BIT61_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BIT61_SCHPO
• UniProt AC: O74547
• Protein Name: Target of rapamycin complex 2 subunit bit61 {ECO:0000303|PubMed:18076573}
• Gene Name: bit61 {ECO:0000303|PubMed:18076573}
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 422
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases..
• Protein Sequence: MVGRGSFSSTSSASSINWIPKNTKTSIESVSNTISLSENGQNQDLETVTTKESNVGDSDTTENIKSPFNGQWPFSRRSSQSSSHPVFEETHWSKHSKRPGKLNVLTPTSPSNVNAEVQSISTKTQLSLLNLSPHKHKKPKDGLDLSALQKTLNGSRNFLRGRRDAGGIFGASIPQSLVTNQIINGFGAASLAFAKLGKVRSPLEGRFNLVPISADETWLIVESEVCSLYSGEALHYSLEDLNGILILHLQALIRDTKMNEFVGHLETLFRKATKCLSDSLSPVPEELFLNRIIETWLFFFSSVLPYVQGVFLPIKTKLFDEQEKTQLPYEVNEFCSTNREKLNVHRLALMTFRDYMVLPIANRIQICIGRAESAENALDNAGEVFARLFQILSLLASVRTNDSKEQEITNLATKVRCLLIAS

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
25	Phosphorylation	WIPKNTKTSIESVSN CCCCCCCCCHHHHHC	32.66	25720772
26	Phosphorylation	IPKNTKTSIESVSNT CCCCCCCCHHHHHCC	26.39	25720772
29	Phosphorylation	NTKTSIESVSNTISL CCCCCHHHHHCCEEE	29.22	25720772
31	Phosphorylation	KTSIESVSNTISLSE CCCHHHHHCCEEECC	37.22	25720772
58	Phosphorylation	KESNVGDSDTTENIK CCCCCCCCCCCCCCC	30.81	25720772
60	Phosphorylation	SNVGDSDTTENIKSP CCCCCCCCCCCCCCC	39.70	25720772
78	Phosphorylation	QWPFSRRSSQSSSHP CCCCCCCCCCCCCCC	31.45	29996109
79	Phosphorylation	WPFSRRSSQSSSHPV CCCCCCCCCCCCCCC	32.07	29996109
83	Phosphorylation	RRSSQSSSHPVFEET CCCCCCCCCCCCCHH	36.74	29996109
106	Phosphorylation	PGKLNVLTPTSPSNV CCCCCEECCCCCCCC	21.90	29996109
108	Phosphorylation	KLNVLTPTSPSNVNA CCCEECCCCCCCCCH	48.29	29996109
109	Phosphorylation	LNVLTPTSPSNVNAE CCEECCCCCCCCCHH	27.77	28889911
111	Phosphorylation	VLTPTSPSNVNAEVQ EECCCCCCCCCHHEE	53.85	29996109
132	Phosphorylation	QLSLLNLSPHKHKKP HHHHHCCCCCCCCCC	24.72	28889911
201	Phosphorylation	AKLGKVRSPLEGRFN HHHCCCCCCCCCCCE	36.50	28889911
281	Phosphorylation	KCLSDSLSPVPEELF HHHHCCCCCCCHHHH	28.01	25720772

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

Oops, there are no upstream regulatory protein records of BIT61_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BIT61_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 BIT61_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XPOT_SCHPO	los1	genetic	22681890
AP3D_SCHPO	apl5	genetic	22681890
YF19_SCHPO	atd1	genetic	22681890
YQ9H_SCHPO	SPCC18.17c	genetic	22681890
YCUD_SCHPO	SPCC965.13	genetic	22681890

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-201, AND MASSSPECTROMETRY.
PubMed: 18257517

"Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutantand organization of two highly phosphorylated TOR complexes byspecific and common subunits.";
Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,Ebe M., Yanagida M.;
Genes Cells 12:1357-1370(2007).
Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION AT SER-109 ANDSER-132, AND MASS SPECTROMETRY.
PubMed: 18076573