DCAF8_HUMAN - dbPTM
DCAF8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCAF8_HUMAN
UniProt AC Q5TAQ9
Protein Name DDB1- and CUL4-associated factor 8
Gene Name DCAF8
Organism Homo sapiens (Human).
Sequence Length 597
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 MSSKGSSTDGRTDLANGSLSSSPEEMSGAEEGRETSSGIEVEASDLSLSLTGDDGGPNRTSTESRGTDTESSGEDKDSDSMEDTGHYSINDENRVHDRSEEEEEEEEEEEEEQPRRRVQRKRANRDQDSSDDERALEDWVSSETSALPRPRWQALPALRERELGSSARFVYEACGARVFVQRFRLQHGLEGHTGCVNTLHFNQRGTWLASGSDDLKVVVWDWVRRQPVLDFESGHKSNVFQAKFLPNSGDSTLAMCARDGQVRVAELSATQCCKNTKRVAQHKGASHKLALEPDSPCTFLSAGEDAVVFTIDLRQDRPASKLVVTKEKEKKVGLYTIYVNPANTHQFAVGGRDQFVRIYDQRKIDENENNGVLKKFCPHHLVNSESKANITCLVYSHDGTELLASYNDEDIYLFNSSHSDGAQYVKRYKGHRNNATVKGVNFYGPKSEFVVSGSDCGHIFLWEKSSCQIIQFMEGDKGGVVNCLEPHPHLPVLATSGLDHDVKIWAPTAEASTELTGLKDVIKKNKRERDEDSLHQTDLFDSHMLWFLMHHLRQRRHHRRWREPGVGATDADSDESPSSSDTSDEEEGPDRVQCMPS
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
2Phosphorylation------MSSKGSSTD
------CCCCCCCCC		40.5321406692
3Phosphorylation-----MSSKGSSTDG
-----CCCCCCCCCC		39.4721406692
6Phosphorylation--MSSKGSSTDGRTD
--CCCCCCCCCCCCC		33.5321406692
7Phosphorylation-MSSKGSSTDGRTDL
-CCCCCCCCCCCCCC		38.9021406692
8PhosphorylationMSSKGSSTDGRTDLA
CCCCCCCCCCCCCCC		44.1421406692
18PhosphorylationRTDLANGSLSSSPEE
CCCCCCCCCCCCHHH		25.5326425664
20PhosphorylationDLANGSLSSSPEEMS
CCCCCCCCCCHHHHC		30.3927251275
21PhosphorylationLANGSLSSSPEEMSG
CCCCCCCCCHHHHCC		56.0326471730
22PhosphorylationANGSLSSSPEEMSGA
CCCCCCCCHHHHCCC		32.7126055452
27PhosphorylationSSSPEEMSGAEEGRE
CCCHHHHCCCCCCCC		37.8226657352
35PhosphorylationGAEEGRETSSGIEVE
CCCCCCCCCCCEEEE		27.1726471730
36PhosphorylationAEEGRETSSGIEVEA
CCCCCCCCCCEEEEE		23.0926471730
37PhosphorylationEEGRETSSGIEVEAS
CCCCCCCCCEEEEEE		51.7326471730
47PhosphorylationEVEASDLSLSLTGDD
EEEEECEEEEEECCC		22.3926657352
49PhosphorylationEASDLSLSLTGDDGG
EEECEEEEEECCCCC		22.1024275569
51PhosphorylationSDLSLSLTGDDGGPN
ECEEEEEECCCCCCC		34.8824275569
51 (in isoform 1)Ubiquitination-34.8821890473
60PhosphorylationDDGGPNRTSTESRGT
CCCCCCCCCCCCCCC		46.7929449344
61PhosphorylationDGGPNRTSTESRGTD
CCCCCCCCCCCCCCC		27.2629449344
62PhosphorylationGGPNRTSTESRGTDT
CCCCCCCCCCCCCCC		37.0529449344
64PhosphorylationPNRTSTESRGTDTES
CCCCCCCCCCCCCCC		35.7829449344
67PhosphorylationTSTESRGTDTESSGE
CCCCCCCCCCCCCCC		38.3423663014
69PhosphorylationTESRGTDTESSGEDK
CCCCCCCCCCCCCCC		37.2923663014
71PhosphorylationSRGTDTESSGEDKDS
CCCCCCCCCCCCCCC		45.8223663014
72PhosphorylationRGTDTESSGEDKDSD
CCCCCCCCCCCCCCC		39.7123663014
78PhosphorylationSSGEDKDSDSMEDTG
CCCCCCCCCCCCCCC		37.0123663014
80PhosphorylationGEDKDSDSMEDTGHY
CCCCCCCCCCCCCCC		28.2030576142
84PhosphorylationDSDSMEDTGHYSIND
CCCCCCCCCCCCCCC		16.7427251275
87PhosphorylationSMEDTGHYSINDENR
CCCCCCCCCCCCCCC		16.7627251275
88PhosphorylationMEDTGHYSINDENRV
CCCCCCCCCCCCCCC		14.8320873877
98 (in isoform 1)Ubiquitination-30.9621890473
99PhosphorylationENRVHDRSEEEEEEE
CCCCCCCCHHHHHHH		56.2522167270
129PhosphorylationRANRDQDSSDDERAL
HHHCCCCCCHHHHHH		29.9926846344
130PhosphorylationANRDQDSSDDERALE
HHCCCCCCHHHHHHH		58.3226846344
141PhosphorylationRALEDWVSSETSALP
HHHHHHHHCCCCCCC		20.4330108239
142PhosphorylationALEDWVSSETSALPR
HHHHHHHCCCCCCCC		34.9628450419
144PhosphorylationEDWVSSETSALPRPR
HHHHHCCCCCCCCCH		22.6520071362
145PhosphorylationDWVSSETSALPRPRW
HHHHCCCCCCCCCHH		24.6122673903
171PhosphorylationGSSARFVYEACGARV
CCCHHHHHHHHCCEE		8.63-
204MethylationNTLHFNQRGTWLASG
EEEEECCCCEEECCC		45.6823455924
236UbiquitinationLDFESGHKSNVFQAK
ECCCCCCCCCEEEEE		47.4521890473
243UbiquitinationKSNVFQAKFLPNSGD
CCCEEEEEECCCCCC		36.33-
