WDR5_HUMAN - dbPTM
WDR5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MATEEKKPE
------CCCCCCCCH
24.5822814378
6Ubiquitination--MATEEKKPETEAA
--CCCCCCCCHHHHH
68.3524816145
7Sumoylation-MATEEKKPETEAAR
-CCCCCCCCHHHHHH
51.9028112733
7Ubiquitination-MATEEKKPETEAAR
-CCCCCCCCHHHHHH
51.90-
18PhosphorylationEAARAQPTPSSSATQ
HHHHCCCCCCCCCCC
24.5925159151
20PhosphorylationARAQPTPSSSATQSK
HHCCCCCCCCCCCCC
39.1325159151
21PhosphorylationRAQPTPSSSATQSKP
HCCCCCCCCCCCCCC
25.7921406692
22PhosphorylationAQPTPSSSATQSKPT
CCCCCCCCCCCCCCC
39.4125159151
24PhosphorylationPTPSSSATQSKPTPV
CCCCCCCCCCCCCCC
35.0121406692
26PhosphorylationPSSSATQSKPTPVKP
CCCCCCCCCCCCCCC
35.9321406692
27UbiquitinationSSSATQSKPTPVKPN
CCCCCCCCCCCCCCC
42.9923000965
27SumoylationSSSATQSKPTPVKPN
CCCCCCCCCCCCCCC
42.9928112733
29PhosphorylationSATQSKPTPVKPNYA
CCCCCCCCCCCCCEE
44.4421406692
32UbiquitinationQSKPTPVKPNYALKF
CCCCCCCCCCEEEEE
28.8423000965
35PhosphorylationPTPVKPNYALKFTLA
CCCCCCCEEEEEEEC
23.1021406692
38MethylationVKPNYALKFTLAGHT
CCCCEEEEEEECCCC
28.29115978643
38UbiquitinationVKPNYALKFTLAGHT
CCCCEEEEEEECCCC
28.2923000965
45PhosphorylationKFTLAGHTKAVSSVK
EEEECCCCEEEEEEE
21.5622210691
46SumoylationFTLAGHTKAVSSVKF
EEECCCCEEEEEEEE
40.91-
46SumoylationFTLAGHTKAVSSVKF
EEECCCCEEEEEEEE
40.9128112733
46AcetylationFTLAGHTKAVSSVKF
EEECCCCEEEEEEEE
40.9126051181
49PhosphorylationAGHTKAVSSVKFSPN
CCCCEEEEEEEECCC
33.98-
54PhosphorylationAVSSVKFSPNGEWLA
EEEEEEECCCCCEEC
16.2520068231
62PhosphorylationPNGEWLASSSADKLI
CCCCEECCCCHHHHH
23.7420068231
63PhosphorylationNGEWLASSSADKLIK
CCCEECCCCHHHHHH
24.7620068231
64PhosphorylationGEWLASSSADKLIKI
CCEECCCCHHHHHHH
37.6820068231
67AcetylationLASSSADKLIKIWGA
ECCCCHHHHHHHHEE
52.4026051181
77UbiquitinationKIWGAYDGKFEKTIS
HHHEECCCCEEEEEC
24.7132015554
78UbiquitinationIWGAYDGKFEKTISG
HHEECCCCEEEEECC
47.6729967540
78AcetylationIWGAYDGKFEKTISG
HHEECCCCEEEEECC
47.6725953088
812-HydroxyisobutyrylationAYDGKFEKTISGHKL
ECCCCEEEEECCCCC
55.05-
81AcetylationAYDGKFEKTISGHKL
ECCCCEEEEECCCCC
55.0527452117
87UbiquitinationEKTISGHKLGISDVA
EEEECCCCCEEEEEE
52.5132015554
96PhosphorylationGISDVAWSSDSNLLV
EEEEEEECCCCCEEE
17.9628348404
97PhosphorylationISDVAWSSDSNLLVS
EEEEEECCCCCEEEE
34.0628348404
99PhosphorylationDVAWSSDSNLLVSAS
EEEECCCCCEEEECC
31.1828348404
112AcetylationASDDKTLKIWDVSSG
CCCCCCEEEEECCCC
47.1619608861
116UbiquitinationKTLKIWDVSSGKCLK
CCEEEEECCCCCEEE
2.7033845483
120AcetylationIWDVSSGKCLKTLKG
EEECCCCCEEEEECC
38.0425953088
