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P84243

- H33_HUMAN

UniProt

P84243 - H33_HUMAN

Protein

Histone H3.3

Gene

H3F3A

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei32 – 321Interaction with ZMYND11 (PubMed:24590075)1 Publication

    GO - Molecular functioni

    1. nucleosomal DNA binding Source: UniProt
    2. protein binding Source: UniProtKB
    3. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProt
    4. RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProt

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. brain development Source: Ensembl
    3. DNA replication-independent nucleosome assembly Source: UniProt
    4. positive regulation of cell growth Source: UniProt
    5. response to hormone Source: Ensembl

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_2232. RNA Polymerase I Promoter Opening.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_27271. Meiotic recombination.
    REACT_75925. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3.3
    Gene namesi
    Name:H3F3A
    Synonyms:H3.3A, H3F3
    ORF Names:PP781
    AND
    Name:H3F3B
    Synonyms:H3.3B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4764. H3F3A.
    HGNC:4765. H3F3B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nuclear chromosome Source: UniProt
    4. nuclear nucleosome Source: UniProt
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProt
    7. protein complex Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29140.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 136135Histone H3.3PRO_0000221247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Asymmetric dimethylarginine; by PRMT6; alternate3 Publications
    Modified residuei3 – 31Citrulline; alternate1 Publication
    Modified residuei4 – 41Phosphothreonine; by GSG22 Publications
    Modified residuei5 – 51Allysine; alternate
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate4 Publications
    Modified residuei5 – 51N6,N6-dimethyllysine; alternate4 Publications
    Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
    Modified residuei5 – 51N6-crotonyllysine; alternate1 Publication
    Modified residuei5 – 51N6-methyllysine; alternate4 Publications
    Modified residuei7 – 71Phosphothreonine; by PKC1 Publication
    Modified residuei9 – 91Citrulline; alternate2 Publications
    Modified residuei9 – 91Symmetric dimethylarginine; by PRMT5; alternateBy similarity
    Modified residuei10 – 101N6,N6,N6-trimethyllysine; alternate6 Publications
    Modified residuei10 – 101N6,N6-dimethyllysine; alternate6 Publications
    Modified residuei10 – 101N6-acetyllysine; alternate5 Publications
    Modified residuei10 – 101N6-crotonyllysine; alternate1 Publication
    Modified residuei10 – 101N6-methyllysine; alternate6 Publications
    Modified residuei11 – 111Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications
    Modified residuei12 – 121Phosphothreonine; by PKC2 Publications
    Modified residuei15 – 151N6-acetyllysine5 Publications
    Modified residuei18 – 181Asymmetric dimethylarginine; by CARM1; alternate3 Publications
    Modified residuei18 – 181Citrulline; alternate3 Publications
    Modified residuei19 – 191N6-acetyllysine; alternate2 Publications
    Modified residuei19 – 191N6-crotonyllysine; alternate1 Publication
    Modified residuei19 – 191N6-methyllysine; alternate2 Publications
    Modified residuei24 – 241N6-acetyllysine; alternate3 Publications
    Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
    Modified residuei24 – 241N6-methyllysine; alternate1 Publication
    Modified residuei27 – 271Citrulline1 Publication
    Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate4 Publications
    Modified residuei28 – 281N6,N6-dimethyllysine; alternate4 Publications
    Modified residuei28 – 281N6-acetyllysine; alternate3 Publications
    Modified residuei28 – 281N6-crotonyllysine; alternate1 Publication
    Modified residuei28 – 281N6-methyllysine; alternate4 Publications
    Modified residuei29 – 291Phosphoserine; by AURKB, AURKC and RPS6KA56 Publications
    Modified residuei32 – 321Phosphoserine2 Publications
    Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate4 Publications
    Modified residuei37 – 371N6,N6-dimethyllysine; alternate4 Publications
    Modified residuei37 – 371N6-acetyllysine; alternate3 Publications
    Modified residuei37 – 371N6-methyllysine; alternate4 Publications
    Modified residuei38 – 381N6-methyllysineBy similarity
    Modified residuei42 – 421Phosphotyrosine1 Publication
    Modified residuei57 – 571N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei57 – 571N6-acetyllysine; alternate1 Publication
    Modified residuei57 – 571N6-crotonyllysine; alternate1 Publication
    Modified residuei57 – 571N6-methyllysine; by EHMT2; alternate2 Publications
    Modified residuei58 – 581Phosphoserine1 Publication
    Modified residuei65 – 651N6-methyllysine2 Publications
    Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternateBy similarity
    Modified residuei80 – 801N6,N6-dimethyllysine; alternate3 Publications
    Modified residuei80 – 801N6-acetyllysine; alternate1 Publication
    Modified residuei80 – 801N6-methyllysine; alternate3 Publications
    Modified residuei81 – 811Phosphothreonine1 Publication
    Modified residuei108 – 1081PhosphothreonineBy similarity
    Modified residuei116 – 1161N6-acetyllysine1 Publication
    Modified residuei123 – 1231N6-acetyllysine; alternate2 Publications
    Modified residuei123 – 1231N6-methyllysine; alternate2 Publications

