UBP12_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBP12_SCHPO
• UniProt AC: O60079
• Protein Name: Probable ubiquitin carboxyl-terminal hydrolase 12
• Gene Name: ubp12
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 979
• Protein Sequence: MDSLSESSTSSYHGKRPRSLSEESQSSSNMDDISQKSISLGDASEISKNLPSIAEQKQLIGELVNNQPELELGQVDNYILSYSWYERLCSYLAEDGPFPGPVDQEDIADLETGTLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPEFPRETVNLGSESHPHLVVEVYPPIFSLTLLSTNAVDANESHKPKKISLSSKSTLEDLLEGVKYTLSLPSDQFRLWRVDTDQPLHRTIDPSSFIKINSKEIIDFLEKSKTLVELGMDSSCSLVAECMINETWPVDRALRLQFLIQQRNNQSSNEEQKQEKRVPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLGMGGQVASIFASLIKSLYSPEHSSFAPRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPDLYEVDEEKIKNTAEECWRLHKLRNDSLIVDLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTNLTPLAIEVVLESKAATIEDLVKYVAEKSGCSDYRKILVTETYKGRFYRFLTQLSKSLLMEISEEDEIYLYELERPYEDGSDDILVPVYHISDDSTNSANSYMSSRDFGHPFVLQLSDNEVTDASFISEKLKLKYQQFTTLKNLKNIDSLESLELGHEDEQVQKGPLDVDMDHSQTPLFEMRVFHDRFEKIPTGWNMSVSNLPLLTERDKKDLESTVDPLDAHSIEEEDDSEFKDVAPGSYPEPSKSNENTKLTAKENDRLLIQGDLLVCEWPEKSYQFVFSVAPSSPQMGRSLWLESKTILSDKKDDSEDSRTITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYRRKTS

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
11	Phosphorylation	LSESSTSSYHGKRPR CCCCCCCCCCCCCCC	22.64	28889911
12	Phosphorylation	SESSTSSYHGKRPRS CCCCCCCCCCCCCCC	17.85	28889911
19	Phosphorylation	YHGKRPRSLSEESQS CCCCCCCCCCHHHHC	38.64	28889911
21	Phosphorylation	GKRPRSLSEESQSSS CCCCCCCCHHHHCCC	40.33	21712547
24	Phosphorylation	PRSLSEESQSSSNMD CCCCCHHHHCCCCHH	31.17	21712547
37	Phosphorylation	MDDISQKSISLGDAS HHHHHHHCCCCCCHH	15.12	28889911
39	Phosphorylation	DISQKSISLGDASEI HHHHHCCCCCCHHHH	33.13	28889911
659	Phosphorylation	KNLKNIDSLESLELG HHCCCCCHHHHHHCC	30.18	25720772
662	Phosphorylation	KNIDSLESLELGHED CCCCHHHHHHCCCCC	32.22	25720772
708	Phosphorylation	IPTGWNMSVSNLPLL CCCCCCCCCCCCCCC	21.12	24763107
725	Phosphorylation	RDKKDLESTVDPLDA HHHHHHHHCCCCCHH	40.82	28889911
726	Phosphorylation	DKKDLESTVDPLDAH HHHHHHHCCCCCHHH	21.39	25720772
734	Phosphorylation	VDPLDAHSIEEEDDS CCCCHHHCCCCCCCC	33.16	24763107
741	Phosphorylation	SIEEEDDSEFKDVAP CCCCCCCCCCCCCCC	58.20	21712547
750	Phosphorylation	FKDVAPGSYPEPSKS CCCCCCCCCCCCCCC	36.13	21712547
755	Phosphorylation	PGSYPEPSKSNENTK CCCCCCCCCCCCCCC	47.24	29996109
810	Phosphorylation	SLWLESKTILSDKKD CEEEEECEECCCCCC	36.11	28889911
819	Phosphorylation	LSDKKDDSEDSRTIT CCCCCCCCCCCCEEE	54.13	28889911
822	Phosphorylation	KKDDSEDSRTITLND CCCCCCCCCEEEHHH	27.54	28889911

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

Oops, there are no upstream regulatory protein records of UBP12_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBP12_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 UBP12_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN1_SCHPO	csn1	physical	12718879
CSN5_SCHPO	csn5	physical	12718879
CUL3_SCHPO	cul3	physical	12718879

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-19; SER-37 AND SER-39,AND MASS SPECTROMETRY.
PubMed: 18257517