UniProt Accession

 K6PF_HUMAN; P08237; J3KNX3; Q16814; Q16815; Q6ZTT1 

Genbank Protein ID

 M59741; M59720; M59721; M59722; M59723; M59724; M59725; M59726; M59727; M59728; M59729; M59730; M59731; M59732; M59733; M59734; M59735; M59736; M59737; M59738; M59739; M59740; M26066; Y00698; AK126229; AC004801; AC074029; BC000534; BC012799; BC013298; BC021203; J05533; M24925 

Genbank Nucleotide ID

 AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA82938.1; AAA60068.1; CAA68692.1; BAC86498.1; AAH00534.1; AAH12799.1; AAH13298.1; AAH21203.1; AAA79220.1; AAA36436.1 

Protein Name

 6-phosphofructokinase, muscle type 

Protein Synonyms/Alias

 Phosphofructo-1-kinase isozyme A; PFK-A; Phosphofructokinase-M; Phosphofructokinase 1; Phosphohexokinase 

Gene Name

 PFKM 

Gene Synonyms/Alias

 PFKX 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
10	HEEHHAAKTLGIGKA	acetylation	[1]
16	AKTLGIGKAIAVLTS	ubiquitination	[2]
141	DLLSDLQKAGKITDE	ubiquitination	[2]
144	SDLQKAGKITDEEAT	ubiquitination	[2]
272	GAIDKNGKPITSEDI	ubiquitination	[2, 3]
280	PITSEDIKNLVVKRL	ubiquitination	[2]
360	QVTKDVTKAMDEKKF	ubiquitination	[2]
366	TKAMDEKKFDEALKL	ubiquitination	[2]
372	KKFDEALKLRGRSFM	ubiquitination	[2, 3]
397	HVRPPVSKSGSHTVA	ubiquitination	[4]
445	DGFEGLAKGQIEEAG	ubiquitination	[2]
466	WTGQGGSKLGTKRTL	ubiquitination	[2]
615	NVEHLVQKMKTTVKR	ubiquitination	[2, 4]
656	KGIFDSRKNVLGHMQ	ubiquitination	[2, 4]
678	FDRNFATKMGAKAMN	ubiquitination	[2, 3, 4]
682	FATKMGAKAMNWMSG	ubiquitination	[2, 3, 4]
727	FQPVAELKDQTDFEH	acetylation	[5]
727	FQPVAELKDQTDFEH	ubiquitination	[2, 3, 4]
738	DFEHRIPKEQWWLKL	ubiquitination	[2]
744	PKEQWWLKLRPILKI	ubiquitination	[4]
750	LKLRPILKILAKYEI	ubiquitination	[4]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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-acetylthreonine (By similarity).
 MOD_RES 667 667 Phosphoserine.
 MOD_RES 775 775 Phosphoserine (By similarity).
 CARBOHYD 530 530 O-linked (GlcNAc...) (By similarity).  

Keyword

 Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding; Complete proteome; Disease mutation; Glycogen storage disease; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 780 AA 

Protein Sequence

Gene Ontology

 GO:0005945; C:6-phosphofructokinase complex; IDA:UniProtKB.
 GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
 GO:0003872; F:6-phosphofructokinase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:BHF-UCL.
 GO:0070061; F:fructose binding; IDA:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006002; P:fructose 6-phosphate metabolic process; IDA:BHF-UCL.
 GO:0006096; P:glycolysis; IMP:UniProtKB.
 GO:0046716; P:muscle cell homeostasis; IMP:BHF-UCL.
 GO:0051259; P:protein oligomerization; IDA:BHF-UCL.
 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.