120UbiquitinationIWDVSSGKCLKTLKG
EEECCCCCEEEEECC
38.0423000965
123UbiquitinationVSSGKCLKTLKGHSN
CCCCCEEEEECCCCC
62.3723000965
126UbiquitinationGKCLKTLKGHSNYVF
CCEEEEECCCCCEEE
60.8623000965
131PhosphorylationTLKGHSNYVFCCNFN
EECCCCCEEEEEECC
9.64-
156UbiquitinationFDESVRIWDVKTGKC
CCCCEEEEECCCCCE
8.1933845483
159UbiquitinationSVRIWDVKTGKCLKT
CEEEEECCCCCEECC
49.4321906983
162UbiquitinationIWDVKTGKCLKTLPA
EEECCCCCEECCCCC
41.4422817900
221UbiquitinationNPPVSFVKFSPNGKY
CCCCEEEEECCCCCE
37.8123000965
227UbiquitinationVKFSPNGKYILAATL
EEECCCCCEEEEEEC
35.4423000965
227AcetylationVKFSPNGKYILAATL
EEECCCCCEEEEEEC
35.4426051181
228PhosphorylationKFSPNGKYILAATLD
EECCCCCEEEEEECC
11.5428152594
245MalonylationLKLWDYSKGKCLKTY
EEEEECCCCCEEEEE
57.0426320211
245AcetylationLKLWDYSKGKCLKTY
EEEEECCCCCEEEEE
57.0427452117
250AcetylationYSKGKCLKTYTGHKN
CCCCCEEEEECCCCC
49.2926051181
267PhosphorylationYCIFANFSVTGGKWI
EEEEEEEEEECCEEE
20.6917924679
290PhosphorylationVYIWNLQTKEIVQKL
EEEEECCHHHHHHHH
33.54-
291UbiquitinationYIWNLQTKEIVQKLQ
EEEECCHHHHHHHHC
32.2729967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR5_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBIP1_HUMANMBIPphysical
16189514
KMT2A_HUMANKMT2Aphysical
15199122
RBBP5_HUMANRBBP5physical
16253997
SET1A_HUMANSETD1Aphysical
16253997
ASH2L_HUMANASH2Lphysical
16253997
CXXC1_HUMANCXXC1physical
16253997
CHD8_HUMANCHD8physical
18378692
SET1A_HUMANSETD1Aphysical
17355966
SET1B_HUMANSETD1Bphysical
17355966
ENL_HUMANMLLT1physical
18829459
ENL_HUMANMLLT1physical
18829457
H31_HUMANHIST1H3Aphysical
16946699
H31_HUMANHIST1H3Aphysical
16829960
H31_HUMANHIST1H3Aphysical
16829959
H31_HUMANHIST1H3Aphysical
16600877
H31_HUMANHIST1H3Aphysical
15960974
ASH2L_HUMANASH2Lphysical
15960974
RBBP5_HUMANRBBP5physical
15960974
KMT2D_HUMANKMT2Dphysical
15960974
PAX7_HUMANPAX7physical
18066051
ASH2L_HUMANASH2Lphysical
18066051
PAXI1_HUMANPAXIP1physical
17500065
RBBP5_HUMANRBBP5physical
17500065
PO5F1_HUMANPOU5F1physical
21477851
RBBP5_HUMANRBBP5physical
21220120
KMT2A_HUMANKMT2Aphysical
21220120
PRS8_HUMANPSMC5physical
19660582
H31T_HUMANHIST3H3physical
21124902
H31T_HUMANHIST3H3physical
21135039
MAVS_HUMANMAVSphysical
20080758
TRAF3_HUMANTRAF3physical
20080758
TRAF6_HUMANTRAF6physical
20080758
MBB1A_HUMANMYBBP1Aphysical
21531708
CSR2B_HUMANCSRP2BPphysical
21531708
ASH2L_HUMANASH2Lphysical
21531708
PK3CA_HUMANPIK3CAphysical
21531708
RBBP5_HUMANRBBP5physical
21531708
PITX2_HUMANPITX2physical
21531708
KDM4B_HUMANKDM4Bphysical
