WDR1_HUMAN - dbPTM
WDR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR1_HUMAN
UniProt AC O75083
Protein Name WD repeat-containing protein 1
Gene Name WDR1
Organism Homo sapiens (Human).
Sequence Length 606
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, podosome . Cell junction .
Protein Description Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. [PubMed: 15629458 Enhances cofilin-mediated actin severing (By similarity Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions]
Protein Sequence MPYEIKKVFASLPQVERGVSKIIGGDPKGNNFLYTNGKCVILRNIDNPALADIYTEHAHQVVVAKYAPSGFYIASGDVSGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDSGSSVGEITGHNKVINSVDIKQSRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIYIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVSVNSVVSTFPMGSTVLDQQLGCLWQKDHLLSVSLSGYINYLDRNNPSKPLHVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGENDSFAGKGHTNQVSRMTVDESGQLISCSMDDTVRYTSLMLRDYSGQGVVKLDVQPKCVAVGPGGYAVVVCIGQIVLLKDQRKCFSIDNPGYEPEVVAVHPGGDTVAIGGVDGNVRLYSILGTTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETRVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY
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
3Phosphorylation-----MPYEIKKVFA
-----CCHHHHHHHH
29.05-
7Ubiquitination-MPYEIKKVFASLPQ
-CCHHHHHHHHCCHH
48.5221890473
7 (in isoform 1)Ubiquitination-48.5221890473
7 (in isoform 3)Ubiquitination-48.5221890473
11PhosphorylationEIKKVFASLPQVERG
HHHHHHHCCHHHHHC
29.1728857561
17MethylationASLPQVERGVSKIIG
HCCHHHHHCCEEECC
52.54115919905
20PhosphorylationPQVERGVSKIIGGDP
HHHHHCCEEECCCCC
22.4420068231
20 (in isoform 1)Phosphorylation-22.44-
21UbiquitinationQVERGVSKIIGGDPK
HHHHCCEEECCCCCC
35.6221890473
21 (in isoform 1)Ubiquitination-35.6221890473
21 (in isoform 3)Ubiquitination-35.6221890473
28AcetylationKIIGGDPKGNNFLYT
EECCCCCCCCCEEEE
78.1219608861
28UbiquitinationKIIGGDPKGNNFLYT
EECCCCCCCCCEEEE
78.1221890473
28 (in isoform 1)Acetylation-78.12-
28 (in isoform 1)Ubiquitination-78.1221890473
28 (in isoform 3)Ubiquitination-78.1221890473
34PhosphorylationPKGNNFLYTNGKCVI
CCCCCEEEECCEEEE
8.2729496907
38AcetylationNFLYTNGKCVILRNI
CEEEECCEEEEEECC
27.6523749302
38UbiquitinationNFLYTNGKCVILRNI
CEEEECCEEEEEECC
27.6521890473
38 (in isoform 1)Ubiquitination-27.6521890473
38 (in isoform 3)Ubiquitination-27.6521890473
54PhosphorylationNPALADIYTEHAHQV
CHHHHHHHCCCCCEE
13.46-
55PhosphorylationPALADIYTEHAHQVV
HHHHHHHCCCCCEEE
22.94-
65UbiquitinationAHQVVVAKYAPSGFY
CCEEEEEEECCCCEE
30.27-
65AcetylationAHQVVVAKYAPSGFY
CCEEEEEEECCCCEE
30.2726051181
66PhosphorylationHQVVVAKYAPSGFYI
CEEEEEEECCCCEEE
17.6321406692
69PhosphorylationVVAKYAPSGFYIASG
EEEEECCCCEEEEEC
33.1028152594
72PhosphorylationKYAPSGFYIASGDVS
