UniProt Accession

 WDR5_HUMAN; P61964; Q91VA5; Q9NWX7; Q9UGP9 

Genbank Protein ID

 AJ011376; AK000552; BC001635 

Genbank Nucleotide ID

 CAB66159.1; BAA91248.1; AAH01635.1 

Protein Name

 WD repeat-containing protein 5 

Protein Synonyms/Alias

 BMP2-induced 3-kb gene protein 

Gene Name

 WDR5 

Gene Synonyms/Alias

 BIG3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MATEEKKPETEAA	ubiquitination	[1]
7	*MATEEKKPETEAAR	ubiquitination	[1]
27	SSSATQSKPTPVKPN	ubiquitination	[1, 2, 3, 4]
32	QSKPTPVKPNYALKF	ubiquitination	[2, 4, 5]
112	ASDDKTLKIWDVSSG	acetylation	[6]
120	IWDVSSGKCLKTLKG	ubiquitination	[1, 3, 5, 7]
159	SVRIWDVKTGKCLKT	ubiquitination	[1, 3, 7, 8]
227	VKFSPNGKYILAATL	ubiquitination	[2, 3, 4, 5]

Reference

 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [8] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional Description

 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. 

Sequence Annotation

 REPEAT 43 82 WD 1.
 REPEAT 85 126 WD 2.
 REPEAT 128 168 WD 3.
 REPEAT 169 208 WD 4.
 REPEAT 212 253 WD 5.
 REPEAT 256 296 WD 6.
 REPEAT 299 333 WD 7.
 MOD_RES 112 112 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Chromatin regulator; Complete proteome; Nucleus; Reference proteome; Repeat; Transcription; Transcription regulation; WD repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 334 AA 

Protein Sequence

Gene Ontology

 GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
 GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0001501; P:skeletal system development; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

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. 

Pfam

 PF00400; WD40 

SMART

 SM00320; WD40 

PROSITE

 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 

PRINTS

 PR00320; GPROTEINBRPT.