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P08898

- H3_CAEEL

UniProt

P08898 - H3_CAEEL

Protein

Histone H3

Gene

his-2

more
Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3
    Gene namesi
    Name:his-2
    ORF Names:T10C6.13
    AND
    Name:his-6
    ORF Names:F45F2.13
    AND
    Name:his-9
    ORF Names:ZK131.3
    AND
    Name:his-13
    ORF Names:ZK131.7
    AND
    Name:his-17
    ORF Names:K06C4.5
    AND
    Name:his-25
    ORF Names:ZK131.2
    AND
    Name:his-27
    ORF Names:K06C4.13
    AND
    Name:his-32
    ORF Names:F17E9.10
    AND
    Name:his-42
    ORF Names:F08G2.3
    AND
    Name:his-45
    ORF Names:B0035.10
    AND
    Name:his-49
    ORF Names:F07B7.5
    AND
    Name:his-55
    ORF Names:F54E12.1
    AND
    Name:his-59
    ORF Names:F55G1.2
    AND
    Name:his-63
    ORF Names:F22B3.2
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome II, UP000001940: Chromosome IV, UP000001940: Chromosome V

    Organism-specific databases

    WormBaseiB0035.10; CE03253; WBGene00001919; his-45.
    F07B7.5; CE03253; WBGene00001923; his-49.
    F08G2.3; CE03253; WBGene00001916; his-42.
    F17E9.10; CE03253; WBGene00001906; his-32.
    F22B3.2; CE03253; WBGene00001937; his-63.
    F45F2.13; CE03253; WBGene00001880; his-6.
    F54E12.1; CE03253; WBGene00001929; his-55.
    F55G1.2; CE03253; WBGene00001933; his-59.
    K06C4.13; CE03253; WBGene00001901; his-27.
    K06C4.5; CE03253; WBGene00001891; his-17.
    T10C6.13; CE03253; WBGene00001876; his-2.
    ZK131.2; CE03253; WBGene00001899; his-25.
    ZK131.3; CE03253; WBGene00001883; his-9.
    ZK131.7; CE03253; WBGene00001887; his-13.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleosome Source: UniProtKB-KW
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 136135Histone H3PRO_0000221297Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate4 Publications
    Modified residuei5 – 51N6,N6-dimethyllysine; alternate4 Publications
    Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
    Modified residuei5 – 51N6-methyllysine; alternate4 Publications
    Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate6 Publications
    Modified residuei10 – 101N6,N6-dimethyllysine; alternate6 Publications
    Modified residuei10 – 101N6-acetyllysine; alternate2 Publications
    Modified residuei11 – 111Phosphoserine7 Publications
    Modified residuei15 – 151N6-acetyllysine3 Publications
    Modified residuei24 – 241N6-acetyllysine1 Publication
    Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei28 – 281N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei28 – 281N6-methyllysine; alternate2 Publications
    Modified residuei29 – 291Phosphoserine2 Publications
    Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate3 Publications
    Modified residuei37 – 371N6,N6-dimethyllysine; alternate3 Publications
    Modified residuei37 – 371N6-methyllysine; alternate3 Publications
    Modified residuei80 – 801N6-methyllysine1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-11 and Ser-29 during M phase. Phosphorylation of Ser-11 requires air-2 but not air-1. Dephosphorylated by gsp-1 and/or gsp-2 during chromosome segregation.7 Publications
    Acetylation is generally linked to gene activation.By similarity
    Methylation at Lys-5 is linked to gene activation and is absent from male inactive X chromosome chromatin. Methylation at Lys-10 is linked to gene repression and is enriched in male inactive X chromosome chromatin. Methylation at Lys-37 occurs on the entire length of autosomes during meiotic prophase. Trimethylation at Lys-10 and Lys-37 is specifically antagonized by jmjd-2. Dimethylation and trimethylation at Lys-28 occurs in all nuclei. The mes-2-mes-3-mes-6 complex may be responsible for Lys-28 methylation in most of the germline and in the early embryo.7 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP08898.

