(data stored in SCRATCH zone)

SWISSPROT: F261_HUMAN

ID   F261_HUMAN              Reviewed;         471 AA.
AC   P16118; B2RA88; B4DUN5; Q5JXS5; Q99951;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   30-AUG-2017, entry version 187.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1;
DE            Short=6PF-2-K/Fru-2,6-P2ase 1;
DE            Short=PFK/FBPase 1;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ase liver 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=PFKFB1; Synonyms=F6PK, PFRX;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=2163524; DOI=10.1093/nar/18.12.3652;
RA   Lange A.J., Pilkis S.J.;
RT   "Sequence of human liver 6-phosphofructo-2-kinase/fructose-2,6-
RT   bisphosphatase.";
RL   Nucleic Acids Res. 18:3652-3652(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 94-471.
RC   TISSUE=Liver;
RX   PubMed=2837207; DOI=10.1016/S0006-291X(88)81226-9;
RA   Algaier J., Uyeda K.;
RT   "Molecular cloning, sequence analysis, and expression of a human liver
RT   cDNA coding for fructose-6-P,2-kinase:fructose-2,6-bisphosphatase.";
RL   Biochem. Biophys. Res. Commun. 153:328-333(1988).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-471 IN COMPLEX WITH ATP
RP   ANALOG, AND SUBUNIT.
RX   PubMed=12379646; DOI=10.1074/jbc.M209105200;
RA   Lee Y.H., Li Y., Uyeda K., Hasemann C.A.;
RT   "Tissue-specific structure/function differentiation of the liver
RT   isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
RL   J. Biol. Chem. 278:523-530(2003).
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: Phosphorylation at Ser-33 inhibits the kinase
CC       and activates the bisphosphatase. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12379646}.
CC   -!- INTERACTION:
CC       Self; NbExp=4; IntAct=EBI-709807, EBI-709807;
CC       Q96D03:DDIT4L; NbExp=4; IntAct=EBI-709807, EBI-742054;
CC       P35557:GCK; NbExp=2; IntAct=EBI-709807, EBI-709928;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P16118-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16118-2; Sequence=VSP_054795;
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family. {ECO:0000305}.
DR   EMBL; X52638; CAA36861.1; -; mRNA.
DR   EMBL; AK314089; BAG36785.1; -; mRNA.
DR   EMBL; AK300724; BAG62397.1; -; mRNA.
DR   EMBL; AL049732; CAI42048.1; -; Genomic_DNA.
DR   EMBL; AL020991; CAI42048.1; JOINED; Genomic_DNA.
DR   EMBL; AL020991; CAI43127.1; -; Genomic_DNA.
DR   EMBL; AL049732; CAI43127.1; JOINED; Genomic_DNA.
DR   EMBL; BC096079; AAH96079.1; -; mRNA.
DR   EMBL; M19938; AAA35818.1; -; mRNA.
DR   CCDS; CCDS14364.1; -. [P16118-1]
DR   CCDS; CCDS65273.1; -. [P16118-2]
DR   PIR; S12732; S12732.
DR   RefSeq; NP_001258733.1; NM_001271804.1.
DR   RefSeq; NP_001258734.1; NM_001271805.1. [P16118-2]
DR   RefSeq; NP_002616.2; NM_002625.3. [P16118-1]
DR   UniGene; Hs.444304; -.
DR   PDB; 1K6M; X-ray; 2.40 A; A/B=40-471.
DR   PDBsum; 1K6M; -.
DR   ProteinModelPortal; P16118; -.
DR   SMR; P16118; -.
DR   BioGrid; 111228; 7.
DR   IntAct; P16118; 12.
DR   MINT; MINT-6772805; -.
DR   STRING; 9606.ENSP00000364145; -.
DR   BindingDB; P16118; -.
DR   ChEMBL; CHEMBL3421524; -.
DR   DrugBank; DB02515; 3-Phosphoglycerol.
DR   DrugBank; DB04493; Fructose-6-Phosphate.
DR   DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR   DrugBank; DB02930; Phosphothiophosphoric Acid-Adenylate Ester.
DR   DEPOD; P16118; -.
