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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

Pfkp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATP; via amide nitrogenUniRule annotation
Metal bindingi127 – 1271Magnesium; catalyticUniRule annotation
Active sitei174 – 1741Proton acceptorUniRule annotation
Binding sitei209 – 2091Substrate; shared with dimeric partnerUniRule annotation
Binding sitei272 – 2721SubstrateUniRule annotation
Binding sitei300 – 3001Substrate; shared with dimeric partnerUniRule annotation
Binding sitei480 – 4801Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei575 – 5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei638 – 6381Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei664 – 6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei743 – 7431Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 972ATPUniRule annotation
Nucleotide bindingi126 – 1294ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein complex binding Source: MGI

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.11. 3474.
ReactomeiREACT_314687. Glycolysis.
SABIO-RKQ9WUA3.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-P
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name:
PFK-C
PhosphohexokinaseUniRule annotation
Gene namesi
Name:Pfkp
Synonyms:Pfkc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1891833. Pfkp.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: MGI
  2. cytosol Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. membrane Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 784784ATP-dependent 6-phosphofructokinase, platelet typePRO_0000112025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei394 – 3941N6-acetyllysineBy similarity
Modified residuei485 – 4851N6-acetyllysineBy similarity
Glycosylationi539 – 5391O-linked (GlcNAc)By similarity
Modified residuei650 – 6501Phosphotyrosine1 Publication
Modified residuei687 – 6871N6-acetyllysine1 Publication

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9WUA3.
PaxDbiQ9WUA3.
PRIDEiQ9WUA3.

PTM databases

PhosphoSiteiQ9WUA3.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9WUA3.
CleanExiMM_PFKP.
ExpressionAtlasiQ9WUA3. baseline and differential.
GenevestigatoriQ9WUA3.

Interactioni

Subunit structurei

Homo- and heterotetramers.UniRule annotation

Protein-protein interaction databases

BioGridi207967. 3 interactions.
IntActiQ9WUA3. 5 interactions.
MINTiMINT-1676159.
STRINGi10090.ENSMUSP00000117030.

Structurei

3D structure databases

ProteinModelPortaliQ9WUA3.
SMRiQ9WUA3. Positions 21-763.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 398398N-terminal catalytic PFK domain 1Add
BLAST
Regioni172 – 1743Substrate bindingUniRule annotation
Regioni216 – 2183Substrate bindingUniRule annotation
Regioni306 – 3094Substrate bindingUniRule annotation
Regioni399 – 41012Interdomain linkerAdd
BLAST
Regioni411 – 784374C-terminal regulatory PFK domain 2Add
BLAST
Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni670 – 6734Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOVERGENiHBG000976.
InParanoidiQ9WUA3.
KOiK00850.
OMAiKMCQKLS.
OrthoDBiEOG7ZSHV5.
TreeFamiTF300411.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WUA3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI
60 70 80 90 100
YTGAKVYFIY EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF
110 120 130 140 150
RSREGRLKAA CNLARLGITN LCVIGGDGSL TGANLFRKEW SGLLEELARN
160 170 180 190 200
GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT DMTIGTDSAL HRIIEVVDAI
210 220 230 240 250
MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE SPPEEDWEEN
260 270 280 290 300
MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR
310 320 330 340 350
VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ
360 370 380 390 400
AVRLPLMECV QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL
410 420 430 440 450
PDEKIVKSNC NVAVINVGAP AAGMNAAVRS AVRVGIADGH KMFAIYDGFE
460 470 480 490 500
GFANGQIKEI GWADVGGWTG QGGSILGTKR TLPGKYLEKI AEQMHSHSIN
510 520 530 540 550
ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN NVPGSDFSIG
560 570 580 590 600
ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD
610 620 630 640 650
AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY
660 670 680 690 700
QLYSEEGKGV FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL
710 720 730 740 750
KGSQGTGKKF VSDDSICVLG ICKRDLLFQP VAELKKVTDF EHRIPKEQWW
760 770 780
LKLRPIMKIL AKYEASYDMS DSGKLESLQH HEEL
Length:784
Mass (Da):85,455
Last modified:October 31, 1999 - v1
Checksum:iE9C5AAABF26FCA65
GO
Isoform 2 (identifier: Q9WUA3-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:496
Mass (Da):53,682
Checksum:i22E3CB5080FD748C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041E → V in strain: NOD. 1 Publication
Natural varianti145 – 1451E → G in strain: C57BL/6J. 1 Publication
Natural varianti180 – 1801T → P in strain: C57BL/6. 1 Publication
Natural varianti261 – 2611R → Q in strain: LG/J and NOD. 2 Publications
Natural varianti292 – 2921V → M in strain: LG/J and NOD. 2 Publications
Natural varianti402 – 4021D → E in strain: C57BL/6J. 1 Publication
Natural varianti679 – 6791P → S in strain: C57BL/6J. 1 Publication
Natural varianti694 – 6941E → D in strain: LG/J and NOD. 2 Publications
Natural varianti696 – 6961I → F in strain: NOD. 1 Publication
Natural varianti777 – 7771S → P in strain: LG/J and NOD. 2 Publications
Natural varianti782 – 7821E → G in strain: LG/J and NOD. 2 Publications

