MPRD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MPRD_HUMAN
• UniProt AC: P20645
• Protein Name: Cation-dependent mannose-6-phosphate receptor
• Gene Name: M6PR
• Organism: Homo sapiens (Human).
• Sequence Length: 277
• Subcellular Localization: Lysosome membrane; Single-pass type I membrane protein.
• Protein Description: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex..
• Protein Sequence: MFPFYSCWRTGLLLLLLAVAVRESWQTEEKTCDLVGEKGKESEKELALVKRLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIMLIYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACSPEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGCDFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM

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
38	2-Hydroxyisobutyrylation	TCDLVGEKGKESEKE HCCCCCCCCCCCHHH	70.16	-
44	Ubiquitination	EKGKESEKELALVKR CCCCCCHHHHHHHHH	68.27	-
50	Ubiquitination	EKELALVKRLKPLFN HHHHHHHHHHHHHHH	53.51	-
50	2-Hydroxyisobutyrylation	EKELALVKRLKPLFN HHHHHHHHHHHHHHH	53.51	-
57	N-linked_Glycosylation	KRLKPLFNKSFESTV HHHHHHHHCCCCCCC	46.90	UniProtKB CARBOHYD
63	O-linked_Glycosylation	FNKSFESTVGQGSDT HHCCCCCCCCCCCCE	22.81	OGP
83	N-linked_Glycosylation	RVCREAGNHTSGAGL EEHHHCCCCCCCCCE	42.16	17660510
83	N-linked_Glycosylation	RVCREAGNHTSGAGL EEHHHCCCCCCCCCE	42.16	19349973
94	N-linked_Glycosylation	GAGLVQINKSNGKET CCCEEEEECCCCCEE	25.31	UniProtKB CARBOHYD
107	N-linked_Glycosylation	ETVVGRLNETHIFNG EEEEEEECCEEEECC	51.24	19159218
107	N-linked_Glycosylation	ETVVGRLNETHIFNG EEEEEEECCEEEECC	51.24	19349973
113	N-linked_Glycosylation	LNETHIFNGSNWIML ECCEEEECCCCEEEE	52.99	UniProtKB CARBOHYD
116	N-linked_Glycosylation	THIFNGSNWIMLIYK EEEECCCCEEEEEEE	33.42	-
116	N-linked_Glycosylation	THIFNGSNWIMLIYK EEEECCCCEEEEEEE	33.42	19349973
255	Phosphorylation	PRNVPAAYRGVGDDQ CCCCCHHHCCCCCCC	15.25	28674419
267	Phosphorylation	DDQLGEESEERDDHL CCCCCCCCHHCCCCC	40.22	22167270
277	Sulfoxidation	RDDHLLPM------- CCCCCCCC-------	9.65	21406390

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MPRD_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 MPRD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GGA3_HUMAN	GGA3	physical	11387475
GGA1_HUMAN	GGA1	physical	11387475
GGA2_HUMAN	GGA2	physical	11387475
PLIN3_HUMAN	PLIN3	physical	9590177
GGA1_HUMAN	GGA1	physical	15044437
PPAL_HUMAN	ACP2	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
NDUS4_HUMAN	NDUFS4	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
NDUB4_HUMAN	NDUFB4	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
RL6_HUMAN	RPL6	physical	22939629

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• DrugBank
• DB01272: Alglucosidase alfa

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83 AND ASN-107, AND MASSSPECTROMETRY.
PubMed: 19159218

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASSSPECTROMETRY.
PubMed: 18669648