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Q01105

- SET_HUMAN

UniProt

Q01105 - SET_HUMAN

Protein

Protein SET

Gene

SET

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei283 – 2842Breakpoint for translocation to form SET-CAN oncogene

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein phosphatase inhibitor activity Source: ProtInc
    5. protein phosphatase type 2A regulator activity Source: UniProtKB

    GO - Biological processi

    1. DNA replication Source: ProtInc
    2. gene expression Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. negative regulation of catalytic activity Source: GOC
    6. negative regulation of histone acetylation Source: UniProtKB
    7. negative regulation of neuron apoptotic process Source: MGI
    8. negative regulation of transcription, DNA-templated Source: UniProtKB
    9. nucleocytoplasmic transport Source: UniProtKB
    10. nucleosome assembly Source: ProtInc
    11. nucleosome disassembly Source: UniProtKB
    12. regulation of catalytic activity Source: GOC
    13. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_172744. Condensation of Prophase Chromosomes.
    REACT_25218. HuR stabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein SET
    Alternative name(s):
    HLA-DR-associated protein II
    Inhibitor of granzyme A-activated DNase
    Short name:
    IGAAD
    PHAPII
    Phosphatase 2A inhibitor I2PP2A
    Short name:
    I-2PP2A
    Template-activating factor I
    Short name:
    TAF-I
    Gene namesi
    Name:SET
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:10760. SET.

    Subcellular locationi

    Cytoplasmcytosol. Endoplasmic reticulum. Nucleusnucleoplasm
    Note: In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavage by GZMA, moves rapidly to the nucleus, where it is found in the nucleoplasm, avoiding the nucleolus. Similar translocation to the nucleus is also observed for lymphocyte-activated killer cells after the addition of calcium.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB-SubCell
    3. endoplasmic reticulum Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB
    7. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving SET is found in some cases of acute undifferentiated leukemia (AUL). Translocation t(6;9)(q21;q34.1) with NUP214/CAN.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA35678.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 290289Protein SETPRO_0000185662Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N,N-trimethylalanineBy similarity
    Modified residuei7 – 71Phosphoserine3 Publications
    Modified residuei68 – 681N6-acetyllysineBy similarity
    Modified residuei132 – 1321N6-acetyllysine1 Publication
    Modified residuei146 – 1461PhosphotyrosineBy similarity
    Modified residuei150 – 1501N6-acetyllysine1 Publication
    Cross-linki154 – 154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei172 – 1721N6-acetyllysine1 Publication

    Post-translational modificationi

    Isoform 2 is phosphorylated on Ser-15 and Thr-23.3 Publications
    Isoform 2 is acetylated on Lys-11.1 Publication
    Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.By similarity
    N-terminus of isoform 1 is methylated by METTL11A/NTM1. Mainly trimethylated By similarity.By similarity
    Isoform 2 is cleaved after Lys-176 by GZMA. The cleavage inhibits its nucelosome assembly activity and disrupts the inhibition on NME1.3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ01105.
    PaxDbiQ01105.
    PeptideAtlasiQ01105.
    PRIDEiQ01105.

    PTM databases

    PhosphoSiteiQ01105.

    Expressioni

    Tissue specificityi

    Widely expressed. Low levels in quiescent cells during serum starvation, contact inhibition or differentiation. Highly expressed in Wilms' tumor.

    Gene expression databases

    ArrayExpressiQ01105.
    BgeeiQ01105.
    CleanExiHS_SET.
    GenevestigatoriQ01105.

    Organism-specific databases

    HPAiCAB005232.

    Interactioni

    Subunit structurei

    Headphone-shaped homodimer. Isoforms 1 and 2 interact directly with each other and with ANP32A within the tripartite INHAT (inhibitor of acetyltransferases) complex. Isoform 1 and isoform 2 interact also with histones. Isoform 2 is a component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1, but not NME2 or TREX2. Within this complex, directly interacts with ANP32A, NME1, HMGB2 and TREX1; the interaction with ANP32A is enhanced after cleavage. Interacts with APBB1, CHTOP, SETBP1, SGOL1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FOXO1Q127785EBI-1053182,EBI-1108782
    MDM2Q009872EBI-1053182,EBI-389668
    PRKAR1AP106442EBI-1053182,EBI-476431
    RAC1P630008EBI-1053182,EBI-413628
    TAF1AQ155732EBI-1053182,EBI-2510647
    TAF1BQ53T943EBI-1053182,EBI-1560239
    TAF1CQ155724EBI-1053182,EBI-2510659
    TBPP202264EBI-1053182,EBI-355371
    UBTFP174804EBI-1053182,EBI-396235

    Protein-protein interaction databases

    BioGridi112316. 105 interactions.
    DIPiDIP-33561N.
    IntActiQ01105. 75 interactions.
    MINTiMINT-4990855.
    STRINGi9606.ENSP00000361777.