    Interactioni

    Subunit structurei

    The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

    Protein-protein interaction databases

    BioGridi42741. 1 interaction.
    45065. 3 interactions.
    50996. 1 interaction.
    IntActiP08898. 1 interaction.
    STRINGi6239.F07B7.5.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Beta strandi25 – 273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N9LX-ray2.80B2-16[»]
    3N9NX-ray2.30B/C2-33[»]
    3N9OX-ray2.31B2-16[»]
    C2-18[»]
    3N9PX-ray2.39B/C2-33[»]
    3N9QX-ray2.30B2-16[»]
    C20-36[»]
    ProteinModelPortaliP08898.
    SMRiP08898. Positions 17-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08898.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    HOGENOMiHOG000155290.
    InParanoidiP08898.
    KOiK11253.
    OrthoDBiEOG7HB5C2.
    PhylomeDBiP08898.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view]
    PANTHERiPTHR11426. PTHR11426. 1 hit.
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00622. HISTONEH3.
    SMARTiSM00428. H3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00322. HISTONE_H3_1. 1 hit.
    PS00959. HISTONE_H3_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08898-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTKQTARK STGGKAPRKQ LATKAARKSA PASGGVKKPH RYRPGTVALR    50
    EIRRYQKSTE LLIRRAPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY 100
    LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA 136
    Length:136
    Mass (Da):15,376
    Last modified:January 23, 2007 - v4
    Checksum:i40D7DE0EF5BA6F1F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti97 – 971C → A.
    Natural varianti101 – 1011L → I.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15634 Genomic DNA. Translation: CAA33644.1.
    FO081018 Genomic DNA. Translation: CCD68531.1.
    FO081059 Genomic DNA. Translation: CCD68868.1.
    FO081135 Genomic DNA. Translation: CCD69390.1.
    FO081223 Genomic DNA. Translation: CCD70027.1.
    FO081551 Genomic DNA. Translation: CCD72363.1.
    FO081551 Genomic DNA. Translation: CCD72373.1.
    Z68336 Genomic DNA. Translation: CAA92733.1.
    Z73102 Genomic DNA. Translation: CAA97411.1.
    Z81495 Genomic DNA. Translation: CAB04057.1.
    Z82271 Genomic DNA. Translation: CAB05209.1.
    Z83245 Genomic DNA. Translation: CAB05831.1.
    Z83245 Genomic DNA. Translation: CAB05833.1.
    Z83245 Genomic DNA. Translation: CAB05834.1.
    Z93388 Genomic DNA. Translation: CAB07653.1.
    AF304122 mRNA. Translation: AAG50235.1.
    PIRiS04241. HSKW3.
    RefSeqiNP_001263958.1. NM_001277029.1.
    NP_496890.1. NM_064489.1.
    NP_496894.1. NM_064493.5.
    NP_496895.1. NM_064494.1.
    NP_496899.1. NM_064498.1.
    NP_501204.1. NM_068803.3.
    NP_501407.1. NM_069006.3.
    NP_502134.1. NM_069733.3.
    NP_502138.1. NM_069737.1.
    NP_502153.1. NM_069752.3.
    NP_505199.1. NM_072798.1.
    NP_505276.1. NM_072875.1.
    NP_505292.1. NM_072891.1.
    NP_505297.1. NM_072896.3.
    NP_507033.1. NM_074632.3.
    UniGeneiCel.12716.
    Cel.12871.
    Cel.21447.
    Cel.21596.
    Cel.21806.
    Cel.21871.
    Cel.2350.
    Cel.27007.
    Cel.29106.
    Cel.29299.
    Cel.32605.
    Cel.32856.
    Cel.33056.

