FAS2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FAS2_SCHPO
• UniProt AC: Q10289
• Protein Name: Fatty acid synthase subunit alpha
• Gene Name: fas2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1842
• Protein Description: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex..
• Protein Sequence: MRPEVEQELAHTLLLELLAYQFASPVRWIETQDVILSPPVSAERIVEIGPSPTLAGMAKRTLKLKYENMDAALSINREVLCYSKDAREIYYNFEDEVADEPAEAPASTSSTPKVETAAAAAPAATPAPAPAQTSAPAAALPDEPPKALEVLHTLVAQKLKKSIEEVSPQKSIKDLVGGKSTLQNEILGDLQKEFGATPEKPEEVPLDELGAIMQSSFNGSLGKQSSSLISRMISSKMPGGFNNSAVRGYLGNRYGLGPGRLESVLLLALTMEPASRLGSEADAKAWLDSVAQKYAARNGVTLSSPTAEGGSSSGSAAVIDEETFKKLTKNNTMLVTQQLELFARYLNKDLRAGQKAQVAEKVISDTLRAQLDLWNEEHGEFYASGIAPIFSPLKARVYDSDWNWARQDALKMFFDIIFGRLKHVDTEIVARCISVMNRSNPTLLEFMQYHIDHCPAEKGETYQLAKTLGQQLIDNCKSVIDAPPVFKNVNHPTAPSTTIDERGNLNYEEIPRPGVRKLTHYVTEMAKGGKLPTESKNKAKVQNDLARIYRIIKSQNKMSRSSKLQIKQLYGQVLHALSLPLPSSNDEQTPVKETIPFLHIRKKSVDGNWEFNKSLTGTYLDVLESGAKNGITYQDKYALVTGAGAGSIGAQIVEGLLAGGAKVVVTTSRFSRKVTEFYQSLYTRHGSRGSCLIVVPFNQGSKTDVEALIDYIYDEKKGLGWNLDYIVPFAAIPENGREIDGIDSRSEFAHRIMLTNILRLLGAVKSQKASRGMDTRPAQVILPLSPNHGTFGNDGLYSESKLGLETLFNRWYSESWANYLTICGAVIGWTRGTGLMAPNNIVSQGIEKYGVRTFSQSEMAFNILGLMSQKVVDLCQSEPIYANLNGGLELLPDLKDLSTRLRTELLETAEIRRAVAAETAFDHSITNGPDSEAVFQKTAIQPRANLKFNFPKLKPYEALSHLSDLRGMVDLEKVPVVTGFSEVGPWGNSRTRWDMECYGEFSLEGCVEIAWIMGLIKNFNGKGKDGKPYSGWVDTKTGEPVDDKDVKAKYEKYILEHCGIRIIEAELFHGYNPEKKELLQEVVIDHDLEPFEASKEAAHEFKLRHGDQVEIFEIPDSTEWSVRFKRGTSMLIPKALRFDRFVAGQIPLGWDPKRYGIPDDIISQVDPTTLYVLVSTVEALVASGITDPYECYKYIHVSELGNTVGSGIGGMSALRGMYKDRWTDKPVQKDILQESFINTANAWINMLLLSASGPIKTPVGACATAVESVDAAVDLITSGKARICISGGYDDFSEEGSYEFANMGATSNAAKETERGRTPQEMSRPATSTRDGFMESQGAGVQIIMQAKLAIEMGVPIHGIVGYVSTAMDKQGRSVPAPGQGILTGAREIATKTPLPIVDLKFRSRQLQRRRSQIGEWAEREYLYLEEELDAMKVQNPDLDLEAYRIERINVIKEEVVRQEKEALNTFGNEFWKRDPTIAPIRGALAVWGLTIDDLGVASFHGTSTKANEKNECDVIDSQLTHLGRSKGNAVYGVFQKYLTGHSKGGAGAWMLNGALQILRSGFVPGNRNADNIDEYLARFDRVMFPSEGIQTDGIKAASVTAFGFGQVGGQVIVIHPDYIYGVIDEATYNAYKAKTAARYKASYRYTHDALVYNNLVRAKDSPPYTKEQEKAVYLNPLARASKSKAGTWTFPATLPAESDISKTNETTRTLQSLTTSLTNSNENVGVDVELVSAISIDNETFIERNFTDTERKYCFAAPNPQASFAGRWSAKEAVFKSLGISGKGAAAPLKDIEIISSESGAPEVVLHGEAAKAATTAGVKSVSVSISHDDNQSVSVALAHK

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
31	Phosphorylation	SPVRWIETQDVILSP CCCCEEEECCEEECC	22.42	29996109
37	Phosphorylation	ETQDVILSPPVSAER EECCEEECCCCCHHH	18.94	29996109
107	Phosphorylation	EPAEAPASTSSTPKV CCCCCCCCCCCCCCC	27.97	25720772
108	Phosphorylation	PAEAPASTSSTPKVE CCCCCCCCCCCCCCH	28.89	21712547
109	Phosphorylation	AEAPASTSSTPKVET CCCCCCCCCCCCCHH	29.71	21712547
110	Phosphorylation	EAPASTSSTPKVETA CCCCCCCCCCCCHHH	49.14	21712547
111	Phosphorylation	APASTSSTPKVETAA CCCCCCCCCCCHHHH	27.22	21712547
125	Phosphorylation	AAAAPAATPAPAPAQ HHHCCCCCCCCCCCC	23.30	27738172
180	Phosphorylation	KDLVGGKSTLQNEIL HHHHCCHHHHHHHHH	37.31	29996109
180	O-(pantetheine 4'-phosphoryl)serine	KDLVGGKSTLQNEIL HHHHCCHHHHHHHHH	37.31	-
181	Phosphorylation	DLVGGKSTLQNEILG HHHCCHHHHHHHHHH	35.53	29996109
604	Phosphorylation	FLHIRKKSVDGNWEF EEEEEEECCCCCCCC	28.60	28889911
614	Phosphorylation	GNWEFNKSLTGTYLD CCCCCCHHCCCCHHH	32.06	25720772
1318	Phosphorylation	KETERGRTPQEMSRP HHCCCCCCCHHHCCC	31.95	29996109
1323	Phosphorylation	GRTPQEMSRPATSTR CCCCHHHCCCCCCCC	34.07	29996109
1327	Phosphorylation	QEMSRPATSTRDGFM HHHCCCCCCCCCCHH	33.06	29996109
1328	Phosphorylation	EMSRPATSTRDGFME HHCCCCCCCCCCHHH	24.45	29996109
1329	Phosphorylation	MSRPATSTRDGFMES HCCCCCCCCCCHHHC	28.55	29996109
1412	Phosphorylation	RQLQRRRSQIGEWAE HHHHHHHHHHHHHHH	25.08	28889911
1526	Phosphorylation	QLTHLGRSKGNAVYG HCHHCCCCCCHHHHH	43.02	25720772
1699	Phosphorylation	PATLPAESDISKTNE CCCCCCCCCCCCCCH	42.21	27738172
1797	Phosphorylation	LKDIEIISSESGAPE HHHCEEEECCCCCCE	33.44	24763107

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

Oops, there are no upstream regulatory protein records of FAS2_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FAS2_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 FAS2_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of FAS2_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-604 AND SER-1412, ANDMASS SPECTROMETRY.
PubMed: 18257517