CCD93_HUMAN - dbPTM
CCD93_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCD93_HUMAN
UniProt AC Q567U6
Protein Name Coiled-coil domain-containing protein 93
Gene Name CCDC93
Organism Homo sapiens (Human).
Sequence Length 631
Subcellular Localization Early endosome .
Protein Description Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with WASHC2C. [PubMed: 25355947]
Protein Sequence MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
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
15UbiquitinationEGQGLPEVETREDEE
CCCCCCCCCCCCCHH
9.5722817900
27UbiquitinationDEEQNVKLTEILELL
CHHHCCHHHHHHHHH
4.5322817900
29UbiquitinationEQNVKLTEILELLVA
HHCCHHHHHHHHHHH
56.8922817900
31UbiquitinationNVKLTEILELLVAAG
CCHHHHHHHHHHHCC
2.8622817900
35UbiquitinationTEILELLVAAGYFRA
HHHHHHHHHCCHHHH
5.5424816145
45UbiquitinationGYFRARIKGLSPFDK
CHHHHHHCCCCHHHH
48.52-
52UbiquitinationKGLSPFDKVVGGMTW
CCCCHHHHHHCCEEE
38.9222817900
64UbiquitinationMTWCITTCNFDVDVD
EEEEEHHCCCCCCHH
3.4122817900
66UbiquitinationWCITTCNFDVDVDLL
EEEHHCCCCCCHHHH
12.0122817900
68UbiquitinationITTCNFDVDVDLLFQ
EHHCCCCCCHHHHEE
7.2722817900
89UbiquitinationQKIALSEKIVSVLPR
HHHHCCHHHHHHCCC
45.06-
92PhosphorylationALSEKIVSVLPRMKC
HCCHHHHHHCCCCCC
22.7832142685
131UbiquitinationVKRAIETKEEMGDYI
HHHHHHCHHHHHHHH
38.6024816145
137PhosphorylationTKEEMGDYIRSYSVS
CHHHHHHHHHHCCHH
7.7824670416
142PhosphorylationGDYIRSYSVSQFQKT
HHHHHHCCHHHHHHH
19.2828857561
148UbiquitinationYSVSQFQKTYSLPED
CCHHHHHHHCCCCCC
51.2021906983
149PhosphorylationSVSQFQKTYSLPEDD
CHHHHHHHCCCCCCC
13.9430624053
150PhosphorylationVSQFQKTYSLPEDDD
HHHHHHHCCCCCCCH
18.4227642862
151PhosphorylationSQFQKTYSLPEDDDF
HHHHHHCCCCCCCHH
42.5529507054
160UbiquitinationPEDDDFIKRKEKAIK
CCCCHHHHHHHHHHH
58.3621906983
162UbiquitinationDDDFIKRKEKAIKTV
CCHHHHHHHHHHHHH
59.5722817900
164UbiquitinationDFIKRKEKAIKTVVD
HHHHHHHHHHHHHHC
59.4522817900
173PhosphorylationIKTVVDLSEVYKPRR
HHHHHCHHHHHCCCH
22.1324719451
176PhosphorylationVVDLSEVYKPRRKYK
HHCHHHHHCCCHHHH
15.9524719451
177UbiquitinationVDLSEVYKPRRKYKR
HCHHHHHCCCHHHHC
36.9029967540
187UbiquitinationRKYKRHQGAEELLDE
HHHHCCCCHHHHCCH
28.9124816145
204UbiquitinationRIHATLLEYGRRYGF
HHHHHHHHHHHHHCC
49.4022817900
209PhosphorylationLLEYGRRYGFSRQSK
HHHHHHHHCCCCHHH
22.59-
216UbiquitinationYGFSRQSKMEKAEDK
HCCCCHHHHCHHCCH
42.6222817900
218UbiquitinationFSRQSKMEKAEDKKT
CCCHHHHCHHCCHHC
53.5022817900
220UbiquitinationRQSKMEKAEDKKTAL
CHHHHCHHCCHHCCC
19.5322817900
224UbiquitinationMEKAEDKKTALPAGL
HCHHCCHHCCCCCCC
51.8829967540
236UbiquitinationAGLSATEKADAHEED
CCCCHHHCCCCCCHH
47.4132015554
240UbiquitinationATEKADAHEEDELRA
HHHCCCCCCHHHHHH
39.2522817900
244UbiquitinationADAHEEDELRAAEEQ
CCCCCHHHHHHHHHH
43.3622817900
255PhosphorylationAEEQRIQSLMTKMTA
HHHHHHHHHHHHHHH
20.1028857561
259UbiquitinationRIQSLMTKMTAMANE
HHHHHHHHHHHHCCH
21.9329967540
261PhosphorylationQSLMTKMTAMANEES
HHHHHHHHHHCCHHH
18.16-
264UbiquitinationMTKMTAMANEESRLT
HHHHHHHCCHHHHCC
20.1622817900
268PhosphorylationTAMANEESRLTASSV
HHHCCHHHHCCHHHH
26.81-
271PhosphorylationANEESRLTASSVGQI
CCHHHHCCHHHHHHH
24.3125072903
273PhosphorylationEESRLTASSVGQIVG
HHHHCCHHHHHHHHH
21.9626657352
274PhosphorylationESRLTASSVGQIVGL
HHHCCHHHHHHHHHH
28.0128857561
277UbiquitinationLTASSVGQIVGLCSA
CCHHHHHHHHHHCHH
25.6622817900
281UbiquitinationSVGQIVGLCSAEIKQ
HHHHHHHHCHHHHHH
1.1222817900
287UbiquitinationGLCSAEIKQIVSEYA
HHCHHHHHHHHHHHH
26.02-
289UbiquitinationCSAEIKQIVSEYAEK
CHHHHHHHHHHHHHH
2.9024816145
296UbiquitinationIVSEYAEKQSELSAE
HHHHHHHHHHHCCCC
51.4529967540
298PhosphorylationSEYAEKQSELSAEES
HHHHHHHHHCCCCCC
52.1223927012
301PhosphorylationAEKQSELSAEESPEK
HHHHHHCCCCCCHHH
29.5929255136
301UbiquitinationAEKQSELSAEESPEK
HHHHHHCCCCCCHHH
29.5922817900
305PhosphorylationSELSAEESPEKLGTS
HHCCCCCCHHHHCCC
29.8429255136
308UbiquitinationSAEESPEKLGTSQLH
CCCCCHHHHCCCHHH
56.4529967540
311PhosphorylationESPEKLGTSQLHRRK
CCHHHHCCCHHHHHH
24.6023403867
312PhosphorylationSPEKLGTSQLHRRKV
CHHHHCCCHHHHHHH
29.0123403867
318UbiquitinationTSQLHRRKVISLNKQ
CCHHHHHHHHHHHHH
43.8329967540
321PhosphorylationLHRRKVISLNKQIAQ
HHHHHHHHHHHHHHH
28.9521712546
324UbiquitinationRKVISLNKQIAQKTK
HHHHHHHHHHHHHHH
48.6629967540
324MalonylationRKVISLNKQIAQKTK
HHHHHHHHHHHHHHH
48.6626320211
326UbiquitinationVISLNKQIAQKTKHL
HHHHHHHHHHHHHCH
4.7224816145
347PhosphorylationHTSLQARYNEAKKTL
HHHHHHHHHHHHHHH
21.9922817900
351UbiquitinationQARYNEAKKTLTELK
HHHHHHHHHHHHHHH
39.8624816145
351AcetylationQARYNEAKKTLTELK
HHHHHHHHHHHHHHH
39.8620167786
352AcetylationARYNEAKKTLTELKT
HHHHHHHHHHHHHHH
56.6820167786
353PhosphorylationRYNEAKKTLTELKTY
HHHHHHHHHHHHHHH
37.9025072903
355PhosphorylationNEAKKTLTELKTYSE
HHHHHHHHHHHHHHH
44.4925072903
358AcetylationKKTLTELKTYSEKLD
HHHHHHHHHHHHHCC
38.907822347
359PhosphorylationKTLTELKTYSEKLDK
HHHHHHHHHHHHCCH
44.9225072903
360PhosphorylationTLTELKTYSEKLDKE
HHHHHHHHHHHCCHH
17.1625072903
361PhosphorylationLTELKTYSEKLDKEQ
HHHHHHHHHHCCHHH
33.2225072903
363UbiquitinationELKTYSEKLDKEQAA
HHHHHHHHCCHHHHH
56.92-
366UbiquitinationTYSEKLDKEQAALEK
HHHHHCCHHHHHHHH
63.2624816145
373UbiquitinationKEQAALEKIESKADP
HHHHHHHHHHHHCCH
53.2622817900
377MalonylationALEKIESKADPSILQ
HHHHHHHHCCHHHHH
43.9826320211
377UbiquitinationALEKIESKADPSILQ
HHHHHHHHCCHHHHH
43.9822817900
388UbiquitinationSILQNLRALVAMNEN
HHHHHHHHHHHHCHH
15.0024816145
397UbiquitinationVAMNENLKSQEQEFK
HHHCHHHHHHHHHHH
62.7722817900
403UbiquitinationLKSQEQEFKAHCREE
HHHHHHHHHHHHHHH
9.4124816145
404UbiquitinationKSQEQEFKAHCREEM
HHHHHHHHHHHHHHH
36.1529967540
422UbiquitinationQQEIENLKAERAPRG
HHHHHHHHHHCCCCC
60.8424816145
428UbiquitinationLKAERAPRGDEKTLS
HHHHCCCCCCCCCCC
65.3022817900