    Genome annotation databases

    GeneIDi175030.
    175031.
    177628.
    180074.
    181821.
    184113.
    184200.
    184804.
    186250.
    186325.
    191668.
    191672.
    191673.
    246024.
    KEGGicel:CELE_B0035.10.
    cel:CELE_F07B7.5.
    cel:CELE_F08G2.3.
    cel:CELE_F17E9.10.
    cel:CELE_F22B3.2.
    cel:CELE_F45F2.13.
    cel:CELE_F54E12.1.
    cel:CELE_F55G1.2.
    cel:CELE_K06C4.13.
    cel:CELE_K06C4.5.
    cel:CELE_T10C6.13.
    cel:CELE_ZK131.2.
    cel:CELE_ZK131.3.
    cel:CELE_ZK131.7.
    UCSCiZK131.7. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15634 Genomic DNA. Translation: CAA33644.1 .
    FO081018 Genomic DNA. Translation: CCD68531.1 .
    FO081059 Genomic DNA. Translation: CCD68868.1 .
    FO081135 Genomic DNA. Translation: CCD69390.1 .
    FO081223 Genomic DNA. Translation: CCD70027.1 .
    FO081551 Genomic DNA. Translation: CCD72363.1 .
    FO081551 Genomic DNA. Translation: CCD72373.1 .
    Z68336 Genomic DNA. Translation: CAA92733.1 .
    Z73102 Genomic DNA. Translation: CAA97411.1 .
    Z81495 Genomic DNA. Translation: CAB04057.1 .
    Z82271 Genomic DNA. Translation: CAB05209.1 .
    Z83245 Genomic DNA. Translation: CAB05831.1 .
    Z83245 Genomic DNA. Translation: CAB05833.1 .
    Z83245 Genomic DNA. Translation: CAB05834.1 .
    Z93388 Genomic DNA. Translation: CAB07653.1 .
    AF304122 mRNA. Translation: AAG50235.1 .
    PIRi S04241. HSKW3.
    RefSeqi NP_001263958.1. NM_001277029.1.
    NP_496890.1. NM_064489.1.
    NP_496894.1. NM_064493.5.
    NP_496895.1. NM_064494.1.
    NP_496899.1. NM_064498.1.
    NP_501204.1. NM_068803.3.
    NP_501407.1. NM_069006.3.
    NP_502134.1. NM_069733.3.
    NP_502138.1. NM_069737.1.
    NP_502153.1. NM_069752.3.
    NP_505199.1. NM_072798.1.
    NP_505276.1. NM_072875.1.
    NP_505292.1. NM_072891.1.
    NP_505297.1. NM_072896.3.
    NP_507033.1. NM_074632.3.
    UniGenei Cel.12716.
    Cel.12871.
    Cel.21447.
    Cel.21596.
    Cel.21806.
    Cel.21871.
    Cel.2350.
    Cel.27007.
    Cel.29106.
    Cel.29299.
    Cel.32605.
    Cel.32856.
    Cel.33056.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3N9L X-ray 2.80 B 2-16 [» ]
    3N9N X-ray 2.30 B/C 2-33 [» ]
    3N9O X-ray 2.31 B 2-16 [» ]
    C 2-18 [» ]
    3N9P X-ray 2.39 B/C 2-33 [» ]
    3N9Q X-ray 2.30 B 2-16 [» ]
    C 20-36 [» ]
    ProteinModelPortali P08898.
    SMRi P08898. Positions 17-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 42741. 1 interaction.
    45065. 3 interactions.
    50996. 1 interaction.
    IntActi P08898. 1 interaction.
    STRINGi 6239.F07B7.5.

    Proteomic databases

    PaxDbi P08898.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 175030.
    175031.
    177628.
    180074.
    181821.
    184113.
    184200.
    184804.
    186250.
    186325.
    191668.
    191672.
    191673.
    246024.
    KEGGi cel:CELE_B0035.10.
    cel:CELE_F07B7.5.
    cel:CELE_F08G2.3.
    cel:CELE_F17E9.10.
    cel:CELE_F22B3.2.
    cel:CELE_F45F2.13.
    cel:CELE_F54E12.1.
    cel:CELE_F55G1.2.
    cel:CELE_K06C4.13.
    cel:CELE_K06C4.5.
    cel:CELE_T10C6.13.
    cel:CELE_ZK131.2.
    cel:CELE_ZK131.3.
    cel:CELE_ZK131.7.
    UCSCi ZK131.7. c. elegans.

    Organism-specific databases

    CTDi 175030.
    175031.
    177628.
    180074.
    181821.
    184113.
    184200.
    184804.
    186250.
    186325.
    191668.
    191672.
    191673.
    246024.
    WormBasei B0035.10 ; CE03253 ; WBGene00001919 ; his-45.
    F07B7.5 ; CE03253 ; WBGene00001923 ; his-49.
    F08G2.3 ; CE03253 ; WBGene00001916 ; his-42.
    F17E9.10 ; CE03253 ; WBGene00001906 ; his-32.
    F22B3.2 ; CE03253 ; WBGene00001937 ; his-63.
    F45F2.13 ; CE03253 ; WBGene00001880 ; his-6.
    F54E12.1 ; CE03253 ; WBGene00001929 ; his-55.
    F55G1.2 ; CE03253 ; WBGene00001933 ; his-59.
    K06C4.13 ; CE03253 ; WBGene00001901 ; his-27.
    K06C4.5 ; CE03253 ; WBGene00001891 ; his-17.
    T10C6.13 ; CE03253 ; WBGene00001876 ; his-2.
    ZK131.2 ; CE03253 ; WBGene00001899 ; his-25.
    ZK131.3 ; CE03253 ; WBGene00001883 ; his-9.
    ZK131.7 ; CE03253 ; WBGene00001887 ; his-13.