21502505
ESR1_HUMANESR1physical
21502505
ASH2L_HUMANASH2Lphysical
20305087
CXXC1_HUMANCXXC1physical
20305087
DPY30_HUMANDPY30physical
20305087
HCFC1_HUMANHCFC1physical
20305087
KMT2A_HUMANKMT2Aphysical
20305087
KMT2B_HUMANKMT2Bphysical
20305087
RBBP5_HUMANRBBP5physical
20305087
SET1A_HUMANSETD1Aphysical
20305087
HDAC3_HUMANHDAC3physical
21884981
ASH2L_HUMANASH2Lphysical
21884981
RBBP5_HUMANRBBP5physical
21884981
KMT2D_HUMANKMT2Dphysical
22266653
KMT2C_HUMANKMT2Cphysical
22266653
KMT2B_HUMANKMT2Bphysical
22266653
SET1A_HUMANSETD1Aphysical
22266653
SET1B_HUMANSETD1Bphysical
22266653
KMT2A_HUMANKMT2Aphysical
22266653
KAT2B_HUMANKAT2Bphysical
18838386
YETS2_HUMANYEATS2physical
18838386
KAT2A_HUMANKAT2Aphysical
18838386
TAD2A_HUMANTADA2Aphysical
18838386
TADA3_HUMANTADA3physical
18838386
MBIP1_HUMANMBIPphysical
18838386
SGF29_HUMANCCDC101physical
18838386
NC2B_HUMANDR1physical
18838386
A4_HUMANAPPphysical
21832049
XPO2_HUMANCSE1Lphysical
22939629
KMT2A_HUMANKMT2Aphysical
22989411
NFE4_HUMANNFE4physical
22689669
KMT2D_HUMANKMT2Dphysical
22689669
HDAC1_HUMANHDAC1physical
22689669
ING2_HUMANING2physical
22689669
MBIP1_HUMANMBIPphysical
25416956
ZXDC_HUMANZXDCphysical
25416956
ADIP_HUMANSSX2IPphysical
25416956
RUAS1_HUMANRUSC1-AS1physical
25416956
H31T_HUMANHIST3H3physical
24793694
BMAL1_HUMANARNTLphysical
23555304
HDAC1_HUMANHDAC1physical
26186194
KANL1_HUMANKANSL1physical
26186194
CSR2B_HUMANCSRP2BPphysical
26186194
YETS2_HUMANYEATS2physical
26186194
BOD1_HUMANBOD1physical
26186194
KMT2D_HUMANKMT2Dphysical
26186194
RBBP5_HUMANRBBP5physical
26186194
ZZZ3_HUMANZZZ3physical
26186194
PDPK1_HUMANPDPK1physical
26186194
HCFC2_HUMANHCFC2physical
26186194
MGAP_HUMANMGAphysical
26186194
KMT2B_HUMANKMT2Bphysical
26186194
KMT2A_HUMANKMT2Aphysical
26186194
SET1B_HUMANSETD1Bphysical
26186194
SET1A_HUMANSETD1Aphysical
26186194
KDM6A_HUMANKDM6Aphysical
26186194
LMBL2_HUMANL3MBTL2physical
26186194
BD1L1_HUMANBOD1L1physical
26186194
ASH2L_HUMANASH2Lphysical
26186194
KAT2B_HUMANKAT2Bphysical
26186194
KAT2A_HUMANKAT2Aphysical
26186194
RYBP_HUMANRYBPphysical
26186194
TADA3_HUMANTADA3physical
26186194
MBIP1_HUMANMBIPphysical
26186194
PPR3F_HUMANPPP1R3Fphysical
26186194
NC2B_HUMANDR1physical
26186194
TAD2A_HUMANTADA2Aphysical
26186194
PAXI1_HUMANPAXIP1physical
26186194
F199X_HUMANFAM199Xphysical
26186194
RING2_HUMANRNF2physical
26186194
CXXC1_HUMANCXXC1physical
26186194
ZXDC_HUMANZXDCphysical
26186194
RERE_HUMANREREphysical
