| UniProt ID | WDR5_HUMAN | |
|---|---|---|
| UniProt AC | P61964 | |
| Protein Name | WD repeat-containing protein 5 | |
| Gene Name | WDR5 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 334 | |
| Subcellular Localization | Nucleus . | |
| Protein 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.. | |
| Protein Sequence | MATEEKKPETEAARAQPTPSSSATQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MATEEKKPE ------CCCCCCCCH | 24.58 | 22814378 | |
| 6 | Ubiquitination | --MATEEKKPETEAA --CCCCCCCCHHHHH | 68.35 | 24816145 | |
| 7 | Sumoylation | -MATEEKKPETEAAR -CCCCCCCCHHHHHH | 51.90 | 28112733 | |
| 7 | Ubiquitination | -MATEEKKPETEAAR -CCCCCCCCHHHHHH | 51.90 | - | |
| 18 | Phosphorylation | EAARAQPTPSSSATQ HHHHCCCCCCCCCCC | 24.59 | 25159151 | |
| 20 | Phosphorylation | ARAQPTPSSSATQSK HHCCCCCCCCCCCCC | 39.13 | 25159151 | |
| 21 | Phosphorylation | RAQPTPSSSATQSKP HCCCCCCCCCCCCCC | 25.79 | 21406692 | |
| 22 | Phosphorylation | AQPTPSSSATQSKPT CCCCCCCCCCCCCCC | 39.41 | 25159151 | |
| 24 | Phosphorylation | PTPSSSATQSKPTPV CCCCCCCCCCCCCCC | 35.01 | 21406692 | |
| 26 | Phosphorylation | PSSSATQSKPTPVKP CCCCCCCCCCCCCCC | 35.93 | 21406692 | |
| 27 | Ubiquitination | SSSATQSKPTPVKPN CCCCCCCCCCCCCCC | 42.99 | 23000965 | |
| 27 | Sumoylation | SSSATQSKPTPVKPN CCCCCCCCCCCCCCC | 42.99 | 28112733 | |
| 29 | Phosphorylation | SATQSKPTPVKPNYA CCCCCCCCCCCCCEE | 44.44 | 21406692 | |
| 32 | Ubiquitination | QSKPTPVKPNYALKF CCCCCCCCCCEEEEE | 28.84 | 23000965 | |
| 35 | Phosphorylation | PTPVKPNYALKFTLA CCCCCCCEEEEEEEC | 23.10 | 21406692 | |
| 38 | Methylation | VKPNYALKFTLAGHT CCCCEEEEEEECCCC | 28.29 | 115978643 | |
| 38 | Ubiquitination | VKPNYALKFTLAGHT CCCCEEEEEEECCCC | 28.29 | 23000965 | |
| 45 | Phosphorylation | KFTLAGHTKAVSSVK EEEECCCCEEEEEEE | 21.56 | 22210691 | |
| 46 | Sumoylation | FTLAGHTKAVSSVKF EEECCCCEEEEEEEE | 40.91 | - | |
| 46 | Sumoylation | FTLAGHTKAVSSVKF EEECCCCEEEEEEEE | 40.91 | 28112733 | |
| 46 | Acetylation | FTLAGHTKAVSSVKF EEECCCCEEEEEEEE | 40.91 | 26051181 | |
| 49 | Phosphorylation | AGHTKAVSSVKFSPN CCCCEEEEEEEECCC | 33.98 | - | |
| 54 | Phosphorylation | AVSSVKFSPNGEWLA EEEEEEECCCCCEEC | 16.25 | 20068231 | |
| 62 | Phosphorylation | PNGEWLASSSADKLI CCCCEECCCCHHHHH | 23.74 | 20068231 | |
| 63 | Phosphorylation | NGEWLASSSADKLIK CCCEECCCCHHHHHH | 24.76 | 20068231 | |
| 64 | Phosphorylation | GEWLASSSADKLIKI CCEECCCCHHHHHHH | 37.68 | 20068231 | |
| 67 | Acetylation | LASSSADKLIKIWGA ECCCCHHHHHHHHEE | 52.40 | 26051181 | |
