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Q9WUA3 (PFKAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase, platelet type

Short name=ATP-PFK
Short name=PFK-P
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphohexokinase
Gene names
Name:Pfkp
Synonyms:Pfkc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. HAMAP-Rule MF_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homo- and heterotetramers By similarity. HAMAP-Rule MF_03184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Tissue specificity

Expression is constant during tumor growth and markedly decreases when cell proliferation stops. Ref.1

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_03184

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WUA3-1)

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: Q9WUA3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     457-496: IKEIGWADVG...LEKIAEQMHS → VSLPGVLGML...LVVGLYQILI
     497-784: Missing.
Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784ATP-dependent 6-phosphofructokinase, platelet type HAMAP-Rule MF_03184
PRO_0000112025

Regions

Nucleotide binding96 – 972ATP By similarity
Nucleotide binding126 – 1294ATP By similarity
Region1 – 398398N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region172 – 1743Substrate binding By similarity
Region216 – 2183Substrate binding By similarity
Region306 – 3094Substrate binding By similarity
Region399 – 41012Interdomain linker HAMAP-Rule MF_03184
Region411 – 784374C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region537 – 5415Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region582 – 5843Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region670 – 6734Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1741Proton acceptor By similarity
Metal binding1271Magnesium; catalytic By similarity
Binding site331ATP; via amide nitrogen By similarity
Binding site2091Substrate; shared with dimeric partner By similarity
Binding site2721Substrate By similarity
Binding site3001Substrate; shared with dimeric partner By similarity
Binding site4801Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6381Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7431Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3941N6-acetyllysine By similarity
Modified residue4851N6-acetyllysine By similarity
Modified residue6501Phosphotyrosine Ref.7
Modified residue6871N6-acetyllysine Ref.8
Glycosylation5391O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence457 – 49640IKEIG…EQMHS → VSLPGVLGMLKCYCIWGGHP PLTAPTKSRFLVVGLYQILI in isoform 2.
VSP_016664
Alternative sequence497 – 784288Missing in isoform 2.
VSP_016665
Natural variant1041E → V in strain: NOD. Ref.4
Natural variant1451E → G in strain: C57BL/6J. Ref.4
Natural variant1801T → P in strain: C57BL/6. Ref.2
Natural variant2611R → Q in strain: LG/J and NOD. Ref.3 Ref.4
Natural variant2921V → M in strain: LG/J and NOD. Ref.3 Ref.4
Natural variant4021D → E in strain: C57BL/6J. Ref.4
Natural variant6791P → S in strain: C57BL/6J. Ref.4
Natural variant6941E → D in strain: LG/J and NOD. Ref.3 Ref.4
Natural variant6961I → F in strain: NOD. Ref.4
Natural variant7771S → P in strain: LG/J and NOD. Ref.3 Ref.4
Natural variant7821E → G in strain: LG/J and NOD. Ref.3 Ref.4

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: E9C5AAABF26FCA65

FASTA78485,455
        10         20         30         40         50         60 
MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI YTGAKVYFIY 

        70         80         90        100        110        120 
EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF RSREGRLKAA CNLARLGITN 

       130        140        150        160        170        180 
LCVIGGDGSL TGANLFRKEW SGLLEELARN GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT 

       190        200        210        220        230        240 
DMTIGTDSAL HRIIEVVDAI MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE 

       250        260        270        280        290        300 
SPPEEDWEEN MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR 

       310        320        330        340        350        360 
VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ AVRLPLMECV 

       370        380        390        400        410        420 
QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL PDEKIVKSNC NVAVINVGAP 

       430        440        450        460        470        480 
AAGMNAAVRS AVRVGIADGH KMFAIYDGFE GFANGQIKEI GWADVGGWTG QGGSILGTKR 

       490        500        510        520        530        540 
TLPGKYLEKI AEQMHSHSIN ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN 

       550        560        570        580        590        600 
NVPGSDFSIG ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD 

       610        620        630        640        650        660 
AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY QLYSEEGKGV 

       670        680        690        700        710        720 
FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL KGSQGTGKKF VSDDSICVLG 

       730        740        750        760        770        780 
ICKRDLLFQP VAELKKVTDF EHRIPKEQWW LKLRPIMKIL AKYEASYDMS DSGKLESLQH 


HEEL 

« Hide

Isoform 2 [UniParc].