251PhosphorylationFLPNSGDSTLAMCAR
ECCCCCCCEEEEECC		28.9228857561
274UbiquitinationLSATQCCKNTKRVAQ
ECHHHHCCCCHHHHC		75.24-
274AcetylationLSATQCCKNTKRVAQ
ECHHHHCCCCHHHHC		75.2426051181
283UbiquitinationTKRVAQHKGASHKLA
CHHHHCCCCCCCEEE		44.05-
321UbiquitinationRQDRPASKLVVTKEK
CCCCCCCEEEEEECC		47.62-
326UbiquitinationASKLVVTKEKEKKVG
CCEEEEEECCCCCEE		56.00-
363UbiquitinationVRIYDQRKIDENENN
EEEEECCCCCCCCCC		49.21-
374UbiquitinationNENNGVLKKFCPHHL
CCCCCHHHHHCCHHH		41.2021906983
375UbiquitinationENNGVLKKFCPHHLV
CCCCHHHHHCCHHHC		48.30-
390 (in isoform 1)Ubiquitination-3.2521890473
438UbiquitinationHRNNATVKGVNFYGP
CCCCCEEEEEEEECC		53.4321890473
477UbiquitinationIQFMEGDKGGVVNCL
EEEEECCCCCEEECC		69.31-
503UbiquitinationSGLDHDVKIWAPTAE
CCCCCCEEEECCCCH		38.29-
519UbiquitinationSTELTGLKDVIKKNK
HHHHHCHHHHHHHCH		51.82-
528 (in isoform 1)Ubiquitination-67.1221890473
569PhosphorylationREPGVGATDADSDES
CCCCCCCCCCCCCCC		26.2820873877
573PhosphorylationVGATDADSDESPSSS
CCCCCCCCCCCCCCC		45.0220873877
576PhosphorylationTDADSDESPSSSDTS
CCCCCCCCCCCCCCC		34.7620873877
578PhosphorylationADSDESPSSSDTSDE
CCCCCCCCCCCCCCC		52.3220873877
579PhosphorylationDSDESPSSSDTSDEE
CCCCCCCCCCCCCCC		35.3020873877
580PhosphorylationSDESPSSSDTSDEEE
CCCCCCCCCCCCCCC		49.6020873877
582PhosphorylationESPSSSDTSDEEEGP
CCCCCCCCCCCCCCC		39.7720873877
583PhosphorylationSPSSSDTSDEEEGPD
CCCCCCCCCCCCCCC		48.2720873877
592 (in isoform 1)Ubiquitination-7.1921890473
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCAF8_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 DCAF8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GTPB3_HUMANGTPBP3physical
16189514
DDB1_HUMANDDB1physical
16964240
IMA5_HUMANKPNA1physical
22500989
IMB1_HUMANKPNB1physical
22500989
XPO1_HUMANXPO1physical
22500989
CSN2_HUMANCOPS2physical
19295130
CSN3_HUMANCOPS3physical
19295130
CUL4A_HUMANCUL4Aphysical
19295130
DDB1_HUMANDDB1physical
19295130
DDA1_HUMANDDA1physical
19295130
MDFI_HUMANMDFIphysical
19060904
ANM1_HUMANPRMT1physical
23455924
SUV91_HUMANSUV39H1physical
23455924
ANM8_HUMANPRMT8physical
23455924
ACTN1_HUMANACTN1physical
22863883
CSN4_HUMANCOPS4physical
22863883
CSN7A_HUMANCOPS7Aphysical
22863883
DCA11_HUMANDCAF11physical
22863883
E41L2_HUMANEPB41L2physical
22863883
ANM5_HUMANPRMT5physical
22863883
STAM2_HUMANSTAM2physical
22863883
MEP50_HUMANWDR77physical
22863883
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
CUL4B_HUMANCUL4Bphysical
16949367
THAP1_HUMANTHAP1physical
25416956
CUL4A_HUMANCUL4Aphysical
28514442
PDE7A_HUMANPDE7Aphysical
28514442
AMPD2_HUMANAMPD2physical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
FARP1_HUMANFARP1physical
28514442
DDB1_HUMANDDB1physical
28514442
ARHGQ_HUMANARHGEF26physical
28514442
ACD11_HUMANACAD11physical
28514442
REXO5_HUMANLOC81691physical
28514442
TCPB_HUMANCCT2physical
28514442
DC8L1_HUMANDCAF8L1physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPD_HUMANCCT4physical
28514442
TCPG_HUMANCCT3physical
28514442
ZN460_HUMANZNF460physical
28514442
GSTK1_HUMANGSTK1physical
28514442
TCPE_HUMANCCT5physical
28514442
TCPH_HUMANCCT7physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610100Giant axonal neuropathy 2, autosomal dominant (GAN2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCAF8_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-99; SER-129 AND SER-130,AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-129 AND SER-130,AND MASS SPECTROMETRY.
"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-99; SER-129 AND SER-130,AND MASS SPECTROMETRY.

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