Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01813

- PFKAP_HUMAN

UniProt

Q01813 - PFKAP_HUMAN

Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

PFKP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    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 sitei34 – 341ATP; via amide nitrogenUniRule annotation
    Metal bindingi128 – 1281Magnesium; catalyticUniRule annotation
    Active sitei175 – 1751Proton acceptorUniRule annotation
    Binding sitei210 – 2101Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei273 – 2731SubstrateUniRule annotation
    Binding sitei301 – 3011Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei481 – 4811Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei576 – 5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei639 – 6391Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei744 – 7441Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi97 – 982ATPUniRule annotation
    Nucleotide bindingi127 – 1304ATPUniRule 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 metabolic process Source: Reactome
    2. carbohydrate phosphorylation Source: GOC
    3. fructose 6-phosphate metabolic process Source: InterPro
    4. glucose metabolic process Source: Reactome
    5. glycolytic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00894-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    SABIO-RKQ01813.
    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:PFKF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8878. PFKP.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33217.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 784784ATP-dependent 6-phosphofructokinase, platelet typePRO_0000112024Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei386 – 3861Phosphoserine5 Publications
    Modified residuei395 – 3951N6-acetyllysine1 Publication
    Modified residuei486 – 4861N6-acetyllysine1 Publication
    Glycosylationi540 – 5401O-linked (GlcNAc)By similarity
    Modified residuei651 – 6511Phosphotyrosine1 Publication
    Modified residuei688 – 6881N6-acetyllysine1 Publication
    Modified residuei783 – 7831Phosphoserine4 Publications

    Post-translational modificationi

    GlcNAcylation decreases enzyme activity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ01813.
    PaxDbiQ01813.
    PeptideAtlasiQ01813.
    PRIDEiQ01813.

    PTM databases

    PhosphoSiteiQ01813.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01813.
    BgeeiQ01813.
    CleanExiHS_PFKP.
    GenevestigatoriQ01813.

    Organism-specific databases

    HPAiHPA018257.

    Interactioni

    Subunit structurei

    Homo- and heterotetramers. Muscle is M4, liver is L4, and red cell is M3L, M2L2, or ML3. A subunit composition with a higher proportion of platelet type subunits is found in platelets, brain and fibroblasts.

    Protein-protein interaction databases

    BioGridi111235. 37 interactions.
    IntActiQ01813. 17 interactions.
    MINTiMINT-1159988.
    STRINGi9606.ENSP00000370517.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01813.
    SMRiQ01813. Positions 22-765.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 399399N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni173 – 1753Substrate bindingUniRule annotation
    Regioni217 – 2193Substrate bindingUniRule annotation
    Regioni307 – 3104Substrate bindingUniRule annotation
    Regioni400 – 41112Interdomain linkerAdd
    BLAST
    Regioni412 – 784373C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni538 – 5425Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni583 – 5853Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni671 – 6744Allosteric 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.
    HOGENOMiHOG000200154.
    HOVERGENiHBG000976.
    InParanoidiQ01813.
    KOiK00850.
    OMAiSAKAMQW.
    OrthoDBiEOG7ZSHV5.
    PhylomeDBiQ01813.
    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: Q01813-1) [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

    MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG    50
    IYVGAKVYFI YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA 100
    FRTREGRLKA ACNLLQRGIT NLCVIGGDGS LTGANLFRKE WSGLLEELAR 150
    NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG TDMTIGTDSA LHRIIEVVDA 200
    IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE 250
    QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT 300
    RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN 350
    HAVRLPLMEC VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK 400
    LPDDQIPKTN CNVAVINVGA PAAGMNAAVR SAVRVGIADG HRMLAIYDGF 450
    DGFAKGQIKE IGWTDVGGWT GQGGSILGTK RVLPGKYLEE IATQMRTHSI 500
    NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS NNVPGSDFSI 550
    GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA 600
    DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI 650
    YQLYSEEGKG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK 700
    LKEARGRGKK FTTDDSICVL GISKRNVIFQ PVAELKKQTD FEHRIPKEQW 750
    WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ PWSV 784
    Length:784
    Mass (Da):85,596
    Last modified:February 1, 1996 - v2
    Checksum:i22522E77E9AF80F6
    GO
    Isoform 2 (identifier: Q01813-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-87: MDADDSRAPK...DWESVSSILQ → MCGYERCRPC...RFPCPGRHAL

    Note: No experimental confirmation available.

