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P10412

- H14_HUMAN

UniProt

P10412 - H14_HUMAN

Protein

Histone H1.4

Gene

HIST1H1E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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
    Name:HIST1H1E
    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.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29096.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 219218Histone H1.4PRO_0000195908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine5 Publications
    Modified residuei17 – 171N6-acetyllysineBy similarity
    Modified residuei18 – 181Phosphothreonine5 Publications
    Modified residuei26 – 261N6-acetyllysine; alternate1 Publication
    Modified residuei26 – 261N6-methyllysine; alternate
    Modified residuei34 – 341N6-succinyllysineBy similarity
    Modified residuei36 – 361PhosphoserineBy similarity
    Modified residuei54 – 541CitrullineBy 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 SIRT1.6 Publications
    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

    1
    219
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 10974H15PROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation
    Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 143 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