DR   iPTMnet; P16118; -.
DR   PhosphoSitePlus; P16118; -.
DR   DMDM; 2507178; -.
DR   EPD; P16118; -.
DR   PaxDb; P16118; -.
DR   PeptideAtlas; P16118; -.
DR   PRIDE; P16118; -.
DR   DNASU; 5207; -.
DR   Ensembl; ENST00000375006; ENSP00000364145; ENSG00000158571. [P16118-1]
DR   Ensembl; ENST00000545676; ENSP00000444074; ENSG00000158571. [P16118-2]
DR   GeneID; 5207; -.
DR   KEGG; hsa:5207; -.
DR   UCSC; uc004dty.3; human. [P16118-1]
DR   CTD; 5207; -.
DR   GeneCards; PFKFB1; -.
DR   HGNC; HGNC:8872; PFKFB1.
DR   MIM; 311790; gene.
DR   neXtProt; NX_P16118; -.
DR   OpenTargets; ENSG00000158571; -.
DR   PharmGKB; PA33211; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   eggNOG; COG0406; LUCA.
DR   GeneTree; ENSGT00390000018751; -.
DR   HOGENOM; HOG000181112; -.
DR   HOVERGEN; HBG005628; -.
DR   InParanoid; P16118; -.
DR   KO; K19028; -.
DR   OMA; HNYLSHE; -.
DR   OrthoDB; EOG091G0A43; -.
DR   PhylomeDB; P16118; -.
DR   TreeFam; TF313541; -.
DR   BioCyc; MetaCyc:HS08310-MONOMER; -.
DR   BRENDA; 2.7.1.105; 2681.
DR   BRENDA; 3.1.3.46; 2681.
DR   Reactome; R-HSA-163358; PKA-mediated phosphorylation of key metabolic factors.
DR   Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR   Reactome; R-HSA-70171; Glycolysis.
DR   Reactome; R-HSA-70263; Gluconeogenesis.
DR   SABIO-RK; P16118; -.
DR   EvolutionaryTrace; P16118; -.
DR   GenomeRNAi; 5207; -.
DR   PRO; PR:P16118; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000158571; -.
DR   CleanEx; HS_PFKFB1; -.
DR   ExpressionAtlas; P16118; baseline and differential.
DR   Genevisible; P16118; HS.
DR   GO; GO:0043540; C:6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; TAS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; TAS:UniProtKB.
DR   GO; GO:0033133; P:positive regulation of glucokinase activity; IEA:Ensembl.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR10606; PTHR10606; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P16118.
DR   SWISS-2DPAGE; P16118.
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Complete proteome; Hydrolase; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P07953}.
FT   CHAIN         2    471       6-phosphofructo-2-kinase/fructose-2,6-
FT                                bisphosphatase 1.
FT                                /FTId=PRO_0000179960.
FT   NP_BIND      49     57       ATP. {ECO:0000269|PubMed:12379646}.
FT   NP_BIND     170    175       ATP. {ECO:0000269|PubMed:12379646}.
FT   NP_BIND     350    353       ATP. {ECO:0000250|UniProtKB:P07953}.
FT   NP_BIND     394    398       ATP. {ECO:0000250|UniProtKB:P07953}.
FT   REGION        2    250       6-phosphofructo-2-kinase.
FT   REGION      251    471       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    131    131       {ECO:0000255}.
FT   ACT_SITE    161    161       {ECO:0000255}.
FT   ACT_SITE    259    259       Tele-phosphohistidine intermediate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   ACT_SITE    328    328       Proton donor/acceptor.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING      82     82       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     105    105       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     133    133       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     139    139       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     175    175       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     196    196       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     200    200       Fructose 6-phosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     258    258       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     265    265       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     271    271       Fructose 2,6-bisphosphate; via amide
FT                                nitrogen. {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     308    308       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:Q16875}.
FT   BINDING     339    339       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     353    353       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     357    357       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     368    368       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     394    394       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     398    398       Fructose 2,6-bisphosphate.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   BINDING     430    430       ATP. {ECO:0000269|PubMed:12379646}.