    Post-translational modificationi

    Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.11 Publications
    Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.4 Publications
    Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters.10 Publications
    Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me), which are linked to gene repression, are underrepresented. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.16 Publications
    Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes.17 Publications
    Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination By similarity.By similarity
    Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (PubMed:22483618).1 Publication
    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

    Keywords - PTMi

    Acetylation, Citrullination, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP84243.
    PaxDbiP84243.
    PRIDEiP84243.

    PTM databases

    PhosphoSiteiP84243.

    Expressioni

    Developmental stagei

    Expressed throughout the cell cycle independently of DNA synthesis.

    Gene expression databases

    ArrayExpressiP84243.
    BgeeiP84243.
    CleanExiHS_H3F3A.
    HS_H3F3B.
    GenevestigatoriP84243.

    Organism-specific databases

    HPAiCAB011481.
    CAB037221.
    HPA042570.

    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. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes. Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBX5P459732EBI-120658,EBI-78219
    DNMT3AQ9Y6K17EBI-120658,EBI-923653
    HIST2H4BP628053EBI-120658,EBI-302023
    PELP1Q8IZL811EBI-120658,EBI-716449
    SfmbtQ9VK3315EBI-120658,EBI-117801From a different organism.
    TAF3Q5VWG93EBI-120658,EBI-1560087

    Protein-protein interaction databases

    BioGridi109272. 78 interactions.
    109273. 10 interactions.
    DIPiDIP-40046N.
    IntActiP84243. 34 interactions.
    MINTiMINT-4825076.
    STRINGi9606.ENSP00000254810.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi8 – 103
    Beta strandi45 – 473
    Helixi49 – 5911
    Helixi65 – 7915
    Beta strandi80 – 823
    Beta strandi84 – 863
    Helixi87 – 11024
    Beta strandi118 – 1203
    Helixi122 – 13211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L43NMR-A2-13[»]
    3ASKX-ray2.90P/Q/R2-14[»]
    3ASLX-ray1.41B2-12[»]
    3AV2X-ray2.80A/E1-136[»]
    3JVKX-ray1.80C13-20[»]
    3MUKX-ray1.75D22-29[»]
    3MULX-ray1.65D13-20[»]
    3QL9X-ray0.93C2-16[»]
    3QLAX-ray1.60C/F2-16[»]
    3QLCX-ray2.50C/D2-16[»]
    4GNEX-ray1.47B2-8[»]
    4GNFX-ray1.55C2-16[»]
    4GNGX-ray1.73B/F2-16[»]
    4GU0X-ray3.10E/F2-27[»]
    4GURX-ray2.51C2-22[»]
    4GUSX-ray2.23C2-22[»]
    4GY5X-ray2.96E/F2-18[»]
    4H9NX-ray1.95A2-136[»]
    4H9OX-ray2.05A2-136[»]
    4H9PX-ray2.20A2-136[»]
    4H9QX-ray1.95A2-136[»]
    4H9RX-ray2.20A2-136[»]
    4H9SX-ray2.60A/B2-136[»]
    4HGAX-ray2.80B1-136[»]
    4L58X-ray1.48B2-13[»]
    4N4IX-ray2.00B20-43[»]
    4O62X-ray1.78D2-12[»]
    ProteinModelPortaliP84243.
    SMRiP84243. Positions 17-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP84243.

    Family & Domainsi

    Domaini

    Specific interaction of trimethylated form at 'Lys-36' (H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-32 residue with a composite pocket formed by the tandem bromo-PWWP domains.1 Publication

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    HOVERGENiHBG001172.
    InParanoidiP84243.
    KOiK11253.
    OMAiHIVMART.
    PhylomeDBiP84243.
    TreeFamiTF314241.

    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.

