Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P61964

- WDR5_HUMAN

UniProt

P61964 - WDR5_HUMAN

(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)

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

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 - 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. positive regulation of gluconeogenesis Source: Ensembl
  8. regulation of transcription, DNA-templated Source: UniProtKB-KW
  9. skeletal system development Source: Ensembl
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiP61964. baseline and differential.
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. 133 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 – 153Combined sources
Beta strandi36 – 416Combined sources
Beta strandi48 – 536Combined sources
Beta strandi57 – 648Combined sources
Beta strandi69 – 735Combined sources
Turni74 – 763Combined sources
Beta strandi79 – 835Combined sources
Beta strandi90 – 956Combined sources
Beta strandi99 – 1068Combined sources
Beta strandi109 – 1157Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi139 – 14810Combined sources
Beta strandi153 – 1575Combined sources
Turni158 – 1603Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi183 – 1908Combined sources
Beta strandi195 – 1995Combined sources
Turni200 – 2023Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi226 – 2338Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 2426Combined sources
Turni243 – 2464Combined sources
Beta strandi247 – 2526Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi283 – 2875Combined sources
Turni288 – 2903Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi311 – 32010Combined sources
Turni322 – 3243Combined sources
Beta strandi327 – 3315Combined sources

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.
GeneTreeiENSGT00760000118869.
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

        10         20         30         40         50
MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS
60 70 80 90 100
VKFSPNGEWL ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN
110 120 130 140 150
LLVSASDDKT LKIWDVSSGK CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD
160 170 180 190 200
ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN RDGSLIVSSS YDGLCRIWDT
210 220 230 240 250
ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL WDYSKGKCLK
260 270 280 290 300
TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH
310 320 330
TDVVISTACH PTENIIASAA LENDKTIKLW KSDC
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. 133 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.
GeneTreei ENSGT00760000118869.
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.
ExpressionAtlasi P61964. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 129 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