MU161_SCHPO - dbPTM
MU161_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MU161_SCHPO
UniProt AC Q10414
Protein Name CWF19-like protein mug161
Gene Name mug161
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 561
Subcellular Localization Nucleus .
Protein Description Has a role in meiosis..
Protein Sequence MIFYDKLKPADVLVIGSADGRVIEAIEYIADLHKQHGFKFAICLGNLFSHKRTTSADVVKLKNEKVKVPIPVYFGVGTAGLPESIISHMAMYGPEVAPNLFCMGICGFMKTFYKFTIAQLGGSYNEEKYYQPPEKFEQSLNEKCFHRSDVQKLSKRCDILFSSEWPEDVQENSTLPERKLPKGCMPLAALAANCMPQYFFVPGPVYYEREPYKNSAAINVNTGTVTHFVALAPFKNSKNEKFSYAFTLYPLTTEYMQPAPPNCTASPFEHRPIPLKRASEDQIIPQQTNKFHKSKSSTALFKSKKDSSSSLNKMHKSESHSALNNLHKSESGTSLNNRRSKVGPGSCFFCLSNPNVALHLIVAIGNEAYMALPKGPLTTTASNTPALASSGHVLIIPIAHASALSTLSDTSYEKTLNEMNRFRKAVTDMYNACDSDALVYEISRANGVHLHWQMIPIPKISSHRIESVFLEMAKEAGYDFEERDVEPHELNYFRVFLPSGKILIHRLQLRERFDLQFGRRAAAKILGLEDRVDWRKCVQTEDEEKAESEAFKMCFKPYDFT
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
53PhosphorylationNLFSHKRTTSADVVK
CCCCCCCCCCCCEEE
29.8824763107
55PhosphorylationFSHKRTTSADVVKLK
CCCCCCCCCCEEECC
23.1227738172
279PhosphorylationPIPLKRASEDQIIPQ
CCCCCCCCCCCCCCC
45.8228889911
288PhosphorylationDQIIPQQTNKFHKSK
CCCCCCCCCCCCCCC
34.8229996109
294PhosphorylationQTNKFHKSKSSTALF
CCCCCCCCCCHHHHH
29.2421712547
296PhosphorylationNKFHKSKSSTALFKS
CCCCCCCCHHHHHHC
39.7628889911
297PhosphorylationKFHKSKSSTALFKSK
CCCCCCCHHHHHHCC
22.8029996109
298PhosphorylationFHKSKSSTALFKSKK
CCCCCCHHHHHHCCC
34.1828889911
303PhosphorylationSSTALFKSKKDSSSS
CHHHHHHCCCCCCHH
37.2921712547
307PhosphorylationLFKSKKDSSSSLNKM
HHHCCCCCCHHHHHH
40.7924763107
308PhosphorylationFKSKKDSSSSLNKMH
HHCCCCCCHHHHHHH
33.8021712547
309PhosphorylationKSKKDSSSSLNKMHK
HCCCCCCHHHHHHHH
42.6824763107
310PhosphorylationSKKDSSSSLNKMHKS
CCCCCCHHHHHHHHH
37.6021712547
317PhosphorylationSLNKMHKSESHSALN
HHHHHHHHHCHHHHH
29.6528889911
319PhosphorylationNKMHKSESHSALNNL
HHHHHHHCHHHHHHH
29.8128889911
321PhosphorylationMHKSESHSALNNLHK
HHHHHCHHHHHHHHH
43.6725720772
329PhosphorylationALNNLHKSESGTSLN
HHHHHHHCCCCCCCC
26.6721712547
331PhosphorylationNNLHKSESGTSLNNR
HHHHHCCCCCCCCCC
55.2328889911
333PhosphorylationLHKSESGTSLNNRRS
HHHCCCCCCCCCCCC
39.0421712547
334PhosphorylationHKSESGTSLNNRRSK
HHCCCCCCCCCCCCC
32.4028889911
340PhosphorylationTSLNNRRSKVGPGSC
CCCCCCCCCCCCCCE
28.5824763107
462PhosphorylationIPIPKISSHRIESVF
EECCCCCHHHHHHHH
21.9127738172
467PhosphorylationISSHRIESVFLEMAK
CCHHHHHHHHHHHHH
18.7927738172

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 MU161_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MU161_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 MU161_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YFE6_SCHPOgmh5genetic
18818364
YNU4_SCHPOSPBC28E12.04genetic
22681890
PPR8_SCHPOppr8genetic
22681890

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MU161_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-296; THR-298; SER-317;SER-319; SER-331 AND SER-334, AND MASS SPECTROMETRY.

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