Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P61964

- WDR5_HUMAN

UniProt

P61964 - WDR5_HUMAN

Protein

WD repeat-containing protein 5

Gene

WDR5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (07 Jun 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei107 – 1071Important for interaction with histone H3
    Sitei133 – 1331Important for interaction with histone H3
    Sitei263 – 2631Important for interaction with histone H3
    Sitei322 – 3221Important for interaction with histone H3

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H3 acetylation Source: BHF-UCL
    3. histone H3-K4 methylation Source: UniProtKB
    4. histone H4-K16 acetylation Source: UniProtKB
    5. histone H4-K5 acetylation Source: UniProtKB
    6. histone H4-K8 acetylation Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. rhythmic process Source: UniProtKB-KW
    9. skeletal system development Source: Ensembl
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    SignaLinkiP61964.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    WD repeat-containing protein 5
    Alternative name(s):
    BMP2-induced 3-kb gene protein
    Gene namesi
    Name:WDR5
    Synonyms:BIG3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12757. WDR5.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
    2. histone acetyltransferase complex Source: UniProtKB
    3. histone methyltransferase complex Source: UniProtKB
    4. MLL1 complex Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. nucleus Source: MGI
    7. Set1C/COMPASS complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471A → E: Strongly reduced affinity for histone H3. 1 Publication
    Mutagenesisi91 – 911S → F: Strongly reduced affinity for histone H3. 1 Publication
    Mutagenesisi107 – 1071D → A or N: Strongly reduced affinity for histone H3. 2 Publications
    Mutagenesisi133 – 1331F → A, D or L: Strongly reduced affinity for histone H3. 2 Publications
    Mutagenesisi263 – 2631F → A or W: Strongly reduced affinity for histone H3. 1 Publication
    Mutagenesisi321 – 3211L → A: Abolishes histone H3 binding. 1 Publication
    Mutagenesisi322 – 3221E → A: Strongly reduced affinity for histone H3. 1 Publication

    Organism-specific databases

    PharmGKBiPA37361.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 334333WD repeat-containing protein 5PRO_0000051350Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei112 – 1121N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP61964.
    PaxDbiP61964.
    PRIDEiP61964.

    PTM databases

    PhosphoSiteiP61964.

    Expressioni

    Gene expression databases

    BgeeiP61964.
    CleanExiHS_WDR5.
    GenevestigatoriP61964.

    Interactioni

    Subunit structurei

    Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3. 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, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KMT2A/MLL1 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. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with PER1.22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ArntlQ9WTL82EBI-540834,EBI-644534From a different organism.
    CHD8Q9HCK83EBI-540834,EBI-1169146
    HCFC1P516104EBI-540834,EBI-396176
    HIST1H3DP6843111EBI-540834,EBI-79722
    KANSL1Q7Z3B39EBI-540834,EBI-740244
    KANSL2Q9H9L42EBI-540834,EBI-2560840
    KAT6AQ927944EBI-540834,EBI-948013
    KMT2AQ0316410EBI-540834,EBI-591370
    KMT2BQ9UMN62EBI-540834,EBI-765774
    NCOA6Q146862EBI-540834,EBI-78670
    RBBP5Q152916EBI-540834,EBI-592823

    Protein-protein interaction databases

    BioGridi116272. 118 interactions.
    DIPiDIP-29223N.
    IntActiP61964. 67 interactions.
    MINTiMINT-1464227.
    STRINGi9606.ENSP00000351446.

