PAN3_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAN3_SCHPO
• UniProt AC: Q9UST1
• Protein Name: PAN2-PAN3 deadenylation complex subunit pan3 {ECO:0000255|HAMAP-Rule:MF_03181}
• Gene Name: ppk26
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 589
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. ppk26/pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1..
• Protein Sequence: MSVRKNSPASPKPTSRSRESSRSPSVTDLKDHSKAKRTLCRNILLYGSCKHSENGCAFRHDGPFIPSSENLEQYSVKKKLNAASASFQPVRALPVKAAGAAVFVPKSQEKSLFLSRERTPVALSPGSHAINPYNNASMLVNEPFHDDSGVYYTRQNQFKPTLYNLYNPQPSPMPTLLPYERTVNGLFIDDTTRERIERKSEASRQTISALPSIISSYTSLAPLNTKLYRYKEQIGFSSWTYKCTSSIDGNAYVLKRLQDCSINIDTSTVDKLKNVFHPNIVPFHSAFHTDTFHDSSLLLIYDFYPCTTTLGELYLNNSKNSVKLEENRKIPERELWNYFFQLTIALSYLHKSGFACNKLTPSRILVDQTERIRISGCADYELVVSNKPPLEERKKQDFVDLGVVIANLATGRTDMDMSSAARAIYSTYSREFYKAVLYFVSEVPEDKNLELFLQNHIESFFPIMSSPYVECEKMERKISDAFQHGRFFNILCKIMFIIDNNRASREYPIAREKEISLIYLLRDYLFHQIDEDECPVIDLYQVLNRLGKLDAGINQAIALISRDELDCVSVSYGELKAWLDNVYEMEINS

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
7	Phosphorylation	-MSVRKNSPASPKPT -CCCCCCCCCCCCCC	25.52	29996109
10	Phosphorylation	VRKNSPASPKPTSRS CCCCCCCCCCCCCCC	36.52	25720772
15	Phosphorylation	PASPKPTSRSRESSR CCCCCCCCCCCCCCC	36.46	29996109
20	Phosphorylation	PTSRSRESSRSPSVT CCCCCCCCCCCCCCC	29.91	29996109
21	Phosphorylation	TSRSRESSRSPSVTD CCCCCCCCCCCCCCC	31.83	29996109
23	Phosphorylation	RSRESSRSPSVTDLK CCCCCCCCCCCCCCC	24.39	29996109
25	Phosphorylation	RESSRSPSVTDLKDH CCCCCCCCCCCCCCC	38.61	29996109
27	Phosphorylation	SSRSPSVTDLKDHSK CCCCCCCCCCCCCHH	39.70	25720772
127	Phosphorylation	PVALSPGSHAINPYN CCEECCCCCCCCCCC	17.09	29996109

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

Oops, there are no upstream regulatory protein records of PAN3_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAN3_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 PAN3_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YBAC_SCHPO	rud3	genetic	18931302
ASK1_SCHPO	ask1	genetic	18931302
ELP3_SCHPO	elp3	genetic	18931302
EHS1_SCHPO	yam8	genetic	18931302
DAD2_SCHPO	dad2	genetic	18931302
YFE6_SCHPO	gmh5	genetic	18931302

Drug and Disease Associations

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