DDA1_HUMAN - dbPTM
DDA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDA1_HUMAN
UniProt AC Q9BW61
Protein Name DET1- and DDB1-associated protein 1
Gene Name DDA1
Organism Homo sapiens (Human).
Sequence Length 102
Subcellular Localization
Protein Description May be involved in ubiquitination and subsequent proteasomal degradation of target proteins. Component of the DDD-E2 complexes which may provide a platform for interaction with CUL4A and WD repeat proteins..
Protein Sequence MADFLKGLPVYNKSNFSRFHADSVCKASNRRPSVYLPTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKRDQEQVELEGESSAPPRKVARTDSPDMHEDT
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
2Acetylation------MADFLKGLP
------CCHHHCCCC
19.0922814378
6Ubiquitination--MADFLKGLPVYNK
--CCHHHCCCCCCCC
59.40-
11PhosphorylationFLKGLPVYNKSNFSR
HHCCCCCCCCCCCCH
18.2228060719
13UbiquitinationKGLPVYNKSNFSRFH
CCCCCCCCCCCCHHC
29.14-
13AcetylationKGLPVYNKSNFSRFH
CCCCCCCCCCCCHHC
29.1426051181
23PhosphorylationFSRFHADSVCKASNR
CCHHCHHHHHHHCCC
30.1421712546
25S-nitrosylationRFHADSVCKASNRRP
HHCHHHHHHHCCCCC
3.3619483679
25S-nitrosocysteineRFHADSVCKASNRRP
HHCHHHHHHHCCCCC
3.36-
26UbiquitinationFHADSVCKASNRRPS
HCHHHHHHHCCCCCC
53.33-
28PhosphorylationADSVCKASNRRPSVY
HHHHHHHCCCCCCEE
19.1626074081
33PhosphorylationKASNRRPSVYLPTRE
HHCCCCCCEECCCCC
22.9123401153
35PhosphorylationSNRRPSVYLPTREYP
CCCCCCEECCCCCCC
15.9929396449
38PhosphorylationRPSVYLPTREYPSEQ
CCCEECCCCCCCCCC
33.2723882029
43PhosphorylationLPTREYPSEQIIVTE
CCCCCCCCCCEEEEE
41.0323882029
49PhosphorylationPSEQIIVTEKTNILL
CCCCEEEEEHHHHHH
22.73-
52PhosphorylationQIIVTEKTNILLRYL
CEEEEEHHHHHHHHH
22.66-
65UbiquitinationYLHQQWDKKNAAKKR
HHHHHHHHHHHHHHC
44.9919608861
65AcetylationYLHQQWDKKNAAKKR
HHHHHHHHHHHHHHC
44.9923749302
66UbiquitinationLHQQWDKKNAAKKRD
HHHHHHHHHHHHHCH
49.71-
71UbiquitinationDKKNAAKKRDQEQVE
HHHHHHHHCHHHHHH
57.38-
83PhosphorylationQVELEGESSAPPRKV
HHHHCCCCCCCCCCC
42.5326074081
84PhosphorylationVELEGESSAPPRKVA
HHHCCCCCCCCCCCC
40.2626074081
93PhosphorylationPPRKVARTDSPDMHE
CCCCCCCCCCCCCCC
30.9625159151
95PhosphorylationRKVARTDSPDMHEDT
CCCCCCCCCCCCCCC
23.3723927012
102PhosphorylationSPDMHEDT-------
CCCCCCCC-------
37.2123927012