    Show »
    Length:776
    Mass (Da):85,316
    Checksum:i649595FEDE1A9187
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti484 – 4852PG → IP(PubMed:1834056)Curated
    Sequence conflicti498 – 4981Missing in AAA36435. (PubMed:1834056)Curated
    Sequence conflicti655 – 6551S → P in BAG52577. (PubMed:14702039)Curated
    Sequence conflicti699 – 6991A → E in AAA36435. (PubMed:1834056)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8787MDADD…SSILQ → MCGYERCRPCRGAHGYLRGG QGVLHLRGLPGHGGRRLKHR RGRLGECLQHPASGAVRGDW REKPGCWSHRFPCPGRHAL in isoform 2. 1 PublicationVSP_046416Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D25328 mRNA. Translation: BAA04998.1.
    AK092597 mRNA. Translation: BAG52577.1.
    AK291841 mRNA. Translation: BAF84530.1.
    AL731533, AL451164 Genomic DNA. Translation: CAH69851.1.
    AL451164, AL731533 Genomic DNA. Translation: CAI39999.1.
    BC002536 mRNA. Translation: AAH02536.1.
    BC029138 mRNA. Translation: AAH29138.1.
    M64784 mRNA. Translation: AAA36435.1.
    CCDSiCCDS55698.1. [Q01813-2]
    CCDS7059.1. [Q01813-1]
    PIRiJC2055.
    RefSeqiNP_001229268.1. NM_001242339.1. [Q01813-2]
    NP_002618.1. NM_002627.4. [Q01813-1]
    UniGeneiHs.26010.

    Genome annotation databases

    EnsembliENST00000381075; ENSP00000370465; ENSG00000067057. [Q01813-2]
    ENST00000381125; ENSP00000370517; ENSG00000067057. [Q01813-1]
    GeneIDi5214.
    KEGGihsa:5214.
    UCSCiuc001igp.3. human. [Q01813-1]

    Polymorphism databases

    DMDMi1346355.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D25328 mRNA. Translation: BAA04998.1 .
    AK092597 mRNA. Translation: BAG52577.1 .
    AK291841 mRNA. Translation: BAF84530.1 .
    AL731533 , AL451164 Genomic DNA. Translation: CAH69851.1 .
    AL451164 , AL731533 Genomic DNA. Translation: CAI39999.1 .
    BC002536 mRNA. Translation: AAH02536.1 .
    BC029138 mRNA. Translation: AAH29138.1 .
    M64784 mRNA. Translation: AAA36435.1 .
    CCDSi CCDS55698.1. [Q01813-2 ]
    CCDS7059.1. [Q01813-1 ]
    PIRi JC2055.
    RefSeqi NP_001229268.1. NM_001242339.1. [Q01813-2 ]
    NP_002618.1. NM_002627.4. [Q01813-1 ]
    UniGenei Hs.26010.

    3D structure databases

    ProteinModelPortali Q01813.
    SMRi Q01813. Positions 22-765.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111235. 37 interactions.
    IntActi Q01813. 17 interactions.
    MINTi MINT-1159988.
    STRINGi 9606.ENSP00000370517.

    Chemistry

    BindingDBi Q01813.

    PTM databases

    PhosphoSitei Q01813.

    Polymorphism databases

    DMDMi 1346355.

    Proteomic databases

    MaxQBi Q01813.
    PaxDbi Q01813.
    PeptideAtlasi Q01813.
    PRIDEi Q01813.

    Protocols and materials databases

    DNASUi 5214.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381075 ; ENSP00000370465 ; ENSG00000067057 . [Q01813-2 ]
    ENST00000381125 ; ENSP00000370517 ; ENSG00000067057 . [Q01813-1 ]
    GeneIDi 5214.
    KEGGi hsa:5214.
    UCSCi uc001igp.3. human. [Q01813-1 ]

    Organism-specific databases

    CTDi 5214.
    GeneCardsi GC10P003109.
    HGNCi HGNC:8878. PFKP.
    HPAi HPA018257.
    MIMi 171840. gene.
    neXtProti NX_Q01813.
    PharmGKBi PA33217.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000200154.
    HOVERGENi HBG000976.
    InParanoidi Q01813.
    KOi K00850.
    OMAi SAKAMQW.
    OrthoDBi EOG7ZSHV5.
    PhylomeDBi Q01813.
    TreeFami TF300411.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci MetaCyc:HS00894-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    SABIO-RK Q01813.

    Miscellaneous databases

    ChiTaRSi PFKP. human.
    GeneWikii PFKP.
    GenomeRNAii 5214.
    NextBioi 20168.
    PROi Q01813.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01813.
    Bgeei Q01813.
    CleanExi HS_PFKP.
    Genevestigatori Q01813.

    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. "Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet."
      Eto K., Sakura H., Yasuda K., Hayakawa T., Kawasaki E., Moriuchi R., Nagataki S., Yazaki Y., Kadowaki T.
      Biochem. Biophys. Res. Commun. 198:990-998(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Pancreatic islet.
    2. "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.
      , 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] (ISOFORMS 1 AND 2).
      Tissue: Prostate.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 Placenta.
    5. "Isolation and sequence of a cDNA encoding human platelet phosphofructokinase."
      Simpson C.J., Fothergill-Gilmore L.A.
      Biochem. Biophys. Res. Commun. 180:197-203(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 484-784 (ISOFORM 1).
    6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-395; LYS-486 AND LYS-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-386 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPFKAP_HUMAN
    AccessioniPrimary (citable) accession number: Q01813
    Secondary accession number(s): B3KS15, Q5VSR7, Q5VSR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3