PIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIP_HUMAN
• UniProt AC: P12273
• Protein Name: Prolactin-inducible protein
• Gene Name: PIP
• Organism: Homo sapiens (Human).
• Sequence Length: 146
• Subcellular Localization: Secreted.
• Protein Sequence: MRLLQLLFRASPATLLLVLCLQLGANKAQDNTRKIIIKNFDIPKSVRPNDEVTAVLAVQTELKECMVVKTYLISSIPLQGAFNYKYTACLCDDNPKTFYWDFYTNRTVQIAAVVDVIRELGICPDDAAVIPIKNNRFYTIEILKVE

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
29	Pyrrolidone_carboxylic_acid	QLGANKAQDNTRKII HHCCCCCCCCCCEEE	46.20	-
29	Pyrrolidone_carboxylic_acid	QLGANKAQDNTRKII HHCCCCCCCCCCEEE	46.20	2013294
29	Pyrrolidone_carboxylic_acid	QLGANKAQDNTRKII HHCCCCCCCCCCEEE	46.20	2013294
45	Phosphorylation	KNFDIPKSVRPNDEV ECCCCCCCCCCCCCH	20.29	20068231
53	Phosphorylation	VRPNDEVTAVLAVQT CCCCCCHHEEEEEEE	14.70	20068231
60	Phosphorylation	TAVLAVQTELKECMV HEEEEEEECHHHCCE	36.36	20068231
84	Phosphorylation	PLQGAFNYKYTACLC CCCCCCCCEEEEEEE	10.02	22817900
105	N-linked_Glycosylation	FYWDFYTNRTVQIAA EEEEECCCCEEHHHH	26.67	18930737
105	N-linked_Glycosylation	FYWDFYTNRTVQIAA EEEEECCCCEEHHHH	26.67	18780401
139	Phosphorylation	IKNNRFYTIEILKVE EECCEEEEEEEEEEC	14.93	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIP_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 PIP_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PIP_HUMAN !!

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 structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from humanseminal plasma.";
Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P.,Singh T.P.;
J. Mol. Biol. 384:663-672(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-146 IN COMPLEX WITH AZGP1,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105.
PubMed: 18930737

"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASSSPECTROMETRY.
PubMed: 18780401

"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASSSPECTROMETRY.
PubMed: 16740002

"Primary structure of a new actin-binding protein from human seminalplasma.";
Schaller J., Akiyama K., Kimura H., Hess D., Affolter M., Rickli E.E.;
Eur. J. Biochem. 196:743-750(1991).
Cited for: PROTEIN SEQUENCE OF 29-146, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-105.
PubMed: 2013294

Pyrrolidone carboxylic acid

"Primary structure of a new actin-binding protein from human seminalplasma.";
Schaller J., Akiyama K., Kimura H., Hess D., Affolter M., Rickli E.E.;
Eur. J. Biochem. 196:743-750(1991).
Cited for: PROTEIN SEQUENCE OF 29-146, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-105.
PubMed: 2013294