    P84243-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR    50
    EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY 100
    LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA 136
    Length:136
    Mass (Da):15,328
    Last modified:January 23, 2007 - v2
    Checksum:i5158ED279E6F9E1C
    GO

    Sequence cautioni

    The sequence CAH73371.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91R → L in AAH81561. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11354 mRNA. Translation: AAA52653.1.
    M11353 mRNA. Translation: AAA52654.1.
    Z48950 Genomic DNA. Translation: CAA88778.1.
    X05855, X05856, X05857 Genomic DNA. Translation: CAA29288.1. Sequence problems.
    AF218029 mRNA. Translation: AAG17271.1.
    BX537379 mRNA. Translation: CAD97621.1.
    AL512343 Genomic DNA. Translation: CAH73371.1. Sequence problems.
    AL512343 Genomic DNA. Translation: CAH73372.1.
    BC001124 mRNA. Translation: AAH01124.1.
    BC006497 mRNA. Translation: AAH06497.1.
    BC012813 mRNA. Translation: AAH12813.1.
    BC017558 mRNA. Translation: AAH17558.1.
    BC029405 mRNA. Translation: AAH29405.1.
    BC038989 mRNA. Translation: AAH38989.1.
    BC066901 mRNA. No translation available.
    BC067757 mRNA. No translation available.
    BC081560 mRNA. Translation: AAH81560.1.
    BC081561 mRNA. Translation: AAH81561.1.
    BC095447 mRNA. Translation: AAH95447.1.
    BC108701 mRNA. Translation: AAI08702.1.
    CCDSiCCDS11729.1.
    CCDS1550.1.
    PIRiA27501. HSHU33.
    RefSeqiNP_002098.1. NM_002107.4.
    NP_005315.1. NM_005324.3.
    UniGeneiHs.180877.
    Hs.533624.
    Hs.726012.

    Genome annotation databases

    EnsembliENST00000254810; ENSP00000254810; ENSG00000132475.
    ENST00000366813; ENSP00000355778; ENSG00000163041.
    ENST00000366815; ENSP00000355780; ENSG00000163041.
    ENST00000366816; ENSP00000355781; ENSG00000163041.
    ENST00000586607; ENSP00000466020; ENSG00000132475.
    ENST00000587560; ENSP00000468714; ENSG00000132475.
    ENST00000589599; ENSP00000465813; ENSG00000132475.
    GeneIDi3020.
    3021.
    KEGGihsa:3020.
    hsa:3021.
    UCSCiuc001hpw.3. human.

    Polymorphism databases

    DMDMi55977062.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Histone H3 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11354 mRNA. Translation: AAA52653.1 .
    M11353 mRNA. Translation: AAA52654.1 .
    Z48950 Genomic DNA. Translation: CAA88778.1 .
    X05855 , X05856 , X05857 Genomic DNA. Translation: CAA29288.1 . Sequence problems.
    AF218029 mRNA. Translation: AAG17271.1 .
    BX537379 mRNA. Translation: CAD97621.1 .
    AL512343 Genomic DNA. Translation: CAH73371.1 . Sequence problems.
    AL512343 Genomic DNA. Translation: CAH73372.1 .
    BC001124 mRNA. Translation: AAH01124.1 .
    BC006497 mRNA. Translation: AAH06497.1 .
    BC012813 mRNA. Translation: AAH12813.1 .
    BC017558 mRNA. Translation: AAH17558.1 .
    BC029405 mRNA. Translation: AAH29405.1 .
    BC038989 mRNA. Translation: AAH38989.1 .
    BC066901 mRNA. No translation available.
    BC067757 mRNA. No translation available.
    BC081560 mRNA. Translation: AAH81560.1 .
    BC081561 mRNA. Translation: AAH81561.1 .
    BC095447 mRNA. Translation: AAH95447.1 .
    BC108701 mRNA. Translation: AAI08702.1 .
    CCDSi CCDS11729.1.
    CCDS1550.1.
    PIRi A27501. HSHU33.
    RefSeqi NP_002098.1. NM_002107.4.
    NP_005315.1. NM_005324.3.
    UniGenei Hs.180877.
    Hs.533624.
    Hs.726012.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L43 NMR - A 2-13 [» ]
    3ASK X-ray 2.90 P/Q/R 2-14 [» ]
    3ASL X-ray 1.41 B 2-12 [» ]
    3AV2 X-ray 2.80 A/E 1-136 [» ]
    3JVK X-ray 1.80 C 13-20 [» ]
    3MUK X-ray 1.75 D 22-29 [» ]
    3MUL X-ray 1.65 D 13-20 [» ]
    3QL9 X-ray 0.93 C 2-16 [» ]
    3QLA X-ray 1.60 C/F 2-16 [» ]
    3QLC X-ray 2.50 C/D 2-16 [» ]
    4GNE X-ray 1.47 B 2-8 [» ]
    4GNF X-ray 1.55 C 2-16 [» ]
    4GNG X-ray 1.73 B/F 2-16 [» ]
    4GU0 X-ray 3.10 E/F 2-27 [» ]
    4GUR X-ray 2.51 C 2-22 [» ]
    4GUS X-ray 2.23 C 2-22 [» ]
    4GY5 X-ray 2.96 E/F 2-18 [» ]
    4H9N X-ray 1.95 A 2-136 [» ]
    4H9O X-ray 2.05 A 2-136 [» ]
    4H9P X-ray 2.20 A 2-136 [» ]
    4H9Q X-ray 1.95 A 2-136 [» ]
    4H9R X-ray 2.20 A 2-136 [» ]
    4H9S X-ray 2.60 A/B 2-136 [» ]
    4HGA X-ray 2.80 B 1-136 [» ]
    4L58 X-ray 1.48 B 2-13 [» ]
    4N4I X-ray 2.00 B 20-43 [» ]
    4O62 X-ray 1.78 D 2-12 [» ]
    ProteinModelPortali P84243.
    SMRi P84243. Positions 17-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109272. 78 interactions.
    109273. 10 interactions.
    DIPi DIP-40046N.
    IntActi P84243. 34 interactions.
    MINTi MINT-4825076.
    STRINGi 9606.ENSP00000254810.