EECCCCEEEEECCCC
10.0920090780
75PhosphorylationPSGFYIASGDVSGKL
CCCEEEEECCCCCCE
26.4328152594
79PhosphorylationYIASGDVSGKLRIWD
EEEECCCCCCEEEEE
34.6421406692
81AcetylationASGDVSGKLRIWDTT
EECCCCCCEEEEECC
27.3819608861
81UbiquitinationASGDVSGKLRIWDTT
EECCCCCCEEEEECC
27.3819608861
83MethylationGDVSGKLRIWDTTQK
CCCCCCEEEEECCCC
31.29115919913
87PhosphorylationGKLRIWDTTQKEHLL
CCEEEEECCCCHHHH
19.0128857561
88PhosphorylationKLRIWDTTQKEHLLK
CEEEEECCCCHHHHE
34.8628857561
90UbiquitinationRIWDTTQKEHLLKYE
EEEECCCCHHHHEEE
45.0490473
90AcetylationRIWDTTQKEHLLKYE
EEEECCCCHHHHEEE
45.0426822725
90 (in isoform 1)Ubiquitination-45.0421890473
95AcetylationTQKEHLLKYEYQPFA
CCCHHHHEEECCCCC
42.2519608861
95UbiquitinationTQKEHLLKYEYQPFA
CCCHHHHEEECCCCC
42.2519608861
95MalonylationTQKEHLLKYEYQPFA
CCCHHHHEEECCCCC
42.2526320211
95 (in isoform 1)Ubiquitination-42.2521890473
96PhosphorylationQKEHLLKYEYQPFAG
CCHHHHEEECCCCCC
21.6028102081
98PhosphorylationEHLLKYEYQPFAGKI
HHHHEEECCCCCCCC
20.5625839225
98 (in isoform 1)Phosphorylation-20.56-
104AcetylationEYQPFAGKIKDIAWT
ECCCCCCCCEEEEEC
43.0623749302
104UbiquitinationEYQPFAGKIKDIAWT
ECCCCCCCCEEEEEC
43.06-
106UbiquitinationQPFAGKIKDIAWTED
CCCCCCCEEEEECCC
46.71-
114PhosphorylationDIAWTEDSKRIAVVG
EEEECCCCCEEEEEE
20.0128857561
115AcetylationIAWTEDSKRIAVVGE
EEECCCCCEEEEEEC
61.2119608861
115UbiquitinationIAWTEDSKRIAVVGE
EEECCCCCEEEEEEC
61.2121906983
1152-HydroxyisobutyrylationIAWTEDSKRIAVVGE
EEECCCCCEEEEEEC
61.21-
115MalonylationIAWTEDSKRIAVVGE
EEECCCCCEEEEEEC
61.2126320211
115 (in isoform 1)Ubiquitination-61.2121890473
126UbiquitinationVVGEGREKFGAVFLW
EEECCHHHEEEEEEE
47.97-
126AcetylationVVGEGREKFGAVFLW
EEECCHHHEEEEEEE
47.9725953088
135PhosphorylationGAVFLWDSGSSVGEI
EEEEEEECCCCCEEE
29.0628857561
137PhosphorylationVFLWDSGSSVGEITG
EEEEECCCCCEEECC
26.2928857561
138PhosphorylationFLWDSGSSVGEITGH
EEEECCCCCEEECCC
37.3528060719
143PhosphorylationGSSVGEITGHNKVIN
CCCCEEECCCCCEEC
28.2528857561
151PhosphorylationGHNKVINSVDIKQSR
CCCCEECEEECCCCC
15.2824076635
155UbiquitinationVINSVDIKQSRPYRL
EECEEECCCCCCEEE
37.44-
1552-HydroxyisobutyrylationVINSVDIKQSRPYRL
EECEEECCCCCCEEE
37.44-
155AcetylationVINSVDIKQSRPYRL
EECEEECCCCCCEEE
37.4425953088
164PhosphorylationSRPYRLATGSDDNCA
CCCEEECCCCCCCCH
41.6420068231
166PhosphorylationPYRLATGSDDNCAAF
CEEECCCCCCCCHHH
37.1225693802
170GlutathionylationATGSDDNCAAFFEGP
CCCCCCCCHHHCCCC
3.5822555962
180AcetylationFFEGPPFKFKFTIGD
HCCCCCEEEEEEECC
54.1125953088
180UbiquitinationFFEGPPFKFKFTIGD
HCCCCCEEEEEEECC
54.11-
182AcetylationEGPPFKFKFTIGDHS
CCCCEEEEEEECCCC
42.0323749302
182UbiquitinationEGPPFKFKFTIGDHS
CCCCEEEEEEECCCC
42.03-
184 (in isoform 3)Ubiquitination-25.3321890473
