CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005150
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transketolase 1 
Protein Synonyms/Alias
 TK 1 
Gene Name
 TKL1 
Gene Synonyms/Alias
 YPR074C; YP9499.29C 
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
268SVHGAPLKADDVKQLacetylation[1]
273PLKADDVKQLKSKFGacetylation[1]
278DVKQLKSKFGFNPDKacetylation[1]
285KFGFNPDKSFVVPQEubiquitination[2]
299EVYDHYQKTILKPGVacetylation[1]
303HYQKTILKPGVEANNacetylation[1]
303HYQKTILKPGVEANNubiquitination[2]
311PGVEANNKWNKLFSEacetylation[1]
314EANNKWNKLFSEYQKacetylation[1]
321KLFSEYQKKFPELGAacetylation[1]
322LFSEYQKKFPELGAEacetylation[1]
352KLPTYTAKDSAVATRacetylation[1]
352KLPTYTAKDSAVATRubiquitination[2]
360DSAVATRKLSETVLEubiquitination[2]
392PSNLTRWKEALDFQPubiquitination[2]
518YKNSLESKHTPSIIAacetylation[1]
641DRFGASGKAPEVFKFacetylation[1]
641DRFGASGKAPEVFKFubiquitination[2]
647GKAPEVFKFFGFTPEacetylation[1]
647GKAPEVFKFFGFTPEubiquitination[3]
662GVAERAQKTIAFYKGacetylation[1]
668QKTIAFYKGDKLISPacetylation[1]
668QKTIAFYKGDKLISPubiquitination[2]
671IAFYKGDKLISPLKKacetylation[1]
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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] 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
Functional Description
 Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. 
Sequence Annotation
 NP_BIND 116 118 Thiamine pyrophosphate.
 ACT_SITE 418 418 Proton donor (Probable).
 METAL 157 157 Magnesium.
 METAL 187 187 Magnesium.
 METAL 189 189 Magnesium; via carbonyl oxygen.
 BINDING 30 30 Substrate.
 BINDING 69 69 Thiamine pyrophosphate.
 BINDING 158 158 Thiamine pyrophosphate; via amide
 BINDING 187 187 Thiamine pyrophosphate.
 BINDING 263 263 Substrate.
 BINDING 263 263 Thiamine pyrophosphate.
 BINDING 359 359 Substrate.
 BINDING 386 386 Substrate.
 BINDING 418 418 Thiamine pyrophosphate.
 BINDING 445 445 Thiamine pyrophosphate.
 BINDING 469 469 Substrate.
 BINDING 477 477 Substrate.
 BINDING 528 528 Substrate.
 MOD_RES 286 286 Phosphoserine.
 MOD_RES 335 335 Phosphoserine.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 492 492 Phosphoserine.  
Keyword
 3D-structure; Calcium; Complete proteome; Direct protein sequencing; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Thiamine pyrophosphate; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 680 AA 
Protein Sequence
MTQFTDIDKL AVSTIRILAV DTVSKANSGH PGAPLGMAPA AHVLWSQMRM NPTNPDWINR 60
DRFVLSNGHA VALLYSMLHL TGYDLSIEDL KQFRQLGSRT PGHPEFELPG VEVTTGPLGQ 120
GISNAVGMAM AQANLAATYN KPGFTLSDNY TYVFLGDGCL QEGISSEASS LAGHLKLGNL 180
IAIYDDNKIT IDGATSISFD EDVAKRYEAY GWEVLYVENG NEDLAGIAKA IAQAKLSKDK 240
PTLIKMTTTI GYGSLHAGSH SVHGAPLKAD DVKQLKSKFG FNPDKSFVVP QEVYDHYQKT 300
ILKPGVEANN KWNKLFSEYQ KKFPELGAEL ARRLSGQLPA NWESKLPTYT AKDSAVATRK 360
LSETVLEDVY NQLPELIGGS ADLTPSNLTR WKEALDFQPP SSGSGNYSGR YIRYGIREHA 420
MGAIMNGISA FGANYKPYGG TFLNFVSYAA GAVRLSALSG HPVIWVATHD SIGVGEDGPT 480
HQPIETLAHF RSLPNIQVWR PADGNEVSAA YKNSLESKHT PSIIALSRQN LPQLEGSSIE 540
SASKGGYVLQ DVANPDIILV ATGSEVSLSV EAAKTLAAKN IKARVVSLPD FFTFDKQPLE 600
YRLSVLPDNV PIMSVEVLAT TCWGKYAHQS FGIDRFGASG KAPEVFKFFG FTPEGVAERA 660
QKTIAFYKGD KLISPLKKAF 680 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004802; F:transketolase activity; IMP:SGD.
 GO:0006098; P:pentose-phosphate shunt; IMP:SGD. 
Interpro
 IPR009014; Transketo_C/Pyr-ferredox_oxred.
 IPR015941; Transketolase-like_C.
 IPR005475; Transketolase-like_Pyr-bd.
 IPR005478; Transketolase_bac-like.
 IPR020826; Transketolase_BS.
 IPR005476; Transketolase_C.
 IPR005474; Transketolase_N. 
Pfam
 PF02779; Transket_pyr
 PF02780; Transketolase_C
 PF00456; Transketolase_N 
SMART
 SM00861; Transket_pyr 
PROSITE
 PS00801; TRANSKETOLASE_1
 PS00802; TRANSKETOLASE_2 
PRINTS