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 8851
    Helixi94 – 1007
    Helixi103 – 1064
    Helixi111 – 1166
    Helixi117 – 1193
    Beta strandi120 – 1278
    Beta strandi135 – 1417
    Beta strandi145 – 1484
    Beta strandi150 – 1567
    Beta strandi166 – 1683
    Helixi203 – 2064
    Helixi215 – 2239
    Turni224 – 2274
    Helixi230 – 2334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E50X-ray2.30A/B/P/Q38-238[»]
    ProteinModelPortaliQ01105.
    SMRiQ01105. Positions 38-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01105.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni31 – 7848DimerizationAdd
    BLAST
    Regioni79 – 225147Earmuff domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi239 – 29052Asp/Glu-rich (highly acidic)Add
    BLAST

    Domaini

    A long alpha helix in the N-terminus mediates dimerization, while the earmuff domain is responsible for core histone and dsDNA binding. The C-terminal acidic domain mediates the inhibition of histone acetyltransferases and is required for the DNA replication stimulatory activity.1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG260846.
    HOGENOMiHOG000232096.
    HOVERGENiHBG014779.
    InParanoidiQ01105.
    KOiK11290.
    OMAiTWFTDHA.
    PhylomeDBiQ01105.
    TreeFamiTF313386.

    Family and domain databases

    InterProiIPR002164. NAP_family.
    [Graphical view]
    PANTHERiPTHR11875. PTHR11875. 1 hit.
    PfamiPF00956. NAP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q01105-1) [UniParc]FASTAAdd to Basket

    Also known as: TAF-I alpha

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPKRQSPLP PQKKKPRPPP ALGPEETSAS AGLPKKGEKE QQEAIEHIDE    50
    VQNEIDRLNE QASEEILKVE QKYNKLRQPF FQKRSELIAK IPNFWVTTFV 100
    NHPQVSALLG EEDEEALHYL TRVEVTEFED IKSGYRIDFY FDENPYFENK 150
    VLSKEFHLNE SGDPSSKSTE IKWKSGKDLT KRSSQTQNKA SRKRQHEEPE 200
    SFFTWFTDHS DAGADELGEV IKDDIWPNPL QYYLVPDMDD EEGEGEEDDD 250
    DDEEEEGLED IDEEGDEDEG EEDEDDDEGE EGEEDEGEDD 290
    Length:290
    Mass (Da):33,489
    Last modified:April 13, 2004 - v3
    Checksum:iF4664118171EF230
    GO
    Isoform 2 (identifier: Q01105-2) [UniParc]FASTAAdd to Basket

    Also known as: TAF-I beta

    The sequence of this isoform differs from the canonical sequence as follows:
         2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MSAPAAKVSKKELNSNHDGADETS

    Note: Contains a N6-acetyllysine at position 11. Contains a phosphoserine at position 15. Contains a phosphoserine at position 24.

    Show »
    Length:278
    Mass (Da):32,234
    Checksum:iCB8FB882987E38F7
    GO
    Isoform 3 (identifier: Q01105-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MPRSHQPPPPPH

    Show »
    Length:266
    Mass (Da):31,124
    Checksum:iA9A076FE734F8EC4
    GO
    Isoform 4 (identifier: Q01105-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-37: APKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKG → MGCRDLLPSLKPTLL

    Note: Gene prediction based on EST data.