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 153
    Beta strandi36 – 416
    Beta strandi48 – 536
    Beta strandi57 – 648
    Beta strandi69 – 735
    Turni74 – 763
    Beta strandi79 – 835
    Beta strandi90 – 956
    Beta strandi99 – 1068
    Beta strandi109 – 1157
    Turni116 – 1183
    Beta strandi121 – 1266
    Beta strandi132 – 1376
    Beta strandi139 – 14810
    Beta strandi153 – 1575
    Turni158 – 1603
    Beta strandi163 – 1675
    Beta strandi174 – 1796
    Beta strandi183 – 1908
    Beta strandi195 – 1995
    Turni200 – 2023
    Beta strandi205 – 2095
    Beta strandi217 – 2226
    Beta strandi226 – 2338
    Turni234 – 2363
    Beta strandi237 – 2426
    Turni243 – 2464
    Beta strandi247 – 2526
    Beta strandi258 – 2603
    Beta strandi264 – 2674
    Beta strandi269 – 2713
    Beta strandi273 – 2764
    Beta strandi279 – 2813
    Beta strandi283 – 2875
    Turni288 – 2903
    Beta strandi293 – 2975
    Beta strandi304 – 3096
    Beta strandi311 – 32010
    Turni322 – 3243
    Beta strandi327 – 3315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CNXX-ray2.10A20-334[»]
    2CO0X-ray2.25A/C20-334[»]
    2G99X-ray1.90A/B27-334[»]
    2G9AX-ray2.70A29-334[»]
    2GNQX-ray1.80A1-334[»]
    2H13X-ray1.58A22-334[»]
    2H14X-ray1.48A22-334[»]
    2H68X-ray1.79A/B23-334[»]
    2H6KX-ray1.89A/B23-334[»]
    2H6NX-ray1.50A/B23-334[»]
    2H6QX-ray1.87A/B23-334[»]
    2H9LX-ray1.75A24-334[»]
    2H9MX-ray1.90A/C24-334[»]
    2H9NX-ray2.00A/C24-334[»]
    2H9PX-ray1.91A24-334[»]
    2O9KX-ray1.90A/C24-334[»]
    3EG6X-ray1.72A23-334[»]
    3EMHX-ray1.37A25-334[»]
    3MXXX-ray2.05A31-334[»]
    3N0DX-ray2.30A31-334[»]
    3N0EX-ray2.50A31-334[»]
    3P4FX-ray2.35A22-334[»]
    3PSLX-ray1.70A/B21-334[»]
    3SMRX-ray1.82A/B/C/D24-334[»]
    3UR4X-ray1.80A/B24-334[»]
    3UVKX-ray1.40A21-334[»]
    3UVLX-ray2.20A21-334[»]
    3UVMX-ray1.57A21-334[»]
    3UVNX-ray1.79A/C21-334[»]
    3UVOX-ray2.20A21-334[»]
    4A7JX-ray1.90A21-334[»]
    4CY1X-ray1.50A/B23-334[»]
    4CY2X-ray2.00A23-334[»]
    4ERQX-ray1.91A/B/C23-334[»]
    4ERYX-ray1.30A23-334[»]
    4ERZX-ray1.75A/B/C23-334[»]
    4ES0X-ray1.82A23-334[»]
    4ESGX-ray1.70A/B23-334[»]
    4EWRX-ray1.50A23-334[»]
    4GM3X-ray3.39A/B/C/D/E/F/G/H22-334[»]
    4GM8X-ray2.60A/B/C/D22-334[»]
    4GM9X-ray2.10A/B22-334[»]
    4GMBX-ray2.78A22-334[»]
    4IA9X-ray1.66A24-334[»]
    4O45X-ray1.87A24-334[»]
    ProteinModelPortaliP61964.
    SMRiP61964. Positions 31-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61964.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati43 – 8240WD 1Add
    BLAST
    Repeati85 – 12642WD 2Add
    BLAST
    Repeati128 – 16841WD 3Add
    BLAST
    Repeati169 – 20840WD 4Add
    BLAST
    Repeati212 – 25342WD 5Add
    BLAST
    Repeati256 – 29641WD 6Add
    BLAST
    Repeati299 – 33335WD 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat WDR5/wds family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000091642.
    HOVERGENiHBG055117.
    InParanoidiP61964.
    KOiK14963.
    OMAiSVKPNYT.
    OrthoDBiEOG7MH0ZD.
    PhylomeDBiP61964.
    TreeFamiTF314125.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 7 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61964-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS    50
    VKFSPNGEWL ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN 100
    LLVSASDDKT LKIWDVSSGK CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD 150
    ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN RDGSLIVSSS YDGLCRIWDT 200
    ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL WDYSKGKCLK 250
    TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH 300
    TDVVISTACH PTENIIASAA LENDKTIKLW KSDC 334
    Length:334
    Mass (Da):36,588
    Last modified:June 7, 2004 - v1
    Checksum:i4BF30914A2250286
    GO

    Sequence cautioni

    The sequence CAB66159.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011376 mRNA. Translation: CAB66159.1. Different initiation.
    AK000552 mRNA. Translation: BAA91248.1.
    BC001635 mRNA. Translation: AAH01635.1.
    CCDSiCCDS6981.1.
    RefSeqiNP_060058.1. NM_017588.2.
    NP_438172.1. NM_052821.3.
    XP_005272220.1. XM_005272163.1.
    UniGeneiHs.397638.

