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O60825

- F262_HUMAN

UniProt

O60825 - F262_HUMAN

Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2

Gene

PFKFB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      Previous versions | rss
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    Functioni

    Synthesis and degradation of fructose 2,6-bisphosphate.

    Catalytic activityi

    Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
    ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

    Enzyme regulationi

    Phosphorylation results in the activation of the kinase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei78 – 781Fructose 6-phosphateBy similarity
    Binding sitei102 – 1021Fructose 6-phosphateBy similarity
    Active sitei128 – 1281Sequence Analysis
    Binding sitei130 – 1301Fructose 6-phosphateBy similarity
    Binding sitei136 – 1361Fructose 6-phosphateBy similarity
    Active sitei158 – 1581Sequence Analysis
    Binding sitei172 – 1721Fructose 6-phosphateBy similarity
    Binding sitei193 – 1931Fructose 6-phosphateBy similarity
    Binding sitei197 – 1971Fructose 6-phosphateBy similarity
    Binding sitei256 – 2561Fructose 2,6-bisphosphateBy similarity
    Active sitei257 – 2571Tele-phosphohistidine intermediateBy similarity
    Binding sitei263 – 2631Fructose 2,6-bisphosphateBy similarity
    Binding sitei269 – 2691Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
    Binding sitei306 – 3061Fructose 2,6-bisphosphateBy similarity
    Active sitei326 – 3261Proton donor/acceptorBy similarity
    Binding sitei337 – 3371Fructose 2,6-bisphosphateBy similarity
    Binding sitei351 – 3511Fructose 2,6-bisphosphateBy similarity
    Binding sitei355 – 3551Fructose 2,6-bisphosphateBy similarity
    Binding sitei366 – 3661Fructose 2,6-bisphosphateBy similarity
    Active sitei391 – 3911Proton donor/acceptorBy similarity
    Binding sitei392 – 3921Fructose 2,6-bisphosphateBy similarity
    Binding sitei396 – 3961Fructose 2,6-bisphosphateBy similarity
    Binding sitei428 – 4281ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi45 – 539ATPBy similarity
    Nucleotide bindingi167 – 1726ATPBy similarity
    Nucleotide bindingi348 – 3514ATPBy similarity
    Nucleotide bindingi392 – 3965ATPBy similarity

    GO - Molecular functioni

    1. 6-phosphofructo-2-kinase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. carbohydrate phosphorylation Source: GOC
    3. fructose 2,6-bisphosphate metabolic process Source: InterPro
    4. fructose metabolic process Source: ProtInc
    5. glucose catabolic process Source: Ensembl
    6. glucose metabolic process Source: Reactome
    7. glycolytic process Source: UniProtKB
    8. lactate metabolic process Source: Ensembl
    9. positive regulation of glucokinase activity Source: Ensembl
    10. positive regulation of insulin secretion Source: Ensembl
    11. response to glucose Source: Ensembl
    12. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.46. 2681.
    ReactomeiREACT_1383. Glycolysis.
    SABIO-RKO60825.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
    Short name:
    6PF-2-K/Fru-2,6-P2ase 2
    Short name:
    PFK/FBPase 2
    Alternative name(s):
    6PF-2-K/Fru-2,6-P2ase heart-type isozyme
    Including the following 2 domains:
    Fructose-2,6-bisphosphatase (EC:3.1.3.46)
    Gene namesi
    Name:PFKFB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8873. PFKFB2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi466 – 4661S → E: Constitutively active mutant that cannot be phosphorylated and further activated by AMPK. 1 Publication

    Organism-specific databases

    PharmGKBiPA33212.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 5055046-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2PRO_0000179964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei29 – 291Phosphoserine; by PKABy similarity
    Modified residuei466 – 4661Phosphoserine; by AMPK4 Publications
    Modified residuei468 – 4681Phosphothreonine1 Publication
    Modified residuei475 – 4751Phosphothreonine; by PKCBy similarity
    Modified residuei483 – 4831Phosphoserine2 Publications
    Modified residuei493 – 4931Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation by AMPK stimulates activity.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60825.
    PaxDbiO60825.
    PRIDEiO60825.

    PTM databases

    PhosphoSiteiO60825.

    Expressioni

    Tissue specificityi

    Heart.

    Gene expression databases

    ArrayExpressiO60825.
    BgeeiO60825.
    CleanExiHS_PFKFB2.
    GenevestigatoriO60825.

    Organism-specific databases

    HPAiHPA049975.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi111229. 6 interactions.
    IntActiO60825. 4 interactions.
    MINTiMINT-3000455.
    STRINGi9606.ENSP00000356047.