188 (in isoform 3)Ubiquitination-18.7021890473
189PhosphorylationKFTIGDHSRFVNCVR
EEEECCCCCEEEEEE
31.9626437602
198PhosphorylationFVNCVRFSPDGNRFA
EEEEEEECCCCCEEE
16.1227067055
208PhosphorylationGNRFATASADGQIYI
CCEEEEEECCCEEEE
23.6528152594
214PhosphorylationASADGQIYIYDGKTG
EECCCEEEEECCCCC
5.8728152594
216PhosphorylationADGQIYIYDGKTGEK
CCCEEEEECCCCCCE
11.1528152594
219AcetylationQIYIYDGKTGEKVCA
EEEEECCCCCCEEEE
50.9226051181
219UbiquitinationQIYIYDGKTGEKVCA
EEEEECCCCCCEEEE
50.9221906983
219MalonylationQIYIYDGKTGEKVCA
EEEEECCCCCCEEEE
50.9226320211
219 (in isoform 1)Ubiquitination-50.9221890473
221 (in isoform 3)Ubiquitination-35.8921890473
223AcetylationYDGKTGEKVCALGGS
ECCCCCCEEEECCCC
43.9123749302
223UbiquitinationYDGKTGEKVCALGGS
ECCCCCCEEEECCCC
43.9121906983
223 (in isoform 1)Ubiquitination-43.9121890473
230PhosphorylationKVCALGGSKAHDGGI
EEEECCCCCCCCCCE
25.5226437602
231UbiquitinationVCALGGSKAHDGGIY
EEECCCCCCCCCCEE
53.68-
231MalonylationVCALGGSKAHDGGIY
EEECCCCCCCCCCEE
53.6826320211
231AcetylationVCALGGSKAHDGGIY
EEECCCCCCCCCCEE
53.6826051181
238PhosphorylationKAHDGGIYAISWSPD
CCCCCCEEEEEECCC
10.9319605366
241PhosphorylationDGGIYAISWSPDSTH
CCCEEEEEECCCCCC
17.2128796482
243PhosphorylationGIYAISWSPDSTHLL
CEEEEEECCCCCCEE
16.4328985074
246PhosphorylationAISWSPDSTHLLSAS
EEEECCCCCCEEECC
22.5528857561
247PhosphorylationISWSPDSTHLLSASG
EEECCCCCCEEECCC
24.7528857561
256AcetylationLLSASGDKTSKIWDV
EEECCCCCCCCEEEE
59.2223954790
256UbiquitinationLLSASGDKTSKIWDV
EEECCCCCCCCEEEE
59.2221906983
2562-HydroxyisobutyrylationLLSASGDKTSKIWDV
EEECCCCCCCCEEEE
59.22-
256MalonylationLLSASGDKTSKIWDV
EEECCCCCCCCEEEE
59.2226320211
256 (in isoform 1)Ubiquitination-59.2221890473
300PhosphorylationLSVSLSGYINYLDRN
EEEEHHHHHHHHCCC
5.21-
310PhosphorylationYLDRNNPSKPLHVIK
HHCCCCCCCCEEEEE
49.3728857561
311UbiquitinationLDRNNPSKPLHVIKG
HCCCCCCCCEEEEEC
53.51-
317UbiquitinationSKPLHVIKGHSKSIQ
CCCEEEEECCCCEEE
49.86-
320PhosphorylationLHVIKGHSKSIQCLT
EEEEECCCCEEEEEE
36.4528857561
321AcetylationHVIKGHSKSIQCLTV
EEEECCCCEEEEEEE
46.0023749302
321UbiquitinationHVIKGHSKSIQCLTV
EEEECCCCEEEEEEE
46.00-
3212-HydroxyisobutyrylationHVIKGHSKSIQCLTV
EEEECCCCEEEEEEE
46.00-
322PhosphorylationVIKGHSKSIQCLTVH
EEECCCCEEEEEEEE
22.3930108239
327PhosphorylationSKSIQCLTVHKNGGK
CCEEEEEEEEECCCE
28.3428857561
327 (in isoform 3)Ubiquitination-28.3421890473
330AcetylationIQCLTVHKNGGKSYI
EEEEEEEECCCEEEE
53.6125953088
330UbiquitinationIQCLTVHKNGGKSYI
EEEEEEEECCCEEEE
53.61-
334UbiquitinationTVHKNGGKSYIYSGS
EEEECCCEEEEEECC
41.29-
334AcetylationTVHKNGGKSYIYSGS
EEEECCCEEEEEECC
41.2926051181
338PhosphorylationNGGKSYIYSGSHDGH
CCCEEEEEECCCCCC
9.9528796482
339PhosphorylationGGKSYIYSGSHDGHI
CCEEEEEECCCCCCE
25.0228857561