| 77 | Ubiquitination | KIWGAYDGKFEKTIS HHHEECCCCEEEEEC | 24.71 | 32015554 | |
| 78 | Ubiquitination | IWGAYDGKFEKTISG HHEECCCCEEEEECC | 47.67 | 29967540 | |
| 78 | Acetylation | IWGAYDGKFEKTISG HHEECCCCEEEEECC | 47.67 | 25953088 | |
| 81 | 2-Hydroxyisobutyrylation | AYDGKFEKTISGHKL ECCCCEEEEECCCCC | 55.05 | - | |
| 81 | Acetylation | AYDGKFEKTISGHKL ECCCCEEEEECCCCC | 55.05 | 27452117 | |
| 87 | Ubiquitination | EKTISGHKLGISDVA EEEECCCCCEEEEEE | 52.51 | 32015554 | |
| 96 | Phosphorylation | GISDVAWSSDSNLLV EEEEEEECCCCCEEE | 17.96 | 28348404 | |
| 97 | Phosphorylation | ISDVAWSSDSNLLVS EEEEEECCCCCEEEE | 34.06 | 28348404 | |
| 99 | Phosphorylation | DVAWSSDSNLLVSAS EEEECCCCCEEEECC | 31.18 | 28348404 | |
| 112 | Acetylation | ASDDKTLKIWDVSSG CCCCCCEEEEECCCC | 47.16 | 19608861 | |
| 116 | Ubiquitination | KTLKIWDVSSGKCLK CCEEEEECCCCCEEE | 2.70 | 33845483 | |
| 120 | Acetylation | IWDVSSGKCLKTLKG EEECCCCCEEEEECC | 38.04 | 25953088 | |
| 120 | Ubiquitination | IWDVSSGKCLKTLKG EEECCCCCEEEEECC | 38.04 | 23000965 | |
| 123 | Ubiquitination | VSSGKCLKTLKGHSN CCCCCEEEEECCCCC | 62.37 | 23000965 | |
| 126 | Ubiquitination | GKCLKTLKGHSNYVF CCEEEEECCCCCEEE | 60.86 | 23000965 | |
| 131 | Phosphorylation | TLKGHSNYVFCCNFN EECCCCCEEEEEECC | 9.64 | - | |
| 156 | Ubiquitination | FDESVRIWDVKTGKC CCCCEEEEECCCCCE | 8.19 | 33845483 | |
| 159 | Ubiquitination | SVRIWDVKTGKCLKT CEEEEECCCCCEECC | 49.43 | 21906983 | |
| 162 | Ubiquitination | IWDVKTGKCLKTLPA EEECCCCCEECCCCC | 41.44 | 22817900 | |
| 221 | Ubiquitination | NPPVSFVKFSPNGKY CCCCEEEEECCCCCE | 37.81 | 23000965 | |
| 227 | Ubiquitination | VKFSPNGKYILAATL EEECCCCCEEEEEEC | 35.44 | 23000965 | |
| 227 | Acetylation | VKFSPNGKYILAATL EEECCCCCEEEEEEC | 35.44 | 26051181 | |
| 228 | Phosphorylation | KFSPNGKYILAATLD EECCCCCEEEEEECC | 11.54 | 28152594 | |
| 245 | Malonylation | LKLWDYSKGKCLKTY EEEEECCCCCEEEEE | 57.04 | 26320211 | |
| 245 | Acetylation | LKLWDYSKGKCLKTY EEEEECCCCCEEEEE | 57.04 | 27452117 | |
| 250 | Acetylation | YSKGKCLKTYTGHKN CCCCCEEEEECCCCC | 49.29 | 26051181 | |
| 267 | Phosphorylation | YCIFANFSVTGGKWI EEEEEEEEEECCEEE | 20.69 | 17924679 | |
| 290 | Phosphorylation | VYIWNLQTKEIVQKL EEEEECCHHHHHHHH | 33.54 | - | |
| 291 | Ubiquitination | YIWNLQTKEIVQKLQ EEEECCHHHHHHHHC | 32.27 | 29967540 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of WDR5_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WDR5_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of WDR5_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASSSPECTROMETRY. | |