WDTC1_HUMAN - dbPTM
WDTC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDTC1_HUMAN
UniProt AC Q8N5D0
Protein Name WD and tetratricopeptide repeats protein 1
Gene Name WDTC1
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization
Protein Description May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex..
Protein Sequence MAKVNITRDLIRRQIKERGALSFERRYHVTDPFIRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMHTGHTANIFSVKFLPHAGDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPMWPNTFWSAAEDGLIRQYDLRENSKHSEVLIDLTEYCGQLVEAKCLTVNPQDNNCLAVGASGPFVRLYDIRMIHNHRKSMKQSPSAGVHTFCDRQKPLPDGAAQYYVAGHLPVKLPDYNNRLRVLVATYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTFLLPRKCHSSGEVQNGKMSTNGVSNGVSNGLHLHSNGFRLPESRGHVSPQVELPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRKWDGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFKGKFPEQAHSSACDALGRDITAALFSKNDGEEKKGPGGGAPVRLRSTSRKDSISEDEMVLRERSYDYQFRYCGHCNTTTDIKEANFFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLTGRVVEDMEGASQANQRRMNADPLEVMLLNMGYRITGLSSGGAGASDDEDSSEGQVQCRPS
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
27PhosphorylationALSFERRYHVTDPFI
CCCHHHHHCCCCHHH
13.5822461510
30PhosphorylationFERRYHVTDPFIRRL
HHHHHCCCCHHHHHH
25.3322461510
80UbiquitinationVWDPLHHKKLLSMHT
EECCCCCHHHHHHCC
34.0829967540
122PhosphorylationKVHVHDLTVKETIHM
CEEEEECCHHHHHHH
35.2725599653
169 (in isoform 1)Ubiquitination-63.8322053931
169UbiquitinationYDLRENSKHSEVLID
EECCCCCCCCEEEEH
63.8322053931
212PhosphorylationSGPFVRLYDIRMIHN
CCCEEEEEEHHHHHH
9.96-
223PhosphorylationMIHNHRKSMKQSPSA
HHHHCHHHHCCCCCC
31.0429214152
227PhosphorylationHRKSMKQSPSAGVHT
CHHHHCCCCCCCCCE
18.4628450419
229PhosphorylationKSMKQSPSAGVHTFC
HHHCCCCCCCCCEEC
42.7928450419
234PhosphorylationSPSAGVHTFCDRQKP
CCCCCCCEECCCCCC
24.4528450419
352 (in isoform 4)Phosphorylation-11.2724719451
352PhosphorylationLPESRGHVSPQVELP
CCCCCCCCCCCCCCC
11.2732142685
353PhosphorylationPESRGHVSPQVELPP
CCCCCCCCCCCCCCH
12.1630266825
361PhosphorylationPQVELPPYLERVKQQ
CCCCCCHHHHHHHHH
21.1824117733
399PhosphorylationAPHNAMLYGNRAAAY
CCCCCCCCCHHHHHH
10.16-
406PhosphorylationYGNRAAAYMKRKWDG
CCHHHHHHHHHHCCC
9.84-
409UbiquitinationRAAAYMKRKWDGDHY
HHHHHHHHHCCCCHH
28.8629967540
410UbiquitinationAAAYMKRKWDGDHYD
HHHHHHHHCCCCHHH
44.0829967540
416PhosphorylationRKWDGDHYDALRDCL
HHCCCCHHHHHHHHH
13.98-
423UbiquitinationYDALRDCLKAISLNP
HHHHHHHHHHHCCCC
5.0032015554
424AcetylationDALRDCLKAISLNPC
HHHHHHHHHHCCCCH
50.437306937
424UbiquitinationDALRDCLKAISLNPC
HHHHHHHHHHCCCCH
50.4332015554
426 (in isoform 4)Phosphorylation-4.6224719451
427PhosphorylationRDCLKAISLNPCHLK
HHHHHHHCCCCHHHH
27.2724719451
459UbiquitinationALECLDDFKGKFPEQ
HHHHHHHHCCCCCHH
12.8729967540
460UbiquitinationLECLDDFKGKFPEQA
HHHHHHHCCCCCHHH
69.0929967540
461UbiquitinationECLDDFKGKFPEQAH
HHHHHHCCCCCHHHH
36.5132015554
462UbiquitinationCLDDFKGKFPEQAHS
HHHHHCCCCCHHHHH
59.3332015554
485UbiquitinationDITAALFSKNDGEEK
HHHHHHHCCCCCCCC
31.2532015554
485PhosphorylationDITAALFSKNDGEEK
HHHHHHHCCCCCCCC
31.2524719451
486UbiquitinationITAALFSKNDGEEKK
HHHHHHCCCCCCCCC
52.2932015554
492UbiquitinationSKNDGEEKKGPGGGA
CCCCCCCCCCCCCCC
59.7427667366
493UbiquitinationKNDGEEKKGPGGGAP
CCCCCCCCCCCCCCC
73.8727667366
505PhosphorylationGAPVRLRSTSRKDSI
CCCCCCCCCCCCCCC
35.0129523821
506PhosphorylationAPVRLRSTSRKDSIS
CCCCCCCCCCCCCCC
26.5629523821
507PhosphorylationPVRLRSTSRKDSISE
CCCCCCCCCCCCCCH
38.2825921289
508UbiquitinationVRLRSTSRKDSISED
CCCCCCCCCCCCCHH
47.0629967540
509UbiquitinationRLRSTSRKDSISEDE
CCCCCCCCCCCCHHH
56.4429967540
510 (in isoform 4)Phosphorylation-50.5224719451
511PhosphorylationRSTSRKDSISEDEMV
CCCCCCCCCCHHHHH
30.9229255136
512PhosphorylationSTSRKDSISEDEMVL
CCCCCCCCCHHHHHH
8.1933259812
513PhosphorylationTSRKDSISEDEMVLR
CCCCCCCCHHHHHHH
42.8430266825
624SulfoxidationTGRVVEDMEGASQAN
CCCCHHCCCHHHHHH
3.0321406390
649PhosphorylationVMLLNMGYRITGLSS
HHHHHCCCEEEECCC
6.5128450419
652PhosphorylationLNMGYRITGLSSGGA
HHCCCEEEECCCCCC
24.0728857561
655PhosphorylationGYRITGLSSGGAGAS
CCEEEECCCCCCCCC
28.4328857561
656PhosphorylationYRITGLSSGGAGASD
CEEEECCCCCCCCCC
46.4128857561
661 (in isoform 4)Phosphorylation-14.8424719451
662PhosphorylationSSGGAGASDDEDSSE
CCCCCCCCCCCCCCC
44.6828450419
667PhosphorylationGASDDEDSSEGQVQC
CCCCCCCCCCCCCEE
28.3925262027
668PhosphorylationASDDEDSSEGQVQCR
CCCCCCCCCCCCEEC
59.0525262027

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 WDTC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDTC1_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 WDTC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
STXB4_HUMANSTXBP4physical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
MIPEP_HUMANMIPEPphysical
28514442
EKI1_HUMANETNK1physical
28514442
DDB1_HUMANDDB1physical
28514442
PPR21_HUMANPPP1R21physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPG_HUMANCCT3physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPD_HUMANCCT4physical
28514442
PHLP_HUMANPDCLphysical
28514442
TCPE_HUMANCCT5physical
28514442
TCPW_HUMANCCT6Bphysical
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 WDTC1_HUMAN

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Related Literatures of Post-Translational Modification
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-511, AND MASSSPECTROMETRY.

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