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P08237 (K6PF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphofructokinase, muscle type

EC=2.7.1.11
Alternative name(s):
Phosphofructo-1-kinase isozyme A
Short name=PFK-A
Short name=Phosphofructokinase-M
Phosphofructokinase 1
Phosphohexokinase
Gene names
Name:PFKM
Synonyms:PFKX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium.

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Tetramer. Muscle is M4, liver is L4, and red cell is M3L, M2L2, or ML3.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_00339

Involvement in disease

Glycogen storage disease 7 (GSD7) [MIM:232800]: A metabolic disorder characterized by exercise intolerance with associated nausea and vomiting, muscle cramping, exertional myopathy and compensated hemolysis. Short bursts of intense activity are particularly difficult. Severe muscle cramps and myoglobinuria develop after vigorous exercise.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14

Miscellaneous

In human PFK exists as a system of 3 types of subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet) isoenzymes.

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Glycogen storage disease
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from direct assay PubMed 6444721. Source: BHF-UCL

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

glycolysis

Inferred from mutant phenotype PubMed 6444532. Source: UniProtKB

muscle cell cellular homeostasis

Inferred from mutant phenotype PubMed 6444532. Source: BHF-UCL

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from direct assay PubMed 6444721. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_component6-phosphofructokinase complex

Inferred from direct assay PubMed 6444532PubMed 6444721. Source: UniProtKB

apical plasma membrane

Inferred from direct assay PubMed 12649290. Source: UniProtKB

   Molecular_function6-phosphofructokinase activity

Inferred from direct assay PubMed 6444721PubMed 8780720. Source: UniProtKB

ATP binding

Inferred from direct assay PubMed 8780720. Source: BHF-UCL

fructose binding

Inferred from direct assay PubMed 8780720. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-514788,EBI-514788
PFKLP178586EBI-514788,EBI-487243

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08237-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P08237-2)

The sequence of this isoform differs from the canonical sequence as follows:
     282-312: Missing.
Isoform 3 (identifier: P08237-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHKDEFHLKFFMCVIQSRQLVRTPQRTAGEASTSSMLIPKPPPKTDILKSLDTMDDPDTVGSIPVFKTEWIM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7807796-phosphofructokinase, muscle type HAMAP-Rule MF_00339
PRO_0000112016

Regions

Nucleotide binding35 – 395ATP By similarity
Nucleotide binding193 – 1975ATP By similarity
Nucleotide binding210 – 22617ATP By similarity

Sites

Active site1661Proton acceptor By similarity
Metal binding2241Magnesium; via carbonyl oxygen By similarity
Binding site2011Substrate By similarity
Binding site2921Substrate By similarity
Binding site2981Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue6671Phosphoserine Ref.10
Modified residue7751Phosphoserine By similarity
Glycosylation5301O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence11M → MHKDEFHLKFFMCVIQSRQL VRTPQRTAGEASTSSMLIPK PPPKTDILKSLDTMDDPDTV GSIPVFKTEWIM in isoform 3.
VSP_046125
Alternative sequence282 – 31231Missing in isoform 2.
VSP_004667
Natural variant391R → L in GSD7; Ashkenazi.
VAR_006063
Natural variant391R → P in GSD7; Italian. Ref.12
VAR_006064
Natural variant1001R → Q in GSD7; Swiss. Ref.13
Corresponds to variant rs2228500 [ dbSNP | Ensembl ].
VAR_006065
Natural variant2091G → D in GSD7; French Canadian. Ref.13
VAR_006066
Natural variant5431D → A in GSD7; Italian. Ref.12
VAR_006067
Natural variant6861W → C in GSD7; Japanese. Ref.14
VAR_006068
Natural variant6961R → H in GSD7; Swiss. Ref.13
Corresponds to variant rs41291971 [ dbSNP | Ensembl ].
VAR_006069

Experimental info

Sequence conflict6701P → S in BAC86498. Ref.4
Isoform 3:
Sequence conflict21H → L in BAC86498. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 769A2C01F97D1122

FASTA78085,183
        10         20         30         40         50         60 
MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD 

        70         80         90        100        110        120 
GGDHIKEATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAYNLVKRGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGADTFRS EWSDLLSDLQ KAGKITDEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRIMEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE 

       250        260        270        280        290        300 
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ 

       310        320        330        340        350        360 
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK 

       370        380        390        400        410        420 
AMDEKKFDEA LKLRGRSFMN NWEVYKLLAH VRPPVSKSGS HTVAVMNVGA PAAGMNAAVR 

       430        440        450        460        470        480 
STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ 

       490        500        510        520        530        540 
ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV 

       550        560        570        580        590        600 
GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF 

       610        620        630        640        650        660 
TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG 

       670        680        690        700        710        720 
HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF 

       730        740        750        760        770        780 
QPVAELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI TRKRSGEAAV 

« Hide

Isoform 2 [UniParc].

Checksum: FA4B5D6B077EDC8B
Show »

FASTA74981,776
Isoform 3 [UniParc].

