Biochem. 100:359-368(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-219.
Tissue: Spleen.
[6]"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.
[7]"Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin."
Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., Reinberg D.
Mol. Cell 16:93-105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-26.
[8]"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.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"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 THR-18; THR-146 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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 THR-18 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"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].
[18]"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] VAL-128.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60748 Genomic DNA. Translation: AAA63187.1.
AF531302 Genomic DNA. Translation: AAN06702.1.
AL353759 Genomic DNA. Translation: CAC04132.1.
BC096168 mRNA. Translation: AAH96168.1.
BC096169 mRNA. Translation: AAH96169.1.
BC099632 mRNA. Translation: AAH99632.1.
CCDSCCDS4586.1.
PIRHSHU1B. C40335.
RefSeqNP_005312.1. NM_005321.2.
UniGeneHs.248133.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TZDX-ray1.81T19-36[»]
ProteinModelPortalP10412.
SMRP10412. Positions 36-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109263. 32 interactions.
IntActP10412. 12 interactions.
MINTMINT-1136873.
STRING9606.ENSP00000307705.

PTM databases

PhosphoSiteP10412.

Polymorphism databases

DMDM121919.

Proteomic databases

MaxQBP10412.
PeptideAtlasP10412.
PRIDEP10412.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304218; ENSP00000307705; ENSG00000168298.
GeneID3008.
KEGGhsa:3008.
UCSCuc003ngq.3. human.

Organism-specific databases

CTD3008.
GeneCardsGC06P026156.
HGNCHGNC:4718. HIST1H1E.
HPACAB011506.
MIM142220. gene.
neXtProtNX_P10412.
PharmGKBPA29096.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000251627.
HOVERGENHBG009035.
InParanoidP10412.
KOK11275.
OMAPRTTAMP.
OrthoDBEOG74TX2T.
PhylomeDBP10412.
TreeFamTF313664.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP10412.
BgeeP10412.
CleanExHS_HIST1H1E.
GenevestigatorP10412.

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

GeneWikiHIST1H1E.
GenomeRNAi3008.
NextBio11928.
PROP10412.
SOURCESearch...

Entry information

Entry nameH14_HUMAN
AccessionPrimary (citable) accession number: P10412
Secondary accession number(s): Q4VB25
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 2 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