CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010884
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 6-phosphofructokinase type C 
Protein Synonyms/Alias
 6-phosphofructokinase, platelet type; Phosphofructo-1-kinase isozyme C; PFK-C; Phosphofructokinase 1; Phosphohexokinase 
Gene Name
 PFKP 
Gene Synonyms/Alias
 PFKF 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10ADDSRAPKGSLRKFLubiquitination[1]
15APKGSLRKFLEHLSGubiquitination[1, 2, 3, 4, 5]
25EHLSGAGKAIGVLTSubiquitination[1, 6, 7]
109RTREGRLKAACNLLQacetylation[5]
109RTREGRLKAACNLLQmethylation[8]
109RTREGRLKAACNLLQubiquitination[1, 5, 9]
139TGANLFRKEWSGLLEubiquitination[1, 2, 4, 5, 6, 7, 9, 10]
156ARNGQIDKEAVQKYAacetylation[5]
156ARNGQIDKEAVQKYAubiquitination[1, 5, 6]
287NKPITSEKIKELVVTubiquitination[6]
289PITSEKIKELVVTQLubiquitination[1, 6, 9]
395AGNLNTYKRLAIKLPacetylation[11]
395AGNLNTYKRLAIKLPubiquitination[1, 2, 3, 4, 6, 7, 9]
400TYKRLAIKLPDDQIPubiquitination[1, 2, 4, 6, 7]
455DGFDGFAKGQIKEIGubiquitination[1, 6]
459GFAKGQIKEIGWTDVubiquitination[1, 2, 4, 6, 7]
480GGSILGTKRVLPGKYubiquitination[1, 6, 7, 9]
486TKRVLPGKYLEEIATacetylation[11]
486TKRVLPGKYLEEIATubiquitination[1, 2, 4, 6, 7]
567TDTCDRIKQSASGTKubiquitination[6]
625NVEHLTEKMKTTIQRubiquitination[1, 6]
627EHLTEKMKTTIQRGLubiquitination[1]
666KGVFDCRKNVLGHMQubiquitination[1, 2, 4, 7]
688FDRNFGTKISARAMEacetylation[11]
688FDRNFGTKISARAMEubiquitination[1, 6, 7]
700AMEWITAKLKEARGRacetylation[12]
700AMEWITAKLKEARGRubiquitination[1]
724ICVLGISKRNVIFQPubiquitination[1]
736FQPVAELKKQTDFEHubiquitination[1, 6]
737QPVAELKKQTDFEHRubiquitination[1]
747DFEHRIPKEQWWLKLacetylation[12]
747DFEHRIPKEQWWLKLubiquitination[1, 2, 4, 6]
753PKEQWWLKLRPLMKIacetylation[11]
759LKLRPLMKILAKYKAubiquitination[1, 7, 9]
763PLMKILAKYKASYDVubiquitination[7]
765MKILAKYKASYDVSDubiquitination[1, 2, 4]
Reference
 [1] 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]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [9] 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]
 [10] 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]
 [11] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [12] 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] 
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 44 48 ATP (By similarity).
 NP_BIND 202 206 ATP (By similarity).
 NP_BIND 219 235 ATP (By similarity).
 ACT_SITE 175 175 Proton acceptor (By similarity).
 METAL 233 233 Magnesium; via carbonyl oxygen (By
 BINDING 210 210 Substrate (By similarity).
 BINDING 301 301 Substrate (By similarity).
 BINDING 307 307 Substrate (By similarity).
 BINDING 310 310 Substrate (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 12 12 Phosphoserine (By similarity).
 MOD_RES 386 386 Phosphoserine.
 MOD_RES 395 395 N6-acetyllysine.
 MOD_RES 486 486 N6-acetyllysine.
 MOD_RES 651 651 Phosphotyrosine.
 MOD_RES 688 688 N6-acetyllysine.
 MOD_RES 783 783 Phosphoserine.
 CARBOHYD 540 540 O-linked (GlcNAc...) (By similarity).  
Keyword
 Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 784 AA 
Protein Sequence
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVYFI 60
YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA FRTREGRLKA ACNLLQRGIT 120
NLCVIGGDGS LTGANLFRKE WSGLLEELAR NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG 180
TDMTIGTDSA LHRIIEVVDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP 240
ESPPEEGWEE QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT 300
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN HAVRLPLMEC 360
VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK LPDDQIPKTN CNVAVINVGA 420
PAAGMNAAVR SAVRVGIADG HRMLAIYDGF DGFAKGQIKE IGWTDVGGWT GQGGSILGTK 480
RVLPGKYLEE IATQMRTHSI NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS 540
NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA 600
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGKG 660
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK LKEARGRGKK FTTDDSICVL 720
GISKRNVIFQ PVAELKKQTD FEHRIPKEQW WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ 780
PWSV 784 
Gene Ontology
 GO:0005945; C:6-phosphofructokinase complex; NAS:UniProtKB.
 GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
 GO:0006096; P:glycolysis; NAS: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.