PDC6I_HUMAN - dbPTM
PDC6I_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDC6I_HUMAN
UniProt AC Q8WUM4
Protein Name Programmed cell death 6-interacting protein
Gene Name PDCD6IP
Organism Homo sapiens (Human).
Sequence Length 868
Subcellular Localization Cytoplasm, cytosol . Melanosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Secreted, exosome . Cell junction, tight junction . Midbody, Midbody ring . Identified by mass spectrometry in melanosome fractions from stage I to
Protein Description Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes. [PubMed: 14739459 The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis]
Protein Sequence MATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYPQQ
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------MATFISVQL
------CCEEEEEEE
15.9522223895
3Phosphorylation-----MATFISVQLK
-----CCEEEEEEEC
21.8723401153
6Phosphorylation--MATFISVQLKKTS
--CCEEEEEEECCCC
10.3023401153
10MethylationTFISVQLKKTSEVDL
EEEEEEECCCCCCCH
36.59-
11MalonylationFISVQLKKTSEVDLA
EEEEEECCCCCCCHH
66.9126320211
11 (in isoform 2)Malonylation-66.9126320211
12PhosphorylationISVQLKKTSEVDLAK
EEEEECCCCCCCHHH
28.6520873877
13PhosphorylationSVQLKKTSEVDLAKP
EEEECCCCCCCHHHH
44.4925849741
13 (in isoform 2)Phosphorylation-44.4927251275
19UbiquitinationTSEVDLAKPLVKFIQ
CCCCCHHHHHHHHHH
46.3021890473
19UbiquitinationTSEVDLAKPLVKFIQ
CCCCCHHHHHHHHHH
46.3021890473
19AcetylationTSEVDLAKPLVKFIQ
CCCCCHHHHHHHHHH
46.3023236377
19MalonylationTSEVDLAKPLVKFIQ
CCCCCHHHHHHHHHH
46.3026320211
19UbiquitinationTSEVDLAKPLVKFIQ
CCCCCHHHHHHHHHH
46.3023000965
19 (in isoform 2)Malonylation-46.3026320211
23UbiquitinationDLAKPLVKFIQQTYP
CHHHHHHHHHHHHCC
44.4221890473
23UbiquitinationDLAKPLVKFIQQTYP
CHHHHHHHHHHHHCC
44.4221890473
23AcetylationDLAKPLVKFIQQTYP
CHHHHHHHHHHHHCC
44.4225953088
23UbiquitinationDLAKPLVKFIQQTYP
CHHHHHHHHHHHHCC
44.4223000965
25UbiquitinationAKPLVKFIQQTYPSG
HHHHHHHHHHHCCCC
2.1622817900
39PhosphorylationGGEEQAQYCRAAEEL
CHHHHHHHHHHHHHH
6.2122817900
40GlutathionylationGEEQAQYCRAAEELS
HHHHHHHHHHHHHHH
1.2622555962
40S-nitrosylationGEEQAQYCRAAEELS
HHHHHHHHHHHHHHH
1.262212679
48AcetylationRAAEELSKLRRAAVG
HHHHHHHHHHHHHHC
59.6519608861
48MalonylationRAAEELSKLRRAAVG
HHHHHHHHHHHHHHC
59.6526320211
48UbiquitinationRAAEELSKLRRAAVG
HHHHHHHHHHHHHHC
59.6533845483
48 (in isoform 2)Malonylation-59.6526320211
60AcetylationAVGRPLDKHEGALET
HHCCCCCCCCCHHHH
51.7623749302
60UbiquitinationAVGRPLDKHEGALET
HHCCCCCCCCCHHHH
51.76-
95UbiquitinationQICLTFTWKDAFDKG
EEEEEEEEHHCCCCC
7.7324816145
100UbiquitinationFTWKDAFDKGSLFGG
EEEHHCCCCCCCCCH
57.0124816145
101UbiquitinationTWKDAFDKGSLFGGS
EEHHCCCCCCCCCHH
43.9021890473
101UbiquitinationTWKDAFDKGSLFGGS
EEHHCCCCCCCCCHH
43.9021890473
101AcetylationTWKDAFDKGSLFGGS
EEHHCCCCCCCCCHH
43.9023236377
101UbiquitinationTWKDAFDKGSLFGGS
EEHHCCCCCCCCCHH
43.9027667366
103O-linked_GlycosylationKDAFDKGSLFGGSVK
HHCCCCCCCCCHHHH
26.6823301498
103PhosphorylationKDAFDKGSLFGGSVK
HHCCCCCCCCCHHHH
26.6862168483
108PhosphorylationKGSLFGGSVKLALAS
CCCCCCHHHHHHHHH
19.2323684312
108 (in isoform 2)Phosphorylation-19.2324719451
113UbiquitinationGGSVKLALASLGYEK
CHHHHHHHHHCCCCC
4.8824816145
115PhosphorylationSVKLALASLGYEKSC
HHHHHHHHCCCCCHH
24.1528152594
118PhosphorylationLALASLGYEKSCVLF
HHHHHCCCCCHHHHH
26.0228152594
118UbiquitinationLALASLGYEKSCVLF
HHHHHCCCCCHHHHH
26.0224816145
122UbiquitinationSLGYEKSCVLFNCAA
HCCCCCHHHHHHHHH
4.5824816145
123UbiquitinationLGYEKSCVLFNCAAL
CCCCCHHHHHHHHHH
9.8624816145
127UbiquitinationKSCVLFNCAALASQI
CHHHHHHHHHHHHHH
1.5124816145
128UbiquitinationSCVLFNCAALASQIA
HHHHHHHHHHHHHHH
13.4524816145
157PhosphorylationAKHYQFASGAFLHIK
HHHHHHCCCCCHHHH
31.7628348404
160UbiquitinationYQFASGAFLHIKETV
HHHCCCCCHHHHHHH
6.1021890473
165UbiquitinationGAFLHIKETVLSALS
CCCHHHHHHHHHHHH
43.4721890473
166PhosphorylationAFLHIKETVLSALSR
CCHHHHHHHHHHHHC
23.0319413330
167UbiquitinationFLHIKETVLSALSRE
CHHHHHHHHHHHHCC
4.1123503661
169PhosphorylationHIKETVLSALSREPT
HHHHHHHHHHHCCCC
23.8721712546
172UbiquitinationETVLSALSREPTVDI
HHHHHHHHCCCCCCC
34.0223503661
184UbiquitinationVDISPDTVGTLSLIM
CCCCCCCHHHHHHHH
7.8024816145
186PhosphorylationISPDTVGTLSLIMLA
CCCCCHHHHHHHHHH
14.6146162323
189UbiquitinationDTVGTLSLIMLAQAQ
CCHHHHHHHHHHHHH
2.7624816145
209MalonylationKATRDKMKDAIIAKL
HHCHHHHHHHHHHHH
50.1526320211
209UbiquitinationKATRDKMKDAIIAKL
HHCHHHHHHHHHHHH
50.1533845483
209 (in isoform 2)Malonylation-50.1526320211
215UbiquitinationMKDAIIAKLANQAAD
HHHHHHHHHHHHHHH
37.4121890473
215AcetylationMKDAIIAKLANQAAD
HHHHHHHHHHHHHHH
37.4119608861
215UbiquitinationMKDAIIAKLANQAAD
HHHHHHHHHHHHHHH
37.4122817900
223PhosphorylationLANQAADYFGDAFKQ
HHHHHHHHHHHHHHH
12.5328152594
229AcetylationDYFGDAFKQCQYKDT
HHHHHHHHHCCCCCC
52.4625953088
229UbiquitinationDYFGDAFKQCQYKDT
HHHHHHHHHCCCCCC
52.4632015554
234UbiquitinationAFKQCQYKDTLPKEV
HHHHCCCCCCCCHHH
20.54-
239UbiquitinationQYKDTLPKEVFPVLA
CCCCCCCHHHHHHHH
70.4029967540
258PhosphorylationIMQANAEYHQSILAK
HHHCCHHHHHHHHHH
11.6246162341
269AcetylationILAKQQKKFGEEIAR
HHHHHHHHHHHHHHH
55.0225953088
269UbiquitinationILAKQQKKFGEEIAR
HHHHHHHHHHHHHHH
55.0229967540
274UbiquitinationQKKFGEEIARLQHAA
HHHHHHHHHHHHHHH
2.0529967540
285AcetylationQHAAELIKTVASRYD
HHHHHHHHHHHHHCH
49.9625953088
285MalonylationQHAAELIKTVASRYD
HHHHHHHHHHHHHCH
49.9626320211
285UbiquitinationQHAAELIKTVASRYD
HHHHHHHHHHHHHCH
49.9632015554
290UbiquitinationLIKTVASRYDEYVNV
HHHHHHHHCHHCCCH
32.9332015554
290 (in isoform 2)Malonylation-32.9326320211
294PhosphorylationVASRYDEYVNVKDFS
HHHHCHHCCCHHHHH
8.4027251275
296UbiquitinationSRYDEYVNVKDFSDK
HHCHHCCCHHHHHHH
33.9323000965
298AcetylationYDEYVNVKDFSDKIN
CHHCCCHHHHHHHHH
48.1023236377
298UbiquitinationYDEYVNVKDFSDKIN
CHHCCCHHHHHHHHH
48.1032015554
299 (in isoform 2)Phosphorylation-43.9627642862
301UbiquitinationYVNVKDFSDKINRAL
CCCHHHHHHHHHHHH
48.4023000965
303AcetylationNVKDFSDKINRALAA
CHHHHHHHHHHHHHH
40.4526822725
303MalonylationNVKDFSDKINRALAA
CHHHHHHHHHHHHHH
40.4526320211
303UbiquitinationNVKDFSDKINRALAA
CHHHHHHHHHHHHHH
40.4532015554
308UbiquitinationSDKINRALAAAKKDN
HHHHHHHHHHHHHCC
2.7724816145
308 (in isoform 2)Malonylation-2.7726320211
311UbiquitinationINRALAAAKKDNDFI
HHHHHHHHHHCCCCC
17.5221890473
312UbiquitinationNRALAAAKKDNDFIY
HHHHHHHHHCCCCCC
56.8024816145
313MalonylationRALAAAKKDNDFIYH
HHHHHHHHCCCCCCC
57.9726320211
313UbiquitinationRALAAAKKDNDFIYH
HHHHHHHHCCCCCCC
57.9724816145
316UbiquitinationAAAKKDNDFIYHDRV
HHHHHCCCCCCCCCC
41.2621890473
317UbiquitinationAAKKDNDFIYHDRVP
HHHHCCCCCCCCCCC
8.1824816145
318UbiquitinationAKKDNDFIYHDRVPD
HHHCCCCCCCCCCCC
3.1333845483
318 (in isoform 2)Malonylation-3.1326320211
319PhosphorylationKKDNDFIYHDRVPDL
HHCCCCCCCCCCCCH
9.5427259358
322MethylationNDFIYHDRVPDLKDL
CCCCCCCCCCCHHHC
28.67-
324 (in isoform 2)Phosphorylation-41.9527642862
327AcetylationHDRVPDLKDLDPIGK
CCCCCCHHHCCCCCC
64.7225953088
327UbiquitinationHDRVPDLKDLDPIGK
CCCCCCHHHCCCCCC
64.7232015554
332UbiquitinationDLKDLDPIGKATLVK
CHHHCCCCCCEEEEE
9.8632015554
334AcetylationKDLDPIGKATLVKST
HHCCCCCCEEEEECC
38.6325953088
334UbiquitinationKDLDPIGKATLVKST
HHCCCCCCEEEEECC
38.6329967540
339AcetylationIGKATLVKSTPVNVP
CCCEEEEECCCCCCC
52.2923236377
339MalonylationIGKATLVKSTPVNVP
CCCEEEEECCCCCCC
52.2926320211
339UbiquitinationIGKATLVKSTPVNVP
CCCEEEEECCCCCCC
52.2932015554
340PhosphorylationGKATLVKSTPVNVPI
CCEEEEECCCCCCCC
30.3925627689
341PhosphorylationKATLVKSTPVNVPIS
CEEEEECCCCCCCCH
26.0725627689
344UbiquitinationLVKSTPVNVPISQKF
EEECCCCCCCCHHHH
34.7432015554
344 (in isoform 2)Malonylation-34.7426320211
350AcetylationVNVPISQKFTDLFEK
CCCCCHHHHHHHHHH
43.3623236377
350UbiquitinationVNVPISQKFTDLFEK
CCCCCHHHHHHHHHH
43.3623000965
355UbiquitinationSQKFTDLFEKMVPVS
HHHHHHHHHHHCCCC
10.6321890473
355UbiquitinationSQKFTDLFEKMVPVS
HHHHHHHHHHHCCCC
10.6323000965
357UbiquitinationKFTDLFEKMVPVSVQ
HHHHHHHHHCCCCHH
37.5521906983
362UbiquitinationFEKMVPVSVQQSLAA
HHHHCCCCHHHHHHH
14.2423503661
366PhosphorylationVPVSVQQSLAAYNQR
CCCCHHHHHHHHHHH
11.6850564661
370PhosphorylationVQQSLAAYNQRKADL
HHHHHHHHHHHHHHH
13.2550564669
374UbiquitinationLAAYNQRKADLVNRS
HHHHHHHHHHHHHHH
36.1724816145
379UbiquitinationQRKADLVNRSIAQMR
HHHHHHHHHHHHHHH
39.0024816145
416PhosphorylationSGDTVPQSILTKSRS
CCCCCCHHHHHHCCH
17.3124719451
421PhosphorylationPQSILTKSRSVIEQG
CHHHHHHCCHHHHHC
25.2629514088
423PhosphorylationSILTKSRSVIEQGGI
HHHHHCCHHHHHCCH
34.2429514088
438UbiquitinationQTVDQLIKELPELLQ
HHHHHHHHHHHHHHH
62.8929967540
443UbiquitinationLIKELPELLQRNREI
HHHHHHHHHHHHHHH
4.6929967540
448UbiquitinationPELLQRNREILDESL
HHHHHHHHHHHHHHH
34.2221963094
450UbiquitinationLLQRNREILDESLRL
HHHHHHHHHHHHHHH
5.4727667366
453UbiquitinationRNREILDESLRLLDE
HHHHHHHHHHHHCCH
48.5021963094
455UbiquitinationREILDESLRLLDEEE
HHHHHHHHHHCCHHH
4.1527667366
456MethylationEILDESLRLLDEEEA
HHHHHHHHHCCHHHC
42.35-
464PhosphorylationLLDEEEATDNDLRAK
HCCHHHCCCHHHHHH
38.32110755291
464UbiquitinationLLDEEEATDNDLRAK
HCCHHHCCCHHHHHH
38.3225015289
469UbiquitinationEATDNDLRAKFKERW
HCCCHHHHHHHHHHH
38.3025015289
471UbiquitinationTDNDLRAKFKERWQR
CCHHHHHHHHHHHHC
51.0029967540
476UbiquitinationRAKFKERWQRTPSNE
HHHHHHHHHCCCCCC
7.9729967540
479PhosphorylationFKERWQRTPSNELYK
HHHHHHCCCCCCCCH
18.9025159151
481PhosphorylationERWQRTPSNELYKPL
HHHHCCCCCCCCHHH
42.1825159151
481UbiquitinationERWQRTPSNELYKPL
HHHHCCCCCCCCHHH
42.1823503661
484 (in isoform 2)Phosphorylation-8.5624719451
485PhosphorylationRTPSNELYKPLRAEG
CCCCCCCCHHHHCCC
12.3728258704
485UbiquitinationRTPSNELYKPLRAEG
CCCCCCCCHHHHCCC
12.3723503661
486AcetylationTPSNELYKPLRAEGT
CCCCCCCHHHHCCCC
50.6423954790
486MalonylationTPSNELYKPLRAEGT
CCCCCCCHHHHCCCC
50.6426320211
486SuccinylationTPSNELYKPLRAEGT
CCCCCCCHHHHCCCC
50.6423954790
486UbiquitinationTPSNELYKPLRAEGT
CCCCCCCHHHHCCCC
50.6423000965
490UbiquitinationELYKPLRAEGTNFRT
CCCHHHHCCCCCHHH
27.5323503661
490 (in isoform 2)Phosphorylation-27.5327642862
491UbiquitinationLYKPLRAEGTNFRTV
CCHHHHCCCCCHHHH
61.1823000965
491 (in isoform 2)Malonylation-61.1826320211
500UbiquitinationTNFRTVLDKAVQADG
CCHHHHHHHHHHCCC
32.3124816145
501AcetylationNFRTVLDKAVQADGQ
CHHHHHHHHHHCCCC
46.4225953088
501UbiquitinationNFRTVLDKAVQADGQ
CHHHHHHHHHHCCCC
46.4223000965
505UbiquitinationVLDKAVQADGQVKEC
HHHHHHHCCCCHHHH
19.1224816145
506UbiquitinationLDKAVQADGQVKECY
HHHHHHCCCCHHHHH
30.8521890473
506UbiquitinationLDKAVQADGQVKECY
HHHHHHCCCCHHHHH
30.8523000965
510UbiquitinationVQADGQVKECYQSHR
HHCCCCHHHHHHHCC
33.8929967540
512GlutathionylationADGQVKECYQSHRDT
CCCCHHHHHHHCCCE
2.8722555962
515UbiquitinationQVKECYQSHRDTIVL
CHHHHHHHCCCEEEE
8.2629967540
517UbiquitinationKECYQSHRDTIVLLC
HHHHHHCCCEEEEEE
48.2723000965
522UbiquitinationSHRDTIVLLCKPEPE
HCCCEEEEEECCCHH
4.0323000965
524GlutathionylationRDTIVLLCKPEPELN
CCEEEEEECCCHHHC
6.3822555962
525AcetylationDTIVLLCKPEPELNA
CEEEEEECCCHHHCC
53.0026051181
541UbiquitinationIPSANPAKTMQGSEV
CCCCCCCCCCCHHHH
45.8732015554
543SulfoxidationSANPAKTMQGSEVVN
CCCCCCCCCHHHHHH
4.1321406390
546UbiquitinationPAKTMQGSEVVNVLK
CCCCCCHHHHHHHHH
15.4432015554
554PhosphorylationEVVNVLKSLLSNLDE
HHHHHHHHHHHCHHH
30.3128348404
557PhosphorylationNVLKSLLSNLDEVKK
HHHHHHHHCHHHHHH
40.4120860994
561UbiquitinationSLLSNLDEVKKEREG
HHHHCHHHHHHHHHH
60.4421890473
563UbiquitinationLSNLDEVKKEREGLE
HHCHHHHHHHHHHHH
47.0429967540
564UbiquitinationSNLDEVKKEREGLEN
HCHHHHHHHHHHHHH
68.15-
566UbiquitinationLDEVKKEREGLENDL
HHHHHHHHHHHHHHH
52.7621890473
568UbiquitinationEVKKEREGLENDLKS
HHHHHHHHHHHHHHH
44.5029967540
575PhosphorylationGLENDLKSVNFDMTS
HHHHHHHHCCHHHHH
29.5925159151
580SulfoxidationLKSVNFDMTSKFLTA
HHHCCHHHHHHHHHH
3.8930846556
581PhosphorylationKSVNFDMTSKFLTAL
HHCCHHHHHHHHHHH
30.5227470641
606MethylationLSVTELDRVYGGLTT
CCHHHHHHHHCCHHH
35.86-
608PhosphorylationVTELDRVYGGLTTKV
HHHHHHHHCCHHHHH
13.3328152594
612PhosphorylationDRVYGGLTTKVQESL
HHHHCCHHHHHHHHH
28.0424719451
613PhosphorylationRVYGGLTTKVQESLK
HHHCCHHHHHHHHHH
33.9724719451
613 (in isoform 2)Phosphorylation-33.9724719451
614UbiquitinationVYGGLTTKVQESLKK
HHCCHHHHHHHHHHH
36.3629967540
617 (in isoform 2)Phosphorylation-62.1124719451
618 (in isoform 2)Phosphorylation-28.5324719451
619UbiquitinationTTKVQESLKKQEGLL
HHHHHHHHHHCCCHH
8.7029967540
620AcetylationTKVQESLKKQEGLLK
HHHHHHHHHCCCHHH
62.7825953088
627UbiquitinationKKQEGLLKNIQVSHQ
HHCCCHHHHHHHCHH
57.9829967540
632UbiquitinationLLKNIQVSHQEFSKM
HHHHHHHCHHHHHHH
11.7729967540
638NeddylationVSHQEFSKMKQSNNE
HCHHHHHHHHHCCCH
56.2732015554
638UbiquitinationVSHQEFSKMKQSNNE
HCHHHHHHHHHCCCH
56.2721906983
640UbiquitinationHQEFSKMKQSNNEAN
HHHHHHHHHCCCHHH
55.0721906983
643NeddylationFSKMKQSNNEANLRE
HHHHHHCCCHHHHHH
48.1132015554
643UbiquitinationFSKMKQSNNEANLRE
HHHHHHCCCHHHHHH
48.1127667366
645UbiquitinationKMKQSNNEANLREEV
HHHHCCCHHHHHHHH
43.0927667366
654UbiquitinationNLREEVLKNLATAYD
HHHHHHHHHHHHHHH
55.9025015289
659UbiquitinationVLKNLATAYDNFVEL
HHHHHHHHHHHHHHH
12.2225015289
671UbiquitinationVELVANLKEGTKFYN
HHHHHHHHCCCCHHH
54.6423503661
675UbiquitinationANLKEGTKFYNELTE
HHHHCCCCHHHHHHH
57.6223503661
676UbiquitinationNLKEGTKFYNELTEI
HHHCCCCHHHHHHHH
8.7623503661
680UbiquitinationGTKFYNELTEILVRF
CCCHHHHHHHHHHHH
4.6623503661
690UbiquitinationILVRFQNKCSDIVFA
HHHHHHHHCCCCEEE
25.0824816145
692PhosphorylationVRFQNKCSDIVFARK
HHHHHHCCCCEEECC
31.79166220823
695UbiquitinationQNKCSDIVFARKTER
HHHCCCCEEECCHHH
3.5424816145
695 (in isoform 2)Malonylation-3.5432601280
707AcetylationTERDELLKDLQQSIA
HHHHHHHHHHHHHHH
69.8525953088
707UbiquitinationTERDELLKDLQQSIA
HHHHHHHHHHHHHHH
69.8523000965
712UbiquitinationLLKDLQQSIAREPSA
HHHHHHHHHHHCCCC
12.7821890473
712PhosphorylationLLKDLQQSIAREPSA
HHHHHHHHHHHCCCC
12.7829255136
712UbiquitinationLLKDLQQSIAREPSA
HHHHHHHHHHHCCCC
12.7823000965
718PhosphorylationQSIAREPSAPSIPTP
HHHHHCCCCCCCCCC
48.3223898821
721PhosphorylationAREPSAPSIPTPAYQ
HHCCCCCCCCCCCCC
40.7069009511
723 (in isoform 2)Phosphorylation-36.3527251275
724PhosphorylationPSAPSIPTPAYQSSP
CCCCCCCCCCCCCCC
20.9130278072
726 (in isoform 2)Phosphorylation-19.9227251275
727PhosphorylationPSIPTPAYQSSPAGG
CCCCCCCCCCCCCCC
15.3330278072
729PhosphorylationIPTPAYQSSPAGGHA
CCCCCCCCCCCCCCC
26.1323401153
730PhosphorylationPTPAYQSSPAGGHAP
CCCCCCCCCCCCCCC
11.8430278072
732 (in isoform 2)Phosphorylation-38.2527642862
734 (in isoform 2)Phosphorylation-18.8527251275
735PhosphorylationQSSPAGGHAPTPPTP
CCCCCCCCCCCCCCC
27.8432142685
738O-linked_GlycosylationPAGGHAPTPPTPAPR
CCCCCCCCCCCCCCC
42.56OGP
738PhosphorylationPAGGHAPTPPTPAPR
CCCCCCCCCCCCCCC
42.5630278072
741PhosphorylationGHAPTPPTPAPRTMP
CCCCCCCCCCCCCCC
33.0325159151
745MethylationTPPTPAPRTMPPTKP
CCCCCCCCCCCCCCC
45.8424129315
746PhosphorylationPPTPAPRTMPPTKPQ
CCCCCCCCCCCCCCC
32.7318669648
751AcetylationPRTMPPTKPQPPARP
CCCCCCCCCCCCCCC
47.6423954790
751MethylationPRTMPPTKPQPPARP
CCCCCCCCCCCCCCC
47.64-
751UbiquitinationPRTMPPTKPQPPARP
CCCCCCCCCCCCCCC
47.6423000965
756UbiquitinationPTKPQPPARPPPPVL
CCCCCCCCCCCCCCC
43.2121890473
756UbiquitinationPTKPQPPARPPPPVL
CCCCCCCCCCCCCCC
43.2121890473
757MethylationTKPQPPARPPPPVLP
CCCCCCCCCCCCCCC
50.46-
767MethylationPPVLPANRAPSATAP
CCCCCCCCCCCCCCC
50.40-

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
-KUbiquitinationE3 ubiquitin ligaseSH3RF1Q7Z6J0
PMID:19393081
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:20519395

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDC6I_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 PDC6I_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDCD6_HUMANPDCD6physical
9880530
PGFRB_HUMANPDGFRBphysical
17082185
NEDD4_HUMANNEDD4physical
20519395
SH3G2_HUMANSH3GL2physical
15456872
SH3R1_HUMANSH3RF1physical
19393081
TS101_HUMANTSG101physical
17229889
ARRD1_HUMANARRDC1physical
21191027
ARRD3_HUMANARRDC3physical
21191027
SH3K1_HUMANSH3KBP1physical
21191027
CHM4A_HUMANCHMP4Aphysical
21191027
PAR1_HUMANF2Rphysical
22547407
SH3K1_HUMANSH3KBP1physical
17428861
SH3G1_HUMANSH3GL1physical
17428861
CD2AP_HUMANCD2APphysical
17428861
SGSM3_HUMANSGSM3physical
17174262
CHM4B_HUMANCHMP4Bphysical
17174262
TS101_HUMANTSG101physical
17174262
SH3G2_HUMANSH3GL2physical
17174262
SH3K1_HUMANSH3KBP1physical
17174262
ALG2_HUMANALG2physical
17174262
PTN23_HUMANPTPN23physical
17174262
SRC_HUMANSRCphysical
15557335
TS101_HUMANTSG101physical
14505570
PDC6I_HUMANPDCD6IPphysical
14505570
TS101_HUMANTSG101physical
19520058
ALG2_HUMANALG2physical
19520058
GAG_HV1H2gagphysical
19282983
CEP55_HUMANCEP55physical
17853893
CD2AP_HUMANCD2APphysical
17853893
TS101_HUMANTSG101physical
16004603
PDC6I_HUMANPDCD6IPphysical
16004603
ALG2_HUMANALG2physical
16004603
CHM4A_HUMANCHMP4Aphysical
14505569
TS101_HUMANTSG101physical
14505569
GAG_HV1H2gagphysical
14505569
CHM4B_HUMANCHMP4Bphysical
20929444
PDC6I_HUMANPDCD6IPphysical
20929444
SRC_HUMANSRCphysical
20929444
TS101_HUMANTSG101physical
20929444
CEP55_HUMANCEP55physical
18948538
PDC6I_HUMANPDCD6IPphysical
18641129
TS101_HUMANTSG101physical
18641129
CHM4A_HUMANCHMP4Aphysical
18641129
SH3K1_HUMANSH3KBP1physical
18641129
ALG2_HUMANALG2physical
18256029
CEP55_HUMANCEP55physical
18940611
PDCD6_HUMANPDCD6physical
18940611
VPS4B_HUMANVPS4Bphysical
22939629
PEF1_HUMANPEF1physical
22939629
CHM4B_HUMANCHMP4Bphysical
23895345
TNIP2_HUMANTNIP2physical
21988832
SH3G1_HUMANSH3GL1physical
21988832
EZRI_HUMANEZRphysical
22863883
IPO9_HUMANIPO9physical
22863883
MCTS1_HUMANMCTS1physical
22863883
NEF_HV1H2nefphysical
25118280
CEP55_HUMANCEP55physical
25416956
SDCB1_HUMANSDCBPphysical
22660413
ENOA_HUMANENO1physical
26344197
ESTD_HUMANESDphysical
26344197
AATC_HUMANGOT1physical
26344197
MIF_HUMANMIFphysical
26344197
TPIS_HUMANTPI1physical
26344197
PDC6I_HUMANPDCD6IPphysical
26490116
GAG_SIVG1gag-polphysical
27839950

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 PDC6I_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-215, AND MASSSPECTROMETRY.
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-730; THR-738 ANDTHR-741, AND MASS SPECTROMETRY.

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