PDGFC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDGFC_HUMAN
• UniProt AC: Q9NRA1
• Protein Name: Platelet-derived growth factor C
• Gene Name: PDGFC
• Organism: Homo sapiens (Human).
• Sequence Length: 345
• Subcellular Localization: Cytoplasm, cytosol . Secreted . Nucleus . Cytoplasmic granule . Cell membrane . Sumoylated form is predominant in the nucleus (PubMed:15247255). Stored in alpha granules in platelets (PubMed:15061151).
• Protein Description: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function..
• Protein Sequence: MSLFGLLLLTSALAGQRQGTQAESNLSSKFQFSSNKEQNGVQDPQHERIITVSTNGSIHSPRFPHTYPRNTVLVWRLVAVEENVWIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGTILGRWCGSGTVPGKQISKGNQIRIRFVSDEYFPSEPGFCIHYNIVMPQFTEAVSPSVLPPSALPLDLLNNAITAFSTLEDLIRYLEPERWQLDLEDLYRPTWQLLGKAFVFGRKSRVVDLNLLTEEVRLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPSKVTKKYHEVLQLRPKTGVRGLHKSLTDVALEHHEECDCVCRGSTGG

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	Phosphorylation	------MSLFGLLLL ------CCHHHHHHH	32.19	26503514
10	Phosphorylation	LFGLLLLTSALAGQR HHHHHHHHHHHHCCC	16.36	24043423
11	Phosphorylation	FGLLLLTSALAGQRQ HHHHHHHHHHHCCCC	22.66	24043423
25	N-linked_Glycosylation	QGTQAESNLSSKFQF CCCCCCHHHHHCCCC	35.13	UniProtKB CARBOHYD
27	Phosphorylation	TQAESNLSSKFQFSS CCCCHHHHHCCCCCC	35.41	26503514
28	Phosphorylation	QAESNLSSKFQFSSN CCCHHHHHCCCCCCC	40.43	26503514
55	N-linked_Glycosylation	RIITVSTNGSIHSPR EEEEEECCCCCCCCC	34.41	UniProtKB CARBOHYD
115	Phosphorylation	FVEVEEPSDGTILGR EEEEECCCCCCEEEE	52.53	23898821
118	Phosphorylation	VEEPSDGTILGRWCG EECCCCCCEEEEEEC	20.30	23898821
146 (in isoform 3)	Phosphorylation	-	23.24	26270265
149 (in isoform 3)	Phosphorylation	-	26.27	26270265
152 (in isoform 3)	Phosphorylation	-	46.66	26270265
155 (in isoform 3)	Phosphorylation	-	26.46	26270265
166 (in isoform 3)	Phosphorylation	-	39.54	26270265
167 (in isoform 3)	Phosphorylation	-	5.70	26270265
233	Phosphorylation	AFVFGRKSRVVDLNL HHHHCCCCCEEEHHH	29.01	-
256	Phosphorylation	SCTPRNFSVSIREEL HCCCCCCEEEHHHHH	20.64	24719451
258	Phosphorylation	TPRNFSVSIREELKR CCCCCEEEHHHHHHC	18.09	24719451
314	Sumoylation	EVLQLRPKTGVRGLH HHHHCCCCCCCCHHH	52.02	-
314	Sumoylation	EVLQLRPKTGVRGLH HHHHCCCCCCCCHHH	52.02	-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of PDGFC_HUMAN !!

Drug and Disease Associations

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