    Genome annotation databases

    EnsembliENST00000358625; ENSP00000351446; ENSG00000196363.
    GeneIDi11091.
    KEGGihsa:11091.
    UCSCiuc004cey.3. human.

    Polymorphism databases

    DMDMi48429182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011376 mRNA. Translation: CAB66159.1 . Different initiation.
    AK000552 mRNA. Translation: BAA91248.1 .
    BC001635 mRNA. Translation: AAH01635.1 .
    CCDSi CCDS6981.1.
    RefSeqi NP_060058.1. NM_017588.2.
    NP_438172.1. NM_052821.3.
    XP_005272220.1. XM_005272163.1.
    UniGenei Hs.397638.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CNX X-ray 2.10 A 20-334 [» ]
    2CO0 X-ray 2.25 A/C 20-334 [» ]
    2G99 X-ray 1.90 A/B 27-334 [» ]
    2G9A X-ray 2.70 A 29-334 [» ]
    2GNQ X-ray 1.80 A 1-334 [» ]
    2H13 X-ray 1.58 A 22-334 [» ]
    2H14 X-ray 1.48 A 22-334 [» ]
    2H68 X-ray 1.79 A/B 23-334 [» ]
    2H6K X-ray 1.89 A/B 23-334 [» ]
    2H6N X-ray 1.50 A/B 23-334 [» ]
    2H6Q X-ray 1.87 A/B 23-334 [» ]
    2H9L X-ray 1.75 A 24-334 [» ]
    2H9M X-ray 1.90 A/C 24-334 [» ]
    2H9N X-ray 2.00 A/C 24-334 [» ]
    2H9P X-ray 1.91 A 24-334 [» ]
    2O9K X-ray 1.90 A/C 24-334 [» ]
    3EG6 X-ray 1.72 A 23-334 [» ]
    3EMH X-ray 1.37 A 25-334 [» ]
    3MXX X-ray 2.05 A 31-334 [» ]
    3N0D X-ray 2.30 A 31-334 [» ]
    3N0E X-ray 2.50 A 31-334 [» ]
    3P4F X-ray 2.35 A 22-334 [» ]
    3PSL X-ray 1.70 A/B 21-334 [» ]
    3SMR X-ray 1.82 A/B/C/D 24-334 [» ]
    3UR4 X-ray 1.80 A/B 24-334 [» ]
    3UVK X-ray 1.40 A 21-334 [» ]
    3UVL X-ray 2.20 A 21-334 [» ]
    3UVM X-ray 1.57 A 21-334 [» ]
    3UVN X-ray 1.79 A/C 21-334 [» ]
    3UVO X-ray 2.20 A 21-334 [» ]
    4A7J X-ray 1.90 A 21-334 [» ]
    4CY1 X-ray 1.50 A/B 23-334 [» ]
    4CY2 X-ray 2.00 A 23-334 [» ]
    4ERQ X-ray 1.91 A/B/C 23-334 [» ]
    4ERY X-ray 1.30 A 23-334 [» ]
    4ERZ X-ray 1.75 A/B/C 23-334 [» ]
    4ES0 X-ray 1.82 A 23-334 [» ]
    4ESG X-ray 1.70 A/B 23-334 [» ]
    4EWR X-ray 1.50 A 23-334 [» ]
    4GM3 X-ray 3.39 A/B/C/D/E/F/G/H 22-334 [» ]
    4GM8 X-ray 2.60 A/B/C/D 22-334 [» ]
    4GM9 X-ray 2.10 A/B 22-334 [» ]
    4GMB X-ray 2.78 A 22-334 [» ]
    4IA9 X-ray 1.66 A 24-334 [» ]
    4O45 X-ray 1.87 A 24-334 [» ]
    ProteinModelPortali P61964.
    SMRi P61964. Positions 31-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116272. 118 interactions.
    DIPi DIP-29223N.
    IntActi P61964. 67 interactions.
    MINTi MINT-1464227.
    STRINGi 9606.ENSP00000351446.