    Phylogenomic databases

    eggNOGi COG2036.
    HOGENOMi HOG000155290.
    InParanoidi P08898.
    KOi K11253.
    OrthoDBi EOG7HB5C2.
    PhylomeDBi P08898.

    Miscellaneous databases

    EvolutionaryTracei P08898.
    NextBioi 886476.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view ]
    PANTHERi PTHR11426. PTHR11426. 1 hit.
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00622. HISTONEH3.
    SMARTi SM00428. H3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00322. HISTONE_H3_1. 1 hit.
    PS00959. HISTONE_H3_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequences of Caenorhabditis elegans core histone genes. Genes for different histone classes share common flanking sequence elements."
      Roberts S.B., Emmons S.W., Childs G.
      J. Mol. Biol. 206:567-577(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS-10).
      Strain: Bristol N2.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    3. "The Caenorhabditis elegans transcriptome project, a complementary view of the genome."
      Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIS-4).
      Strain: Bristol N2.
    4. "The primary structure of histone H3 from the nematode Caenorhabditis elegans."
      Vanfleteren J.R., van Bun S.M., van Beeumen J.J.
      FEBS Lett. 211:59-63(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-136, ACETYLATION AT LYS-5; LYS-15 AND LYS-24, METHYLATION AT LYS-10; LYS-28; LYS-37 AND LYS-80.
      Strain: DR27.
    5. "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes."
      Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D.
      Cell 102:279-291(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11.
    6. "The aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous Chromosomes during meiosis."
      Kaitna S., Pasierbek P., Jantsch M., Loidl J., Glotzer M.
      Curr. Biol. 12:798-812(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    7. "X-chromosome silencing in the germline of C. elegans."
      Kelly W.G., Schaner C.E., Dernburg A.F., Lee M.-H., Kim S.K., Villeneuve A.M., Reinke V.
      Development 129:479-492(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5 AND LYS-10, PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-10 AND LYS-15.
    8. "Germline X chromosomes exhibit contrasting patterns of histone H3 methylation in Caenorhabditis elegans."
      Reuben M., Lin R.
      Dev. Biol. 245:71-82(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5 AND LYS-10.
    9. "The C. elegans Tousled-like kinase (TLK-1) has an essential role in transcription."
      Han Z., Saam J.R., Adams H.P., Mango S.E., Schumacher J.M.
      Curr. Biol. 13:1921-1929(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, METHYLATION AT LYS-5; LYS-10 AND LYS-37.
    10. "Role of Caenorhabditis elegans protein phosphatase type 1, CeGLC-7 beta, in metaphase to anaphase transition during embryonic development."
      Sassa T., Ueda-Ohba H., Kitamura K., Harada S., Hosono R.
      Exp. Cell Res. 287:350-360(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11.
    11. "Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal condensation and segregation, and cytokinesis."
      Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.
      Genes Cells 8:857-872(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    12. "The MES-2/MES-3/MES-6 complex and regulation of histone H3 methylation in C. elegans."
      Bender L.B., Cao R., Zhang Y., Strome S.
      Curr. Biol. 14:1639-1643(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-28.
    13. "Meiotic pairing and imprinted X chromatin assembly in Caenorhabditis elegans."
      Bean C.J., Schaner C.E., Kelly W.G.
      Nat. Genet. 36:100-105(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT LYS-5 AND LYS-10, PHOSPHORYLATION AT SER-11.
    14. "Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases."
      Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z., Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.
      Cell 125:467-481(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-10 AND LYS-37.

    Entry informationi

    Entry nameiH3_CAEEL
    AccessioniPrimary (citable) accession number: P08898
    Secondary accession number(s): Q9TW44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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