Checksum: A09ABE529E682EC4
Show »

FASTA85193,254

References

« Hide 'large scale' references
[1]"Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system."
Yamasaki T., Nakajima H., Kono N., Hotta K., Yamada K., Imai E., Kuwajima M., Noguchi T., Tanaka T., Tarui S.
Gene 104:277-282(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Muscle.
[2]"Cloning and expression of a human muscle phosphofructokinase cDNA."
Sharma P.M., Reddy G.R., Vora S., Babior B.M., McLachlan A.
Gene 77:177-183(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
[3]"Cloning of human muscle phosphofructokinase cDNA."
Nakajima H., Noguchi T., Yamasaki T., Kono N., Tanaka T., Tarui S.
FEBS Lett. 223:113-116(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Thymus.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Muscle.
[7]"Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase."
Sharma P.M., Reddy G.R., Babior B.M., McLachlan A.
J. Biol. Chem. 265:9006-9010(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 272-681 (ISOFORM 2).
Tissue: Muscle.
[8]"Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon."
Valdez B.C., Chen Z., Sosa M.G., Younathan E.S., Chang S.H.
Gene 76:167-169(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
Tissue: Muscle.
[9]"Mutations in muscle phosphofructokinase gene."
Raben N., Sherman J.B.
Hum. Mutat. 6:1-6(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON GSD7 VARIANTS.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency."
Tsujino S., Servidei S., Tonin P., Shanske S., Azan G., DiMauro S.
Am. J. Hum. Genet. 54:812-819(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD7 PRO-39 AND ALA-543.
[13]"Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency."
Raben N., Exelbert R., Spiegel R., Sherman J.B., Plotz P., Heinisch J.J.
Am. J. Hum. Genet. 56:131-141(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD7 GLN-100; ASP-209 AND HIS-696.
[14]"Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII."
Hamaguchi T., Nakajima H., Noguchi T., Nakagawa C., Kuwajima M., Kono N., Tarui S., Matsuzawa Y.
Hum. Mutat. 8:273-275(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD7 CYS-686.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59741 expand/collapse EMBL AC list , M59720, M59721, M59722, M59723, M59724, M59725, M59726, M59727, M59728, M59729, M59730, M59731, M59732, M59733, M59734, M59735, M59736, M59737, M59738, M59739, M59740 Genomic DNA. Translation: AAA82938.1.
M26066 mRNA. Translation: AAA60068.1.
Y00698 mRNA. Translation: CAA68692.1.
AK126229 mRNA. Translation: BAC86498.1.
AC004801 Genomic DNA. No translation available.
AC074029 Genomic DNA. No translation available.
BC000534 mRNA. Translation: AAH00534.1.
BC012799 mRNA. Translation: AAH12799.1.
BC013298 mRNA. Translation: AAH13298.1.
BC021203 mRNA. Translation: AAH21203.1.
J05533 mRNA. Translation: AAA79220.1.
M24925 Genomic DNA. Translation: AAA36436.1.
PIRKIHUFM. A91605.
RefSeqNP_000280.1. NM_000289.5.
NP_001160158.1. NM_001166686.1.
NP_001160159.1. NM_001166687.1.
NP_001160160.1. NM_001166688.1.
XP_005269034.1. XM_005268977.1.
XP_005269035.1. XM_005268978.1.
XP_005269036.1. XM_005268979.1.
UniGeneHs.75160.

3D structure databases

ProteinModelPortalP08237.
SMRP08237. Positions 9-756.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111234. 19 interactions.
IntActP08237. 7 interactions.
MINTMINT-5005297.
STRING9606.ENSP00000352842.

Chemistry

BindingDBP08237.
ChEMBLCHEMBL3291.

PTM databases

PhosphoSiteP08237.

Polymorphism databases

DMDM125126.

2D gel databases

UCD-2DPAGEP08237.

Proteomic databases

PaxDbP08237.
PRIDEP08237.

Protocols and materials databases

DNASU5213.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312352; ENSP00000309438; ENSG00000152556. [P08237-1]
ENST00000340802; ENSP00000345771; ENSG00000152556. [P08237-3]
ENST00000359794; ENSP00000352842; ENSG00000152556. [P08237-1]
ENST00000395233; ENSP00000378656; ENSG00000152556. [P08237-2]
ENST00000547587; ENSP00000449426; ENSG00000152556. [P08237-1]
ENST00000551804; ENSP00000448177; ENSG00000152556. [P08237-2]
GeneID5213.
KEGGhsa:5213.
UCSCuc001rra.2. human. [P08237-1]
uc001rrg.2. human. [P08237-2]

Organism-specific databases

CTD5213.
GeneCardsGC12P048501.
HGNCHGNC:8877. PFKM.
HPAHPA002117.
MIM232800. phenotype.
610681. gene.
neXtProtNX_P08237.
Orphanet371. Glycogen storage disease due to muscle phosphofructokinase deficiency.
PharmGKBPA33216.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidP08237.
KOK00850.
OMAVYHMASK.
OrthoDBEOG7ZSHV5.
PhylomeDBP08237.
TreeFamTF300411.

Enzyme and pathway databases

BioCycMetaCyc:HS07832-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP08237.
UniPathwayUPA00109; UER00182.

Gene expression databases

ArrayExpressP08237.
BgeeP08237.
CleanExHS_PFKM.
GenevestigatorP08237.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPFKM. human.
GeneWikiPFKM.
GenomeRNAi5213.
NextBio20164.
PMAP-CutDBP08237.
PROP08237.
SOURCESearch...

Entry information

Entry nameK6PF_HUMAN
AccessionPrimary (citable) accession number: P08237
Secondary accession number(s): J3KNX3 expand/collapse secondary AC list , Q16814, Q16815, Q6ZTT1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM