SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10412

- H14_HUMAN

UniProt

P10412 - H14_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Histone H1.4
Gene
HIST1H1E, H1F4
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

  1. chromatin DNA binding Source: UniProt
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. nucleosome assembly Source: InterPro
  2. nucleosome positioning Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_13462. Activation of DNA fragmentation factor.
REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.4
Alternative name(s):
Histone H1b
Histone H1s-4
Gene namesi
Synonyms:H1F4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4718. HIST1H1E.

Subcellular locationi

Nucleus. Chromosome
Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.2 Publications

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. nuclear heterochromatin Source: UniProt
  3. nucleosome Source: InterPro
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 219218Histone H1.4
PRO_0000195908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine5 Publications
Modified residuei17 – 171N6-acetyllysine By similarity
Modified residuei18 – 181Phosphothreonine5 Publications
Modified residuei26 – 261N6-acetyllysine; alternate1 Publication
Modified residuei26 – 261N6-methyllysine; alternate
Modified residuei34 – 341N6-succinyllysine By similarity
Modified residuei36 – 361Phosphoserine By similarity
Modified residuei54 – 541Citrulline By similarity
Modified residuei146 – 1461Phosphothreonine1 Publication
Modified residuei187 – 1871Phosphoserine3 Publications

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.
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.1 Publication
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.

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP10412.
PeptideAtlasiP10412.
PRIDEiP10412.

PTM databases

PhosphoSiteiP10412.

Expressioni

Gene expression databases

ArrayExpressiP10412.
BgeeiP10412.
CleanExiHS_HIST1H1E.
GenevestigatoriP10412.

Organism-specific databases

HPAiCAB011506.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
L3MBTL1Q9Y4687EBI-358163,EBI-1265089
NCK1P163332EBI-358163,EBI-389883

Protein-protein interaction databases

BioGridi109263. 23 interactions.
IntActiP10412. 12 interactions.
MINTiMINT-1136873.
STRINGi9606.ENSP00000307705.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 256

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TZDX-ray1.81T19-36[»]
ProteinModelPortaliP10412.
SMRiP10412. Positions 36-109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the histone H1/H5 family.

Phylogenomic databases

HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP10412.
KOiK11275.
OMAiPRTTAMP.
OrthoDBiEOG74TX2T.
PhylomeDBiP10412.
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]
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10412-1 [UniParc]FASTAAdd to Basket

« Hide

MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA    50
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG 100
ASGSFKLNKK AASGEAKPKA KKAGAAKAKK PAGAAKKPKK ATGAATPKKS 150
AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK PKKAPKSPAK AKAVKPKAAK 200
PKTAKPKAAK PKKAAAKKK 219
Length:219
Mass (Da):21,865
Last modified:January 23, 2007 - v2
Checksum:i1720FECCCBEBCC7F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036203
Natural varianti152 – 1521K → R.
Corresponds to variant rs2298090 [ dbSNP | Ensembl ].
VAR_049307

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4586.1.
PIRiC40335. HSHU1B.
RefSeqiNP_005312.1. NM_005321.2.
UniGeneiHs.248133.

Genome annotation databases

EnsembliENST00000304218; ENSP00000307705; ENSG00000168298.
GeneIDi3008.
KEGGihsa:3008.
UCSCiuc003ngq.3. human.

Polymorphism databases

DMDMi121919.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4586.1.
PIRi C40335. HSHU1B.
RefSeqi NP_005312.1. NM_005321.2.
UniGenei Hs.248133.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TZD X-ray 1.81 T 19-36 [» ]
ProteinModelPortali P10412.
SMRi P10412. Positions 36-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109263. 23 interactions.
IntActi P10412. 12 interactions.
MINTi MINT-1136873.
STRINGi 9606.ENSP00000307705.

PTM databases

PhosphoSitei P10412.

Polymorphism databases

DMDMi 121919.

Proteomic databases

MaxQBi P10412.
PeptideAtlasi P10412.
PRIDEi P10412.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304218 ; ENSP00000307705 ; ENSG00000168298 .
GeneIDi 3008.
KEGGi hsa:3008.
UCSCi uc003ngq.3. human.

Organism-specific databases

CTDi 3008.
GeneCardsi GC06P026156.
HGNCi HGNC:4718. HIST1H1E.
HPAi CAB011506.
MIMi 142220. gene.
neXtProti NX_P10412.
PharmGKBi PA29096.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000251627.
HOVERGENi HBG009035.
InParanoidi P10412.
KOi K11275.
OMAi PRTTAMP.
OrthoDBi EOG74TX2T.
PhylomeDBi P10412.
TreeFami TF313664.

Enzyme and pathway databases

Reactomei REACT_13462. Activation of DNA fragmentation factor.
REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

GeneWikii HIST1H1E.
GenomeRNAii 3008.
NextBioi 11928.
PROi P10412.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10412.
Bgeei P10412.
CleanExi HS_HIST1H1E.
Genevestigatori P10412.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00538. Linker_histone. 1 hit.
[Graphical view ]
PRINTSi PR00624. HISTONEH5.
SMARTi SM00526. H15. 1 hit.
[Graphical view ]
PROSITEi PS51504. H15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-128.

Entry informationi

Entry nameiH14_HUMAN
AccessioniPrimary (citable) accession number: P10412
Secondary accession number(s): Q4VB25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 142 of the entry and version 2 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

Miscellaneous

This variant accounts for 60% of histone H1.

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

External Data

Dasty 3

Similar proteinsi