    PTM databases

    PhosphoSitei P84243.

    Polymorphism databases

    DMDMi 55977062.

    Proteomic databases

    MaxQBi P84243.
    PaxDbi P84243.
    PRIDEi P84243.

    Protocols and materials databases

    DNASUi 3020.
    3021.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254810 ; ENSP00000254810 ; ENSG00000132475 .
    ENST00000366813 ; ENSP00000355778 ; ENSG00000163041 .
    ENST00000366815 ; ENSP00000355780 ; ENSG00000163041 .
    ENST00000366816 ; ENSP00000355781 ; ENSG00000163041 .
    ENST00000586607 ; ENSP00000466020 ; ENSG00000132475 .
    ENST00000587560 ; ENSP00000468714 ; ENSG00000132475 .
    ENST00000589599 ; ENSP00000465813 ; ENSG00000132475 .
    GeneIDi 3020.
    3021.
    KEGGi hsa:3020.
    hsa:3021.
    UCSCi uc001hpw.3. human.

    Organism-specific databases

    CTDi 3020.
    3021.
    H-InvDB HIX0135637.
    HGNCi HGNC:4764. H3F3A.
    HGNC:4765. H3F3B.
    HPAi CAB011481.
    CAB037221.
    HPA042570.
    MIMi 601058. gene.
    601128. gene.
    neXtProti NX_P84243.
    PharmGKBi PA29140.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2036.
    HOVERGENi HBG001172.
    InParanoidi P84243.
    KOi K11253.
    OMAi HIVMART.
    PhylomeDBi P84243.
    TreeFami TF314241.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_2232. RNA Polymerase I Promoter Opening.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_27271. Meiotic recombination.
    REACT_75925. Amyloids.

    Miscellaneous databases

    EvolutionaryTracei P84243.
    GeneWikii H3F3A.
    NextBioi 11966.
    PROi P84243.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P84243.
    Bgeei P84243.
    CleanExi HS_H3F3A.
    HS_H3F3B.
    Genevestigatori P84243.

