PPAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPAP_HUMAN
• UniProt AC: P15309
• Protein Name: Prostatic acid phosphatase
• Gene Name: ACPP
• Organism: Homo sapiens (Human).
• Sequence Length: 386
• Subcellular Localization: Isoform 1: Secreted .; Isoform 2: Cell membrane ; Single-pass type I membrane protein . Lysosome membrane ; Single-pass type I membrane protein . Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell
• Protein Description: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.; Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling..
• Protein Sequence: MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD

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
94	N-linked_Glycosylation	KRYRKFLNESYKHEQ HHHHHHHCHHCCCCC	39.02	10639192
96	Phosphorylation	YRKFLNESYKHEQVY HHHHHCHHCCCCCEE	38.11	23532336
171	Phosphorylation	FQELESETLKSEEFQ HHHHHHHCCCCHHHH	49.09	46157985
220	N-linked_Glycosylation	LYCESVHNFTLPSWA CEECCCCCCCCCCCC	29.46	12525165
231	Phosphorylation	PSWATEDTMTKLREL CCCCCHHHHHHHHHH	22.10	11362225
233	Phosphorylation	WATEDTMTKLRELSE CCCHHHHHHHHHHHH	29.08	11362235
239	Phosphorylation	MTKLRELSELSLLSL HHHHHHHHHHHHHHH	31.57	7295967
333	N-linked_Glycosylation	FVEMYYRNETQHEPY EEEEEEECCCCCCCC	40.31	12525165

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PPAP_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 PPAP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPAP_HUMAN	ACPP	physical	9804805

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

"Crystal structures of human prostatic acid phosphatase in complexwith a phosphate ion and alpha-benzylaminobenzylphosphonic acid updatethe mechanistic picture and offer new insights into inhibitordesign.";
Ortlund E., LaCount M.W., Lebioda L.;
Biochemistry 42:383-389(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-386 IN COMPLEX WITH APHOSPHATE ION AND INHIBITOR ALPHA-BENZYLAMINOBENZYLPHOSPHONIC ACID,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-220 AND ASN-333.
PubMed: 12525165

"Crystal structure of human prostatic acid phosphatase.";
Jakob C.G., Lewinski K., Kuciel R., Ostrowski W., Lebioda L.;
Prostate 42:211-218(2000).
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 33-374, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-94 AND ASN-220.
PubMed: 10639192