dbPTM

PAN3L_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAN3L_SCHPO
UniProt AC	O13865
Protein Name	PAB-dependent poly(A)-specific ribonuclease subunit pan3-like
Gene Name	SPAC1B1.04c
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	681
Subcellular Localization	Cytoplasm .
Protein Description	Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex..
Protein Sequence	MDERRSSIFSTNIPCRNEQLYGRCPYIDKGCFFQHKNQDNAPASSKPPSATAIDPQNSGFSTKLSINSPSFTPLKLSKTSISSASNKESVPLTRPKSYSSALSSGKNGAAAQQAANSPKTVSLMTSSSKAANALQTHKSSLARAASAVPFSPSKATTVSLKESASLTSLSNNKSVSNLNSISGASSPSGSLVNLHSLTRSASFVPQPSVPNSGQLSNADMSRHILARFPPFFHNLNEQQQKTTSFFLADDHLKWFTYLTQEFYQFANIPKLPSHVLSYHSLIPRRMIVTVLPVLRYATSIYKVIDGNNGLPYSFVQLRDFTLLNDRNITNVSPWTKVDSPHVIKIREAFTTHAFEQKSIVFVYNYLPSCPSLYDLFFASPVFRKRTSSFYFSQPLKATKEVLWCFASQLISALYSIHSSGLAAKMVSLKNVLMVGKMRLAIFGLGIMDVIQEESTEPLTSLQRNDCRDVGLILLALATDTENVTLSTAKAHLTRLKTIVSTDASLVELIEVLIFNEELRIQTLLPTMLSYMVNNYESVLLMEDVYETYLAEQVENDRLLRLLLKLEFLDDRPEYVDDPDWSASGVYFVIRLFRKYMFQVQTIDDASKKPTLQSTTTPPRKLLNKAHLLSCLNKLDAGTDEQILLEDEFTRIIMSFKEVKTTINTAFMELERRCSNNLSVKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MDERRSSIFSTNI --CCHHHHHCCCCCC	33.72	29996109
7	Phosphorylation	-MDERRSSIFSTNIP -CCHHHHHCCCCCCC	26.33	29996109
68	Phosphorylation	STKLSINSPSFTPLK CCEEEECCCCCCCEE	21.91	25720772
70	Phosphorylation	KLSINSPSFTPLKLS EEEECCCCCCCEEEC	41.39	25720772
117	Phosphorylation	AAQQAANSPKTVSLM HHHHHHCCCCCEEEE	24.05	21712547
151	Phosphorylation	AASAVPFSPSKATTV HHHCCCCCCCCCEEE	23.38	24763107
153	Phosphorylation	SAVPFSPSKATTVSL HCCCCCCCCCEEEEH	33.45	29996109
163	Phosphorylation	TTVSLKESASLTSLS EEEEHHHHHCCEECC	22.90	24763107
165	Phosphorylation	VSLKESASLTSLSNN EEHHHHHCCEECCCC	41.27	28889911
167	Phosphorylation	LKESASLTSLSNNKS HHHHHCCEECCCCCC	25.73	21712547
168	Phosphorylation	KESASLTSLSNNKSV HHHHCCEECCCCCCC	34.78	21712547
174	Phosphorylation	TSLSNNKSVSNLNSI EECCCCCCCCCCCCC	32.66	25720772
182	Phosphorylation	VSNLNSISGASSPSG CCCCCCCCCCCCCCC	28.29	29996109
185	Phosphorylation	LNSISGASSPSGSLV CCCCCCCCCCCCCEE	46.43	29996109
186	Phosphorylation	NSISGASSPSGSLVN CCCCCCCCCCCCEEE	23.66	25720772
188	Phosphorylation	ISGASSPSGSLVNLH CCCCCCCCCCEEEHH	42.85	25720772
190	Phosphorylation	GASSPSGSLVNLHSL CCCCCCCCEEEHHHC	33.22	25720772
200	Phosphorylation	NLHSLTRSASFVPQP EHHHCCCCCCCCCCC	24.03	27738172

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
Oops, there are no upstream regulatory protein records of PAN3L_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PAN3L_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PAN3L_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PAN3L_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of PAN3L_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-165, AND MASSSPECTROMETRY.	18257517 [Abstract]