    Show »
    Length:269
    Mass (Da):31,404
    Checksum:i5D51BD1DC837D602
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q01105-2)
    Natural varianti4 – 41A → Q.
    Corresponds to variant rs1141138 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 3736APKRQ…LPKKG → MSAPAAKVSKKELNSNHDGA DETS in isoform 2. 9 PublicationsVSP_009868Add
    BLAST
    Alternative sequencei2 – 3736APKRQ…LPKKG → MPRSHQPPPPPH in isoform 3. 1 PublicationVSP_045175Add
    BLAST
    Alternative sequencei2 – 3736APKRQ…LPKKG → MGCRDLLPSLKPTLL in isoform 4. CuratedVSP_046741Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93651 mRNA. Translation: AAA60318.1.
    X75091 mRNA. Translation: CAA52982.1.
    D45198 mRNA. Translation: BAA08139.1.
    U51924 mRNA. Translation: AAC50460.1.
    AY349172 mRNA. Translation: AAQ79833.1.
    CR536543 mRNA. Translation: CAG38780.1.
    CR542050 mRNA. Translation: CAG46847.1.
    AK223556 mRNA. Translation: BAD97276.1.
    AK300609 mRNA. Translation: BAG62304.1.
    AL356481 Genomic DNA. Translation: CAH71410.1.
    AL359678 Genomic DNA. No translation available.
    BC032749 mRNA. Translation: AAH32749.1.
    EF534308 mRNA. Translation: ABP96841.1.
    CCDSiCCDS48037.1. [Q01105-1]
    CCDS59150.1. [Q01105-3]
    PIRiA57984. A45018.
    I59377.
    RefSeqiNP_001116293.1. NM_001122821.1. [Q01105-1]
    NP_001234929.1. NM_001248000.1.
    NP_001234930.1. NM_001248001.1. [Q01105-3]
    NP_003002.2. NM_003011.3.
    UniGeneiHs.436687.

    Genome annotation databases

    EnsembliENST00000372688; ENSP00000361773; ENSG00000119335. [Q01105-3]
    ENST00000372692; ENSP00000361777; ENSG00000119335. [Q01105-1]
    GeneIDi6418.
    KEGGihsa:6418.
    UCSCiuc004bvt.4. human. [Q01105-1]
    uc004bvu.4. human. [Q01105-2]
    uc011mbj.2. human.

    Polymorphism databases

    DMDMi46397790.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93651 mRNA. Translation: AAA60318.1 .
    X75091 mRNA. Translation: CAA52982.1 .
    D45198 mRNA. Translation: BAA08139.1 .
    U51924 mRNA. Translation: AAC50460.1 .
    AY349172 mRNA. Translation: AAQ79833.1 .
    CR536543 mRNA. Translation: CAG38780.1 .
    CR542050 mRNA. Translation: CAG46847.1 .
    AK223556 mRNA. Translation: BAD97276.1 .
    AK300609 mRNA. Translation: BAG62304.1 .
    AL356481 Genomic DNA. Translation: CAH71410.1 .
    AL359678 Genomic DNA. No translation available.
    BC032749 mRNA. Translation: AAH32749.1 .
    EF534308 mRNA. Translation: ABP96841.1 .
    CCDSi CCDS48037.1. [Q01105-1 ]
    CCDS59150.1. [Q01105-3 ]
    PIRi A57984. A45018.
    I59377.
    RefSeqi NP_001116293.1. NM_001122821.1. [Q01105-1 ]
    NP_001234929.1. NM_001248000.1.
    NP_001234930.1. NM_001248001.1. [Q01105-3 ]
    NP_003002.2. NM_003011.3.
    UniGenei Hs.436687.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E50 X-ray 2.30 A/B/P/Q 38-238 [» ]
    ProteinModelPortali Q01105.
    SMRi Q01105. Positions 38-236.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112316. 105 interactions.
    DIPi DIP-33561N.
    IntActi Q01105. 75 interactions.
    MINTi MINT-4990855.
    STRINGi 9606.ENSP00000361777.

    PTM databases

    PhosphoSitei Q01105.

    Polymorphism databases

    DMDMi 46397790.

    Proteomic databases

    MaxQBi Q01105.
    PaxDbi Q01105.
    PeptideAtlasi Q01105.
    PRIDEi Q01105.

    Protocols and materials databases

    DNASUi 6418.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372688 ; ENSP00000361773 ; ENSG00000119335 . [Q01105-3 ]
    ENST00000372692 ; ENSP00000361777 ; ENSG00000119335 . [Q01105-1 ]
    GeneIDi 6418.
    KEGGi hsa:6418.
    UCSCi uc004bvt.4. human. [Q01105-1 ]
    uc004bvu.4. human. [Q01105-2 ]
    uc011mbj.2. human.

