dbPTM

PPIA_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPIA_DROME
UniProt AC	P25007
Protein Name	Peptidyl-prolyl cis-trans isomerase
Gene Name	Cyp1
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	227
Subcellular Localization	Cytoplasm.
Protein Description	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides..
Protein Sequence	MVSFCATLIRQFRHRSAAAFQIAESAILANKSITLASSACSVNRGQLQFGIQIVREYSKASKMSTLPRVFFDMTADNEPLGRIVMELRSDVVPKTAENFRALCTGEKGFGYKGSIFHRVIPNFMCQGGDFTNHNGTGGKSIYGNKFPDENFELKHTGSGILSMANAGANTNGSQFFICTVKTAWLDNKHVVFGEVVEGLDVVKKIESYGSQSGKTSKKIIVANSGSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
94	Acetylation	LRSDVVPKTAENFRA HHCCCCCCHHHHHHH	49.08	21791702
107	Acetylation	RALCTGEKGFGYKGS HHHHCCCCCCCCCCC	61.97	21791702
112	Acetylation	GEKGFGYKGSIFHRV CCCCCCCCCCEEEEE	46.70	21791702
145	Acetylation	GKSIYGNKFPDENFE CCCCCCCCCCCCCCE	54.64	21791702
156	Phosphorylation	ENFELKHTGSGILSM CCCEECCCCCCHHHC	31.30	21082442
158	Phosphorylation	FELKHTGSGILSMAN CEECCCCCCHHHCCC	24.66	18327897
181	Acetylation	QFFICTVKTAWLDNK CEEEEEEEEEEECCC	17.86	21791702
210	Phosphorylation	KKIESYGSQSGKTSK HHHHHCCCCCCCCCC	16.97	19429919
212	Phosphorylation	IESYGSQSGKTSKKI HHHCCCCCCCCCCEE	43.91	19429919
214	Acetylation	SYGSQSGKTSKKIIV HCCCCCCCCCCEEEE	55.67	21791702
226	Phosphorylation	IIVANSGSL------ EEEECCCCC------	30.63	19060867

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of PPIA_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PPIA_DROME !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PPIA_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FKB12_DROME	FK506-bp2	physical	22036573
CALR_DROME	Crc	physical	22036573
SH3BG_DROME	Sh3beta	physical	22036573
THIO2_DROME	Trx-2	physical	22036573
TNG2_DROME	Tango2	physical	22036573
NLP_DROME	Nlp	physical	22036573

Drug and Disease Associations

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

Regulatory Network of PPIA_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND MASSSPECTROMETRY.	18327897 [Abstract]