UniProt Accession

 TPIS_YEAST; P00942; D6VS37 

Genbank Protein ID

 J01366; Z49209; AY557654; BK006938 

Genbank Nucleotide ID

 AAA88757.1; CAA89080.1; AAS55980.1; DAA11897.1 

Protein Name

 Triosephosphate isomerase 

Protein Synonyms/Alias

 TIM; Triose-phosphate isomerase 

Gene Name

 TPI1 

Gene Synonyms/Alias

 YDR050C; YD9609.05C 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
12	FFVGGNFKLNGSKQS	acetylation	[1]
12	FFVGGNFKLNGSKQS	ubiquitination	[2]
21	NGSKQSIKEIVERLN	acetylation	[1]
56	YSVSLVKKPQVTVGA	acetylation	[3]
56	YSVSLVKKPQVTVGA	ubiquitination	[2]
69	GAQNAYLKASGAFTG	acetylation	[1]
69	GAQNAYLKASGAFTG	ubiquitination	[2, 4]
84	ENSVDQIKDVGAKWV	acetylation	[1]
84	ENSVDQIKDVGAKWV	ubiquitination	[2]
89	QIKDVGAKWVILGHS	acetylation	[1]
107	SYFHEDDKFIADKTK	acetylation	[1]
138	LEEKKAGKTLDVVER	acetylation	[1]
195	IRKFLASKLGDKAAS	acetylation	[1]
199	LASKLGDKAASELRI	acetylation	[1]
199	LASKLGDKAASELRI	ubiquitination	[2]
221	GSNAVTFKDKADVDG	acetylation	[1]
223	NAVTFKDKADVDGFL	ubiquitination	[2, 4]
237	LVGGASLKPEFVDII	acetylation	[1]
237	LVGGASLKPEFVDII	ubiquitination	[5]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211]
 [4] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [5] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232] 

Functional Description

  

Sequence Annotation

 ACT_SITE 95 95 Electrophile.
 ACT_SITE 165 165 Proton acceptor.
 BINDING 10 10 Substrate.
 BINDING 12 12 Substrate.
 MOD_RES 4 4 Phosphothreonine.
 MOD_RES 71 71 Phosphoserine.
 MOD_RES 215 215 Phosphoserine.  

Keyword

 3D-structure; Complete proteome; Direct protein sequencing; Gluconeogenesis; Glycolysis; Isomerase; Pentose shunt; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 248 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0004807; F:triose-phosphate isomerase activity; IDA:SGD.
 GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
 GO:0006096; P:glycolysis; IMP:SGD.
 GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW. 

Interpro

 IPR013785; Aldolase_TIM.
 IPR022896; TrioseP_Isoase_bac/euk.
 IPR000652; Triosephosphate_isomerase.
 IPR020861; Triosephosphate_isomerase_AS. 

Pfam

 PF00121; TIM 

SMART

  

PROSITE

 PS00171; TIM_1
 PS51440; TIM_2 

PRINTS