340 (in isoform 1)Acetylation-16.42-
340AcetylationGKSYIYSGSHDGHIN
CEEEEEECCCCCCEE
16.4219608861
340UbiquitinationGKSYIYSGSHDGHIN
CEEEEEECCCCCCEE
16.4219608861
341PhosphorylationKSYIYSGSHDGHINY
EEEEEECCCCCCEEE
16.6828857561
348PhosphorylationSHDGHINYWDSETGE
CCCCCEEEEECCCCC
15.2528796482
351PhosphorylationGHINYWDSETGENDS
CCEEEEECCCCCCCC
23.9428348404
353PhosphorylationINYWDSETGENDSFA
EEEEECCCCCCCCCC
54.4728348404
358PhosphorylationSETGENDSFAGKGHT
CCCCCCCCCCCCCCC
28.6927251275
362UbiquitinationENDSFAGKGHTNQVS
CCCCCCCCCCCCCEE
44.0521906983
362AcetylationENDSFAGKGHTNQVS
CCCCCCCCCCCCCEE
44.0526051181
362 (in isoform 1)Ubiquitination-44.0521890473
371 (in isoform 1)Acetylation-3.14-
371SulfoxidationHTNQVSRMTVDESGQ
CCCCEEEEEECCCCC
3.1421406390
371AcetylationHTNQVSRMTVDESGQ
CCCCEEEEEECCCCC
3.1419608861
372PhosphorylationTNQVSRMTVDESGQL
CCCEEEEEECCCCCE
24.5621406692
376PhosphorylationSRMTVDESGQLISCS
EEEEECCCCCEEEEE
27.6321406692
381PhosphorylationDESGQLISCSMDDTV
CCCCCEEEEECCCHH
14.5621406692
383PhosphorylationSGQLISCSMDDTVRY
CCCEEEEECCCHHEE
20.6021406692
384SulfoxidationGQLISCSMDDTVRYT
CCEEEEECCCHHEEE
6.7430846556
387PhosphorylationISCSMDDTVRYTSLM
EEEECCCHHEEEEEE
11.5621406692
390PhosphorylationSMDDTVRYTSLMLRD
ECCCHHEEEEEEEEC
9.0621406692
391PhosphorylationMDDTVRYTSLMLRDY
CCCHHEEEEEEEECC
12.5721406692
392PhosphorylationDDTVRYTSLMLRDYS
CCHHEEEEEEEECCC
11.6621406692
394SulfoxidationTVRYTSLMLRDYSGQ
HHEEEEEEEECCCCC
2.6321406390
396MethylationRYTSLMLRDYSGQGV
EEEEEEEECCCCCCE
27.19115919909
398PhosphorylationTSLMLRDYSGQGVVK
EEEEEECCCCCCEEE
14.3123911959
398NitrationTSLMLRDYSGQGVVK
EEEEEECCCCCCEEE
14.31-
399PhosphorylationSLMLRDYSGQGVVKL
EEEEECCCCCCEEEE
29.0028857561
405UbiquitinationYSGQGVVKLDVQPKC
CCCCCEEEEEEECCE
36.2421890473
405AcetylationYSGQGVVKLDVQPKC
CCCCCEEEEEEECCE
36.2426051181
405 (in isoform 1)Ubiquitination-36.2421890473
437UbiquitinationVLLKDQRKCFSIDNP
EEECCCCCCEECCCC
33.72-
440PhosphorylationKDQRKCFSIDNPGYE
CCCCCCEECCCCCCC
38.2028857561
445 (in isoform 3)Ubiquitination-45.7721890473
446PhosphorylationFSIDNPGYEPEVVAV
EECCCCCCCCEEEEE
29.5728857561
449 (in isoform 3)Ubiquitination-37.3721890473
472PhosphorylationVDGNVRLYSILGTTL
CCCCEEEEEEECCEE
5.3228796482
473PhosphorylationDGNVRLYSILGTTLK
CCCEEEEEEECCEEC
18.8728796482
477PhosphorylationRLYSILGTTLKDEGK
EEEEEECCEECCCCE
26.0528152594
478PhosphorylationLYSILGTTLKDEGKL
EEEEECCEECCCCEE
29.9728857561
480AcetylationSILGTTLKDEGKLLE
EEECCEECCCCEEEE
52.2019608861
480UbiquitinationSILGTTLKDEGKLLE
EEECCEECCCCEEEE
52.2019608861
480SuccinylationSILGTTLKDEGKLLE
EEECCEECCCCEEEE
52.2023954790
480 (in isoform 1)Ubiquitination-52.2021890473
484UbiquitinationTTLKDEGKLLEAKGP
CEECCCCEEEEECCC
48.102190698
