PDC6I_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDC6I_RAT
• UniProt AC: Q9QZA2
• Protein Name: Programmed cell death 6-interacting protein
• Gene Name: Pdcd6ip
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 873
• 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 (By similarity)..
• Protein Sequence: MASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDALPKYFYFQEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNVPISQKFTDLFEKMVPVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTAVVEQGGIQTVDQLIKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEIKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRIYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNSEASLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPPPAYQSSPAGGHATAPTPAPRTMPPAKPQPPARPPPPVLPANRVPPAAAATAPAGVGTASAAPPQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYTYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPFPQPPQQSYYPQQ

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	-
12	Phosphorylation	IWVQLKKTSEVDLAK EEEEECCCCCCCHHH	28.65	25575281
13	Phosphorylation	WVQLKKTSEVDLAKP EEEECCCCCCCHHHH	44.49	25575281
19	Acetylation	TSEVDLAKPLVKFIQ CCCCCHHHHHHHHHH	46.30	22902405
19	Ubiquitination	TSEVDLAKPLVKFIQ CCCCCHHHHHHHHHH	46.30	-
23	Ubiquitination	DLAKPLVKFIQQTYP CHHHHHHHHHHHHCC	44.42	-
48	Ubiquitination	RAAEELSKLRRSALG HHHHHHHHHHHHHHC	59.65	-
48	Acetylation	RAAEELSKLRRSALG HHHHHHHHHHHHHHC	59.65	22902405
60	Ubiquitination	ALGRPLDKHEGALET HHCCCCHHCCCHHHH	51.76	-
60	Acetylation	ALGRPLDKHEGALET HHCCCCHHCCCHHHH	51.76	22902405
108	Phosphorylation	KGSLFGGSVKLALAS CCCCCCHHHHHHHHH	19.23	23984901
215	Acetylation	MKDAIIAKLANQAAD HHHHHHHHHHHHHHH	37.41	22902405
274	Acetylation	ILAKQQKKFGEEIAR HHHHHHHHHHHHHHH	55.02	22902405
303	Acetylation	YDEYVNVKDFSDKIN CHHCCCHHHHHHHHH	48.10	22902405
344	Acetylation	IGKATLVKPTPVNVP CCCEEEECCCCCCCC	46.41	22902405
484	Phosphorylation	FKDRWQRTPSNDLYK HHHHHCCCCCCCCCH	18.90	-
486	Phosphorylation	DRWQRTPSNDLYKPL HHHCCCCCCCCCHHH	42.22	-
491	Succinylation	TPSNDLYKPLRAEGA CCCCCCCHHHHHCCH	44.89	26843850
491	Acetylation	TPSNDLYKPLRAEGA CCCCCCCHHHHHCCH	44.89	22902405
506	Ubiquitination	KFRAVLDKAVQADGQ HHHHHHHHHHHCCCH	46.42	-
717	Phosphorylation	LLKDLQQSIAREPSA HHHHHHHHHHHCCCC	12.78	23984901
723	Phosphorylation	QSIAREPSAPSIPPP HHHHHCCCCCCCCCC	48.32	23984901
726	Phosphorylation	AREPSAPSIPPPAYQ HHCCCCCCCCCCCCC	47.66	23984901
732	Phosphorylation	PSIPPPAYQSSPAGG CCCCCCCCCCCCCCC	18.07	23984901
734	Phosphorylation	IPPPAYQSSPAGGHA CCCCCCCCCCCCCCC	26.13	23984901
735	Phosphorylation	PPPAYQSSPAGGHAT CCCCCCCCCCCCCCC	11.84	23984901
742	Phosphorylation	SPAGGHATAPTPAPR CCCCCCCCCCCCCCC	27.74	23984901
745	Phosphorylation	GGHATAPTPAPRTMP CCCCCCCCCCCCCCC	29.62	30181290
749	Methylation	TAPTPAPRTMPPAKP 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_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDC6I_RAT !!

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of PDC6I_RAT !!

Drug and Disease Associations

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