YLA3_SCHPO - dbPTM
YLA3_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YLA3_SCHPO
UniProt AC Q9P6K0
Protein Name Uncharacterized HTH La-type RNA-binding protein C1527.03
Gene Name SPAC1527.03
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 475
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MSHKEPSAAETSTVVHSEEDKAFCIGTGAVISEEREKEVLKNLQNSLTGKTAEENLNDEANHTSSDKSKSEDYQPSNVNVWALRKEKMIPKKHSHVKQEKRFSKSLQLQDPNVWPSPEIAEKQVEDRKLSDDSQKPLAPKANGKEKWVTITPNFTHTPISNRKSSRSRNDGSRRNGNGRRRGNYSSHGSNKRQTNYSREKDASRSIDSSNPSAEYRDDINNTFGSQTVSSANGKEVPQTSEDSSSQAPHHSSSSGHAPSQQGGNKHSYKKSDSQQSFHHKGRNTRKGQRHNNGFYRNIANNIQGPFPNYPVVVNGNGVNPYLCDVQAFLTSQLEYYFSIENLCKDMFLRKHMDDEGYVPLAFLASFNRIKSFSTDLNLLHAACKASDIIDVAIDLQSPMSIKVRRKETWSPWILPSESRLKFEMAKYPQINSSSSMSPLASSISNLTISPPFIPSSVDSIIKRDVQTEVEDKLTV
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 Orthologous
Protein Cluster
2Phosphorylation------MSHKEPSAA
------CCCCCCCCC
43.1824763107
7Phosphorylation-MSHKEPSAAETSTV
-CCCCCCCCCCCCCC
41.0021712547
11PhosphorylationKEPSAAETSTVVHSE
CCCCCCCCCCCCCCC
25.6029996109
12PhosphorylationEPSAAETSTVVHSEE
CCCCCCCCCCCCCCC
15.6521712547
13PhosphorylationPSAAETSTVVHSEED
CCCCCCCCCCCCCCC
33.6929996109
46PhosphorylationVLKNLQNSLTGKTAE
HHHHHHHHHCCCCHH
17.8524763107
48PhosphorylationKNLQNSLTGKTAEEN
HHHHHHHCCCCHHHH
36.1325720772
51PhosphorylationQNSLTGKTAEENLND
HHHHCCCCHHHHCCC
40.4224763107
64PhosphorylationNDEANHTSSDKSKSE
CCCCCCCCCCCCCCC
29.0521712547
65PhosphorylationDEANHTSSDKSKSED
CCCCCCCCCCCCCCC
50.6521712547
70PhosphorylationTSSDKSKSEDYQPSN
CCCCCCCCCCCCCCC
42.6727738172
116PhosphorylationQDPNVWPSPEIAEKQ
CCCCCCCCHHHHHHH
21.3228889911
130PhosphorylationQVEDRKLSDDSQKPL
HHHHHCCCCCCCCCC
42.2729996109
203PhosphorylationYSREKDASRSIDSSN
CCHHHHHHHCCCCCC
36.3721712547
205PhosphorylationREKDASRSIDSSNPS
HHHHHHHCCCCCCCC
28.4028889911
208PhosphorylationDASRSIDSSNPSAEY
HHHHCCCCCCCCHHH
30.2821712547
230PhosphorylationFGSQTVSSANGKEVP
CCCCEECCCCCCCCC
22.7821712547
239PhosphorylationNGKEVPQTSEDSSSQ
CCCCCCCCCCCCCCC
28.1921712547
240PhosphorylationGKEVPQTSEDSSSQA
CCCCCCCCCCCCCCC
33.8725720772
243PhosphorylationVPQTSEDSSSQAPHH
CCCCCCCCCCCCCCC
28.0425720772
245PhosphorylationQTSEDSSSQAPHHSS
CCCCCCCCCCCCCCC
34.0227738172
408PhosphorylationIKVRRKETWSPWILP
EEEEECCCCCCCCCC
33.9928889911
410PhosphorylationVRRKETWSPWILPSE
EEECCCCCCCCCCCC
20.1328889911
427PhosphorylationLKFEMAKYPQINSSS
HHHHHCCCCCCCCCC
7.2829996109
447PhosphorylationASSISNLTISPPFIP
HHHHHCCEECCCCCC
24.5329996109
467PhosphorylationIIKRDVQTEVEDKLT
HHHHHHCCHHHHCCC
41.6725720772
474PhosphorylationTEVEDKLTV------
CHHHHCCCC------
29.8825720772

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 YLA3_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YLA3_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 YLA3_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of YLA3_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YLA3_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-408 AND SER-410, ANDMASS SPECTROMETRY.

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