FRDS_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FRDS_YEAST
• UniProt AC: P32614
• Protein Name: Fumarate reductase 1
• Gene Name: FRD1
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 470
• Subcellular Localization: Cytoplasm .
• Protein Description: Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2)..
• Protein Sequence: MSLSPVVVIGTGLAGLAAANELVNKYNIPVTILEKASSIGGNSIKASSGINGACTETQRHFHIEDSPRLFEDDTIKSAKGKGVQELMAKLANDSPLAIEWLKNEFDLKLDLLAQLGGHSVARTHRSSGKLPPGFEIVSALSNNLKKLAETKPELVKINLDSKVVDIHEKDGSISAVVYEDKNGEKHMVSANDVVFCSGGFGFSKEMLKEYAPELVNLPTTNGQQTTGDGQRLLQKLGADLIDMDQIQVHPTGFIDPNDRSSSWKFLAAESLRGLGGILLNPITGRRFVNELTTRDVVTAAIQKVCPQEDNRALLVMGEKMYTDLKNNLDFYMFKKLVQKLTLSQVVSEYNLPITVAQLCEELQTYSSFTTKADPLGRTVILNEFGSDVTPETVVFIGEVTPVVHFTMGGARINVKAQVIGKNDERLLKGLYAAGEVSGGVHGANRLGGSSLLECVVFGRTAAESIANDRK

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
37	Phosphorylation	VTILEKASSIGGNSI EEEHHCCHHCCCCCC	33.29	22369663
38	Phosphorylation	TILEKASSIGGNSIK EEHHCCHHCCCCCCC	30.06	22369663
43	Phosphorylation	ASSIGGNSIKASSGI CHHCCCCCCCCCCCC	28.83	22369663
45	Ubiquitination	SIGGNSIKASSGING HCCCCCCCCCCCCCC	41.87	23749301
47	Phosphorylation	GGNSIKASSGINGAC CCCCCCCCCCCCCCC	24.89	22369663
48	Phosphorylation	GNSIKASSGINGACT CCCCCCCCCCCCCCC	48.85	22369663
66	Phosphorylation	RHFHIEDSPRLFEDD ECCCCCCCCCCCCCC	10.10	22369663
74	Phosphorylation	PRLFEDDTIKSAKGK CCCCCCCCHHHCCCC	42.50	22369663
76	Acetylation	LFEDDTIKSAKGKGV CCCCCCHHHCCCCCH	46.59	24489116
145	Acetylation	SALSNNLKKLAETKP HHHHHHHHHHHHHCH	48.11	24489116
151	Acetylation	LKKLAETKPELVKIN HHHHHHHCHHHEECC	28.18	24489116
156	Acetylation	ETKPELVKINLDSKV HHCHHHEECCCCCCE	38.20	24489116
162	Acetylation	VKINLDSKVVDIHEK EECCCCCCEEEEEEC	46.04	24489116
181	Acetylation	SAVVYEDKNGEKHMV EEEEEECCCCCEEEE	55.71	24489116
208	Acetylation	GFSKEMLKEYAPELV CCCHHHHHHHCHHHC	47.58	24489116
303	Ubiquitination	VVTAAIQKVCPQEDN HHHHHHHHHCCCCCC	39.43	23749301
325	Acetylation	EKMYTDLKNNLDFYM HHHHHHHHHHHCHHH	46.75	22865919
334	Succinylation	NLDFYMFKKLVQKLT HHCHHHHHHHHHHCC	28.77	23954790
334	Acetylation	NLDFYMFKKLVQKLT HHCHHHHHHHHHHCC	28.77	24489116
415	2-Hydroxyisobutyrylation	GGARINVKAQVIGKN CCEEEEEEEEEECCC	28.72	-
421	Acetylation	VKAQVIGKNDERLLK EEEEEECCCHHHHHH	50.53	22865919
460	Phosphorylation	ECVVFGRTAAESIAN HHHHHCHHHHHHHHH	30.51	28889911

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FRDS_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 FRDS_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OSM1_YEAST	OSM1	genetic	12393208
GLYC_YEAST	SHM2	physical	16554755
MSH4_YEAST	MSH4	genetic	20093466
XRN1_YEAST	XRN1	genetic	20093466
GBLP_YEAST	ASC1	genetic	20093466
ATG3_YEAST	ATG3	genetic	20093466
YME1_YEAST	YME1	genetic	20093466
MSH4_YEAST	MSH4	genetic	27708008
GBLP_YEAST	ASC1	genetic	27708008
TMA23_YEAST	TMA23	genetic	27708008
ATG3_YEAST	ATG3	genetic	27708008
PA1B3_HUMAN	PAFAH1B3	physical	27107014

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.
PubMed: 17330950