Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9WUA3 (K6PP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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:
6-phosphofructokinase type C

EC=2.7.1.11
Alternative name(s):
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphofructokinase 1
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 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 By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate By similarity. 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

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_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains 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 – 7847846-phosphofructokinase type C HAMAP-Rule MF_00339
PRO_0000112025

Regions

Nucleotide binding43 – 475ATP By similarity
Nucleotide binding201 – 2055ATP By similarity
Nucleotide binding218 – 23417ATP By similarity

Sites

Active site1741Proton acceptor By similarity
Metal binding2321Magnesium; via carbonyl oxygen By similarity
Binding site2091Substrate By similarity
Binding site3001Substrate By similarity
Binding site3061Substrate By similarity
Binding site3091Substrate 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.
RefSeqNP_062677.1. NM_019703.3.
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

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.
OMAPLVECVQ.
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_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

NextBio312572.
PROQ9WUA3.
SOURCESearch...

Entry information

Entry nameK6PP_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: April 16, 2014
This is version 112 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