    Chemistry

    BindingDBi P61964.
    ChEMBLi CHEMBL1075317.

    PTM databases

    PhosphoSitei P61964.

    Polymorphism databases

    DMDMi 48429182.

    Proteomic databases

    MaxQBi P61964.
    PaxDbi P61964.
    PRIDEi P61964.

    Protocols and materials databases

    DNASUi 11091.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358625 ; ENSP00000351446 ; ENSG00000196363 .
    GeneIDi 11091.
    KEGGi hsa:11091.
    UCSCi uc004cey.3. human.

    Organism-specific databases

    CTDi 11091.
    GeneCardsi GC09P137001.
    HGNCi HGNC:12757. WDR5.
    MIMi 609012. gene.
    neXtProti NX_P61964.
    PharmGKBi PA37361.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000091642.
    HOVERGENi HBG055117.
    InParanoidi P61964.
    KOi K14963.
    OMAi SVKPNYT.
    OrthoDBi EOG7MH0ZD.
    PhylomeDBi P61964.
    TreeFami TF314125.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    SignaLinki P61964.

    Miscellaneous databases

    EvolutionaryTracei P61964.
    GeneWikii WDR5.
    GenomeRNAii 11091.
    NextBioi 42156.
    PROi P61964.
    SOURCEi Search...

    Gene expression databases

    Bgeei P61964.
    CleanExi HS_WDR5.
    Genevestigatori P61964.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 7 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a sugar transporter gene, a G-beta subunit like gene and three novel genes in human chromosome 9q34."
      Young J.M., Woodward K.J., Aziz S., Burley M., Kwiatkowski D.J., Povey S.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Uterus.
    2. "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].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    4. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
      Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
      Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCFC1.
    5. Cited for: IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
    6. "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression."
      Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L.
      Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL-LIKE COMPLEX.
    7. "CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex."
      Lee J.-H., Skalnik D.G.
      J. Biol. Chem. 280:41725-41731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
    8. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    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]
      Cited for: IDENTIFICATION IN THE MLL2/3 (ASCOM) COMPLEX.
    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.
      J. Biol. Chem. 282:13419-13428(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET1 COMPLEX.
    11. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
      Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
      J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    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."
      Lee J.H., Skalnik D.G.
      Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A.
    13. "CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes."
      Thompson B.A., Tremblay V., Lin G., Bochar D.A.
      Mol. Cell. Biol. 28:3894-3904(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CHD8.
    14. "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
      Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
      Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN SET1 COMPLEX.
    15. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
      Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
      J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ASCL2; C11ORF30; HCFC1; HSPA8; CCAR2; MATR3; MKI67; RBBP5 AND ZNF335.
    16. "On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex."
      Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.
      J. Biol. Chem. 284:24242-24256(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH KMT2A AND RBBP5.
    17. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
      Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
      Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
    18. "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-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
      Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: INTERACTION WITH ZNF335.
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    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]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH HISTONE H3 PEPTIDE, INTERACTION WITH HISTONE H3.
    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. Cell 22:137-144(2006) [PubMed] [Europe PMC] [Abstract]
      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. "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]
      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. "Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex."
      Ruthenburg A.J., Wang W., Graybosch D.M., Li H., Allis C.D., Patel D.J., Verdine G.L.
      Nat. Struct. Mol. Biol. 13:704-712(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 20-334 IN COMPLEX WITH HISTONE H3 PEPTIDE, INTERACTION WITH HISTONE H3.
    27. "Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide."
      Patel A., Dharmarajan V., Cosgrove M.S.
      J. Biol. Chem. 283:32158-32161(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 23-334 IN COMPLEX WITH KMT2A.
    28. "WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket."
      Song J.J., Kingston R.E.
      J. Biol. Chem. 283:35258-35264(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 25-334 IN COMPLEX WITH KMT2A PEPTIDE, SUBUNIT.

    Entry informationi

    Entry nameiWDR5_HUMAN
    AccessioniPrimary (citable) accession number: P61964
    Secondary accession number(s): Q91VA5, Q9NWX7, Q9UGP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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, 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