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P61964 (WDR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
WD repeat-containing protein 5
Alternative name(s):
BMP2-induced 3-kb gene protein
Gene names
Name:WDR5
Synonyms:BIG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation. Ref.16 Ref.17 Ref.19 Ref.24 Ref.25

Subunit structure

Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3 By similarity. 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 By similarity. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28

Subcellular location

Nucleus Ref.10 Ref.19.

Sequence similarities

Belongs to the WD repeat WDR5/wds family.

Contains 7 WD repeats.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionChromatin regulator
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

histone H3-K4 methylation

Inferred from direct assay Ref.10Ref.16. Source: UniProtKB

histone H4-K16 acetylation

Inferred from direct assay Ref.19. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.19. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.19. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

skeletal system development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

MLL1 complex

Inferred from direct assay Ref.8. Source: UniProtKB

Set1C/COMPASS complex

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

histone acetyltransferase complex

Inferred from direct assay Ref.19. Source: UniProtKB

histone methyltransferase complex

Inferred from direct assay Ref.10Ref.16. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.11. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.22
Chain2 – 334333WD repeat-containing protein 5
PRO_0000051350

Regions

Repeat43 – 8240WD 1
Repeat85 – 12642WD 2
Repeat128 – 16841WD 3
Repeat169 – 20840WD 4
Repeat212 – 25342WD 5
Repeat256 – 29641WD 6
Repeat299 – 33335WD 7

Sites

Site1071Important for interaction with histone H3
Site1331Important for interaction with histone H3
Site2631Important for interaction with histone H3
Site3221Important for interaction with histone H3

Amino acid modifications

Modified residue21N-acetylalanine Ref.22
Modified residue1121N6-acetyllysine Ref.18

Experimental info

Mutagenesis471A → E: Strongly reduced affinity for histone H3. Ref.24
Mutagenesis911S → F: Strongly reduced affinity for histone H3. Ref.24
Mutagenesis1071D → A or N: Strongly reduced affinity for histone H3. Ref.24 Ref.25
Mutagenesis1331F → A, D or L: Strongly reduced affinity for histone H3. Ref.24 Ref.25
Mutagenesis2631F → A or W: Strongly reduced affinity for histone H3. Ref.25
Mutagenesis3211L → A: Abolishes histone H3 binding. Ref.25
Mutagenesis3221E → A: Strongly reduced affinity for histone H3. Ref.24

Secondary structure

........................................................................ 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61964 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 4BF30914A2250286

FASTA33436,588
        10         20         30         40         50         60 
MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS VKFSPNGEWL 

        70         80         90        100        110        120 
ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN LLVSASDDKT LKIWDVSSGK 

       130        140        150        160        170        180 
CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN 

       190        200        210        220        230        240 
RDGSLIVSSS YDGLCRIWDT ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL 

       250        260        270        280        290        300 
WDYSKGKCLK TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH 

       310        320        330 
TDVVISTACH PTENIIASAA LENDKTIKLW KSDC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus."
Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M.
Mol. Cell 13:587-597(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
Cell 151:1097-1112(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF335.
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011376 mRNA. Translation: CAB66159.1. Different initiation.
AK000552 mRNA. Translation: BAA91248.1.
BC001635 mRNA. Translation: AAH01635.1.
RefSeqNP_060058.1. NM_017588.2.
NP_438172.1. NM_052821.3.
XP_005272220.1. XM_005272163.1.
UniGeneHs.397638.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortalP61964.
SMRP61964. Positions 31-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116272. 116 interactions.
DIPDIP-29223N.
IntActP61964. 63 interactions.
MINTMINT-1464227.
STRING9606.ENSP00000351446.

Chemistry

BindingDBP61964.
ChEMBLCHEMBL1075317.

PTM databases

PhosphoSiteP61964.

Polymorphism databases

DMDM48429182.

Proteomic databases

PaxDbP61964.
PRIDEP61964.

Protocols and materials databases

DNASU11091.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358625; ENSP00000351446; ENSG00000196363.
ENST00000425041; ENSP00000401889; ENSG00000196363.
GeneID11091.
KEGGhsa:11091.
UCSCuc004cey.3. human.

Organism-specific databases

CTD11091.
GeneCardsGC09P137001.
HGNCHGNC:12757. WDR5.
MIM609012. gene.
neXtProtNX_P61964.
PharmGKBPA37361.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000091642.
HOVERGENHBG055117.
InParanoidP61964.
KOK14963.
OMASVKPNYT.
OrthoDBEOG7MH0ZD.
PhylomeDBP61964.
TreeFamTF314125.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
SignaLinkP61964.

Gene expression databases

BgeeP61964.
CleanExHS_WDR5.
GenevestigatorP61964.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. 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]
PfamPF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61964.
GeneWikiWDR5.
GenomeRNAi11091.
NextBio42156.
PROP61964.
SOURCESearch...

Entry information

Entry nameWDR5_HUMAN
AccessionPrimary (citable) accession number: P61964
Secondary accession number(s): Q91VA5, Q9NWX7, Q9UGP9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM