BPIB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BPIB2_HUMAN
• UniProt AC: Q8N4F0
• Protein Name: BPI fold-containing family B member 2
• Gene Name: BPIFB2
• Organism: Homo sapiens (Human).
• Sequence Length: 458
• Subcellular Localization: Secreted.
• Protein Sequence: MAWASRLGLLLALLLPVVGASTPGTVVRLNKAALSYVSEIGKAPLQRALQVTVPHFLDWSGEALQPTRIRILNVHVPRLHLKFIAGFGVRLLAAANFTFKVFRAPEPLELTLPVELLADTRVTQSSIRTPVVSISACSLFSGHANEFDGSNSTSHALLVLVQKHIKAVLSNKLCLSISNLVQGVNVHLGTLIGLNPVGPESQIRYSMVSVPTVTSDYISLEVNAVLFLLGKPIILPTDATPFVLPRHVGTEGSMATVGLSQQLFDSALLLLQKAGALNLDITGQLRSDDNLLNTSALGRLIPEVARQFPEPMPVVLKVRLGATPVAMLHTNNATLRLQPFVEVLATASNSAFQSLFSLDVVVNLRLQLSVSKVKLQGTTSVLGDVQLTVASSNVGFIDTDQVRTLMGTVFEKPLLDHLNALLAMGIALPGVVNLHYVAPEIFVYEGYVVISSGLFYQS

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
25	Phosphorylation	VGASTPGTVVRLNKA HCCCCCCHHHHCCHH	19.61	22210691
35	Phosphorylation	RLNKAALSYVSEIGK HCCHHHHHHHHHHCC	20.82	-
36	Phosphorylation	LNKAALSYVSEIGKA CCHHHHHHHHHHCCC	14.62	-
38	Phosphorylation	KAALSYVSEIGKAPL HHHHHHHHHHCCCHH	18.44	22210691
52	Phosphorylation	LQRALQVTVPHFLDW HHHHHHCCCCCCCCC	18.50	26091039
60	Phosphorylation	VPHFLDWSGEALQPT CCCCCCCCCCCCCCE	26.82	26091039
96	N-linked_Glycosylation	VRLLAAANFTFKVFR HHHHHHCCCEEEEEE	31.59	16740002
96	N-linked_Glycosylation	VRLLAAANFTFKVFR HHHHHHCCCEEEEEE	31.59	17623646
151	N-linked_Glycosylation	ANEFDGSNSTSHALL CCCCCCCCCHHHHHH	55.63	UniProtKB CARBOHYD
209	Phosphorylation	QIRYSMVSVPTVTSD HHCEEEEECCCCCCC	17.46	25332170
212	Phosphorylation	YSMVSVPTVTSDYIS EEEEECCCCCCCCEE	33.97	25332170
293	N-linked_Glycosylation	RSDDNLLNTSALGRL CCCCCCCCHHHHHHH	34.84	17623646
293	N-linked_Glycosylation	RSDDNLLNTSALGRL CCCCCCCCHHHHHHH	34.84	16740002
330	Phosphorylation	TPVAMLHTNNATLRL CEEEEEECCCCEEEC	26.63	-
332	N-linked_Glycosylation	VAMLHTNNATLRLQP EEEEECCCCEEECHH	35.14	16740002
332	N-linked_Glycosylation	VAMLHTNNATLRLQP EEEEECCCCEEECHH	35.14	17623646
334	Phosphorylation	MLHTNNATLRLQPFV EEECCCCEEECHHHH	17.97	-
346	Phosphorylation	PFVEVLATASNSAFQ HHHHHHHHCCCHHHH	26.85	27174698
348	Phosphorylation	VEVLATASNSAFQSL HHHHHHCCCHHHHHH	27.28	27174698
350	Phosphorylation	VLATASNSAFQSLFS HHHHCCCHHHHHHCC	28.15	27174698
354	Phosphorylation	ASNSAFQSLFSLDVV CCCHHHHHHCCCHHE	25.57	27174698
357	Phosphorylation	SAFQSLFSLDVVVNL HHHHHHCCCHHEEEE	29.02	27174698
369	Phosphorylation	VNLRLQLSVSKVKLQ EEEEEEEEEEEEEEE	16.04	24719451
371	Phosphorylation	LRLQLSVSKVKLQGT EEEEEEEEEEEEECC	28.49	27174698

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
52	T	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot
60	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BPIB2_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 BPIB2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of BPIB2_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-96; ASN-293 AND ASN-332,AND MASS SPECTROMETRY.
PubMed: 16740002