PAI2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAI2B_HUMAN
• UniProt AC: Q9ULR5
• Protein Name: Polyadenylate-binding protein-interacting protein 2B
• Gene Name: PAIP2B
• Organism: Homo sapiens (Human).
• Sequence Length: 123
• Protein Description: Inhibits translation of capped and polyadenylated mRNAs by displacing PABPC1 from the poly(A) tail..
• Protein Sequence: MNGSNMANTSPSVKSKEDQGLSGHDEKENPFAEYMWMENEEDFNRQVEEELQEQDFLDRCFQEMLDEEDQDWFIPSRDLPQAMGQLQQQLNGLSVSEGHDSEDILSKSNLNPDAKEFIPGEKY

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
1	Acetylation	-------MNGSNMAN -------CCCCCCCC	13.30	19413330
4	Phosphorylation	----MNGSNMANTSP ----CCCCCCCCCCC	20.59	21406692
9	Phosphorylation	NGSNMANTSPSVKSK CCCCCCCCCCCCCCH	32.26	22199227
10	Phosphorylation	GSNMANTSPSVKSKE CCCCCCCCCCCCCHH	18.25	25849741
12	Phosphorylation	NMANTSPSVKSKEDQ CCCCCCCCCCCHHHC	41.78	22199227
15	Phosphorylation	NTSPSVKSKEDQGLS CCCCCCCCHHHCCCC	38.84	24043423
34	Phosphorylation	KENPFAEYMWMENEE CCCCHHHHHHHHCHH	7.83	28796482

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

Oops, there are no upstream regulatory protein records of PAI2B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAI2B_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 PAI2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PABP1_HUMAN	PABPC1	physical	16804161

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

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY.
PubMed: 19413330