PRDC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PRDC1_HUMAN
• UniProt AC: Q9NRG1
• Protein Name: Phosphoribosyltransferase domain-containing protein 1
• Gene Name: PRTFDC1
• Organism: Homo sapiens (Human).
• Sequence Length: 225
• Protein Description: Has low, barely detectable phosphoribosyltransferase activity (in vitro). Binds GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). Is not expected to contribute to purine metabolism or GMP salvage..
• Protein Sequence: MAGSSEEAPDYGRGVVIMDDWPGYDLNLFTYPQHYYGDLEYVLIPHGIIVDRIERLAKDIMKDIGYSDIMVLCVLKGGYKFCADLVEHLKNISRNSDRFVSMKVDFIRLKSYRNDQSMGEMQIIGGDDLSTLAGKNVLIVEDVVGTGRTMKALLSNIEKYKPNMIKVASLLVKRTSRSDGFRPDYAGFEIPNLFVVGYALDYNEYFRDLNHICVINEHGKEKYRV

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	------MAGSSEEAP ------CCCCCCCCC	26.95	22814378
4	Phosphorylation	----MAGSSEEAPDY ----CCCCCCCCCCC	25.66	26852163
5	Phosphorylation	---MAGSSEEAPDYG ---CCCCCCCCCCCC	38.24	26852163
67	Phosphorylation	IMKDIGYSDIMVLCV HHHHCCCCCCHHHHH	18.56	20068231
130	Phosphorylation	IIGGDDLSTLAGKNV EECCCCHHHHCCCCE	28.50	-
160	Phosphorylation	LLSNIEKYKPNMIKV HHHHHHHHCCCHHHH	20.91	-
173	Ubiquitination	KVASLLVKRTSRSDG HHHHHHHHHCCCCCC	50.34	21890473
205	Phosphorylation	YALDYNEYFRDLNHI EEECHHHHCCCCCCE	10.56	-

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

Oops, there are no upstream regulatory protein records of PRDC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PRDC1_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 PRDC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NIF3L_HUMAN	NIF3L1	physical	16189514
FAD1_HUMAN	FLAD1	physical	16189514
EF2KT_HUMAN	EEF2KMT	physical	16189514
RTN3_HUMAN	RTN3	physical	22939629
MCMBP_HUMAN	MCMBP	physical	25416956
EF2KT_HUMAN	EEF2KMT	physical	25416956
LEG9B_HUMAN	LGALS9B	physical	25416956
TM14B_HUMAN	TMEM14B	physical	21516116

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

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330