PRP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PRP1_HUMAN
• UniProt AC: P04280
• Protein Name: Basic salivary proline-rich protein 1
• Gene Name: PRB1
• Organism: Homo sapiens (Human).
• Sequence Length: 392
• Subcellular Localization: Secreted .
• Protein Sequence: MLLILLSVALLALSSAQNLNEDVSQEESPSLIAGNPQGPSPQGGNKPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSRSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSQSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSQSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPQQGGNRPQGPPPPGKPQGPPPQGDKSRSPQSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPAQGGSKSQSARSPPGKPQGPPQQEGNNPQGPPPPAGGNPQQPQAPPAGQPQGPPRPPQGGRPSRPPQ

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
17	Pyrrolidone_carboxylic_acid	LLALSSAQNLNEDVS HHHHHHHHCCCCCCC	57.82	-
17	Pyrrolidone_carboxylic_acid	LLALSSAQNLNEDVS HHHHHHHHCCCCCCC	57.82	20879038
17	Pyrrolidone_carboxylic_acid	LLALSSAQNLNEDVS HHHHHHHHCCCCCCC	57.82	20879038
24	Phosphorylation	QNLNEDVSQEESPSL HCCCCCCCCCCCCCH	44.17	3521730
40	Phosphorylation	AGNPQGPSPQGGNKP CCCCCCCCCCCCCCC	36.36	20879038
40	O-linked_Glycosylation	AGNPQGPSPQGGNKP CCCCCCCCCCCCCCC	36.36	20879038
87	O-linked_Glycosylation	PPPQGDKSRSPRSPP CCCCCCCCCCCCCCC	42.61	20879038
87	Phosphorylation	PPPQGDKSRSPRSPP CCCCCCCCCCCCCCC	42.61	19651622
89	Phosphorylation	PQGDKSRSPRSPPGK CCCCCCCCCCCCCCC	31.58	19651622
92	Phosphorylation	DKSRSPRSPPGKPQG CCCCCCCCCCCCCCC	38.54	19651622
150	O-linked_Glycosylation	PQGDKSQSPRSPPGK CCCCCCCCCCCCCCC	29.40	20879038
150	Phosphorylation	PQGDKSQSPRSPPGK CCCCCCCCCCCCCCC	29.40	6089212
153	Phosphorylation	DKSQSPRSPPGKPQG CCCCCCCCCCCCCCC	38.54	21299198
211	Phosphorylation	PQGDKSQSPRSPPGK CCCCCCCCCCCCCCC	29.40	6089212
214	Phosphorylation	DKSQSPRSPPGKPQG CCCCCCCCCCCCCCC	38.54	21299198
330	O-linked_Glycosylation	GPPAQGGSKSQSARS CCCCCCCCCCCCCCC	35.64	-
330	Phosphorylation	GPPAQGGSKSQSARS CCCCCCCCCCCCCCC	35.64	24505115
388	Phosphorylation	PPQGGRPSRPPQ--- CCCCCCCCCCCC---	56.93	21299198

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

Oops, there are no upstream regulatory protein records of PRP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
87	S	Glycosylation	O-glycosylation on Ser-87 is prevalent in head and neck cancer patients.	20879038
330	S	Glycosylation	O-Glycosylation on Ser-330 has a 5 times prevalence in head and neck cancers.	20879038

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PRP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBQL1_HUMAN	UBQLN1	physical	25416956

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

O-linked Glycosylation

"Finding new posttranslational modifications in salivary proline-richproteins.";
Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C.,Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L.;
Proteomics 10:3732-3742(2010).
Cited for: GLYCOSYLATION AT SER-40; SER-87 AND SER-150, PHOSPHORYLATION ATSER-40; SER-92 AND SER-150, PYROGLUTAMATE FORMATION AT GLN-17, MASSSPECTROMETRY, AND VARIANTS ALLELE M AND S AND CLONE CP-5.
PubMed: 20879038

Phosphorylation

"Finding new posttranslational modifications in salivary proline-richproteins.";
Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C.,Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L.;
Proteomics 10:3732-3742(2010).
Cited for: GLYCOSYLATION AT SER-40; SER-87 AND SER-150, PHOSPHORYLATION ATSER-40; SER-92 AND SER-150, PYROGLUTAMATE FORMATION AT GLN-17, MASSSPECTROMETRY, AND VARIANTS ALLELE M AND S AND CLONE CP-5.
PubMed: 20879038