P61964 (WDR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
WD repeat-containing protein 5

Alternative name(s):
BMP2-induced 3-kb gene protein

Gene names

Name:	WDR5
Synonyms:	BIG3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15 Ref.16 Ref.18 Ref.21 Ref.22
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 (MLL, MLL2/ALR, MLL3 and MLL4/WBP7), 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 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. 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.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25
Subcellular location	Nucleus Ref.10 Ref.18.
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat WD repeat
Molecular function	Chromatin regulator
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from direct assay PubMed 18838386. Source: BHF-UCL histone H3-K4 methylation Inferred from direct assay Ref.10Ref.15. Source: UniProtKB histone H4-K16 acetylation Inferred from direct assay Ref.18. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.18. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.18. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW skeletal system development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ada2/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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arntl	Q9WTL8	2	EBI-540834,EBI-644534	From a different organism.
HCFC1	P51610	4	EBI-540834,EBI-396176
KAT6A	Q92794	4	EBI-540834,EBI-948013
MLL	Q03164	9	EBI-540834,EBI-591370
RBBP5	Q15291	6	EBI-540834,EBI-592823

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 334

334

WD repeat-containing protein 5

PRO_0000051350

Regions

Repeat

43 – 82

40

WD 1

Repeat

85 – 126

42

WD 2

Repeat

128 – 168

41

WD 3

Repeat

169 – 208

40

WD 4

Repeat

212 – 253

42

WD 5

Repeat

256 – 296

41

WD 6

Repeat

299 – 333

35

WD 7

Sites

Site

107

1

Important for interaction with histone H3

Site

133

1

Important for interaction with histone H3

Site

263

1

Important for interaction with histone H3

Site

322

1

Important for interaction with histone H3

Amino acid modifications

Modified residue

112

1

N6-acetyllysine Ref.17

Experimental info

Mutagenesis

47

1

A → E: Strongly reduced affinity for histone H3. Ref.21

Mutagenesis

91

1

S → F: Strongly reduced affinity for histone H3. Ref.21

Mutagenesis

107

1

D → A or N: Strongly reduced affinity for histone H3. Ref.21 Ref.22

Mutagenesis

133

1

F → A, D or L: Strongly reduced affinity for histone H3. Ref.21 Ref.22

Mutagenesis

263

1

F → A or W: Strongly reduced affinity for histone H3. Ref.22

Mutagenesis

321

1

L → A: Abolishes histone H3 binding. Ref.22

Mutagenesis

322

1

E → A: Strongly reduced affinity for histone H3. Ref.21

Secondary structure

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334

Helix Strand Turn

Details...

Helix

13 – 15

3

Beta strand

36 – 41

6

Beta strand

48 – 53

6

Beta strand

57 – 64

8

Beta strand

69 – 73

5

Turn

74 – 76

3

Beta strand

79 – 83

5

Beta strand

90 – 95

6

Beta strand

99 – 106

8

Beta strand

109 – 115

7

Turn

116 – 118

3

Beta strand

121 – 126

6

Beta strand

132 – 137

6

Beta strand

139 – 148

10

Beta strand

153 – 157

5

Turn

158 – 160

3

Beta strand

163 – 167

5

Beta strand

174 – 179

6

Beta strand

183 – 190

8

Beta strand

195 – 199

5

Turn

200 – 202

3

Beta strand

205 – 209

5

Beta strand

217 – 222

6

Beta strand

226 – 233

8

Turn

234 – 236

3

Beta strand

237 – 242

6

Turn

243 – 246

4

Beta strand

247 – 252

6

Beta strand

253 – 255

3

Beta strand

258 – 260

3

Beta strand

264 – 267

4

Beta strand

269 – 271

3

Beta strand

273 – 276

4

Beta strand

279 – 281

3

Beta strand

283 – 287

5

Turn

288 – 290

3

Beta strand

293 – 297

5

Beta strand

304 – 309

6

Beta strand

311 – 320

10

Turn

322 – 324

3

Beta strand

327 – 331

5

Sequences

	Sequence		Length	Mass (Da)
	P61964 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: 4BF30914A2250286	FASTA	334	36,588
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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 MLL AND RBBP5.
[16]	"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.
[17]	"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, MASS SPECTROMETRY.
[18]	"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.
[19]	"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].
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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 MLL.
[25]	"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 MLL 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.

IPI

IPI00005492.

RefSeq

NP_060058.1. NM_017588.2.
NP_438172.1. NM_052821.3.

UniGene

Hs.397638.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	[»]
4IA9	X-ray	1.66	A	24-334	[»]

ProteinModelPortal

P61964.

ModBase

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Protein-protein interaction databases

DIP

DIP-29223N.

IntAct

P61964. 55 interactions.

MINT

MINT-1464227.

STRING

9606.ENSP00000351446.

PTM databases

PhosphoSite

P61964.

Polymorphism databases

DMDM

48429182.

Proteomic databases

PaxDb

P61964.

PRIDE

P61964.

Protocols and materials databases

DNASU

11091.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000358625; ENSP00000351446; ENSG00000196363.
ENST00000425041; ENSP00000401889; ENSG00000196363.

GeneID

11091.

KEGG

hsa:11091.

UCSC

uc004cey.3. human.

Organism-specific databases

CTD

11091.

GeneCards

GC09P137001.

HGNC

HGNC:12757. WDR5.

MIM

609012. gene.

neXtProt

NX_P61964.

PharmGKB

PA37361.

GenAtlas

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Phylogenomic databases

eggNOG

COG2319.

HOGENOM

HOG000091642.

HOVERGEN

HBG055117.

InParanoid

P61964.

KO

K14963.

OMA

KLWKSDT.

OrthoDB

EOG4QVCCF.

PhylomeDB

P61964.

Enzyme and pathway databases

Pathway_Interaction_DB

circadianpathway. Circadian rhythm pathway.

Gene expression databases

Bgee

P61964.

CleanEx

HS_WDR5.

Genevestigator

P61964.

GermOnline

ENSG00000196363. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 2 hits.

InterPro

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]

Pfam

PF00400. WD40. 7 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 7 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

P61964.

ChEMBL

CHEMBL1075317.

EvolutionaryTrace

P61964.

GenomeRNAi

11091.

NextBio

42156.

SOURCE

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Entry information

Entry name

WDR5_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.