DCAF8_MOUSE - dbPTM
DCAF8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCAF8_MOUSE
UniProt AC Q8N7N5
Protein Name DDB1- and CUL4-associated factor 8
Gene Name Dcaf8
Organism Mus musculus (Mouse).
Sequence Length 591
Subcellular Localization Nucleus . Cytoplasm . It shuttles between the nucleus and the cytoplasm. Nuclear import is mediated by KPNA1 and KPNB1 under the regulation of nuclear GTPase RAN. Nuclear export to the cytoplasm is XPO1 dependent.
Protein Description May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex..
Protein Sequence MSNKRPNTTDGRTDLANGSLSSSPEEMSGAEEGRETSSGIEVEASDLSLSLTGDDGGPNRTSTESRGTDTESSGEEKDSDSMEDTGHYSINDESRGHGHSDEEDEEQPRHRGQRKRASRDQDSSDDERALEDWVSSETTALPRPRWQALPALRERELGSSARFVYEACGARVFVQRFRLQHGLEGHTGCVNTLHFNQRGTWLASGSDDLKVVVWDWVRRQPVLDFESGHKSNVFQAKFLPNSGDSTLAMCARDGQVRVAELSATQCCKNTKRVAQHKGASHKLALEPDSPCTFLSAGEDAVVFTIDLRQDRPASKLVVTKEKEKKVGLYTIYVNPANTHQFAVGGRDQYVRIYDQRKIDENENNGVLKKFCPHHLVNSESKANITCLVYSHDGTELLASYNDEDIYLFNSSHSDGAQYIKRYKGHRNNATVKGVNFYGPKSEFVVSGSDCGHIFLWEKSSCQIIQFMEGDKGGVVNCLEPHPHLPVLATSGLDHDVKIWAPTAEASTELTGLKEVIKKNKRERDEDSLHHTDLFDSHMLWFLMHHLRQRRHHRRWREPGVGATDADSDESPSSSDTSDEEEGPDRVQCMPS
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
13PhosphorylationPNTTDGRTDLANGSL
CCCCCCCCCCCCCCC
40.6825293948
19PhosphorylationRTDLANGSLSSSPEE
CCCCCCCCCCCCHHH
25.5319060867
21PhosphorylationDLANGSLSSSPEEMS
CCCCCCCCCCHHHHC
30.3919060867
22PhosphorylationLANGSLSSSPEEMSG
CCCCCCCCCHHHHCC
56.0325521595
23PhosphorylationANGSLSSSPEEMSGA
CCCCCCCCHHHHCCC
32.7125521595
28PhosphorylationSSSPEEMSGAEEGRE
CCCHHHHCCCCCCCC
37.8225521595
61PhosphorylationDDGGPNRTSTESRGT
CCCCCCCCCCCCCCC
46.7925293948
62PhosphorylationDGGPNRTSTESRGTD
CCCCCCCCCCCCCCC
27.2625293948
63PhosphorylationGGPNRTSTESRGTDT
CCCCCCCCCCCCCCC
37.0529514104
65PhosphorylationPNRTSTESRGTDTES
CCCCCCCCCCCCCCC
35.7829472430
68PhosphorylationTSTESRGTDTESSGE
CCCCCCCCCCCCCCC
38.3425521595
70PhosphorylationTESRGTDTESSGEEK
CCCCCCCCCCCCCCC
37.2929472430
72PhosphorylationSRGTDTESSGEEKDS
CCCCCCCCCCCCCCC
45.8225521595
73PhosphorylationRGTDTESSGEEKDSD
CCCCCCCCCCCCCCC
43.9527087446
79PhosphorylationSSGEEKDSDSMEDTG
CCCCCCCCCCCCCCC
42.5323737553
81PhosphorylationGEEKDSDSMEDTGHY
CCCCCCCCCCCCCCC
28.2023737553
85PhosphorylationDSDSMEDTGHYSIND
CCCCCCCCCCCCCCC
16.7423737553
88PhosphorylationSMEDTGHYSINDESR
CCCCCCCCCCCCCCC
16.7623737553
100PhosphorylationESRGHGHSDEEDEEQ
CCCCCCCCCCCCCCC
51.8427087446
118PhosphorylationRGQRKRASRDQDSSD
HHHHHHHCCCCCCCH
40.1823684622
123PhosphorylationRASRDQDSSDDERAL
HHCCCCCCCHHHHHH
29.9923684622
124PhosphorylationASRDQDSSDDERALE
HCCCCCCCHHHHHHH
58.3226824392
135PhosphorylationRALEDWVSSETTALP
HHHHHHHHCCCCCCC
20.4323984901
138PhosphorylationEDWVSSETTALPRPR
HHHHHCCCCCCCCCH
21.2225367039
198MethylationNTLHFNQRGTWLASG
EEEEECCCCEEECCC
45.68-
230UbiquitinationLDFESGHKSNVFQAK
ECCCCCCCCCEEEEE
47.4522790023
237UbiquitinationKSNVFQAKFLPNSGD
CCCEEEEEECCCCCC
36.3322790023
268UbiquitinationLSATQCCKNTKRVAQ
ECHHHHCCCCHHHHC
75.2422790023
315UbiquitinationRQDRPASKLVVTKEK
CCCCCCCEEEEEECC
47.6222790023
357UbiquitinationVRIYDQRKIDENENN
EEEEECCCCCCCCCC
49.2122790023
369UbiquitinationENNGVLKKFCPHHLV
CCCCHHHHHCCHHHC
48.3022790023
385 (in isoform 2)Phosphorylation-10.2930635358
387 (in isoform 2)Phosphorylation-2.8030635358
389 (in isoform 2)Phosphorylation-6.3230635358
390 (in isoform 2)Phosphorylation-13.9730635358
393 (in isoform 2)Phosphorylation-18.7030635358
398 (in isoform 2)Phosphorylation-23.6930635358
432UbiquitinationHRNNATVKGVNFYGP
CCCCCEEEEEEEECC
53.4322790023
513UbiquitinationSTELTGLKEVIKKNK
HHHHHCHHHHHHHCC
51.8122790023
567PhosphorylationVGATDADSDESPSSS
CCCCCCCCCCCCCCC
45.0230165576
570PhosphorylationTDADSDESPSSSDTS
CCCCCCCCCCCCCCC
34.7630165576
572PhosphorylationADSDESPSSSDTSDE
CCCCCCCCCCCCCCC
52.3230165576
573PhosphorylationDSDESPSSSDTSDEE
CCCCCCCCCCCCCCC
35.3030165576
574PhosphorylationSDESPSSSDTSDEEE
CCCCCCCCCCCCCCC
49.6030165576
576PhosphorylationESPSSSDTSDEEEGP
CCCCCCCCCCCCCCC
39.7730165576
577PhosphorylationSPSSSDTSDEEEGPD
CCCCCCCCCCCCCCC
48.2730165576

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 DCAF8_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCAF8_MOUSE !!

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 DCAF8_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DCAF8_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCAF8_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.

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