26186194
YAF2_HUMANYAF2physical
26186194
ATN1_HUMANATN1physical
26186194
SESN2_HUMANSESN2physical
26186194
NCOA6_HUMANNCOA6physical
26186194
KANL1_HUMANKANSL1physical
24788516
KANL2_HUMANKANSL2physical
24788516
KMT2D_HUMANKMT2Dphysical
24788516
H31T_HUMANHIST3H3physical
24788516
SYHC_HUMANHARSphysical
26344197
ASH2L_HUMANASH2Lphysical
25666610
RBBP5_HUMANRBBP5physical
25666610
DPY30_HUMANDPY30physical
25666610
H31_HUMANHIST1H3Aphysical
25666610
KIF23_HUMANKIF23physical
25666610
RGAP1_HUMANRACGAP1physical
25666610
CEP55_HUMANCEP55physical
25666610
CHM1B_HUMANCHMP1Bphysical
25666610
ECT2_HUMANECT2physical
25666610
PDC6I_HUMANPDCD6IPphysical
25666610
TS101_HUMANTSG101physical
25666610
PRC1_HUMANPRC1physical
25666610
MYCN_HUMANMYCNphysical
26471359
KMT2D_HUMANKMT2Dphysical
28514442
ATN1_HUMANATN1physical
28514442
KANL1_HUMANKANSL1physical
28514442
KDM6A_HUMANKDM6Aphysical
28514442
KMT2B_HUMANKMT2Bphysical
28514442
MBIP1_HUMANMBIPphysical
28514442
PAXI1_HUMANPAXIP1physical
28514442
RERE_HUMANREREphysical
28514442
CXXC1_HUMANCXXC1physical
28514442
TAD2A_HUMANTADA2Aphysical
28514442
SET1B_HUMANSETD1Bphysical
28514442
PDPK1_HUMANPDPK1physical
28514442
PPR3F_HUMANPPP1R3Fphysical
28514442
CSR2B_HUMANCSRP2BPphysical
28514442
KAT2B_HUMANKAT2Bphysical
28514442
SET1A_HUMANSETD1Aphysical
28514442
ZZZ3_HUMANZZZ3physical
28514442
KMT2A_HUMANKMT2Aphysical
28514442
BOD1_HUMANBOD1physical
28514442
TADA3_HUMANTADA3physical
28514442
YETS2_HUMANYEATS2physical
28514442
SESN2_HUMANSESN2physical
28514442
BD1L1_HUMANBOD1L1physical
28514442
NCOA6_HUMANNCOA6physical
28514442
LMBL2_HUMANL3MBTL2physical
28514442
KAT2A_HUMANKAT2Aphysical
28514442
F199X_HUMANFAM199Xphysical
28514442
PCGF6_HUMANPCGF6physical
28514442
MGAP_HUMANMGAphysical
28514442
ZXDC_HUMANZXDCphysical
28514442
ASH2L_HUMANASH2Lphysical
28514442
RBBP5_HUMANRBBP5physical
28514442
HCFC2_HUMANHCFC2physical
28514442
HDAC1_HUMANHDAC1physical
28514442
RING2_HUMANRNF2physical
28514442
RYBP_HUMANRYBPphysical
28514442
NC2B_HUMANDR1physical
28514442
HDAC2_HUMANHDAC2physical
28514442
MYC_HUMANMYCphysical
27320920
RBBP5_HUMANRBBP5physical
27320920

Drug and Disease Associations
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.
Regulatory Network of WDR5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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
ReferencePubMed
"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.

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