HOSM_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HOSM_YEAST
• UniProt AC: Q12122
• Protein Name: Homocitrate synthase, mitochondrial
• Gene Name: LYS21
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 440
• Subcellular Localization: Mitochondrion .
• Protein Sequence: MSENNEFQSVTESTTAPTTSNPYGPNPADYLSNVKNFQLIDSTLREGEQFANAFFDTEKKIEIARALDDFGVDYIELTSPVASEQSRKDCEAICKLGLKAKILTHIRCHMDDARVAVETGVDGVDVVIGTSKFLRQYSHGKDMNYIAKSAVEVIEFVKSKGIEIRFSSEDSFRSDLVDLLNIYKTVDKIGVNRVGIADTVGCANPRQVYELIRTLKSVVSCDIECHFHNDTGCAIANAYTALEGGARLIDVSVLGIGERNGITPLGGLMARMIVAAPDYVRSKYKLHKIRDIENLVADAVEVNIPFNNPITGFCAFTHKAGIHAKAILANPSTYEILDPHDFGMKRYIHFANRLTGWNAIKSRVDQLNLNLTDDQIKEVTAKIKKLGDVRPLNIDDVDSIIKDFHAELSTPLLKPVNKGTDDDNIDISNGHVSKKAKVTK

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
2	Phosphorylation	------MSENNEFQS ------CCCCCCCCC	49.37	30377154
9	Phosphorylation	SENNEFQSVTESTTA CCCCCCCCCCCCCCC	36.01	30377154
35	Ubiquitination	ADYLSNVKNFQLIDS HHHHHCCCCCCCCCC	57.19	17644757
59	Ubiquitination	NAFFDTEKKIEIARA HHHCCHHHHHHHHHH	62.23	17644757
60	Ubiquitination	AFFDTEKKIEIARAL HHCCHHHHHHHHHHH	39.06	17644757
74	Phosphorylation	LDDFGVDYIELTSPV HHHHCCCEEEECCCC	8.22	22369663
78	Phosphorylation	GVDYIELTSPVASEQ CCCEEEECCCCCCHH	20.42	22369663
79	Phosphorylation	VDYIELTSPVASEQS CCEEEECCCCCCHHH	29.96	22369663
83	Phosphorylation	ELTSPVASEQSRKDC EECCCCCCHHHHHHH	36.08	22369663
86	Phosphorylation	SPVASEQSRKDCEAI CCCCCHHHHHHHHHH	36.93	22369663
88	Ubiquitination	VASEQSRKDCEAICK CCCHHHHHHHHHHHH	72.48	17644757
148	Ubiquitination	KDMNYIAKSAVEVIE CCHHHHHHHHHHHHH	29.41	17644757
158	Ubiquitination	VEVIEFVKSKGIEIR HHHHHHHHHCCCEEE	52.34	17644757
168	Phosphorylation	GIEIRFSSEDSFRSD CCEEEECCCCCCCHH	42.59	30377154
184	Ubiquitination	VDLLNIYKTVDKIGV HHHHHHHHHHHHCCC	37.97	24961812
216	Ubiquitination	YELIRTLKSVVSCDI HHHHHHHHHHHCCEE	40.36	17644757
217	Phosphorylation	ELIRTLKSVVSCDIE HHHHHHHHHHCCEEE	30.75	28889911
288	Ubiquitination	RSKYKLHKIRDIENL HHHHHHHCHHCHHHH	50.28	17644757
319	Ubiquitination	GFCAFTHKAGIHAKA CEEEECCCCCCCCEE	45.29	17644757
325	Ubiquitination	HKAGIHAKAILANPS CCCCCCCEEEECCCC	23.07	24961812
332	Phosphorylation	KAILANPSTYEILDP EEEECCCCCCCCCCH	43.35	22369663
333	Phosphorylation	AILANPSTYEILDPH EEECCCCCCCCCCHH	26.82	22369663
334	Phosphorylation	ILANPSTYEILDPHD EECCCCCCCCCCHHH	12.81	22369663
345	Ubiquitination	DPHDFGMKRYIHFAN CHHHHCHHHHHHHHH	42.29	23749301
361	Ubiquitination	LTGWNAIKSRVDQLN HHCHHHHHHHHHHHC	29.78	17644757
377	Ubiquitination	NLTDDQIKEVTAKIK CCCHHHHHHHHHHHH	40.26	17644757
382	Ubiquitination	QIKEVTAKIKKLGDV HHHHHHHHHHHHCCC	45.77	17644757
399	Phosphorylation	LNIDDVDSIIKDFHA CCHHHHHHHHHHHHH	26.51	23749301
409	Phosphorylation	KDFHAELSTPLLKPV HHHHHHHCCCCCCCC	21.34	22369663
410	Phosphorylation	DFHAELSTPLLKPVN HHHHHHCCCCCCCCC	30.49	22369663
414	Acetylation	ELSTPLLKPVNKGTD HHCCCCCCCCCCCCC	55.38	24489116
420	Phosphorylation	LKPVNKGTDDDNIDI CCCCCCCCCCCCCCC	37.55	22369663
428	Phosphorylation	DDDNIDISNGHVSKK CCCCCCCCCCCCCCC	32.77	22369663
433	Phosphorylation	DISNGHVSKKAKVTK CCCCCCCCCCCCCCC	23.82	22369663
434	Acetylation	ISNGHVSKKAKVTK- CCCCCCCCCCCCCC-	56.51	24489116
435	Acetylation	SNGHVSKKAKVTK-- CCCCCCCCCCCCC--	46.03	25381059

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HOSM_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HOSM_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HOSC_YEAST	LYS20	physical	18467557
HOSM_YEAST	LYS21	physical	18467557
HOSC_YEAST	LYS20	genetic	18408719
ESA1_YEAST	ESA1	genetic	20810648
HOSC_YEAST	LYS20	physical	22615397

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-332; THR-333;SER-409 AND THR-410, AND MASS SPECTROMETRY.
PubMed: 18407956

"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND THR-410, ANDMASS SPECTROMETRY.
PubMed: 17563356

"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND THR-410, ANDMASS SPECTROMETRY.
PubMed: 17287358