WDR70_HUMAN - dbPTM
WDR70_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR70_HUMAN
UniProt AC Q9NW82
Protein Name WD repeat-containing protein 70
Gene Name WDR70
Organism Homo sapiens (Human).
Sequence Length 654
Subcellular Localization
Protein Description
Protein Sequence MERSGPSEVTGSDASGPDPQLAVTMGFTGFGKKARTFDLEAMFEQTRRTAVERSRKTLEAREKEEEMNREKELRRQNEDIEPTSSRSNVVRDCSKSSSRDTSSSESEQSSDSSDDELIGPPLPPKMVGKPVNFMEEDILGPLPPPLNEEEEEAEEEEEEEEEEENPVHKIPDSHEITLKHGTKTVSALGLDPSGARLVTGGYDYDVKFWDFAGMDASFKAFRSLQPCECHQIKSLQYSNTGDMILVVSGSSQAKVIDRDGFEVMECIKGDQYIVDMANTKGHTAMLHTGSWHPKIKGEFMTCSNDATVRTWEVENPKKQKSVFKPRTMQGKKVIPTTCTYSRDGNLIAAACQNGSIQIWDRNLTVHPKFHYKQAHDSGTDTSCVTFSYDGNVLASRGGDDSLKLWDIRQFNKPLFSASGLPTMFPMTDCCFSPDDKLIVTGTSIQRGCGSGKLVFFERRTFQRVYEIDITDASVVRCLWHPKLNQIMVGTGNGLAKVYYDPNKSQRGAKLCVVKTQRKAKQAETLTQDYIITPHALPMFREPRQRSTRKQLEKDRLDPLKSHKPEPPVAGPGRGGRVGTHGGTLSSYIVKNIALDKTDDSNPREAILRHAKAAEDSPYWVSPAYSKTQPKTMFAQVESDDEEAKNEPEWKKRKI
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
4Phosphorylation----MERSGPSEVTG
----CCCCCCCCCCC
41.5728555341
6Ubiquitination--MERSGPSEVTGSD
--CCCCCCCCCCCCC
28.6722817900
32MethylationMGFTGFGKKARTFDL
ECCCCCCCHHHEECH
40.7830593423
32AcetylationMGFTGFGKKARTFDL
ECCCCCCCHHHEECH
40.7825953088
33UbiquitinationGFTGFGKKARTFDLE
CCCCCCCHHHEECHH
43.40-
36PhosphorylationGFGKKARTFDLEAMF
CCCCHHHEECHHHHH
26.7620860994
52UbiquitinationQTRRTAVERSRKTLE
HHHHHHHHHHHHHHH
42.3423000965
54PhosphorylationRRTAVERSRKTLEAR
HHHHHHHHHHHHHHH
25.3223312004
54UbiquitinationRRTAVERSRKTLEAR
HHHHHHHHHHHHHHH
25.3223000965
56AcetylationTAVERSRKTLEAREK
HHHHHHHHHHHHHHH
59.7226051181
57PhosphorylationAVERSRKTLEAREKE
HHHHHHHHHHHHHHH
28.8120068231
81UbiquitinationRRQNEDIEPTSSRSN
HHCCCCCCCCCCCCC
55.6423000965
83UbiquitinationQNEDIEPTSSRSNVV
CCCCCCCCCCCCCHH
26.9223000965
84PhosphorylationNEDIEPTSSRSNVVR
CCCCCCCCCCCCHHH
34.1728555341
87PhosphorylationIEPTSSRSNVVRDCS
CCCCCCCCCHHHCHH
35.6028555341
98PhosphorylationRDCSKSSSRDTSSSE
HCHHCCCCCCCCCCC
41.0730576142
109PhosphorylationSSSESEQSSDSSDDE
CCCCCCCCCCCCCCC
31.8730576142
110PhosphorylationSSESEQSSDSSDDEL
CCCCCCCCCCCCCCC
41.0030576142
157UbiquitinationEEEAEEEEEEEEEEE
HHHHHHHHHHHHHHC
74.1829967540
161UbiquitinationEEEEEEEEEEENPVH
HHHHHHHHHHCCCCC
74.1822817900
178UbiquitinationPDSHEITLKHGTKTV
CCCCEEEECCCCEEE
4.7829967540
179UbiquitinationDSHEITLKHGTKTVS
CCCEEEECCCCEEEE
31.1929967540
182UbiquitinationEITLKHGTKTVSALG
EEEECCCCEEEEECC
24.2229967540
183UbiquitinationITLKHGTKTVSALGL
EEECCCCEEEEECCC
52.0729967540
184PhosphorylationTLKHGTKTVSALGLD
EECCCCEEEEECCCC
21.3820860994
190UbiquitinationKTVSALGLDPSGARL
EEEEECCCCCCCCEE
10.2122817900
197UbiquitinationLDPSGARLVTGGYDY
CCCCCCEEEECCCCC
3.9221963094
217PhosphorylationDFAGMDASFKAFRSL
CCCCCCHHHHHHHCC
24.0224719451
218UbiquitinationFAGMDASFKAFRSLQ
CCCCCHHHHHHHCCC
7.6821963094
219UbiquitinationAGMDASFKAFRSLQP
CCCCHHHHHHHCCCC
44.0821963094
258UbiquitinationSQAKVIDRDGFEVME
CCEEEECCCCCEEEE
34.5229967540
272UbiquitinationECIKGDQYIVDMANT
EEECCCEEEEECCCC
13.9823000965
274UbiquitinationIKGDQYIVDMANTKG
ECCCEEEEECCCCCC
3.3323000965
279UbiquitinationYIVDMANTKGHTAML
EEEECCCCCCCEEEE
28.9429967540
279PhosphorylationYIVDMANTKGHTAML
EEEECCCCCCCEEEE
28.9422210691
280UbiquitinationIVDMANTKGHTAMLH
EEECCCCCCCEEEEE
48.8029967540
293UbiquitinationLHTGSWHPKIKGEFM
EECCCCCCCCCCEEE
33.5323000965
294UbiquitinationHTGSWHPKIKGEFMT
ECCCCCCCCCCEEEE
44.1323000965
295UbiquitinationTGSWHPKIKGEFMTC
CCCCCCCCCCEEEEE
9.0323000965
296SumoylationGSWHPKIKGEFMTCS
CCCCCCCCCEEEEEC
59.52-
296SumoylationGSWHPKIKGEFMTCS
CCCCCCCCCEEEEEC
59.5225218447
296UbiquitinationGSWHPKIKGEFMTCS
CCCCCCCCCEEEEEC
59.5223000965
310UbiquitinationSNDATVRTWEVENPK
CCCCEEEEEEECCCC
22.9529967540
318UbiquitinationWEVENPKKQKSVFKP
EEECCCCCCCCCCCC
65.30-
321O-linked_GlycosylationENPKKQKSVFKPRTM
CCCCCCCCCCCCCCC
30.2330379171
331UbiquitinationKPRTMQGKKVIPTTC
CCCCCCCCEEECCEE
27.2929967540
332SumoylationPRTMQGKKVIPTTCT
CCCCCCCEEECCEEE
52.82-
332SumoylationPRTMQGKKVIPTTCT
CCCCCCCEEECCEEE
52.82-
332UbiquitinationPRTMQGKKVIPTTCT
CCCCCCCEEECCEEE
52.8229967540
336PhosphorylationQGKKVIPTTCTYSRD
CCCEEECCEEEEECC
24.3129759185
337PhosphorylationGKKVIPTTCTYSRDG
CCEEECCEEEEECCC
9.4829759185
339PhosphorylationKVIPTTCTYSRDGNL
EEECCEEEEECCCCE
23.5729759185
340PhosphorylationVIPTTCTYSRDGNLI
EECCEEEEECCCCEE
12.1229759185
341PhosphorylationIPTTCTYSRDGNLIA
ECCEEEEECCCCEEE
13.0229759185
346UbiquitinationTYSRDGNLIAAACQN
EEECCCCEEEEEEEC
3.2629967540
367UbiquitinationDRNLTVHPKFHYKQA
ECCEEECCCCEEEEC
36.3529967540
368UbiquitinationRNLTVHPKFHYKQAH
CCEEECCCCEEEECC
29.8729967540
371PhosphorylationTVHPKFHYKQAHDSG
EECCCCEEEECCCCC
14.13-
381UbiquitinationAHDSGTDTSCVTFSY
CCCCCCCCCEEEEEE
24.7022817900
401PhosphorylationASRGGDDSLKLWDIR
ECCCCCCCCEEECHH
31.95-
402UbiquitinationSRGGDDSLKLWDIRQ
CCCCCCCCEEECHHH
7.3222817900
403SumoylationRGGDDSLKLWDIRQF
CCCCCCCEEECHHHC
52.03-
403UbiquitinationRGGDDSLKLWDIRQF
CCCCCCCEEECHHHC
52.0322817900
403SumoylationRGGDDSLKLWDIRQF
CCCCCCCEEECHHHC
52.03-
432PhosphorylationPMTDCCFSPDDKLIV
CCCCCCCCCCCCEEE
17.3221815630
452AcetylationQRGCGSGKLVFFERR
ECCCCCCCEEEEECC
43.0819608861
452UbiquitinationQRGCGSGKLVFFERR
ECCCCCCCEEEEECC
43.0819608861
465PhosphorylationRRTFQRVYEIDITDA
CCCCCEEEEEECCCH
14.89-
474UbiquitinationIDITDASVVRCLWHP
EECCCHHHHHHHCCC
3.1829967540
481UbiquitinationVVRCLWHPKLNQIMV
HHHHHCCCCCCEEEE
31.1129967540
482UbiquitinationVRCLWHPKLNQIMVG
HHHHCCCCCCEEEEE
47.37-
482AcetylationVRCLWHPKLNQIMVG
HHHHCCCCCCEEEEE
47.3725953088
487UbiquitinationHPKLNQIMVGTGNGL
CCCCCEEEEECCCCE
1.3129967540
492UbiquitinationQIMVGTGNGLAKVYY
EEEEECCCCEEEEEE
41.9929967540
495UbiquitinationVGTGNGLAKVYYDPN
EECCCCEEEEEECCC
10.7329967540
496UbiquitinationGTGNGLAKVYYDPNK
ECCCCEEEEEECCCC
35.4929967540
502UbiquitinationAKVYYDPNKSQRGAK
EEEEECCCCCCCCCE
54.4329967540
503UbiquitinationKVYYDPNKSQRGAKL
EEEECCCCCCCCCEE
54.0429967540
504PhosphorylationVYYDPNKSQRGAKLC
EEECCCCCCCCCEEE
31.58-
508UbiquitinationPNKSQRGAKLCVVKT
CCCCCCCCEEEEEEC
12.1129967540
509AcetylationNKSQRGAKLCVVKTQ
CCCCCCCEEEEEECH
45.2923749302
509SumoylationNKSQRGAKLCVVKTQ
CCCCCCCEEEEEECH
45.29-
509SumoylationNKSQRGAKLCVVKTQ
CCCCCCCEEEEEECH
45.29-
509UbiquitinationNKSQRGAKLCVVKTQ
CCCCCCCEEEEEECH
45.2929967540
513UbiquitinationRGAKLCVVKTQRKAK
CCCEEEEEECHHHHH
5.6129967540
514UbiquitinationGAKLCVVKTQRKAKQ
CCEEEEEECHHHHHH
20.6729967540
514AcetylationGAKLCVVKTQRKAKQ
CCEEEEEECHHHHHH
20.6725953088
520AcetylationVKTQRKAKQAETLTQ
EECHHHHHHCCCCCC
53.7419608861
524PhosphorylationRKAKQAETLTQDYII
HHHHHCCCCCCCEEC
37.8121406692
526PhosphorylationAKQAETLTQDYIITP
HHHCCCCCCCEECCC
27.1521406692
529PhosphorylationAETLTQDYIITPHAL
CCCCCCCEECCCCHH
5.6121406692
532PhosphorylationLTQDYIITPHALPMF
CCCCEECCCCHHHCC
10.2421406692
563SumoylationLDPLKSHKPEPPVAG
CCHHHHCCCCCCCCC
59.16-
563SumoylationLDPLKSHKPEPPVAG
CCHHHHCCCCCCCCC
59.16-
563AcetylationLDPLKSHKPEPPVAG
CCHHHHCCCCCCCCC
59.1626051181
573MethylationPPVAGPGRGGRVGTH
CCCCCCCCCCCCCCC
47.7512020327
576MethylationAGPGRGGRVGTHGGT
CCCCCCCCCCCCCCC
26.9026494429
579PhosphorylationGRGGRVGTHGGTLSS
CCCCCCCCCCCCHHH
