MU190_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MU190_SCHPO
• UniProt AC: Q9USG8
• Protein Name: Meiotically up-regulated gene 190 protein
• Gene Name: mug190
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1188
• Subcellular Localization: Cytoplasm . Endoplasmic reticulum membrane ; Single-pass membrane protein . Nucleus membrane ; Single-pass membrane protein . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body .
• Protein Description: Has a role in meiosis..
• Protein Sequence: MSTHSGDSTKQQHYRSSDPYSGRRPIPTIPKFFRDRKQRAEKKEEQQREQTENEKLFDPITQRDVEINDVHFDYAKTYDDPSFTVPNQSIQGSSLPSEKPYLSSNQPTNVYKQHQDDLAPPEADNQITRDVPISDEKTNILFFPSPSIDLSYVSKEVKQKTGQYSLFAYIFSLVISWFFTHSIIISAVLPLAISSCMYLWMQNIYAVAKDAEWGAEQKRGEYARLNLIPESAEWMNHLLEKVWPLINPEMFSSVADQIEDVMQASIPSFVENVRVASLDQGSHPVRVVSIRSLPSGEASESFSEKQASEAEHKDEPEQQRKQFYNFELCLAYHAKPVEDATSTSARASNLHLRIVFYPGIKGTVGFPLPIWVEIKGFVARIRFRCELMPEVPFLKNVTFSLMGLPELNVSAVPVAEGGVNIFGLPLISKFVNDAISAAANEYVSPKSMTIDLSKTLLGDDIKKEVNALGVIFVHINRAEDLSKQDVNGLSDAYITVGFHKFGKPLYCTRVVKQDLNPIWNEYAFIPVFPDQVKAGEKISIELWDSDRFSPDDVVGRTKIGLHLLIQDSGKMHERCDTLTGISEDTSLPGRVFYEIGYFPRAEFKPSLKTSGHDITIPRSMRDDPAFQNPHGSLDNKEEEAAVTTAPDEEYPSGILSFTVHQAVNLQMNHPTGTFGNVSGNYNTSPAQSVGDVTAEEGSELPSSYVCVDLDDTLVYKTRTKVFTSNPIYNAGSEKFVKDWRNAMLCFTVRDFKLREHDSILGVVNIPLATTLTTSSQLTKWYPIQGGIGFGSVRISILFRSMKLKIPRNLLGWDIGTLEFMDRQIVAEGTGSVSDVSFSSIRVNIAGVKITAKSSTSNSSSTAEYHVRSRHAVIPVNNRYRSAVVFEFRKQLQRKHNVFAMVWLVDLEDNVEQNIRVPIFTSSKPAHVLQNMIDFDHPDKESEFKIIGYLSTRICFHRGLDDSHEQLVDNDDEAAIFETYRCLKSMGLRRGYVKDMKNPLADQRASLDESRETTTASSKFESDDSVDTEDEETTTDRTPIECTQTVSMVDPNVNGDIQGRNSLGTMNSNERNLEQEFISLGYASKNRPKAHAQEGTNQPGASENVEPVLADDSDAVTIHSNISSDDQKRKLVNADDRELEKRLHRGPYNSKIVRTGEWVKDGAKMGWRNLRRKFALNGRQPDVETEISK

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
16	Phosphorylation	TKQQHYRSSDPYSGR CCCCCCCCCCCCCCC	31.74	28889911
1005	Phosphorylation	PLADQRASLDESRET CHHHHHHCCCCHHHH	38.24	28889911
1009	Phosphorylation	QRASLDESRETTTAS HHHCCCCHHHHCCCC	34.77	21712547
1012	Phosphorylation	SLDESRETTTASSKF CCCCHHHHCCCCHHC	28.47	21712547
1013	Phosphorylation	LDESRETTTASSKFE CCCHHHHCCCCHHCC	18.66	21712547
1014	Phosphorylation	DESRETTTASSKFES CCHHHHCCCCHHCCC	31.78	21712547
1061	Phosphorylation	GDIQGRNSLGTMNSN CCCCCCCCCCCCCCC	27.15	29996109
1064	Phosphorylation	QGRNSLGTMNSNERN CCCCCCCCCCCCCCC	20.62	29996109
1067	Phosphorylation	NSLGTMNSNERNLEQ CCCCCCCCCCCCHHH	29.28	28889911
1112	Phosphorylation	EPVLADDSDAVTIHS CCCCCCCCCCEEEEC	28.19	21712547
1116	Phosphorylation	ADDSDAVTIHSNISS CCCCCCEEEECCCCC	18.07	21712547
1119	Phosphorylation	SDAVTIHSNISSDDQ CCCEEEECCCCCHHH	31.82	21712547
1122	Phosphorylation	VTIHSNISSDDQKRK EEEECCCCCHHHHHH	31.78	21712547

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

Oops, there are no upstream regulatory protein records of MU190_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MU190_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 MU190_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of MU190_SCHPO !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-1005, AND MASSSPECTROMETRY.
PubMed: 18257517