Checksum: 22E3CB5080FD748C
Show »

FASTA49653,682

References

« Hide 'large scale' references
[1]"Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties."
Sanchez-Martinez C., Estevez A.M., Aragon J.J.
Biochem. Biophys. Res. Commun. 271:635-640(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Ascitic tumor.
[2]"Genomic organization, 5'flanking region and tissue-specific expression of mouse phosphofructokinase C gene."
Gunasekera D., Kemp R.G.
Gene 260:103-112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PRO-180.
Strain: C57BL/6.
Tissue: Brain.
[3]"Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x SM/J murine model of obesity."
Ehrich T.H., Hrbek T., Kenney-Hunt J.P., Pletscher L.S., Wang B., Semenkovich C.F., Cheverud J.M.
Diabetes 54:1863-1872(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-261; MET-292; ASP-694; PRO-777 AND GLY-782.
Strain: LG/J and SM/J.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-104; GLY-145; GLN-261; MET-292; GLU-402; SER-679; ASP-694; PHE-696; PRO-777 AND GLY-782.
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Hippocampus, Kidney and Olfactory bulb.
[5]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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).
Strain: FVB/N-3.
Tissue: Mammary gland.
[7]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y19008 mRNA. Translation: CAB64347.1.
AF123533 mRNA. Translation: AAD23571.1.
AF249893 expand/collapse EMBL AC list , AF250369, AF250370, AF250371, AF250372, AF251021 Genomic DNA. Translation: AAF75700.1.
AY779275 mRNA. Translation: AAX11357.1.
AY779276 mRNA. Translation: AAX11358.1.
AK049841 mRNA. Translation: BAC33949.1.
AK078254 mRNA. Translation: BAC37195.1.
AK152670 mRNA. Translation: BAE31405.1.
AK154125 mRNA. Translation: BAE32390.1.
AK165422 mRNA. Translation: BAE38177.1.
AK165425 mRNA. Translation: BAE38180.1.
AK170624 mRNA. Translation: BAE41918.1.
AK171062 mRNA. Translation: BAE42221.1.
CT010268 mRNA. Translation: CAJ18476.1.
BC006926 mRNA. Translation: AAH06926.1.
CCDSCCDS26230.1. [Q9WUA3-1]
RefSeqNP_001278000.1. NM_001291071.1.
NP_062677.1. NM_019703.4. [Q9WUA3-1]
UniGeneMm.273874.

3D structure databases

ProteinModelPortalQ9WUA3.
SMRQ9WUA3. Positions 21-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207967. 3 interactions.
IntActQ9WUA3. 5 interactions.
MINTMINT-1676159.
STRING10090.ENSMUSP00000117030.

PTM databases

PhosphoSiteQ9WUA3.

Proteomic databases

MaxQBQ9WUA3.
PaxDbQ9WUA3.
PRIDEQ9WUA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000138703; ENSMUSP00000117030; ENSMUSG00000021196. [Q9WUA3-1]
GeneID56421.
KEGGmmu:56421.
UCSCuc007pjz.1. mouse. [Q9WUA3-1]
uc007pkc.1. mouse. [Q9WUA3-2]

Organism-specific databases

CTD5214.
MGIMGI:1891833. Pfkp.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOVERGENHBG000976.
InParanoidQ9WUA3.
KOK00850.
OMASAKAMQW.
OrthoDBEOG7ZSHV5.
TreeFamTF300411.

Enzyme and pathway databases

BRENDA2.7.1.11. 3474.
SABIO-RKQ9WUA3.
UniPathwayUPA00109; UER00182.

Gene expression databases

ArrayExpressQ9WUA3.
BgeeQ9WUA3.
CleanExMM_PFKP.
GenevestigatorQ9WUA3.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
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

NextBio312572.
PROQ9WUA3.
SOURCESearch...

Entry information

Entry namePFKAP_MOUSE
AccessionPrimary (citable) accession number: Q9WUA3
Secondary accession number(s): Q3TNA9 expand/collapse secondary AC list , Q3U4P1, Q3U7G4, Q4KUG1, Q543K8, Q8C5I6, Q9JI86
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot