PDC6I_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDC6I_MOUSE
• UniProt AC: Q9WU78
• Protein Name: Programmed cell death 6-interacting protein
• Gene Name: Pdcd6ip
• Organism: Mus musculus (Mouse).
• Sequence Length: 869
• Subcellular Localization: Cytoplasm, cytosol . Melanosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Secreted, exosome . Cell junction, tight junction . Midbody, Midbody ring . Colocalized with CEP55 in the midbody during cytokinesis and at centros
• 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. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP (By similarity). By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier. [PubMed: 27336173]
• Protein Sequence: MASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNVPVSQKFTDLFEKMVPVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPPPAYQSSPAAGHAAAPPTPAPRTMPPAKPQPPARPPPPVLPANRVPPASAAAAPAGVGTASAAPPQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPFPQPPQQSYYPQQ

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
2	Acetylation	------MASFIWVQL ------CCCEEEEEE	17.10	-
11	Malonylation	FIWVQLKKTSEVDLA EEEEEECCCCCCCHH	66.91	26320211
12	Phosphorylation	IWVQLKKTSEVDLAK EEEEECCCCCCCHHH	28.65	29550500
13	Phosphorylation	WVQLKKTSEVDLAKP EEEECCCCCCCHHHH	44.49	26824392
19	Acetylation	TSEVDLAKPLVKFIQ CCCCCHHHHHHHHHH	46.30	22826441
19	Ubiquitination	TSEVDLAKPLVKFIQ CCCCCHHHHHHHHHH	46.30	-
23	Ubiquitination	DLAKPLVKFIQQTYP CHHHHHHHHHHHHCC	44.42	-
31	Phosphorylation	FIQQTYPSGGEEQAQ HHHHHCCCCHHHHHH	49.36	25338131
40	S-nitrosocysteine	GEEQAQYCRAAEELS HHHHHHHHHHHHHHH	1.26	-
40	S-nitrosylation	GEEQAQYCRAAEELS HHHHHHHHHHHHHHH	1.26	21278135
40	Glutathionylation	GEEQAQYCRAAEELS HHHHHHHHHHHHHHH	1.26	24333276
48	Acetylation	RAAEELSKLRRSALG HHHHHHHHHHHHHHC	59.65	22826441
48	Ubiquitination	RAAEELSKLRRSALG HHHHHHHHHHHHHHC	59.65	-
48	Malonylation	RAAEELSKLRRSALG HHHHHHHHHHHHHHC	59.65	26320211
60	Acetylation	ALGRPLDKHEGALET HHCCCCHHCCCHHHH	51.76	23236377
60	Ubiquitination	ALGRPLDKHEGALET HHCCCCHHCCCHHHH	51.76	-
101	Ubiquitination	TWKDAFDKGSLFGGS EEHHCCCCCCCCCHH	43.90	-
101	Acetylation	TWKDAFDKGSLFGGS EEHHCCCCCCCCCHH	43.90	22826441
108	Phosphorylation	KGSLFGGSVKLALAS CCCCCCHHHHHHHHH	19.23	62170609
209	Malonylation	KATRDKMKDAIIAKL HHCHHHHHHHHHHHH	50.15	26320211
215	Acetylation	MKDAIIAKLANQAAD HHHHHHHHHHHHHHH	37.41	22826441
229	Acetylation	DYFGDAFKQCQYKDT HHHHHHHHHCCCCCC	52.46	22826441
234	Acetylation	AFKQCQYKDTLPKEV HHHHCCCCCCCCHHH	20.54	22826441
258	Phosphorylation	IMQANAEYHQSILAK HHHHCHHHHHHHHHH	11.62	25338131
261	Phosphorylation	ANAEYHQSILAKQQK HCHHHHHHHHHHHHH	13.27	25338131
268	Acetylation	SILAKQQKKFGEEIA HHHHHHHHHHHHHHH	47.80	6569569
269	Acetylation	ILAKQQKKFGEEIAR HHHHHHHHHHHHHHH	55.02	6568927
285	Ubiquitination	QHAAELIKNVASRYD HHHHHHHHHHHHHCH	58.98	-
298	Acetylation	YDEYVNVKDFSDKIN CHHCCCHHHHHHHHH	48.10	23954790
298	Succinylation	YDEYVNVKDFSDKIN CHHCCCHHHHHHHHH	48.10	23954790
298	Ubiquitination	YDEYVNVKDFSDKIN CHHCCCHHHHHHHHH	48.10	-
319	Phosphorylation	KKDNDFIYHDRVPDL HHCCCCCCCCCCCCH	9.54	29514104
339	Acetylation	IGKATLVKPTPVNVP CCCEEEECCCCCCCC	46.41	23236377
339	Malonylation	IGKATLVKPTPVNVP CCCEEEECCCCCCCC	46.41	26320211
350	Ubiquitination	VNVPVSQKFTDLFEK CCCCCHHHHHHHHHH	42.60	-
421	Phosphorylation	PQSILTKSTSVVEQG CHHHHCCCCCHHHCC	22.22	26643407
422	Phosphorylation	QSILTKSTSVVEQGG HHHHCCCCCHHHCCC	27.39	26643407
423	Phosphorylation	SILTKSTSVVEQGGI HHHCCCCCHHHCCCH	31.12	26824392
464	Phosphorylation	LLDEEEATDNDLRAK HCCHHHCCCCHHHHH	38.32	26525534
479	Phosphorylation	FKDRWQRTPSNDLYK HHHHHCCCCCCCCCH	18.90	28066266
481	Phosphorylation	DRWQRTPSNDLYKPL HHHCCCCCCCCCHHH	42.22	28066266
486	Acetylation	TPSNDLYKPLRAEGA CCCCCCCHHHHHCCH	44.89	22826441
501	Malonylation	KFRAVLDKAVQADGQ HHHHHHHHHHHCCCH	46.42	26320211
501	Ubiquitination	KFRAVLDKAVQADGQ HHHHHHHHHHHCCCH	46.42	-
627	Ubiquitination	KKQEGLLKNIQVSHQ HHCCCHHHHHHCCHH	57.98	-
638	Ubiquitination	VSHQEFSKMKQSNNE CCHHHHHHHHHCCCH	56.27	-
640	Ubiquitination	HQEFSKMKQSNNEAN HHHHHHHHHCCCHHH	55.07	-
690	Acetylation	ILVRFQNKCSDIVFA HHHHHHHHCCCCEEE	25.08	22826441
692	Phosphorylation	VRFQNKCSDIVFARK HHHHHHCCCCEEECC	31.79	26643407
700	Phosphorylation	DIVFARKTERDELLK CCEEECCHHHHHHHH	30.60	26643407
707	Ubiquitination	TERDELLKDLQQSIA HHHHHHHHHHHHHHH	69.85	-
712	Phosphorylation	LLKDLQQSIAREPSA HHHHHHHHHHHCCCC	12.78	23984901
718	Phosphorylation	QSIAREPSAPSIPPP HHHHHCCCCCCCCCC	48.32	25619855
721	Phosphorylation	AREPSAPSIPPPAYQ HHCCCCCCCCCCCCC	47.66	23984901
727	Phosphorylation	PSIPPPAYQSSPAAG CCCCCCCCCCCCCCC	18.07	25619855
729	Phosphorylation	IPPPAYQSSPAAGHA CCCCCCCCCCCCCCC	26.13	25619855
730	Phosphorylation	PPPAYQSSPAAGHAA CCCCCCCCCCCCCCC	11.75	23984901
734	Phosphorylation	YQSSPAAGHAAAPPT CCCCCCCCCCCCCCC	17.05	24719451
741	Phosphorylation	GHAAAPPTPAPRTMP CCCCCCCCCCCCCCC	30.90	25619855
745	Methylation	APPTPAPRTMPPAKP CCCCCCCCCCCCCCC	45.84	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PDC6I_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDC6I_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PDC6I_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.