CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004618
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 6-phosphofructokinase, liver type 
Protein Synonyms/Alias
 Phosphofructo-1-kinase isozyme B; PFK-B; Phosphofructokinase 1; Phosphohexokinase 
Gene Name
 PFKL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MAAVDLEKLRASGAGubiquitination[1, 2]
16LRASGAGKAIGVLTSubiquitination[2, 3, 4, 5]
144EELVAEGKISETTARubiquitination[3, 4]
272GAIDRNGKPISSSYVubiquitination[2, 3]
280PISSSYVKDLVVQRLubiquitination[2]
356MECVQMTKEVQKAMDubiquitination[2, 4]
365VQKAMDDKRFDEATQubiquitination[2]
386ENNWNIYKLLAHQKPubiquitination[2]
392YKLLAHQKPPKEKSNubiquitination[6]
397HQKPPKEKSNFSLAIubiquitination[2]
469GGSMLGTKRTLPKGQubiquitination[3]
474GTKRTLPKGQLESIVubiquitination[2, 3]
556MESCDRIKQSASGTKubiquitination[3]
563KQSASGTKRRVFIVEubiquitination[3]
614NVEHMTEKMKTDIQRubiquitination[3]
616EHMTEKMKTDIQRGLubiquitination[2]
677FDRNYGTKLGVKAMLubiquitination[2, 3, 6]
681YGTKLGVKAMLWLSEubiquitination[2]
689AMLWLSEKLREVYRKacetylation[7]
714ACVIGLKKKAVAFSPubiquitination[2]
715CVIGLKKKAVAFSPVubiquitination[2]
726FSPVTELKKDTDFEHacetylation[8]
778RRTLSMDKGF*****ubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP. 
Sequence Annotation
 NP_BIND 35 39 ATP (By similarity).
 NP_BIND 193 197 ATP (By similarity).
 NP_BIND 210 226 ATP (By similarity).
 ACT_SITE 166 166 Proton acceptor (By similarity).
 METAL 224 224 Magnesium; via carbonyl oxygen (By
 BINDING 201 201 Substrate (By similarity).
 BINDING 292 292 Substrate (By similarity).
 BINDING 298 298 Substrate (By similarity).
 BINDING 301 301 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 640 640 Phosphotyrosine (By similarity).
 MOD_RES 775 775 Phosphoserine.
 CARBOHYD 529 529 O-linked (GlcNAc...).  
Keyword
 Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 780 AA 
Protein Sequence
MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE 60
GGENIKQANW LSVSNIIQLG GTIIGSARCK AFTTREGRRA AAYNLVQHGI TNLCVIGGDG 120
SLTGANIFRS EWGSLLEELV AEGKISETTA RTYSHLNIAG LVGSIDNDFC GTDMTIGTDS 180
ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE 240
NFMCERLGET RSRGSRLNII IIAEGAIDRN GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 300
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVTLSG NQSVRLPLME CVQMTKEVQK 360
AMDDKRFDEA TQLRGGSFEN NWNIYKLLAH QKPPKEKSNF SLAILNVGAP AAGMNAAVRS 420
AVRTGISHGH TVYVVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKGQLESI 480
VENIRIYGIH ALLVVGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG 540
SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 600
IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV FDCRTNVLGH 660
LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL REVYRKGRVF ANAPDSACVI GLKKKAVAFS 720
PVTELKKDTD FEHRMPREQW WLSLRLMLKM LAQYRISMAA YVSGELEHVT RRTLSMDKGF 780 
Gene Ontology
 GO:0005945; C:6-phosphofructokinase complex; IDA:UniProtKB.
 GO:0003872; F:6-phosphofructokinase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0070061; F:fructose binding; IDA:BHF-UCL.
 GO:0070095; F:fructose-6-phosphate binding; IDA:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:UniProtKB.
 GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
 GO:0006096; P:glycolysis; IDA:UniProtKB.
 GO:0046676; P:negative regulation of insulin secretion; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0051259; P:protein oligomerization; IDA:BHF-UCL.
 GO:0009749; P:response to glucose stimulus; IDA:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR009161; 6-phosphofructokinase_euk.
 IPR022953; Phosphofructokinase.
 IPR015912; Phosphofructokinase_CS.
 IPR000023; Phosphofructokinase_dom. 
Pfam
 PF00365; PFK 
SMART
  
PROSITE
 PS00433; PHOSPHOFRUCTOKINASE 
PRINTS
 PR00476; PHFRCTKINASE.