    Structurei

    3D structure databases

    ProteinModelPortaliO60825.
    SMRiO60825. Positions 37-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2482476-phosphofructo-2-kinaseAdd
    BLAST
    Regioni249 – 505257Fructose-2,6-bisphosphataseAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG0406.
    HOGENOMiHOG000181112.
    HOVERGENiHBG005628.
    InParanoidiO60825.
    KOiK01103.
    OMAiHPRTIYL.
    OrthoDBiEOG7M3J03.
    PhylomeDBiO60825.
    TreeFamiTF313541.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003094. 6Pfruct_kin.
    IPR013079. 6Phosfructo_kin.
    IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
    IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR027417. P-loop_NTPase.
    IPR001345. PG/BPGM_mutase_AS.
    [Graphical view]
    PANTHERiPTHR10606. PTHR10606. 1 hit.
    PfamiPF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSiPR00991. 6PFRUCTKNASE.
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60825-1) [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

    MSGASSSEQN NNSYETKTPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG    50
    KTYVSKKLTR YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK 100
    IRKQCALVAL EDVKAYLTEE NGQIAVFDAT NTTRERRDMI LNFAEQNSFK 150
    VFFVESVCDD PDVIAANILE VKVSSPDYPE RNRENVMEDF LKRIECYKVT 200
    YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY YLMNIHVQPR 250
    TIYLCRHGES EFNLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW 300
    TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL 350
    RDQEKYLYRY PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA 400
    YFLDKGADEL PYLRCPLHTI FKLTPVAYGC KVETIKLNVE AVNTHRDKPT 450
    NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR NYSVGSRPLK PLSPLRAQDM 500
    QEGAD 505
    Length:505
    Mass (Da):58,477
    Last modified:January 24, 2001 - v2
    Checksum:i5CD6A933A7EBF604
    GO
    Isoform 2 (identifier: O60825-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         451-505: NNFPKNQTPV...RAQDMQEGAD → AAETTLAVRRRPSAASLMLPC

    Show »
    Length:471
    Mass (Da):54,406
    Checksum:i2B9C8957889F4D61
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281Missing in CAA06605. (PubMed:9652401)Curated
    Sequence conflicti303 – 3042QL → HV in CAA06606. (PubMed:9652401)Curated
    Sequence conflicti372 – 3721R → L in CAA06606. (PubMed:9652401)Curated
    Sequence conflicti396 – 3961R → H in CAA06606. (PubMed:9652401)Curated
    Sequence conflicti406 – 4061G → D in CAA06606. (PubMed:9652401)Curated
    Sequence conflicti427 – 4271A → T in CAA06606. (PubMed:9652401)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei451 – 50555NNFPK…QEGAD → AAETTLAVRRRPSAASLMLP C in isoform 2. 3 PublicationsVSP_004675Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005577 Genomic DNA. Translation: CAA06605.1.
    AJ005578 mRNA. Translation: CAA06606.1.
    AB044805 mRNA. Translation: BAB19681.1.
    AF470623 mRNA. Translation: AAL99386.1.
    AK292883 mRNA. Translation: BAF85572.1.
    AL445493 Genomic DNA. Translation: CAH70777.1.
    AL445493 Genomic DNA. Translation: CAH70778.1.
    CH471100 Genomic DNA. Translation: EAW93508.1.
    BC069350 mRNA. Translation: AAH69350.1.
    BC069385 mRNA. Translation: AAH69385.1.
    BC069583 mRNA. Translation: AAH69583.1.
    BC069586 mRNA. Translation: AAH69586.1.
    BC069600 mRNA. Translation: AAH69600.1.
    BC075075 mRNA. Translation: AAH75075.1.
    BC075076 mRNA. Translation: AAH75076.1.
    BC112103 mRNA. Translation: AAI12104.1.
    BC112105 mRNA. Translation: AAI12106.1.
    CCDSiCCDS31003.1. [O60825-2]
    CCDS31004.1. [O60825-1]
    RefSeqiNP_001018063.1. NM_001018053.1. [O60825-2]
    NP_006203.2. NM_006212.2. [O60825-1]
    UniGeneiHs.282702.

