PADC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PADC1_HUMAN
• UniProt AC: Q9BSG0
• Protein Name: Protease-associated domain-containing protein 1
• Gene Name: PRADC1
• Organism: Homo sapiens (Human).
• Sequence Length: 188
• Subcellular Localization: Secreted .
• Protein Sequence: MVPGAAGWCCLVLWLPACVAAHGFRIHDYLYFQVLSPGDIRYIFTATPAKDFGGIFHTRYEQIHLVPAEPPEACGELSNGFFIQDQIALVERGGCSFLSKTRVVQEHGGRAVIISDNAVDNDSFYVEMIQDSTQRTADIPALFLLGRDGYMIRRSLEQHGLPWAIISIPVNVTSIPTFELLQPPWTFW

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
50	Ubiquitination	IFTATPAKDFGGIFH EEEECCCHHCCCEEE	55.59	22817900
50	Ubiquitination	IFTATPAKDFGGIFH EEEECCCHHCCCEEE	55.59	21890473
100	Ubiquitination	GGCSFLSKTRVVQEH CCCCCCCCCEEEEEE	42.36	21963094
121	N-linked_Glycosylation	ISDNAVDNDSFYVEM ECCCCCCCCCEEEEE	39.98	-
121	N-linked_Glycosylation	ISDNAVDNDSFYVEM ECCCCCCCCCEEEEE	39.98	15498570
171	N-linked_Glycosylation	AIISIPVNVTSIPTF EEEEEECCCCCCCCC	26.45	15498570
171	N-linked_Glycosylation	AIISIPVNVTSIPTF EEEEEECCCCCCCCC	26.45	15498570

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

Oops, there are no upstream regulatory protein records of PADC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PADC1_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 PADC1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PADC1_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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"N-glycosylation is required for efficient secretion of a novel humansecreted glycoprotein, hPAP21.";
Zhou Y.-B., Liu F., Zhu Z.-D., Zhu H., Zhang X., Wang Z.-Q.,Liu J.-H., Han Z.-G.;
FEBS Lett. 576:401-407(2004).
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-171,PROBABLE ABSENCE OF GLYCOSYLATION AT ASN-121, AND MUTAGENESIS OFASN-121 AND ASN-171.
PubMed: 15498570