BPIA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BPIA2_HUMAN
• UniProt AC: Q96DR5
• Protein Name: BPI fold-containing family A member 2
• Gene Name: BPIFA2
• Organism: Homo sapiens (Human).
• Sequence Length: 249
• Subcellular Localization: Secreted.
• Protein Description: Has strong antibacterial activity against P. aeruginosa..
• Protein Sequence: MLQLWKLVLLCGVLTGTSESLLDNLGNDLSNVVDKLEPVLHEGLETVDNTLKGILEKLKVDLGVLQKSSAWQLAKQKAQEAEKLLNNVISKLLPTNTDIFGLKISNSLILDVKAEPIDDGKGLNLSFPVTANVTVAGPIIGQIINLKASLDLLTAVTIETDPQTHQPVAVLGECASDPTSISLSLLDKHSQIINKFVNSVINTLKSTVSSLLQKEICPLIRIFIHSLDVNVIQQVVDNPQHKTQLQTLI

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
124	N-linked_Glycosylation	IDDGKGLNLSFPVTA CCCCCCCCEECEEEE	42.16	16740002
132	N-linked_Glycosylation	LSFPVTANVTVAGPI EECEEEECEEEECCH	22.19	16740002
210	Phosphorylation	TLKSTVSSLLQKEIC HHHHHHHHHHHHHHH	28.85	24719451

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

Oops, there are no upstream regulatory protein records of BPIA2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BPIA2_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 BPIA2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of BPIA2_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

"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-124 AND ASN-132, AND MASSSPECTROMETRY.
PubMed: 16740002