    Genome annotation databases

    EnsembliENST00000367079; ENSP00000356046; ENSG00000123836. [O60825-2]
    ENST00000367080; ENSP00000356047; ENSG00000123836. [O60825-1]
    GeneIDi5208.
    KEGGihsa:5208.
    UCSCiuc001hfg.3. human. [O60825-1]
    uc001hfh.3. human. [O60825-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005577 Genomic DNA. Translation: CAA06605.1 .
    AJ005578 mRNA. Translation: CAA06606.1 .
    AB044805 mRNA. Translation: BAB19681.1 .
    AF470623 mRNA. Translation: AAL99386.1 .
    AK292883 mRNA. Translation: BAF85572.1 .
    AL445493 Genomic DNA. Translation: CAH70777.1 .
    AL445493 Genomic DNA. Translation: CAH70778.1 .
    CH471100 Genomic DNA. Translation: EAW93508.1 .
    BC069350 mRNA. Translation: AAH69350.1 .
    BC069385 mRNA. Translation: AAH69385.1 .
    BC069583 mRNA. Translation: AAH69583.1 .
    BC069586 mRNA. Translation: AAH69586.1 .
    BC069600 mRNA. Translation: AAH69600.1 .
    BC075075 mRNA. Translation: AAH75075.1 .
    BC075076 mRNA. Translation: AAH75076.1 .
    BC112103 mRNA. Translation: AAI12104.1 .
    BC112105 mRNA. Translation: AAI12106.1 .
    CCDSi CCDS31003.1. [O60825-2 ]
    CCDS31004.1. [O60825-1 ]
    RefSeqi NP_001018063.1. NM_001018053.1. [O60825-2 ]
    NP_006203.2. NM_006212.2. [O60825-1 ]
    UniGenei Hs.282702.

    3D structure databases

    ProteinModelPortali O60825.
    SMRi O60825. Positions 37-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111229. 6 interactions.
    IntActi O60825. 4 interactions.
    MINTi MINT-3000455.
    STRINGi 9606.ENSP00000356047.

    PTM databases

    PhosphoSitei O60825.

    Proteomic databases

    MaxQBi O60825.
    PaxDbi O60825.
    PRIDEi O60825.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367079 ; ENSP00000356046 ; ENSG00000123836 . [O60825-2 ]
    ENST00000367080 ; ENSP00000356047 ; ENSG00000123836 . [O60825-1 ]
    GeneIDi 5208.
    KEGGi hsa:5208.
    UCSCi uc001hfg.3. human. [O60825-1 ]
    uc001hfh.3. human. [O60825-2 ]

    Organism-specific databases

    CTDi 5208.
    GeneCardsi GC01P207226.
    HGNCi HGNC:8873. PFKFB2.
    HPAi HPA049975.
    MIMi 171835. gene.
    neXtProti NX_O60825.
    PharmGKBi PA33212.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0406.
    HOGENOMi HOG000181112.
    HOVERGENi HBG005628.
    InParanoidi O60825.
    KOi K01103.
    OMAi HPRTIYL.
    OrthoDBi EOG7M3J03.
    PhylomeDBi O60825.
    TreeFami TF313541.

    Enzyme and pathway databases

    BRENDAi 3.1.3.46. 2681.
    Reactomei REACT_1383. Glycolysis.
    SABIO-RK O60825.

    Miscellaneous databases

    ChiTaRSi PFKFB2. human.
    GeneWikii PFKFB2.
    GenomeRNAii 5208.
    NextBioi 20140.
    PROi O60825.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60825.
    Bgeei O60825.
    CleanExi HS_PFKFB2.
    Genevestigatori O60825.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003094. 6Pfruct_kin.
    IPR013079. 6Phosfructo_kin.
    IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
    IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR027417. P-loop_NTPase.
    IPR001345. PG/BPGM_mutase_AS.
    [Graphical view ]
    PANTHERi PTHR10606. PTHR10606. 1 hit.
    Pfami PF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSi PR00991. 6PFRUCTKNASE.
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)."
      Heine-Suner D., Diaz-Guillen M.A., Lange A.J., Rodriguez de Cordoba S.
      Eur. J. Biochem. 254:103-110(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Heart.
    3. "Human insulinoma PFK2/F26DPase."
      Matsutani A.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "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] (ISOFORM 2).
      Tissue: Trachea.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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.
    8. "Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia."
      Marsin A.S., Bertrand L., Rider M.H., Deprez J., Beauloye C., Vincent M.F., Van den Berghe G., Carling D., Hue L.
      Curr. Biol. 10:1247-1255(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-466, MUTAGENESIS OF SER-466.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-468; SER-483 AND SER-493, 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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-466; SER-483 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-466, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiF262_HUMAN
    AccessioniPrimary (citable) accession number: O60825
    Secondary accession number(s): O60824
    , Q5VVQ3, Q5VVQ4, Q9H3P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 144 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

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3