17.9423917254
583PhosphorylationRVGTHGGTLSSYIVK
CCCCCCCCHHHEEEE
28.2328555341
585PhosphorylationGTHGGTLSSYIVKNI
CCCCCCHHHEEEEEE
22.4228555341
587PhosphorylationHGGTLSSYIVKNIAL
CCCCHHHEEEEEEEC
13.3227642862
589UbiquitinationGTLSSYIVKNIALDK
CCHHHEEEEEEECCC
2.7029967540
590SumoylationTLSSYIVKNIALDKT
CHHHEEEEEEECCCC
32.83-
590SumoylationTLSSYIVKNIALDKT
CHHHEEEEEEECCCC
32.8328112733
596SumoylationVKNIALDKTDDSNPR
EEEEECCCCCCCCHH
55.49-
596SumoylationVKNIALDKTDDSNPR
EEEEECCCCCCCCHH
55.4928112733
600PhosphorylationALDKTDDSNPREAIL
ECCCCCCCCHHHHHH
52.0928555341
604UbiquitinationTDDSNPREAILRHAK
CCCCCHHHHHHHHHH
41.1232015554
610UbiquitinationREAILRHAKAAEDSP
HHHHHHHHHHHCCCC
9.2129967540
611AcetylationEAILRHAKAAEDSPY
HHHHHHHHHHCCCCC
41.8420167786
611SumoylationEAILRHAKAAEDSPY
HHHHHHHHHHCCCCC
41.84-
611SumoylationEAILRHAKAAEDSPY
HHHHHHHHHHCCCCC
41.84-
611UbiquitinationEAILRHAKAAEDSPY
HHHHHHHHHHCCCCC
41.8429967540
616PhosphorylationHAKAAEDSPYWVSPA
HHHHHCCCCCCCCCC
16.0521945579
618PhosphorylationKAAEDSPYWVSPAYS
HHHCCCCCCCCCCCC
23.5321945579
621PhosphorylationEDSPYWVSPAYSKTQ
CCCCCCCCCCCCCCC
6.9421945579
624PhosphorylationPYWVSPAYSKTQPKT
CCCCCCCCCCCCCCC
17.6821945579
625PhosphorylationYWVSPAYSKTQPKTM
CCCCCCCCCCCCCCE
31.1921945579
625UbiquitinationYWVSPAYSKTQPKTM
CCCCCCCCCCCCCCE
31.1932015554
626AcetylationWVSPAYSKTQPKTMF
CCCCCCCCCCCCCEE
38.2020167786
626UbiquitinationWVSPAYSKTQPKTMF
CCCCCCCCCCCCCEE
38.2032015554
627PhosphorylationVSPAYSKTQPKTMFA
CCCCCCCCCCCCEEE
44.1326074081
631PhosphorylationYSKTQPKTMFAQVES
CCCCCCCCEEEEECC
24.9723927012
637PhosphorylationKTMFAQVESDDEEAK
CCEEEEECCCCHHHH
36.0532645325
638PhosphorylationTMFAQVESDDEEAKN
CEEEEECCCCHHHHC
52.0519664994

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 WDR70_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR70_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 WDR70_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZCH18_HUMANZC3H18physical
22939629
PR38A_HUMANPRPF38Aphysical
27173435

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 WDR70_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-452 AND LYS-520, AND MASSSPECTROMETRY.
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 SER-638, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND MASSSPECTROMETRY.

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