P70266 (F261_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Short name=6PF-2-K/Fru-2,6-P2ase 1
Short name=PFK/FBPase 1

Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme

Including the following 2 domains:

1. 6-phosphofructo-2-kinase
   EC=2.7.1.105
2. Fructose-2,6-bisphosphatase
   EC=3.1.3.46

Gene names

Name:

Pfkfb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Synthesis and degradation of fructose 2,6-bisphosphate.
Catalytic activity	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 regulation	Phosphorylation results in inhibition of the kinase activity By similarity.
Subunit structure	Homodimer By similarity.
Tissue specificity	Liver.
Sequence similarities	In the C-terminal section; belongs to the phosphoglycerate mutase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	fructose 2,6-bisphosphate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB fructose metabolic process Inferred from electronic annotation. Source: InterPro organ regeneration Inferred from electronic annotation. Source: Compara positive regulation of glucokinase activity Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to glucagon stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara response to starvation Inferred from electronic annotation. Source: Compara
Cellular_component	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	6-phosphofructo-2-kinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fructose-2,6-bisphosphate 2-phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB fructose-6-phosphate binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70266-1)

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.

Isoform 2 (identifier: P70266-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSREMGELTQTRLQKIWIPHSSSSSLLQRRRGS → MEEKASKRAA

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 471	470	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1		PRO_0000179961
Regions
	Nucleotide binding	49 – 56	8	ATP Potential
	Region	2 – 250	249	6-phosphofructo-2-kinase By similarity
	Region	251 – 471	221	Fructose-2,6-bisphosphatase By similarity
Sites
	Active site	131	1	Potential
	Active site	161	1	Potential
	Active site	259	1	Tele-phosphohistidine intermediate By similarity
	Active site	328	1	Potential
	Active site	393	1	Proton donor By similarity
	Binding site	105	1	Fructose-6-phosphate By similarity
	Binding site	196	1	Fructose-6-phosphate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	33	1	Phosphoserine; by PKA By similarity
Natural variations
	Alternative sequence	1 – 33	33	MSREM…RRRGS → MEEKASKRAA in isoform 2.		VSP_022168
Experimental info
	Sequence conflict	460	1	P → A in CAA67353. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: A8EA464FB4B2DA42	FASTA	471	54,849
	10 20 30 40 50 60 MSREMGELTQ TRLQKIWIPH SSSSSLLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST 70 80 90 100 110 120 KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNME AQLIRKQCAL AALKDVHKYL 130 140 150 160 170 180 SREEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPDIIAEN IKQVKLGSPD 190 200 210 220 230 240 YIDCDQEKVL EDFLKRIECY EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT 250 260 270 280 290 300 AYYLMNIHVT PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQSISSLK 310 320 330 340 350 360 VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY 370 380 390 400 410 420 RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH 430 440 450 460 470 TVLKLTPVAY GCRVESIYLN VEAVNTHRDK PENVDITREP EEALDTVPAH Y
	Isoform 2 [UniParc]. Checksum: 6CF417A9F775B167	FASTA	448	52,112
	10 20 30 40 50 60 MEEKASKRAA SIPQFTNSPT MVIMVGLPAR GKTYISTKLT RYLNWIGTPT KVFNLGQYRR 70 80 90 100 110 120 EAVSYRNYEF FRPDNMEAQL IRKQCALAAL KDVHKYLSRE EGHVAVFDAT NTTRERRSLI 130 140 150 160 170 180 LQFAKEHGYK VFFIESICND PDIIAENIKQ VKLGSPDYID CDQEKVLEDF LKRIECYEIN 190 200 210 220 230 240 YQPLDEELDS HLSYIKIFDV GTRYMVNRVQ DHVQSRTAYY LMNIHVTPRS IYLCRHGESE 250 260 270 280 290 300 LNLRGRIGGD SGLSARGKQY AYALANFIRS QSISSLKVWT SHMKRTIQTA EALGVPYEQW 310 320 330 340 350 360 KALNEIDAGV CEEMTYEEIQ EHYPEEFALR DQDKYRYRYP KGESYEDLVQ RLEPVIMELE 370 380 390 400 410 420 RQENVLVICH QAVMRCLLAY FLDKSSDELP YLKCPLHTVL KLTPVAYGCR VESIYLNVEA 430 440 VNTHRDKPEN VDITREPEEA LDTVPAHY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 2). Strain: C57BL/6J. Tissue: Head.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Molecular cloning and tissue-specific expression of mouse kidney 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase." Batra R.S., Brown R.M., Brown G.K., Craig I.W. FEBS Lett. 393:167-173(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 402-471 (ISOFORM 1). Strain: BALB/c. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK132629 mRNA. Translation: BAE21271.1. AL672150 Genomic DNA. Translation: CAM21428.1. X98848 mRNA. Translation: CAA67353.1.
IPI	IPI00653772. IPI00816928.
PIR	S74243.
RefSeq	NP_032850.1. NM_008824.2.
UniGene	Mm.249131.
3D structure databases
ProteinModelPortal	P70266.
SMR	P70266. Positions 7-471.
ModBase	Search...
PTM databases
PhosphoSite	P70266.
Proteomic databases
PaxDb	P70266.
PRIDE	P70266.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080884; ENSMUSP00000079692; ENSMUSG00000025271. ENSMUST00000112713; ENSMUSP00000108333; ENSMUSG00000025271.
GeneID	18639.
KEGG	mmu:18639.
Organism-specific databases
CTD	5207.
MGI	MGI:107816. Pfkfb1.
Phylogenomic databases
eggNOG	COG0406.
GeneTree	ENSGT00390000018751.
HOGENOM	HOG000181112.
HOVERGEN	HBG005628.
InParanoid	P70266.
KO	K01103.
OrthoDB	EOG4HX50X.
Gene expression databases
ArrayExpress	P70266.
Bgee	P70266.
Genevestigator	P70266.
GermOnline	ENSMUSG00000025271. Mus musculus.
Family and domain databases
InterPro	IPR003094. 6Pfruct_kin. IPR013079. 6Phosfructo_kin. IPR016260. Bifunct_6PFK/fruc_bisP_Ptase. IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. [Graphical view]
PANTHER	PTHR10606. PTHR10606. 1 hit.
Pfam	PF01591. 6PF2K. 1 hit. PF00300. His_Phos_1. 1 hit. [Graphical view]
PIRSF	PIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTS	PR00991. 6PFRUCTKNASE.
SMART	SM00855. PGAM. 1 hit. [Graphical view]
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	294618.
SOURCE	Search...

Entry information

Entry name

F261_MOUSE

Accession

Primary (citable) accession number: P70266
Secondary accession number(s): A2AFN0, Q3V180

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 9, 2007
Last modified:	April 3, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program