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Q9WUA3

- PFKAP_MOUSE

UniProt

Q9WUA3 - PFKAP_MOUSE

Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

Pfkp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    Magnesium.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

    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.
    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: 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

    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

    ArrayExpressiQ9WUA3.
    BgeeiQ9WUA3.
    CleanExiMM_PFKP.
    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 21-764.
    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.
    OMAiSAKAMQW.
    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. Align

    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

    MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI    50
    YTGAKVYFIY EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF 100
    RSREGRLKAA CNLARLGITN LCVIGGDGSL TGANLFRKEW SGLLEELARN 150
    GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT DMTIGTDSAL HRIIEVVDAI 200
    MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE SPPEEDWEEN 250
    MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR 300
    VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ 350
    AVRLPLMECV QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL 400
    PDEKIVKSNC NVAVINVGAP AAGMNAAVRS AVRVGIADGH KMFAIYDGFE 450
    GFANGQIKEI GWADVGGWTG QGGSILGTKR TLPGKYLEKI AEQMHSHSIN 500
    ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN NVPGSDFSIG 550
    ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD 600
    AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY 650
    QLYSEEGKGV FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL 700
    KGSQGTGKKF VSDDSICVLG ICKRDLLFQP VAELKKVTDF EHRIPKEQWW 750
    LKLRPIMKIL AKYEASYDMS DSGKLESLQH HEEL 784
    Length:784
    Mass (Da):85,455
    Last modified:November 1, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS26230.1. [Q9WUA3-1 ]
    RefSeqi NP_001278000.1. NM_001291071.1.
    NP_062677.1. NM_019703.4. [Q9WUA3-1 ]
    UniGenei Mm.273874.

    3D structure databases

    ProteinModelPortali Q9WUA3.
    SMRi Q9WUA3. Positions 21-764.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207967. 3 interactions.
    IntActi Q9WUA3. 5 interactions.
    MINTi MINT-1676159.
    STRINGi 10090.ENSMUSP00000117030.

    PTM databases

    PhosphoSitei Q9WUA3.

    Proteomic databases

    MaxQBi Q9WUA3.
    PaxDbi Q9WUA3.
    PRIDEi Q9WUA3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000138703 ; ENSMUSP00000117030 ; ENSMUSG00000021196 . [Q9WUA3-1 ]
    GeneIDi 56421.
    KEGGi mmu:56421.
    UCSCi uc007pjz.1. mouse. [Q9WUA3-1 ]
    uc007pkc.1. mouse. [Q9WUA3-2 ]

    Organism-specific databases

    CTDi 5214.
    MGIi MGI:1891833. Pfkp.

    Phylogenomic databases

    eggNOGi COG0205.
    GeneTreei ENSGT00390000013209.
    HOVERGENi HBG000976.
    InParanoidi Q9WUA3.
    KOi K00850.
    OMAi SAKAMQW.
    OrthoDBi EOG7ZSHV5.
    TreeFami TF300411.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BRENDAi 2.7.1.11. 3474.
    SABIO-RK Q9WUA3.

    Miscellaneous databases

    NextBioi 312572.
    PROi Q9WUA3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WUA3.
    Bgeei Q9WUA3.
    CleanExi MM_PFKP.
    Genevestigatori Q9WUA3.

    Family and domain databases

    HAMAPi MF_03184. Phosphofructokinase_I_E.
    InterProi IPR009161. 6-phosphofructokinase_euk.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view ]
    Pfami PF00365. PFK. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 2 hits.
    TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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 27, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 116 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