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
33SPhosphorylationKinaseAURKBQ96GD4
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDA1_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 DDA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCAF1_HUMANVPRBPphysical
20562859
DCA17_HUMANDCAF17physical
20562859
AMRA1_HUMANAMBRA1physical
20562859
DDB2_HUMANDDB2physical
20562859
DDB1_HUMANDDB1physical
20562859
DCA11_HUMANDCAF11physical
20562859
ANFY1_HUMANANKFY1physical
20562859
LKHA4_HUMANLTA4Hphysical
20562859
ASNS_HUMANASNSphysical
20562859
FKBP4_HUMANFKBP4physical
20562859
SYLC_HUMANLARSphysical
20562859
PGK1_HUMANPGK1physical
20562859
SYTC_HUMANTARSphysical
20562859
ECHM_HUMANECHS1physical
20562859
PA2G4_HUMANPA2G4physical
20562859
ECHA_HUMANHADHAphysical
20562859
GLYM_HUMANSHMT2physical
20562859
ETFA_HUMANETFAphysical
20562859
COPA_HUMANCOPAphysical
20562859
PRKDC_HUMANPRKDCphysical
20562859
CBR1_HUMANCBR1physical
20562859
SYFB_HUMANFARSBphysical
20562859
SPEE_HUMANSRMphysical
20562859
AMPL_HUMANLAP3physical
20562859
DCAF5_HUMANDCAF5physical
20562859
WDTC1_HUMANWDTC1physical
20562859
SEPT9_HUMANSEPT9physical
20562859
SIAS_HUMANNANSphysical
20562859
ESTD_HUMANESDphysical
20562859
CAND1_HUMANCAND1physical
20562859
SYWC_HUMANWARSphysical
20562859
AAPK1_HUMANPRKAA1physical
20562859
IDH3A_HUMANIDH3Aphysical
20562859
MCM2_HUMANMCM2physical
20562859
AL7A1_HUMANALDH7A1physical
20562859
PUR8_HUMANADSLphysical
20562859
AL9A1_HUMANALDH9A1physical
20562859
NAMPT_HUMANNAMPTphysical
20562859
GUAA_HUMANGMPSphysical
20562859
IF5_HUMANEIF5physical
20562859
COPB2_HUMANCOPB2physical
20562859
ECHB_HUMANHADHBphysical
20562859
UB2E3_HUMANUBE2E3physical
17452440
DDB1_HUMANDDB1physical
17452440
CUL4A_HUMANCUL4Aphysical
17452440
CSN3_HUMANCOPS3physical
17452440
DCAF1_HUMANVPRBPphysical
17609381
DDB1_HUMANDDB1physical
17609381
RBX1_HUMANRBX1physical
19295130
CUL4A_HUMANCUL4Aphysical
19295130
CUL4B_HUMANCUL4Bphysical
19295130
RFWD2_HUMANRFWD2physical
19295130
CSN2_HUMANCOPS2physical
19295130
CSN3_HUMANCOPS3physical
19295130
CSN4_HUMANCOPS4physical
19295130
CSN5_HUMANCOPS5physical
19295130
CSN6_HUMANCOPS6physical
19295130
CSN7A_HUMANCOPS7Aphysical
19295130
CSN7B_HUMANCOPS7Bphysical
19295130
CSN8_HUMANCOPS8physical
19295130
DDB1_HUMANDDB1physical
19295130
DCAF1_HUMANVPRBPphysical
19295130
PWP1_HUMANPWP1physical
19295130
DCAF5_HUMANDCAF5physical
19295130
DCA12_HUMANDCAF12physical
19295130
ERCC8_HUMANERCC8physical
19295130
WDTC1_HUMANWDTC1physical
19295130
DCAF6_HUMANDCAF6physical
19295130
AMRA1_HUMANAMBRA1physical
19295130
DCA11_HUMANDCAF11physical
19295130
DCA10_HUMANDCAF10physical
19295130
DTL_HUMANDTLphysical
19295130
DCAF8_HUMANDCAF8physical
19295130
DET1_HUMANDET1physical
19295130
DCA15_HUMANDCAF15physical
19295130
DCA16_HUMANDCAF16physical
19295130
DCA17_HUMANDCAF17physical
19295130
TOIP2_HUMANTOR1AIP2physical
19295130
IFG15_HUMANTOR1AIP2physical
19295130
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
CUL4B_HUMANCUL4Bphysical
16949367
CKLF5_HUMANCMTM5physical
25416956
DET1_HUMANDET1physical
17452440
DDB1_HUMANDDB1physical
26344197
DCAF1_HUMANVPRBPphysical
26344197

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 DDA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-33 AND SER-95, AND MASSSPECTROMETRY.

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