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei457 – 49640IKEIG…EQMHS → VSLPGVLGMLKCYCIWGGHP PLTAPTKSRFLVVGLYQILI in isoform 2. 1 PublicationVSP_016664Add
BLAST
Alternative sequencei497 – 784288Missing in isoform 2. 1 PublicationVSP_016665Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y19008 mRNA. Translation: CAB64347.1.
AF123533 mRNA. Translation: AAD23571.1.
AF249893
, 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.
CCDSiCCDS26230.1. [Q9WUA3-1]
RefSeqiNP_001278000.1. NM_001291071.1.
NP_062677.1. NM_019703.4. [Q9WUA3-1]
UniGeneiMm.273874.

Genome annotation databases

EnsembliENSMUST00000138703; ENSMUSP00000117030; ENSMUSG00000021196. [Q9WUA3-1]
GeneIDi56421.
KEGGimmu:56421.
UCSCiuc007pjz.1. mouse. [Q9WUA3-1]
uc007pkc.1. mouse. [Q9WUA3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y19008 mRNA. Translation: CAB64347.1.
AF123533 mRNA. Translation: AAD23571.1.
AF249893
, 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.
CCDSiCCDS26230.1. [Q9WUA3-1]
RefSeqiNP_001278000.1. NM_001291071.1.
NP_062677.1. NM_019703.4. [Q9WUA3-1]
UniGeneiMm.273874.

3D structure databases

ProteinModelPortaliQ9WUA3.
SMRiQ9WUA3. Positions 21-763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207967. 3 interactions.
IntActiQ9WUA3. 5 interactions.
MINTiMINT-1676159.
STRINGi10090.ENSMUSP00000117030.

PTM databases

PhosphoSiteiQ9WUA3.

Proteomic databases

MaxQBiQ9WUA3.
PaxDbiQ9WUA3.
PRIDEiQ9WUA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000138703; ENSMUSP00000117030; ENSMUSG00000021196. [Q9WUA3-1]
GeneIDi56421.
KEGGimmu:56421.
UCSCiuc007pjz.1. mouse. [Q9WUA3-1]
uc007pkc.1. mouse. [Q9WUA3-2]

Organism-specific databases

CTDi5214.
MGIiMGI:1891833. Pfkp.

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOVERGENiHBG000976.
InParanoidiQ9WUA3.
KOiK00850.
OMAiKMCQKLS.
OrthoDBiEOG7ZSHV5.
TreeFamiTF300411.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BRENDAi2.7.1.11. 3474.
ReactomeiREACT_314687. Glycolysis.
SABIO-RKQ9WUA3.

Miscellaneous databases

ChiTaRSiPfkp. mouse.
NextBioi312572.
PROiQ9WUA3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUA3.
CleanExiMM_PFKP.
ExpressionAtlasiQ9WUA3. baseline and differential.
GenevestigatoriQ9WUA3.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(1999) [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(2004) [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.
    , 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(2004) [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 (JUN-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(2003) [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(2006) [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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPFKAP_MOUSE
AccessioniPrimary (citable) accession number: Q9WUA3
Secondary accession number(s): Q3TNA9
, Q3U4P1, Q3U7G4, Q4KUG1, Q543K8, Q8C5I6, Q9JI86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2001
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.