UniProt Accession

 KPYK1_YEAST; P00549; D6VPH8; Q2VQG5 

Genbank Protein ID

 V01321; X14400; AY949862; AY949863; AY949864; AY949865; AY949866; AY949867; AY949868; AY949869; AY949870; AY949871; AY949872; AY949873; AY949874; AY949875; AY949876; AY949877; AY949878; AY949879; AY949880; AY949881; AY949882; AY949883; AY949884; AY949885; AY949886; AY949887; AY949888; AY949889; AY949890; U12980; AY693107; BK006935 

Genbank Nucleotide ID

 CAA24631.1; CAA32573.1; AAY27264.1; AAY27265.1; AAY27266.1; AAY27267.1; AAY27268.1; AAY27269.1; AAY27270.1; AAY27271.1; AAY27272.1; AAY27273.1; AAY27274.1; AAY27275.1; AAY27276.1; AAY27277.1; AAY27278.1; AAY27279.1; AAY27280.1; AAY27281.1; AAY27282.1; AAY27283.1; AAY27284.1; AAY27285.1; AAY27286.1; AAY27287.1; AAY27288.1; AAY27289.1; AAY27290.1; AAY27291.1; AAY27292.1; AAC04993.1; AAT93126.1; DAA06948.1 

Protein Name

 Pyruvate kinase 1 

Protein Synonyms/Alias

 PK 1; cell division cycle protein 19 

Gene Name

 CDC19 

Gene Synonyms/Alias

 PYK1; YAL038W 

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
30	IIGTIGPKTNNPETL	acetylation	[1]
30	IIGTIGPKTNNPETL	ubiquitination	[2]
42	ETLVALRKAGLNIVR	ubiquitination	[2]
61	HGSYEYHKSVIDNAR	acetylation	[1]
61	HGSYEYHKSVIDNAR	ubiquitination	[2]
69	SVIDNARKSEELYPG	acetylation	[1]
69	SVIDNARKSEELYPG	ubiquitination	[2]
86	LAIALDTKGPEIRTG	acetylation	[1]
86	LAIALDTKGPEIRTG	ubiquitination	[3, 4]
116	MIFTTDDKYAKACDD	acetylation	[1]
124	YAKACDDKIMYVDYK	acetylation	[1]
124	YAKACDDKIMYVDYK	ubiquitination	[2]
131	KIMYVDYKNITKVIS	acetylation	[1]
135	VDYKNITKVISAGRI	acetylation	[1]
135	VDYKNITKVISAGRI	ubiquitination	[2]
166	DDKTLKVKALNAGKI	ubiquitination	[2]
172	VKALNAGKICSHKGV	ubiquitination	[2]
177	AGKICSHKGVNLPGT	acetylation	[1]
177	AGKICSHKGVNLPGT	ubiquitination	[2]
194	DLPALSEKDKEDLRF	acetylation	[1]
196	PALSEKDKEDLRFGV	acetylation	[1]
204	EDLRFGVKNGVHMVF	ubiquitination	[2, 4]
233	EVLGEQGKDVKIIVK	acetylation	[1]
233	EVLGEQGKDVKIIVK	ubiquitination	[2]
240	KDVKIIVKIENQQGV	ubiquitination	[2]
255	NNFDEILKVTDGVMV	acetylation	[1]
255	NNFDEILKVTDGVMV	ubiquitination	[2, 4]
286	VQKKLIAKSNLAGKP	ubiquitination	[2]
292	AKSNLAGKPVICATQ	acetylation	[1]
292	AKSNLAGKPVICATQ	ubiquitination	[2]
374	DMRNCTPKPTSTTET	ubiquitination	[2, 4]
394	VAAVFEQKAKAIIVL	acetylation	[1]
394	VAAVFEQKAKAIIVL	ubiquitination	[2, 4]
396	AVFEQKAKAIIVLST	ubiquitination	[2]
446	VFPFVFEKEPVSDWT	ubiquitination	[2, 4]
466	RINFGIEKAKEFGIL	acetylation	[1]
466	RINFGIEKAKEFGIL	ubiquitination	[2]
468	NFGIEKAKEFGILKK	acetylation	[1]
468	NFGIEKAKEFGILKK	ubiquitination	[2]
475	KEFGILKKGDTYVSI	acetylation	[1, 5]
486	YVSIQGFKAGAGHSN	acetylation	[1]
486	YVSIQGFKAGAGHSN	ubiquitination	[2]

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] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [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] 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] 

Functional Description

  

Sequence Annotation

 METAL 51 51 Potassium (By similarity).
 METAL 53 53 Potassium (By similarity).
 METAL 84 84 Potassium (By similarity).
 METAL 85 85 Potassium; via carbonyl oxygen (By
 METAL 242 242 Magnesium (Potential).
 METAL 266 266 Magnesium (By similarity).
 BINDING 49 49 Substrate (By similarity).
 BINDING 265 265 Substrate; via amide nitrogen (By
 BINDING 266 266 Substrate; via amide nitrogen (By
 BINDING 298 298 Substrate (By similarity).
 BINDING 337 337 ADP (Potential).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 9 9 Phosphoserine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 31 31 Phosphothreonine.
 MOD_RES 70 70 Phosphoserine.
 MOD_RES 184 184 Phosphothreonine.
 MOD_RES 213 213 Phosphoserine.
 MOD_RES 316 316 Phosphoserine.
 MOD_RES 450 450 Phosphoserine.
 MOD_RES 478 478 Phosphothreonine.  

Keyword

 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 500 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0030955; F:potassium ion binding; IEA:InterPro.
 GO:0004743; F:pyruvate kinase activity; IDA:SGD.
 GO:0006096; P:glycolysis; IMP:SGD.
 GO:0006090; P:pyruvate metabolic process; IMP:SGD. 

Interpro

 IPR001697; Pyr_Knase.
 IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
 IPR011037; Pyrv_Knase-like_insert_dom.
 IPR015794; Pyrv_Knase_a/b.
 IPR018209; Pyrv_Knase_AS.
 IPR015793; Pyrv_Knase_brl.
 IPR015795; Pyrv_Knase_C.
 IPR015806; Pyrv_Knase_insert_dom. 

Pfam

 PF00224; PK
 PF02887; PK_C 

SMART

  

PROSITE

 PS00110; PYRUVATE_KINASE 

PRINTS

 PR01050; PYRUVTKNASE.