PCOC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PCOC1_HUMAN
• UniProt AC: Q15113
• Protein Name: Procollagen C-endopeptidase enhancer 1
• Gene Name: PCOLCE
• Organism: Homo sapiens (Human).
• Sequence Length: 449
• Subcellular Localization: Secreted.
• Protein Description: Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity.; C-terminal processed part of PCPE (CT-PCPE) may have an metalloproteinase inhibitory activity..
• Protein Sequence: MLPAATASLLGPLLTACALLPFAQGQTPNYTRPVFLCGGDVKGESGYVASEGFPNLYPPNKECIWTITVPEGQTVSLSFRVFDLELHPACRYDALEVFAGSGTSGQRLGRFCGTFRPAPLVAPGNQVTLRMTTDEGTGGRGFLLWYSGRATSGTEHQFCGGRLEKAQGTLTTPNWPESDYPPGISCSWHIIAPPDQVIALTFEKFDLEPDTYCRYDSVSVFNGAVSDDSRRLGKFCGDAVPGSISSEGNELLVQFVSDLSVTADGFSASYKTLPRGTAKEGQGPGPKRGTEPKVKLPPKSQPPEKTEESPSAPDAPTCPKQCRRTGTLQSNFCASSLVVTATVKSMVREPGEGLAVTVSLIGAYKTGGLDLPSPPTGASLKFYVPCKQCPPMKKGVSYLLMGQVEENRGPVLPPESFVVLHRPNQDQILTNLSKRKCPSQPVRAAASQD

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
29	N-linked_Glycosylation	FAQGQTPNYTRPVFL HHCCCCCCCCCCEEE	54.95	UniProtKB CARBOHYD
50	Phosphorylation	GESGYVASEGFPNLY CCCCCCCCCCCCCCC	28.36	-
78	Phosphorylation	EGQTVSLSFRVFDLE CCCEEEEEEEEECEE	11.96	24719451
133	Phosphorylation	QVTLRMTTDEGTGGR EEEEEEEECCCCCCC	23.78	-
137	Phosphorylation	RMTTDEGTGGRGFLL EEEECCCCCCCEEEE	34.12	-
152	O-linked_Glycosylation	WYSGRATSGTEHQFC EEECCCCCCCCCCCC	42.61	OGP
154	Phosphorylation	SGRATSGTEHQFCGG ECCCCCCCCCCCCCC	30.02	-
154	O-linked_Glycosylation	SGRATSGTEHQFCGG ECCCCCCCCCCCCCC	30.02	OGP
169	Phosphorylation	RLEKAQGTLTTPNWP CEEECCCCCCCCCCC	14.62	23879269
219	Phosphorylation	YCRYDSVSVFNGAVS CCCCCEEEEECCCCC	25.58	24275569
300	O-linked_Glycosylation	KVKLPPKSQPPEKTE CCCCCCCCCCCCCCC	54.41	OGP
309	Phosphorylation	PPEKTEESPSAPDAP CCCCCCCCCCCCCCC	20.23	25159151
309	O-linked_Glycosylation	PPEKTEESPSAPDAP CCCCCCCCCCCCCCC	20.23	OGP
311	Phosphorylation	EKTEESPSAPDAPTC CCCCCCCCCCCCCCC	62.81	28857561
311	O-linked_Glycosylation	EKTEESPSAPDAPTC CCCCCCCCCCCCCCC	62.81	OGP
325	Phosphorylation	CPKQCRRTGTLQSNF CCHHHCCCCCCCCCC	18.37	29083192
327	Phosphorylation	KQCRRTGTLQSNFCA HHHCCCCCCCCCCCC	22.47	29083192
330	Phosphorylation	RRTGTLQSNFCASSL CCCCCCCCCCCCHHH	34.68	29083192
335	Phosphorylation	LQSNFCASSLVVTAT CCCCCCCHHHEEEEE	25.94	29083192
340	Phosphorylation	CASSLVVTATVKSMV CCHHHEEEEEHHHHH	14.77	29083192
342	Phosphorylation	SSLVVTATVKSMVRE HHHEEEEEHHHHHCC	21.07	29083192
398	Phosphorylation	PMKKGVSYLLMGQVE CCCCCCCEEEECCCC	11.05	22817900
430	Phosphorylation	PNQDQILTNLSKRKC CCHHHHHHHHHCCCC	35.42	26270265
431	N-linked_Glycosylation	NQDQILTNLSKRKCP CHHHHHHHHHCCCCC	38.58	UniProtKB CARBOHYD
433	Phosphorylation	DQILTNLSKRKCPSQ HHHHHHHHCCCCCCC	32.27	26270265

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

Oops, there are no upstream regulatory protein records of PCOC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PCOC1_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 PCOC1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PCOC1_HUMAN !!

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.