PAN2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAN2_SCHPO
• UniProt AC: Q09798
• Protein Name: PAN2-PAN3 deadenylation complex catalytic subunit pan2 {ECO:0000255|HAMAP-Rule:MF_03182}
• Gene Name: pan2 {ECO:0000255|HAMAP-Rule:MF_03182}
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1088
• Subcellular Localization: Cytoplasm .
• Protein Description: Catalytic 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..
• Protein Sequence: MDAWKEITKTTENDGVSTCSLSSIAFDPYSELVWTGHKNGQIKSSFGPSLTSYTQFIGHEGPVHQVLPQERGVFSLSSKSLRLSNRKGTIRWRYQDSDCIDYRAMFYQSRNNPEVVIGGYHQKLTVVNAERGISIHKDKNVSDIFIMRRNRLLCCGSTNGEIILRDPNSFQPVNKVVAHTGTISDIDTSGNLLLSCGYSLRHGTYMLDPFVKVWDLRNLSSLVPIPFPAGPTIIRMHPKLSTTAVVCSCSGQFHIVDTGNPLDAKLMQIPLTSYLTGMDIASTGDAMVFTDVEDNIHLWSPLENPSFSDLKLPIQLPNTSTETVQLENNDPLNSIGLPYYKDELLSSWSKYLIFDVGKPILDSNLLIAKQISENSHPVPQEIKSFHRNQIIEVPWLNRKLISEGATPKFHSERQKDIMSGNDIEGSASYFEEIEDTISGPDSIPKFYQRPVIKYSKFGIEDFDFGFYNKTKYAGLETDITNSYCNSVLQLLSYVPSFSKAAISHSLGPCDLMECLLCELGFLFAMLKESTGRNCQATNFLRAFSNSSFAQSLGIVFDDYSDGTFPDSFVIQKFTKFMLTEISRIADYEDKKDGTSFPVSFLLKSFCIPEMQTYRCGICGITSQKIKSSLYIIDLHYPSQQLESILSFEWLFKMSLDRRVDLPPGWCEYCLAHQPFLLRSFIRSLPDCLFINTQVKHHEHWKLWARKNWLPKKLHLRRVNDTMQCVSQKISNLDKDQQSLSVYVLRGIIYEIRQNGEEPHFVSTIRVSDNTSSDNPDDNRWYIFNDFLVKEVTEEEALTVHGPWKIPIIVYYEKLDTKIPQWDEVSDYTLLYQPYSLNKNPPINKIQPLTTDEMLYPKMLVGIDSEFVALQQEETEVRSDGTKSTIKPSKLSLARVSVLRGEGPNKGLPFIDDYVATDDKVTDYLTEYSGIHPGDLDPDRSPYNVVPLKVAYKKLRLLVNAGCIFVGHGLQKDFRIINLLVPPEQVVDTVDLFFLSSRQRKLSLKFLAWYLLDEEIQLTEHDSIEDALTALKLYDCYDKLKSQGKLEETLDNIYEVGRRFKFRPPSVASMSLEDRNSYGDESVISNQTN

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
482	Phosphorylation	LETDITNSYCNSVLQ CCCHHCHHHHHHHHH	23.55	25720772
492	Phosphorylation	NSVLQLLSYVPSFSK HHHHHHHHCCCCCCH	32.45	25720772
493	Phosphorylation	SVLQLLSYVPSFSKA HHHHHHHCCCCCCHH	19.15	25720772
1065	Phosphorylation	RFKFRPPSVASMSLE HCCCCCCCCEECCCC	32.76	25720772
1070	Phosphorylation	PPSVASMSLEDRNSY CCCCEECCCCCCCCC	26.55	24763107

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

Oops, there are no upstream regulatory protein records of PAN2_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAN2_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 PAN2_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of PAN2_SCHPO !!

Drug and Disease Associations

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