    Organism-specific databases

    CTDi 6418.
    GeneCardsi GC09P131445.
    HGNCi HGNC:10760. SET.
    HPAi CAB005232.
    MIMi 600960. gene.
    neXtProti NX_Q01105.
    PharmGKBi PA35678.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260846.
    HOGENOMi HOG000232096.
    HOVERGENi HBG014779.
    InParanoidi Q01105.
    KOi K11290.
    OMAi TWFTDHA.
    PhylomeDBi Q01105.
    TreeFami TF313386.

    Enzyme and pathway databases

    Reactomei REACT_172744. Condensation of Prophase Chromosomes.
    REACT_25218. HuR stabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi SET. human.
    EvolutionaryTracei Q01105.
    GeneWikii Protein_SET.
    GenomeRNAii 6418.
    NextBioi 24926.
    PROi Q01105.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01105.
    Bgeei Q01105.
    CleanExi HS_SET.
    Genevestigatori Q01105.

    Family and domain databases

    InterProi IPR002164. NAP_family.
    [Graphical view ]
    PANTHERi PTHR11875. PTHR11875. 1 hit.
    Pfami PF00956. NAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene."
      von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., Grosveld G.
      Mol. Cell. Biol. 12:3346-3355(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII."
      Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N.
      Biol. Chem. Hoppe-Seyler 375:113-126(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
    3. "Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis."
      Nagata K., Kawase H., Handa H., Yano K., Yamasaki M., Ishimi Y., Okuda A., Kikuchi A., Matsumoto K.
      Proc. Natl. Acad. Sci. U.S.A. 92:4279-4283(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 14-35; 40-60; 75-90 AND 155-167, ACTIVATION OF DNA REPLICATION.
      Tissue: Cervix carcinoma.
    4. "The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A."
      Li M., Makkinje A., Damuni Z.
      J. Biol. Chem. 271:11059-11062(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Kidney.
    5. "Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau."
      Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K.
      FEBS Lett. 579:363-372(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    8. "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] (ISOFORM 3).
    9. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 2).
      Tissue: Testis.
    11. "Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia."
      Adachi Y., Pavlaki G.N., Copeland T.D.
      J. Biol. Chem. 269:2258-2262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    12. "A relative factor in human rectum carcinoma."
      Wang L.C., Chen Y.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-241 (ISOFORM 2).
    13. "Expression of SET, an inhibitor of protein phosphatase 2A, in renal development and Wilms' tumor."
      Carlson S.G., Eng E., Kim E.-G., Perlman E.J., Copeland T.D., Ballermann B.J.
      J. Am. Soc. Nephrol. 9:1873-1880(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPRESSION IN THE KIDNEY.
    14. "Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein."
      Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D.
      Cell 104:119-130(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION OF HISTONE ACETYLATION.
    15. "Identification and characterization of SEB, a novel protein that binds to the acute undifferentiated leukemia-associated protein SET."
      Minakuchi M., Kakazu N., Gorrin-Rivas M.J., Abe T., Copeland T.D., Ueda K., Adachi Y.
      Eur. J. Biochem. 268:1340-1351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETBP1.
      Tissue: Cervix carcinoma.
    16. "Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
      Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
      J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AN32A, CLEAVAGE AT LYS-189, SUBCELLULAR LOCATION.
    17. "HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A."
      Fan Z., Beresford P.J., Zhang D., Lieberman J.
      Mol. Cell. Biol. 22:2810-2820(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HMGB2, IDENTIFICATION IN THE SET COMPLEX.
    18. "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
      Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
      Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NME1 INHIBITION, INTERACTION WITH NME1, SUBCELLULAR LOCATION, DESCRIPTION OF THE SET COMPLEX, CLEAVAGE BY GZMA.
    19. Erratum
      Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
      Cell 115:241-241(2003)
    20. "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
      Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
      Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    21. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
      Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
      Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX, CLEAVAGE BY GZMA, SUBCELLULAR LOCATION.
    23. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
      Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
      Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGOL1.
    24. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: INTERACTION WITH APBB1.
    27. "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-132; LYS-150 AND LYS-172, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity."
      Muto S., Senda M., Akai Y., Sato L., Suzuki T., Nagai R., Senda T., Horikoshi M.
      Proc. Natl. Acad. Sci. U.S.A. 104:4285-4290(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-238, DNA-BINDING, DOMAINS, SUBUNIT.

    Entry informationi

    Entry nameiSET_HUMAN
    AccessioniPrimary (citable) accession number: Q01105
    Secondary accession number(s): A5A5H4
    , A6NGV1, B4DUE2, Q15541, Q5VXV1, Q5VXV2, Q6FHZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 154 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3