432UbiquitinationRAPRGDEKTLSSGEP
CCCCCCCCCCCCCCC
60.5522817900
433PhosphorylationAPRGDEKTLSSGEPP
CCCCCCCCCCCCCCC
29.80-
452UbiquitinationSAMTHDEDLDRRYNM
CCCCCCHHHHHHHCC
60.9822817900
457PhosphorylationDEDLDRRYNMEKEKL
CHHHHHHHCCCHHHH
21.5429083192
477UbiquitinationLQARRNREIAILHRK
HHHHCCCHHHEEECC
40.0824816145
484UbiquitinationEIAILHRKIDEVPSR
HHHEEECCHHHCCCH
43.7024816145
499UbiquitinationAELIQYQKRFIELYR
HHHHHHHHHHHHHHH
44.3224816145
509PhosphorylationIELYRQISAVHKETK
HHHHHHHHHHHHHHH
18.8528509920
539UbiquitinationLEKEISLLNSIHENF
HHHHHHHHHHHHHHH
3.6424816145
552PhosphorylationNFSQAMASPAARDQF
HHHHHHCCHHHHHHH
11.2926329039
554UbiquitinationSQAMASPAARDQFLR
HHHHCCHHHHHHHHH
16.7824816145
571UbiquitinationEQIVEGIKQSRMKME
HHHHHHHHHHHHHHH
53.75-
573PhosphorylationIVEGIKQSRMKMEKK
HHHHHHHHHHHHHHH
29.37-
601UbiquitinationQYLELLEKQRLYFKT
HHHHHHHHHCHHHHH
40.4629967540
625UbiquitinationKNEMLLSKVKAKAS-
CCHHHHHHHHHHCC-
47.96-

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 CCD93_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCD93_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 CCD93_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C40_HUMANKRT40physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
CCD22_HUMANCCDC22physical
25355947
CP062_HUMANC16orf62physical
25355947
COMD1_HUMANCOMMD1physical
25355947
COMD6_HUMANCOMMD6physical
25355947
CCD22_HUMANCCDC22physical
26344197
COMDA_HUMANCOMMD10physical
26344197
COMD2_HUMANCOMMD2physical
26344197
MNS1_HUMANMNS1physical
26344197
GOGB1_HUMANGOLGB1physical
26496610
HNRPC_HUMANHNRNPCphysical
26496610
PDK1_HUMANPDK1physical
26496610
PRS6A_HUMANPSMC3physical
26496610
FXR1_HUMANFXR1physical
26496610
DSCR3_HUMANDSCR3physical
26496610
COMD3_HUMANCOMMD3physical
26496610
LTN1_HUMANLTN1physical
26496610
CCD22_HUMANCCDC22physical
26496610
COMD5_HUMANCOMMD5physical
26496610
COMD9_HUMANCOMMD9physical
26496610
COMD2_HUMANCOMMD2physical
26496610
COMDA_HUMANCOMMD10physical
26496610
VPS29_HUMANVPS29physical
26496610
COMD8_HUMANCOMMD8physical
26496610
TM248_HUMANTMEM248physical
26496610
CP062_HUMANC16orf62physical
26496610
CPSF7_HUMANCPSF7physical
26496610
ZIC4_HUMANZIC4physical
26496610
COMD7_HUMANCOMMD7physical
26496610
COMD1_HUMANCOMMD1physical
26496610
DHX36_HUMANDHX36physical
26496610
COMD6_HUMANCOMMD6physical
26496610
FA45A_HUMANFAM45Aphysical
26496610
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
VPS50_HUMANCCDC132physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
EIPR1_HUMANTSSC1physical
27173435
JUN_HUMANJUNphysical
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 CCD93_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-305, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301 ANDSER-305, AND MASS SPECTROMETRY.

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