SOG2_SCHPO - dbPTM
SOG2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOG2_SCHPO
UniProt AC O94294
Protein Name Leucine-rich repeat-containing protein sog2
Gene Name sog2 {ECO:0000250|UniProtKB:Q08817}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 886
Subcellular Localization Cytoplasm . Nucleus . Barrier septum. Cell tip.
Protein Description
Protein Sequence MSAHEVSSTKNSEIERIIKEAEDAGPENALTLDLSHLNLRELPYEQLERIQGRIARLALGHNFIKSIGPEILKFTRLRYLNIRSNVLREFPESLCRLESLEILDISRNKIKQLPESFGALMNLKVLSISKNRLFELPTYIAHMPNLEILKIENNHIVFPPPHIANNDLQDSDMQLFIANIKGYLSRNESVFRTRSESTVSAALSASANLSHSEENDSSVVDSYLFSAPSDTSHAVSPGMLTFVTPSPHSHSPAGHQQSTPKSTLSKTNENSEGTLYDSNVAHGCTHPPSLNQLNKFHLDASPRQARPRRSVSLATGLNSPSVSKPPSSATGPLYHSPQSSLTNSSVASADVQERTHNTNGASPIQDQISEFTDQHQNPSNNDAASTQSILKTAPTQLSASAKTSAISLPEVAKKERNRSNSTNDDYSSTRLPSSVLHRLEALKEARKLSEQLPNRIFAQDPHPSPRLKKEETHENGSNLTNDSVNSYFSNIGGSEVEMKHSAFEKTLESSRGILFSLSQVQQALRQQLLFCSNPVVLDSMRHVLHTANVQIKRLILCFEDTQQSNDGTANINSIVNASLSCISSFRKLIEVTKKFLNELTSRADVRYVRLLLLILFDAAKELQNALVPLSPSQPHSGNNIFADQVRQSPTSMIRTASGLTNRIVSVEKPASVMNPEIDKQIQDQVALATNSAMSVLTLLIDAVPKNNQPDLVNENIAPNLISKLRELGSLSAAACDVTRKLKHRLLTFQTNPEELEWQLFLDDTQAFVKSIIAVANLAKALSSEYTFQKSVLAGLSAATRSTKDLTILLSSSARHYTESSLATPVPLMSPIARVPATPLSAALGSAAQSITSPLIMSPAAIPASAYSTNKIDYFTDADGNVEGLQR
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
301PhosphorylationNKFHLDASPRQARPR
CCCCCCCCCCCCCCC
21.9328889911
362PhosphorylationTHNTNGASPIQDQIS
HCCCCCCCCHHHHHH
24.7629996109
392PhosphorylationSTQSILKTAPTQLSA
HHHHHHHHCCCCCCC
34.1321712547
395PhosphorylationSILKTAPTQLSASAK
HHHHHCCCCCCCCCC
39.4125720772
398PhosphorylationKTAPTQLSASAKTSA
HHCCCCCCCCCCCCC
15.4524763107
400PhosphorylationAPTQLSASAKTSAIS
CCCCCCCCCCCCCCC
27.2428889911
403PhosphorylationQLSASAKTSAISLPE
CCCCCCCCCCCCHHH
24.0925720772
404PhosphorylationLSASAKTSAISLPEV
CCCCCCCCCCCHHHH
23.9324763107
407PhosphorylationSAKTSAISLPEVAKK
CCCCCCCCHHHHHHH
37.2725720772
419PhosphorylationAKKERNRSNSTNDDY
HHHHHCCCCCCCCCC
38.3925720772
421PhosphorylationKERNRSNSTNDDYSS
HHHCCCCCCCCCCHH
29.8125720772
422PhosphorylationERNRSNSTNDDYSST
HHCCCCCCCCCCHHC
47.0929996109
449PhosphorylationLKEARKLSEQLPNRI
HHHHHHHHHHCCCCH
26.7429996109
464PhosphorylationFAQDPHPSPRLKKEE
HCCCCCCCCCCCHHH
21.4428889911
648PhosphorylationFADQVRQSPTSMIRT
CHHHHHCCCCHHHHH
21.4128889911
657PhosphorylationTSMIRTASGLTNRIV
CHHHHHCCCCCCCEE
33.4527738172
823PhosphorylationYTESSLATPVPLMSP
CCCCCCCCCCCCCCC
30.0629996109
829PhosphorylationATPVPLMSPIARVPA
CCCCCCCCCCCCCCC
22.3428889911
851PhosphorylationGSAAQSITSPLIMSP
HHHHHHCCCCCCCCC
29.5529996109
852PhosphorylationSAAQSITSPLIMSPA
HHHHHCCCCCCCCCC
18.9529996109
857PhosphorylationITSPLIMSPAAIPAS
CCCCCCCCCCCCCCH
12.3729996109

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 SOG2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOG2_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 SOG2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAK1_SCHPOnak1genetic
24972934
CSK2A_SCHPOcka1physical
23462181
NAK1_SCHPOnak1physical
23462181
CSK2B_SCHPOckb1physical
23462181
CSK2C_SCHPOckb2physical
23462181

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SOG2_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 SER-301 AND SER-464, ANDMASS SPECTROMETRY.

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