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Index > Protein center > WDR5(Gene name) > Human
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  • WDR5 (Gene name),
  • WD repeat-containing protein 5 (Protein name ),  WDR5_HUMAN from NCBI database.
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  • General Annotation
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  • Gene name:
    WDR5(BIG3);
    Protein name:
    WD repeat-containing protein 5;
    Alternative:
    BMP2-induced 3-kb gene protein;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Interacts with HCFC1. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Core component of several methyltransferase-containing complexes including MLL1/MLL, ASCOM, MLL2/MLL3 and MLL3/MLL4. Each complex is at least composed of ASH2L, RBBP5, DPY30, WDR5, one or more specific histone methyltransferases (MLL, MLL2, MLL3 and MLL4), and the facultative components C16orf53/PA1, C17orf49, CHD8, E2F6, HCFC1, HCFC2, HSP70, IN80C, KDM6A, KIAA1267, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with MLL and RBBP5; the interaction is direct. Component ofthe ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, MBIP and CSRP2BP. Interacts with histone H3. Interacts with SETD1A.
    Function:
    Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May regulate osteoblasts differentiation.
    Subcellular Location:
    Nucleus
    Protein Attributes:
    Sequence length:
    334
    Sequence:
    50:
    MATEEKKPET | EAARAQPTPS | SSATQSKPTP | VKPNYALKFT | LAGHTKAVSS | 
    100:
    VKFSPNGEWL | ASSSADKLIK | IWGAYDGKFE | KTISGHKLGI | SDVAWSSDSN | 
    150:
    LLVSASDDKT | LKIWDVSSGK | CLKTLKGHSN | YVFCCNFNPQ | SNLIVSGSFD | 
    200:
    ESVRIWDVKT | GKCLKTLPAH | SDPVSAVHFN | RDGSLIVSSS | YDGLCRIWDT | 
    250:
    ASGQCLKTLI | DDDNPPVSFV | KFSPNGKYIL | AATLDNTLKL | WDYSKGKCLK | 
    300:
    TYTGHKNEKY | CIFANFSVTG | GKWIVSGSED | NLVYIWNLQT | KEIVQKLQGH | 
    334:
    TDVVISTACH | PTENIIASAA | LENDKTIKLW | KSDC
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    KEGG:
    Pfam:
    MIM:
    SMR:
    UniGene:
    String:
    Uniprot:
     
    FOR
    ELISA Kit for Human WD repeat-containing protein 5
    ELISA Kit for Human WD repeat-containing protein 5
    ELISA Kit for Human WD repeat-containing protein 5
    ELISA Kit for Human WD repeat-containing protein 5
    CLIA Kit for Human WD repeat-containing protein 5
    CLIA Kit for Human WD repeat-containing protein 5
    CLIA Kit for Human WD repeat-containing protein 5
    CLIA Kit for Human WD repeat-containing protein 5
    Polyclonal Antibody for Human WD repeat-containing protein 5
    Polyclonal Antibody for Human WD repeat-containing protein 5
    Polyclonal Antibody for Human WD repeat-containing protein 5
    Polyclonal Antibody for Human WD repeat-containing protein 5
    Monoclonal Antibody for Human WD repeat-containing protein 5
    Monoclonal Antibody for Human WD repeat-containing protein 5
    Monoclonal Antibody for Human WD repeat-containing protein 5
    Monoclonal Antibody for Human WD repeat-containing protein 5
    Protein for Human WD repeat-containing protein 5
    Protein for Human WD repeat-containing protein 5
    Protein for Human WD repeat-containing protein 5
    Protein for Human WD repeat-containing protein 5

    R&D Technical Data
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    Precision
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    Recovery
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    Linearity
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    References
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
      tissue: Uterus.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH HCFC1
    5. 5.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX
    6. 6.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE MLL-LIKE COMPLEX
    7. 7.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE SET1 COMPLEX
    8. 8.
      "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
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      Cell121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX
    9. 9.
      "Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases."
      Lee S. , Lee D.K. , Dou Y. , Lee J. , Lee B. , Kwak E. , Kong Y.Y. , Lee S.K. , Roeder R.G. , Lee J.W.
      Proc. Natl. Acad. Sci. U.S.A.103:15392-15397(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX
    10. 10.
      "Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex."
      Lee J.-H. , Tate C.M. , You J.-S. , Skalnik D.G.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUBCELLULAR LOCATION;IDENTIFICATION IN THE SET1 COMPLEX
    11. 11.
      "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY;IDENTIFICATION IN THE MLL2/3 COMPLEX
    12. 12.
      "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN SET1 COMPLEX;INTERACTION WITH SETD1A
    13. 13.
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN A COMPLEX WITH CHD8
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN A COMPLEX WITH ASCL2; C11ORF30; HCFC1; HSPA8; CCAR2; MATR3; MKI67; RBBP5 AND ZNF335
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;CHARACTERIZATION OF THE MLL1/MLL COMPLEX;INTERACTION WITH KMT2A AND RBBP5
    17. 17.
      "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
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      Science325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    19. 19.
      "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
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      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN HISTONE H4 ACETYLATION;IDENTIFICATION IN NSL COMPLEX;SUBCELLULAR LOCATION
    20. 20.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    21. 21.
      "Microcephaly gene links trithorax and REST/NRSF to control neural stem cell proliferation and differentiation."
      Yang Y.J. , Baltus A.E. , Mathew R.S. , Murphy E.A. , Evrony G.D. , Gonzalez D.M. , Wang E.P. , Marshall-Walker C.A. , Barry B.J. , Murn J. , Tatarakis A. , Mahajan M.A. , Samuels H.H. , Shi Y. , Golden J.A. , Mahajnah M. , Shenhav R. , Walsh C.A.
      Cell151:1097-1112(2012) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH ZNF335
    22. 22.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
    23. 23.
      "Structural basis for molecular recognition and presentation of histone H3 by WDR5."
      Schuetz A. , Allali-Hassani A. , Martin F. , Loppnau P. , Vedadi M. , Bochkarev A. , Plotnikov A.N. , Arrowsmith C.H. , Min J.
      EMBO J.25:4245-4252(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH HISTONE H3 PEPTIDE;INTERACTION WITH HISTONE H3
    24. 24.
      "Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5."
      Han Z. , Guo L. , Wang H. , Shen Y. , Deng X.W. , Chai J.
      Mol. Cell22:137-144(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-334 IN COMPLEX WITH HISTONE H3 PEPTIDE;INTERACTION WITH HISTONE H3;MUTAGENESIS OF ALA-47; SER-91; ASP-107; PHE-133 AND GLU-322;FUNCTION
    25. 25.
      "Molecular recognition of histone H3 by the WD40 protein WDR5."
      Couture J.F. , Collazo E. , Trievel R.C.
      Nat. Struct. Mol. Biol.13:698-703(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 22-334 IN COMPLEX WITH HISTONE H3 PEPTIDE;INTERACTION WITH HISTONE H3;MUTAGENESIS OF ASP-107; PHE-133; PHE-263 AND LEU-321;FUNCTION
    26. 26.
      "Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex."
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