CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004499
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 6-phosphofructokinase subunit beta 
Protein Synonyms/Alias
 6PF-1-K subunit beta; Phosphofructokinase 2; Phosphohexokinase 
Gene Name
 PFK2 
Gene Synonyms/Alias
 YMR205C; YM8325.06C 
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
33AAIDFYTKFLSLENRubiquitination[1]
66ILLRPDEKINKNVEAacetylation[2]
69RPDEKINKNVEAHLKacetylation[2]
76KNVEAHLKELNSITKacetylation[2]
83KELNSITKTQDWRSHacetylation[2]
150TKNAVSTKPTPPPAPubiquitination[1]
180TDLAYRMKTTDTYPSmethylation[3]
180TDLAYRMKTTDTYPSubiquitination[4]
190DTYPSLPKPLNRPQKacetylation[2]
248RGGPEYIKEFHWEDVacetylation[2]
369SALDRICKAIDYVEAubiquitination[1]
529NENKIVRKPLMESVKubiquitination[1]
536KPLMESVKLTKAVAEubiquitination[1]
539MESVKLTKAVAEAIQacetylation[2]
539MESVKLTKAVAEAIQubiquitination[1]
548VAEAIQAKDFKRAMSacetylation[2]
548VAEAIQAKDFKRAMSubiquitination[1]
641SVRSLNWKDMLGWQSubiquitination[1]
815EGRGRFGKLILKSTNacetylation[2]
815EGRGRFGKLILKSTNubiquitination[1]
819RFGKLILKSTNASKAubiquitination[1]
825LKSTNASKALSATKLubiquitination[1]
831SKALSATKLAEVITAubiquitination[1]
847ADGRFDAKPAYPGHVacetylation[2]
847ADGRFDAKPAYPGHVubiquitination[1]
938EVSMRMPKVIHWQATubiquitination[1, 5]
Reference
 [1] 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]
 [2] 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]
 [3] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [4] Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.
 Chi A, Huttenhower C, Geer LY, Coon JJ, Syka JE, Bai DL, Shabanowitz J, Burke DJ, Troyanskaya OG, Hunt DF.
 Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2193-8. [PMID: 17287358]
 [5] 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
  
Sequence Annotation
 NP_BIND 216 220 ATP (By similarity).
 NP_BIND 375 379 ATP (By similarity).
 NP_BIND 392 408 ATP (By similarity).
 ACT_SITE 348 348 Proton acceptor (By similarity).
 BINDING 383 383 Substrate (By similarity).
 BINDING 481 481 Substrate (By similarity).
 BINDING 484 484 Substrate (By similarity).
 MOD_RES 152 152 Phosphothreonine.
 MOD_RES 163 163 Phosphoserine.
 MOD_RES 171 171 Phosphoserine.
 MOD_RES 803 803 Phosphoserine.  
Keyword
 3D-structure; Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 959 AA 
Protein Sequence
MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL SNDSISLKIL 60
LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS DILAVKDTLN AMNAPLQGYP 120
TELFPMQLYT LDPLGNVVGV TSTKNAVSTK PTPPPAPEAS AESGLSSKVH SYTDLAYRMK 180
TTDTYPSLPK PLNRPQKAIA VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV 240
RGGPEYIKEF HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG 300
DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND MSTTDATIGA 360
YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL AGIATSADYI FIPEKPATSS 420
EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI AADLTPISPS DVHKVLVDRL GLDTRITTLG 480
HVQRGGTAVA YDRILATLQG LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA 540
VAEAIQAKDF KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG 600
INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG GSEIGTNRVT 660
PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR ESYPAFRIPM VLIPATLSNN 720
VPGTEYSLGS DTALNALMEY CDVVKQSASS TRGRAFVVDC QGGNSGYLAT YASLAVGAQV 780
SYVPEEGISL EQLSEDIEYL AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA 840
DGRFDAKPAY PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD 900
KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD HLVGRKRVD 959 
Gene Ontology
 GO:0005945; C:6-phosphofructokinase complex; IMP:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0003872; F:6-phosphofructokinase activity; IMP:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
 GO:0006096; P:glycolysis; IDA:SGD.
 GO:0015992; P:proton transport; IGI:UniProtKB. 
Interpro
 IPR009161; 6-phosphofructokinase_euk.
 IPR022953; Phosphofructokinase.
 IPR015912; Phosphofructokinase_CS.
 IPR000023; Phosphofructokinase_dom. 
Pfam
 PF00365; PFK 
SMART
  
PROSITE
 PS00433; PHOSPHOFRUCTOKINASE 
PRINTS
 PR00476; PHFRCTKINASE.