PABP_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PABP_SCHPO
• UniProt AC: P31209
• Protein Name: Polyadenylate-binding protein, cytoplasmic and nuclear
• Gene Name: pab1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 653
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN (By similarity)..
• Protein Sequence: MPSTDLKKQADAAVESDVNTNNEAVESSTKEESSNTPSTETQPEKKAEEPEAAAEPSESTSTPTNASSVATPSGTAPTSASLYVGELDPSVTEAMLFELFNSIGPVASIRVCRDAVTRRSLGYAYVNFHNMEDGEKALDELNYTLIKGRPCRIMWSQRDPSLRKMGTGNVFIKNLDPAIDNKALHDTFSAFGKILSCKVAVDELGNAKGYGFVHFDSVESANAAIEHVNGMLLNDKKVYVGHHVSRRERQSKVEALKANFTNVYIKNLDTEITEQEFSDLFGQFGEITSLSLVKDQNDKPRGFGFVNYANHECAQKAVDELNDKEYKGKKLYVGRAQKKHEREEELRKRYEQMKLEKMNKYQGVNLFIKNLQDEVDDERLKAEFSAFGTITSAKIMTDEQGKSKGFGFVCYTTPEEANKAVTEMNQRMLAGKPLYVALAQRKEVRRSQLEAQIQARNQFRLQQQVAAAAGIPAVQYGATGPLIYGPGGYPIPAAVNGRGMPMVPGHNGPMPMYPGMPTQFPAGGPAPGYPGMNARGPVPAQGRPMMMPGSVPSAGPAEAEAVPAVPGMPERFTAADLAAVPEESRKQVLGELLYPKVFVREEKLSGKITGMLLEMPNSELLELLEDDSALNERVNEAIGVLQEFVDQEPGFTE

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
16	Phosphorylation	QADAAVESDVNTNNE HHHHHHHCCCCCCCH	40.01	28889911
20	Phosphorylation	AVESDVNTNNEAVES HHHCCCCCCCHHHHH	38.99	24763107
27	Phosphorylation	TNNEAVESSTKEESS CCCHHHHHHCCCCCC	36.39	21712547
28	Phosphorylation	NNEAVESSTKEESSN CCHHHHHHCCCCCCC	29.96	21712547
33	Phosphorylation	ESSTKEESSNTPSTE HHHCCCCCCCCCCCC	29.94	21712547
34	Phosphorylation	SSTKEESSNTPSTET HHCCCCCCCCCCCCC	48.26	29996109
36	Phosphorylation	TKEESSNTPSTETQP CCCCCCCCCCCCCCC	22.14	21712547
38	Phosphorylation	EESSNTPSTETQPEK CCCCCCCCCCCCCCH	36.52	29996109
167	Phosphorylation	PSLRKMGTGNVFIKN HHHHCCCCCCEEEEC	23.29	28889911
245	Phosphorylation	VYVGHHVSRRERQSK EECCCCCCHHHHHHH	22.66	29996109
447	Phosphorylation	QRKEVRRSQLEAQIQ HCHHHHHHHHHHHHH	28.66	25720772
550	Phosphorylation	RPMMMPGSVPSAGPA CCCCCCCCCCCCCHH	25.61	27738172
553	Phosphorylation	MMPGSVPSAGPAEAE CCCCCCCCCCHHHHH	43.64	27738172
618	Phosphorylation	MLLEMPNSELLELLE EEEECCCHHHHHHHC	24.61	29996109
628	Phosphorylation	LELLEDDSALNERVN HHHHCCCHHHHHHHH	47.15	29996109
652	Phosphorylation	VDQEPGFTE------ HHCCCCCCC------	46.85	25720772

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PABP_SCHPO !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of PABP_SCHPO !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND MASSSPECTROMETRY.
PubMed: 18257517