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P16401

- H15_HUMAN

UniProt

P16401 - H15_HUMAN

Protein

Histone H1.5

Gene

HIST1H1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (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. histone deacetylase binding Source: UniProt
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: UniProt
    2. establishment of protein localization to chromatin Source: UniProt
    3. negative regulation of transcription from RNA polymerase II promoter Source: UniProt
    4. nucleosome assembly Source: InterPro
    5. positive regulation of cell growth Source: UniProt
    6. positive regulation of histone H3-K9 methylation Source: UniProt
    7. protein stabilization Source: UniProt

    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 H1.5
    Alternative name(s):
    Histone H1a
    Histone H1b
    Histone H1s-3
    Gene namesi
    Name:HIST1H1B
    Synonyms:H1F5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4719. HIST1H1B.

    Subcellular locationi

    Nucleus. Chromosome
    Note: According to PubMed:15911621 more commonly found in heterochromatin. According to PubMed:10997781 associates with actively transcribed chromatin and not heterochromatin.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29097.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed7 Publications
    Chaini2 – 226225Histone H1.5PRO_0000195909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine; partial6 Publications
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei11 – 111Phosphothreonine; by GSK33 Publications
    Modified residuei17 – 171N6-acetyllysineBy similarity
    Modified residuei18 – 181Phosphoserine5 Publications
    Modified residuei27 – 271N6-methyllysine1 Publication
    Modified residuei37 – 371N6-succinyllysineBy similarity
    Modified residuei39 – 391Phosphothreonine1 Publication
    Modified residuei49 – 491N6-acetyllysineBy similarity
    Modified residuei57 – 571CitrullineBy similarity
    Modified residuei78 – 781N6-acetyllysineBy similarity
    Modified residuei138 – 1381Phosphothreonine3 Publications
    Modified residuei155 – 1551Phosphothreonine1 Publication
    Modified residuei168 – 1681N6-acetyllysine1 Publication
    Modified residuei173 – 1731Phosphoserine1 Publication
    Modified residuei189 – 1891Phosphoserine1 Publication

    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. Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase.By similarity6 Publications
    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, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP16401.
    PaxDbiP16401.
    PeptideAtlasiP16401.
    PRIDEiP16401.

    PTM databases

    PhosphoSiteiP16401.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiP16401.
    CleanExiHS_HIST1H1B.
    GenevestigatoriP16401.

    Organism-specific databases

    HPAiCAB012241.

    Interactioni

    Protein-protein interaction databases

    BioGridi109264. 42 interactions.
    IntActiP16401. 4 interactions.
    MINTiMINT-3008567.
    STRINGi9606.ENSP00000330074.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FE2model-A2-226[»]
    2RHIX-ray1.66B23-27[»]
    ProteinModelPortaliP16401.
    SMRiP16401. Positions 40-112.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16401.

    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.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

    eggNOGiNOG258621.
    HOGENOMiHOG000251627.
    HOVERGENiHBG009035.
    InParanoidiP16401.
    KOiK11275.
    OMAiTRVAKAK.
    OrthoDBiEOG74TX2T.
    PhylomeDBiP16401.
    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.

    P16401-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA    50
    VAASKERNGL SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK 100
    GTGASGSFKL NKKAASGEAK PKAKKAGAAK AKKPAGATPK KAKKAAGAKK 150
    AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA AKPKKATKSP AKPKAVKPKA 200
    AKPKAAKPKA AKPKAAKAKK AAAKKK 226
    Length:226
    Mass (Da):22,580
    Last modified:January 23, 2007 - v3
    Checksum:i0BA1402101766FDF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti216 – 2183Missing AA sequence (PubMed:2613692)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861G → D in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036204
    Natural varianti144 – 1441K → R.
    Corresponds to variant rs11970638 [ dbSNP | Ensembl ].
    VAR_049308
    Natural varianti211 – 2111A → T.
    Corresponds to variant rs34144478 [ dbSNP | Ensembl ].
    VAR_049309

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4635.1.
    PIRiS51660.
    RefSeqiNP_005313.1. NM_005322.2.
    UniGeneiHs.131956.

    Genome annotation databases

    EnsembliENST00000331442; ENSP00000330074; ENSG00000184357.
    GeneIDi3009.
    KEGGihsa:3009.
    UCSCiuc003njx.3. human.

    Polymorphism databases

    DMDMi19856407.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4635.1.
    PIRi S51660.
    RefSeqi NP_005313.1. NM_005322.2.
    UniGenei Hs.131956.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FE2 model - A 2-226 [» ]
    2RHI X-ray 1.66 B 23-27 [» ]
    ProteinModelPortali P16401.
    SMRi P16401. Positions 40-112.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109264. 42 interactions.
    IntActi P16401. 4 interactions.
    MINTi MINT-3008567.
    STRINGi 9606.ENSP00000330074.

    PTM databases

    PhosphoSitei P16401.

    Polymorphism databases

    DMDMi 19856407.

    Proteomic databases

    MaxQBi P16401.
    PaxDbi P16401.
    PeptideAtlasi P16401.
    PRIDEi P16401.

    Protocols and materials databases

    DNASUi 3009.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331442 ; ENSP00000330074 ; ENSG00000184357 .
    GeneIDi 3009.
    KEGGi hsa:3009.
    UCSCi uc003njx.3. human.

    Organism-specific databases

    CTDi 3009.
    GeneCardsi GC06M027835.
    HGNCi HGNC:4719. HIST1H1B.
    HPAi CAB012241.
    MIMi 142711. gene.
    neXtProti NX_P16401.
    PharmGKBi PA29097.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258621.
    HOGENOMi HOG000251627.
    HOVERGENi HBG009035.
    InParanoidi P16401.
    KOi K11275.
    OMAi TRVAKAK.
    OrthoDBi EOG74TX2T.
    PhylomeDBi P16401.
    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

    EvolutionaryTracei P16401.
    GeneWikii HIST1H1B.
    GenomeRNAii 3009.
    NextBioi 11932.
    PROi P16401.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16401.
    CleanExi HS_HIST1H1B.
    Genevestigatori P16401.

    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. "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.
      , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-86.

    Entry informationi

    Entry nameiH15_HUMAN
    AccessioniPrimary (citable) accession number: P16401
    Secondary accession number(s): Q14529, Q3MJ42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 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

    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