(data stored in ACNUC4932 zone)

HOVERGEN: F262_MOUSE

ID   F262_MOUSE              Reviewed;         519 AA.
AC   P70265; Q8VEI9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   13-OCT-2009, entry version 88.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2;
DE   AltName: Full=PFK-2/FBPase-2;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE heart-type isozyme;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   Name=Pfkfb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Kidney;
RX   MEDLINE=96409301; PubMed=8814283; DOI=10.1016/0014-5793(96)00878-2;
RA   Batra R.S., Brown R.M., Brown G.K., Craig I.W.;
RT   "Molecular cloning and tissue-specific expression of mouse kidney 6-
RT   phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
RL   FEBS Lett. 393:167-173(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 AND SER-496, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18973353; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
CC       fructose 2,6-bisphosphate.
CC   -!- ENZYME REGULATION: The most important regulatory mechanism of
CC       these opposing activities is by phosphorylation and
CC       dephosphorylation of the enzyme (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- TISSUE SPECIFICITY: Highest levels in kidney; also found in heart,
CC       brain, spleen, lung, liver, skeletal muscle and testis.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
CC   -!- GENE_FAMILY: HBG005628 [ FAMILY / ALN / TREE ]
DR   EMBL; X98847; CAA67352.1; -; mRNA.
DR   EMBL; BC018418; AAH18418.1; -; mRNA.
DR   IPI; IPI00137533; -.
DR   PIR; S74242; S74242.
DR   RefSeq; NP_032851.2; -.
DR   UniGene; Mm.249861; -.
DR   HSSP; P07953; 1C80.
DR   STRING; P70265; -.
DR   PhosphoSite; P70265; -.
DR   PRIDE; P70265; -.
DR   Ensembl; ENSMUST00000066863; ENSMUSP00000066426; ENSMUSG00000026409; Mus musculus.
DR   GeneID; 18640; -.
DR   MGI; MGI:107815; Pfkfb2.
DR   HOGENOM; P70265; -.
DR   HOVERGEN; P70265; -.
DR   BRENDA; 2.7.1.105; 244.
DR   BRENDA; 3.1.3.46; 244.
DR   ArrayExpress; P70265; -.
DR   Bgee; P70265; -.
DR   Genevestigator; P70265; -.
DR   GermOnline; ENSMUSG00000026409; Mus musculus.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; IEA:EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AC.
DR   InterPro; IPR013078; PG_mutase.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P70265.
DR   SWISS-2DPAGE; P70265.
KW   ATP-binding; Hydrolase; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   DOMAIN       47    253       PRODOM:2005.1:PD324818  79
FT   DOMAIN      260    452       PRODOM:2005.1:PD858890  96
FT   DOMAIN      454    508       PRODOM:2005.1:PD016232  4
FT   CHAIN         1    519       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 2.
FT                                /FTId=PRO_0000179965.
FT   NP_BIND      48     55       ATP (Potential).
FT   REGION        1    251       6-phosphofructo-2-kinase.
FT   REGION      252    519       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    131    131       Potential.
FT   ACT_SITE    161    161       Potential.
FT   ACT_SITE    260    260       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    329    329       Potential.
FT   ACT_SITE    394    394       Proton donor (By similarity).
FT   BINDING     105    105       Fructose-6-phosphate (By similarity).
FT   BINDING     196    196       Fructose-6-phosphate (By similarity).
FT   MOD_RES      32     32       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     469    469       Phosphoserine; by PKA.
FT   MOD_RES     471    471       Phosphothreonine (By similarity).
FT   MOD_RES     478    478       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES     486    486       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine.
FT   CONFLICT      9      9       T -> P (in Ref. 2; AAH18418).
FT   CONFLICT     12     12       Missing (in Ref. 2; AAH18418).
FT   CONFLICT    222    222       M -> I (in Ref. 2; AAH18418).
FT   CONFLICT    496    496       S -> K (in Ref. 1; CAA67352).
SQ   SEQUENCE   519 AA;  59925 MW;  FD4CF41AEDF22F89 CRC64;
     MSENSTFSTE DSCNSSYKPH ASNLRRAGKT CSWASYMTNS PTLIVMIGLP ARGKTYVSKK
     LTRYLNWIGV PTKVFNLGVY RREAVKSYQS YDFFRHDNEE AMKIRKQCAL VALEDVKAYF
     TEESGQIAVF DATNTTRERR DMILNFAKQN AFKVFFVESV CDDPDVIAAN ILEVKVSSPD
     YPERNRENVM EDFLKRIECY KVTYQPLDPD NYDKDLSFIK VMNVGQRFLV NRVQDYIQSK
     IVYYLMNIHV HPRTIYLCRH GESEFNLLGK IGGDSGLSVR GKQFAHALKK FLEEQEIQDL
     KVWTSQLKRT IQTAESLGVT YEQWKILNEI DAGVCEEMTY SEIEQRYPEE FALRDQEKYL
     YRYPGGESYQ DLVQRLEPVI MELERQGNIL VISHQAVMRC LLAYFLDKGA DELPYLRCPL
     HIIFKLTPVA YGCKVETITL NVDAVDTHRD KPTHNFPKSQ TPVRMRRNSF TPLSSSNTIR
     RPRNYSVGSR PLKPLSPLRA LDMQEGADQP KTQVSIPVV
//

If you have problems or comments...

PBIL Back to PBIL home page