    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. "Structure of a human histone cDNA: evidence that basally expressed histone genes have intervening sequences and encode polyadenylylated mRNAs."
      Wells D., Kedes L.
      Proc. Natl. Acad. Sci. U.S.A. 82:2834-2838(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A).
      Tissue: Fibroblast.
    2. "Unusual structure, evolutionary conservation of non-coding sequences and numerous pseudogenes characterize the human H3.3 histone multigene family."
      Wells D., Hoffman D., Kedes L.
      Nucleic Acids Res. 15:2871-2889(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (H3F3A).
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3F3B).
      Tissue: Testis.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3F3B).
      Tissue: Retina.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (H3F3A AND H3F3B).
      Tissue: Bone marrow, Brain, Colon, Eye, Lung, Muscle, Spinal cord, Testis and Uterus.
    8. "Human spleen histone H3. Isolation and amino acid sequence."
      Ohe Y., Iwai K.
      J. Biochem. 90:1205-1211(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-10; LYS-28 AND LYS-37, ACETYLATION AT LYS-15 AND LYS-24.
    9. Cited for: PROTEIN SEQUENCE OF 28-41, METHYLATION AT LYS-5; LYS-10; LYS-28 AND LYS-37, PHOSPHORYLATION AT THR-4; SER-11; SER-29 AND SER-32, ACETYLATION AT LYS-10 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation."
      Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M., Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.
      J. Biol. Chem. 274:25543-25549(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, PHOSPHORYLATION AT SER-11 AND SER-29.
    11. "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins."
      Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.
      Nature 410:116-120(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-10.
    12. "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
      Goto H., Yasui Y., Nigg E.A., Inagaki M.
      Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
    13. "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase."
      Preuss U., Landsberg G., Scheidtmann K.H.
      Nucleic Acids Res. 31:878-885(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.
    14. "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis."
      Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.
      Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIRA.
    15. "Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1."
      Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.
      J. Biol. Chem. 279:54348-54357(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-18.
    16. Cited for: METHYLATION AT LYS-80.
    17. Cited for: CITRULLINATION AT ARG-9 AND ARG-18, METHYLATION AT ARG-18.
    18. "Variant histone H3.3 marks promoters of transcriptionally active genes during mammalian cell division."
      Chow C.-M., Georgiou A., Szutorisz H., Maia e Silva A., Pombo A., Barahona I., Dargelos E., Canzonetta C., Dillon N.
      EMBO Rep. 6:354-360(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment."
      Dai J., Sultan S., Taylor S.S., Higgins J.M.G.
      Genes Dev. 19:472-488(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
    20. "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
      Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
      J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-29.
    21. "Serine 31 phosphorylation of histone variant H3.3 is specific to regions bordering centromeres in metaphase chromosomes."
      Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J., Hunt D.F., Allis C.D.
      Proc. Natl. Acad. Sci. U.S.A. 102:6344-6349(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11; SER-29 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY.
    22. "Histone H3.3 deposition at E2F-regulated genes is linked to transcription."
      Daury L., Chailleux C., Bonvallet J., Trouche D.
      EMBO Rep. 7:66-71(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Expression patterns and post-translational modifications associated with mammalian histone H3 variants."
      Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G., Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.
      J. Biol. Chem. 281:559-568(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
    24. "Mass spectrometric characterization of human histone H3: a bird's eye view."
      Thomas C.E., Kelleher N.L., Mizzen C.A.
      J. Proteome Res. 5:240-247(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10, IDENTIFICATION BY MASS SPECTROMETRY.
    25. "Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17."
      Miao F., Li S., Chavez V., Lanting L., Natarajan R.
      Mol. Endocrinol. 20:1562-1573(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, CITRULLINATION AT ARG-18.
    26. "PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation."
      Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y., Hsieh J., Bauer U.M.
      Genes Dev. 21:3369-3380(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-3 BY PRMT6.
    27. "Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
      Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
      Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
    28. "Organismal differences in post-translational modifications in histones H3 and H4."
      Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
      J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
      Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
      J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-37.
    30. "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive."
      Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M., Schuchlautz H., Luescher B., Amati B.
      Nature 449:933-937(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-3 BY PRMT6.
    31. "Arginine methylation of the histone H3 tail impedes effector binding."
      Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J., Richard S., Bedford M.T.
      J. Biol. Chem. 283:3006-3010(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-3 BY PRMT6.
    32. "Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation."
      Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K., Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H., Buettner R., Schule R.
      Nat. Cell Biol. 10:53-60(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-12.
    33. Cited for: ACETYLATION AT LYS-116 AND LYS-123.
    34. "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin."
      Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.
      Nature 461:819-822(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-42.
    35. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    36. "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-28 AND LYS-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
      Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
      Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
    38. Cited for: PHOSPHORYLATION AT THR-7.
    39. "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-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
    40. "Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA."
      Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M.
      Mol. Cell 46:7-17(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-57.
    41. Cited for: ALLYSINE AT LYS-5.
    42. "Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer."
      Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.
      Cell 152:859-872(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-123.
    43. "ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression."
      Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K., Ren Y., Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.
      Nature 508:263-268(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-43 IN COMPLEX WITH ZMYND11.

    Entry informationi

    Entry nameiH33_HUMAN
    AccessioniPrimary (citable) accession number: P84243
    Secondary accession number(s): P06351
    , P33155, Q5VV55, Q5VV56, Q66I33, Q9V3W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 115 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

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

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3