FT   SITE        393    393       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P00950}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   MOD_RES      33     33       Phosphoserine; by PKA.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07953}.
FT   MOD_RES     466    466       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P26285}.
FT   VAR_SEQ       1     73       MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNS
FT                                PTMVIMVGLPARGKTYISTKLTRYLNWIGTPT -> MEEKT
FT                                SRI (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054795.
FT   CONFLICT    305    305       H -> R (in Ref. 1; CAA36861).
FT                                {ECO:0000305}.
FT   CONFLICT    359    359       R -> H (in Ref. 5; AAA35818).
FT                                {ECO:0000305}.
FT   CONFLICT    397    398       MR -> HA (in Ref. 5; AAA35818).
FT                                {ECO:0000305}.
FT   STRAND       43     48       {ECO:0000244|PDB:1K6M}.
FT   HELIX        55     68       {ECO:0000244|PDB:1K6M}.
FT   STRAND       73     77       {ECO:0000244|PDB:1K6M}.
FT   HELIX        78     83       {ECO:0000244|PDB:1K6M}.
FT   HELIX        91     94       {ECO:0000244|PDB:1K6M}.
FT   HELIX        99    121       {ECO:0000244|PDB:1K6M}.
FT   STRAND      126    132       {ECO:0000244|PDB:1K6M}.
FT   HELIX       137    150       {ECO:0000244|PDB:1K6M}.
FT   STRAND      153    160       {ECO:0000244|PDB:1K6M}.
FT   HELIX       164    175       {ECO:0000244|PDB:1K6M}.
FT   HELIX       187    201       {ECO:0000244|PDB:1K6M}.
FT   TURN        209    214       {ECO:0000244|PDB:1K6M}.
FT   STRAND      217    221       {ECO:0000244|PDB:1K6M}.
FT   TURN        222    225       {ECO:0000244|PDB:1K6M}.
FT   STRAND      226    230       {ECO:0000244|PDB:1K6M}.
FT   HELIX       235    244       {ECO:0000244|PDB:1K6M}.
FT   STRAND      254    258       {ECO:0000244|PDB:1K6M}.
FT   HELIX       263    266       {ECO:0000244|PDB:1K6M}.
FT   HELIX       278    293       {ECO:0000244|PDB:1K6M}.
FT   STRAND      300    303       {ECO:0000244|PDB:1K6M}.
FT   HELIX       307    314       {ECO:0000244|PDB:1K6M}.
FT   HELIX       324    326       {ECO:0000244|PDB:1K6M}.
FT   HELIX       332    334       {ECO:0000244|PDB:1K6M}.
FT   HELIX       339    345       {ECO:0000244|PDB:1K6M}.
FT   HELIX       347    355       {ECO:0000244|PDB:1K6M}.
FT   TURN        357    359       {ECO:0000244|PDB:1K6M}.
FT   HELIX       368    384       {ECO:0000244|PDB:1K6M}.
FT   STRAND      386    392       {ECO:0000244|PDB:1K6M}.
FT   HELIX       394    405       {ECO:0000244|PDB:1K6M}.
FT   TURN        409    411       {ECO:0000244|PDB:1K6M}.
FT   HELIX       412    414       {ECO:0000244|PDB:1K6M}.
FT   STRAND      421    427       {ECO:0000244|PDB:1K6M}.
FT   STRAND      429    438       {ECO:0000244|PDB:1K6M}.
FT   HELIX       460    464       {ECO:0000244|PDB:1K6M}.
SQ   SEQUENCE   471 AA;  54681 MW;  C4FF081A295FB7D3 CRC64;
     MSPEMGELTQ TRLQKIWIPH SSGSSRLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST
     KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME ALQIRKQCAL AALKDVHNYL
     SHEEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPGIIAEN IRQVKLGSPD
     YIDCDREKVL EDFLKRIECY EVNYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT
     VYYLMNIHVT PRSIYLCRHG ESELNIRGRI GGDSGLSVRG KQYAYALANF IQSQGISSLK
     VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY
     RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH
     TVLKLTPVAY GCKVESIYLN VEAVNTHREK PENVDITREP EEALDTVPAH Y
//

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