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P16403

- H12_HUMAN

UniProt

P16403 - H12_HUMAN

Protein

Histone H1.2

Gene

HIST1H1C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (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: UniProt

    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 H1.2
    Alternative name(s):
    Histone H1c
    Histone H1d
    Histone H1s-1
    Gene namesi
    Name:HIST1H1C
    Synonyms:H1F2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4716. HIST1H1C.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Mainly localizes in euchromatin. Distribution goes in parallel with DNA concentration.

    GO - Cellular componenti

    1. nuclear euchromatin Source: UniProt
    2. nucleosome Source: InterPro
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871K → R: Abolishes methylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA29094.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed8 Publications
    Chaini2 – 213212Histone H1.2PRO_0000195906Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine; partial7 Publications
    Modified residuei2 – 21Phosphoserine2 Publications
    Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
    Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
    Modified residuei34 – 341N6-crotonyllysine; alternate1 Publication
    Modified residuei34 – 341N6-methyllysine; alternate1 Publication
    Modified residuei54 – 541CitrullineBy similarity
    Modified residuei64 – 641N6-crotonyllysine1 Publication
    Modified residuei85 – 851N6-crotonyllysine1 Publication
    Modified residuei90 – 901N6-crotonyllysine1 Publication
    Modified residuei97 – 971N6-crotonyllysine; alternate1 Publication
    Modified residuei97 – 971N6-succinyllysine; alternateBy similarity
    Modified residuei104 – 1041Phosphoserine; by PKCBy similarity
    Modified residuei146 – 1461Phosphothreonine1 Publication
    Modified residuei159 – 1591N6-crotonyllysine1 Publication
    Modified residuei168 – 1681N6-crotonyllysine1 Publication
    Modified residuei187 – 1871N6-methyllysine; by EHMT1 and EHMT21 Publication
    Cross-linki206 – 206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 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
    Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.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, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP16403.
    PaxDbiP16403.
    PeptideAtlasiP16403.
    PRIDEiP16403.

    PTM databases

    PhosphoSiteiP16403.

    Expressioni

    Gene expression databases

    BgeeiP16403.
    CleanExiHS_HIST1H1C.
    GenevestigatoriP16403.

    Organism-specific databases

    HPAiCAB011507.

    Interactioni

    Protein-protein interaction databases

    BioGridi109261. 66 interactions.
    IntActiP16403. 21 interactions.
    MINTiMINT-1149485.
    STRINGi9606.ENSP00000339566.

    Structurei

    3D structure databases

    ProteinModelPortaliP16403.
    SMRiP16403. 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

    eggNOGiNOG258621.
    HOGENOMiHOG000251627.
    HOVERGENiHBG009035.
    InParanoidiP16403.
    KOiK11275.
    OMAiMSETAPX.
    OrthoDBiEOG74TX2T.
    PhylomeDBiP16403.
    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.

    P16403-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSETAPAAPA AAPPAEKAPV KKKAAKKAGG TPRKASGPPV SELITKAVAA    50
    SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG 100
    ASGSFKLNKK AASGEAKPKV KKAGGTKPKK PVGAAKKPKK AAGGATPKKS 150
    AKKTPKKAKK PAAATVTKKV AKSPKKAKVA KPKKAAKSAA KAVKPKAAKP 200
    KVVKPKKAAP KKK 213
    Length:213
    Mass (Da):21,365
    Last modified:January 23, 2007 - v2
    Checksum:iAA66EA1901D8D56B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181A → V.
    Corresponds to variant rs2230653 [ dbSNP | Ensembl ].
    VAR_003618
    Natural varianti113 – 1131S → A.
    Corresponds to variant rs34810376 [ dbSNP | Ensembl ].
    VAR_049304
    Natural varianti124 – 1241G → A.
    Corresponds to variant rs12111009 [ dbSNP | Ensembl ].
    VAR_049305

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57129 Genomic DNA. Translation: CAA40408.1.
    AF531300 Genomic DNA. Translation: AAN06700.1.
    AK290947 mRNA. Translation: BAF83636.1.
    AB451259 mRNA. Translation: BAG70073.1.
    AB451385 mRNA. Translation: BAG70199.1.
    U91328 Genomic DNA. No translation available.
    CH471087 Genomic DNA. Translation: EAW55515.1.
    BC002649 mRNA. No translation available.
    CCDSiCCDS4577.1.
    PIRiS26364. HSHU11.
    RefSeqiNP_005310.1. NM_005319.3.
    UniGeneiHs.7644.

    Genome annotation databases

    EnsembliENST00000343677; ENSP00000339566; ENSG00000187837.
    GeneIDi3006.
    KEGGihsa:3006.
    UCSCiuc003nfw.3. human.

    Polymorphism databases

    DMDMi417101.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57129 Genomic DNA. Translation: CAA40408.1 .
    AF531300 Genomic DNA. Translation: AAN06700.1 .
    AK290947 mRNA. Translation: BAF83636.1 .
    AB451259 mRNA. Translation: BAG70073.1 .
    AB451385 mRNA. Translation: BAG70199.1 .
    U91328 Genomic DNA. No translation available.
    CH471087 Genomic DNA. Translation: EAW55515.1 .
    BC002649 mRNA. No translation available.
    CCDSi CCDS4577.1.
    PIRi S26364. HSHU11.
    RefSeqi NP_005310.1. NM_005319.3.
    UniGenei Hs.7644.

    3D structure databases

    ProteinModelPortali P16403.
    SMRi P16403. Positions 36-109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109261. 66 interactions.
    IntActi P16403. 21 interactions.
    MINTi MINT-1149485.
    STRINGi 9606.ENSP00000339566.

    PTM databases

    PhosphoSitei P16403.

    Polymorphism databases

    DMDMi 417101.

    Proteomic databases

    MaxQBi P16403.
    PaxDbi P16403.
    PeptideAtlasi P16403.
    PRIDEi P16403.

    Protocols and materials databases

    DNASUi 3006.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343677 ; ENSP00000339566 ; ENSG00000187837 .
    GeneIDi 3006.
    KEGGi hsa:3006.
    UCSCi uc003nfw.3. human.

    Organism-specific databases

    CTDi 3006.
    GeneCardsi GC06M026055.
    HGNCi HGNC:4716. HIST1H1C.
    HPAi CAB011507.
    MIMi 142710. gene.
    neXtProti NX_P16403.
    PharmGKBi PA29094.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258621.
    HOGENOMi HOG000251627.
    HOVERGENi HBG009035.
    InParanoidi P16403.
    KOi K11275.
    OMAi MSETAPX.
    OrthoDBi EOG74TX2T.
    PhylomeDBi P16403.
    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 HIST1H1C.
    GenomeRNAii 3006.
    NextBioi 11920.
    PROi P16403.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16403.
    CleanExi HS_HIST1H1C.
    Genevestigatori P16403.

    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. "Human H1 histones: conserved and varied sequence elements in two H1 subtype genes."
      Eick S., Nicolai M., Mumberg D., Doenecke D.
      Eur. J. Cell Biol. 49:110-115(1989) [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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Uterus.
    8. "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 2-213.
      Tissue: Spleen.
    9. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 34-46; 55-75 AND 86-97, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    10. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 34-46; 55-63 AND 65-75, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    11. "A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences."
      Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.
      Protein Sci. 3:575-587(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    12. "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.
    13. "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.
    14. "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.
    15. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206.
      Tissue: Mammary cancer.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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].
    18. "Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D."
      Weiss T., Hergeth S., Zeissler U., Izzo A., Tropberger P., Zee B.M., Dundr M., Garcia B.A., Daujat S., Schneider R.
      Epigenetics Chromatin 3:7-7(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-187 BY EHMT1 AND EHMT2, MUTAGENESIS OF LYS-187, IDENTIFICATION BY MASS SPECTROMETRY.
    19. "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-2 AND THR-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
      Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
      Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-90; LYS-97; LYS-159 AND LYS-168.
    22. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiH12_HUMAN
    AccessioniPrimary (citable) accession number: P16403
    Secondary accession number(s): A8K4I2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 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

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3