4842-HydroxyisobutyrylationTTLKDEGKLLEAKGP
CEECCCCEEEEECCC
48.10-
484 (in isoform 1)Ubiquitination-48.1021890473
489UbiquitinationEGKLLEAKGPVTDVA
CCEEEEECCCCCEEE
55.14-
4892-HydroxyisobutyrylationEGKLLEAKGPVTDVA
CCEEEEECCCCCEEE
55.14-
507S-palmitoylationDGAFLAVCDASKVVT
CCEEEEEECHHCEEE
2.7729575903
511AcetylationLAVCDASKVVTVFSV
EEEECHHCEEEEEEE
42.3119608861
517PhosphorylationSKVVTVFSVADGYSE
HCEEEEEEECCCCCC
16.4428152594
522PhosphorylationVFSVADGYSENNVFY
EEEECCCCCCCCEEE
17.2328152594
523PhosphorylationFSVADGYSENNVFYG
EEECCCCCCCCEEEC
39.1028152594
529PhosphorylationYSENNVFYGHHAKIV
CCCCCEEECCCCEEE
15.9728152594
557PhosphorylationGGMDMMVYVWTLSDP
CCCEEEEEEEECCCH
3.4126074081
560PhosphorylationDMMVYVWTLSDPETR
EEEEEEEECCCHHHE
13.3126074081
562PhosphorylationMVYVWTLSDPETRVK
EEEEEECCCHHHEEE
43.6826074081
569AcetylationSDPETRVKIQDAHRL
CCHHHEEEHHHHHHH
31.2123749302
569UbiquitinationSDPETRVKIQDAHRL
CCHHHEEEHHHHHHH
31.21-
5692-HydroxyisobutyrylationSDPETRVKIQDAHRL
CCHHHEEEHHHHHHH
31.21-
580PhosphorylationAHRLHHVSSLAWLDE
HHHHHCCCEEEEECC
18.4428857561
581PhosphorylationHRLHHVSSLAWLDEH
HHHHCCCEEEEECCC
22.4828348404

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 WDR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR1_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 WDR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KEAP1_HUMANKEAP1physical
23382044
IF5A1_HUMANEIF5Aphysical
22863883
CH10_HUMANHSPE1physical
22863883
RBBP7_HUMANRBBP7physical
22863883
RENR_HUMANATP6AP2physical
26344197
CALR_HUMANCALRphysical
26344197
COF1_HUMANCFL1physical
26344197
COF2_HUMANCFL2physical
26344197
DEST_HUMANDSTNphysical
26344197
ENOA_HUMANENO1physical
26344197
ENOG_HUMANENO2physical
26344197
AATC_HUMANGOT1physical
26344197
G6PI_HUMANGPIphysical
26344197
CH10_HUMANHSPE1physical
26344197
GILT_HUMANIFI30physical
26344197
ITPA_HUMANITPAphysical
26344197
LACB2_HUMANLACTB2physical
26344197
LDHA_HUMANLDHAphysical
26344197
LDH6A_HUMANLDHAL6Aphysical
26344197
LDH6B_HUMANLDHAL6Bphysical
26344197
LDHB_HUMANLDHBphysical
26344197
LDHC_HUMANLDHCphysical
26344197
MSI2H_HUMANMSI2physical
26344197
NDKB_HUMANNME2physical
26344197
PABP4_HUMANPABPC4physical
26344197
PHS_HUMANPCBD1physical
26344197
PPIH_HUMANPPIHphysical
26344197
PRDX6_HUMANPRDX6physical
26344197
PSMG4_HUMANPSMG4physical
26344197
TKT_HUMANTKTphysical
26344197
POTEE_HUMANPOTEEphysical
28514442
ATRX_HUMANATRXphysical
28514442

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 WDR1_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-28; LYS-81; LYS-95; LYS-115AND LYS-480, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASSSPECTROMETRY.

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