dbPTM

SAP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAP_MOUSE
UniProt AC	Q61207
Protein Name	Prosaposin
Gene Name	Psap
Organism	Mus musculus (Mouse).
Sequence Length	557
Subcellular Localization	Prosaposin: Secreted . Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. Lysosome .
Protein Description	Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.; Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.; Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.; Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).; Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases..
Protein Sequence	MYALALFASLLATALTSPVQDPKTCSGGSAVLCRDVKTAVDCGAVKHCQQMVWSKPTAKSLPCDICKTVVTEAGNLLKDNATQEEILHYLEKTCEWIHDSSLSASCKEVVDSYLPVILDMIKGEMSNPGEVCSALNLCQSLQEYLAEQNQKQLESNKIPEVDMARVVAPFMSNIPLLLYPQDHPRSQPQPKANEDVCQDCMKLVSDVQTAVKTNSSFIQGFVDHVKEDCDRLGPGVSDICKNYVDQYSEVCVQMLMHMQDQQPKEICVLAGFCNEVKRVPMKTLVPATETIKNILPALEMMDPYEQNLVQAHNVILCQTCQFVMNKFSELIVNNATEELLVKGLSNACALLPDPARTKCQEVVGTFGPSLLDIFIHEVNPSSLCGVIGLCAARPELVEALEQPAPAIVSALLKEPTPPKQPAQPKQSALPAHVPPQKNGGFCEVCKKLVLYLEHNLEKNSTKEEILAALEKGCSFLPDPYQKQCDDFVAEYEPLLLEILVEVMDPGFVCSKIGVCPSAYKLLLGTEKCVWGPSYWCQNMETAARCNAVDHCKRHVWN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MYALALFAS ------CHHHHHHHH	15.43	25777480
9	Phosphorylation	YALALFASLLATALT HHHHHHHHHHHHHHC	19.31	25777480
13	Phosphorylation	LFASLLATALTSPVQ HHHHHHHHHHCCCCC	23.36	25777480
16	Phosphorylation	SLLATALTSPVQDPK HHHHHHHCCCCCCCC	28.64	25777480
17	Phosphorylation	LLATALTSPVQDPKT HHHHHHCCCCCCCCC	24.75	25777480
80	N-linked_Glycosylation	AGNLLKDNATQEEIL HHHHHCCCCCHHHHH	43.21	19349973
214	N-linked_Glycosylation	VQTAVKTNSSFIQGF HHHHHHCCCHHHHHH	29.91	-
237	Phosphorylation	DRLGPGVSDICKNYV HHHCCCHHHHHHHHH	27.46	22324799
334	N-linked_Glycosylation	FSELIVNNATEELLV CHHHHHCCCCHHHHH	37.03	19349973
446	Acetylation	GGFCEVCKKLVLYLE CCHHHHHHHHHHHHH	55.08	23576753
459	N-linked_Glycosylation	LEHNLEKNSTKEEIL HHHHCCCCCCHHHHH	45.60	-
460	O-linked_Glycosylation	EHNLEKNSTKEEILA HHHCCCCCCHHHHHH	52.50	30059200

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 SAP_MOUSE !!

Functions of PTM Sites

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

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 SAP_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SEM4A_MOUSE	Sema4a	physical	22465952
SORT_MOUSE	Sort1	physical	22465952

Drug and Disease Associations

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

Regulatory Network of SAP_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-334, AND MASSSPECTROMETRY.	19349973 [Abstract]