[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). STRAIN=C57BL/6J; TISSUE=Head; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=C57BL/6J; The mouse genome sequencing consortium; Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 402-471 (ISOFORM 1). STRAIN=BALB/c; TISSUE=Liver; DOI=10.1016/0014-5793(96)00878-2; PubMed=8814283 [NCBI, ExPASy, EBI, Israel, Japan] Batra R.S., Brown R.M., Brown G.K., Craig I.W.; "Molecular cloning and tissue-specific expression of mouse kidney 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; FEBS Lett. 393:167-173(1996).

Comments

FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
CATALYTIC ACTIVITY: 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: Homodimer (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P70266-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P70266-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_022168.

TISSUE SPECIFICITY: Liver.
SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate mutase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AK132629; BAE21271.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL672150; CAM21428.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X98848; CAA67353.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S74243; S74243.

NP_032850.1; -.

3D structure databases

HSSP

P07953; 1FBT. [HSSP ENTRY / PDB]

SMR

P70266; 42-470.

ModBase

P70266.

Protein-protein interaction databases

IntAct

P70266; -.

PTM databases

PhosphoSite

P70266; -.

Organism-specific databases

MGI

MGI:107816; Pfkfb1.

Gene expression databases

ArrayExpress

P70266; -.

GermOnline

ENSMUSG00000025271; Mus musculus.

Ontologies

GO:0043540;	Cellular component: 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex (inferred from sequence or structural similarity from UniProtKB).
GO:0003873;	Molecular function: 6-phosphofructo-2-kinase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004331;	Molecular function: fructose-2,6-bisphosphate 2-phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006003;	Biological process: fructose 2,6-bisphosphate metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003094; 6Pfruct_kin.
IPR013079; 6Phosfructo_kin.
IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
Graphical view of domain structure.

PANTHER

PTHR10606; 6Pfruct_kin; 1.

Pfam

PF01591; 6PF2K; 1.
PF00300; PGAM; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000709; 6PFK_2-Ptase; 1.

PRINTS

PR00991; 6PFRUCTKNASE.

PROSITE

PS00175; PG_MUTASE; 1.

ProtoNet

P70266.

Genome annotation databases

Ensembl

ENSMUSG00000025271; Mus musculus. [Contig view]

GeneID

18639; -.

KEGG

mmu:18639; -.

Phylogenomic databases

HOGENOM

P70266; -.

HOVERGEN

P70266; -.

Other

NextBio

294618; -.

SOURCE

Pfkfb1; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 471`	`471`	`6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1.`	`PRO_0000179961`
`NP_BIND`	`49 56`	`8`	`ATP (Potential).`
`REGION`	`1 250`	`250`	`6-phosphofructo-2-kinase (By similarity).`
`REGION`	`251 471`	`221`	`Fructose-2,6-bisphosphatase (By similarity).`
`ACT_SITE`	`131 131`		`Potential.`
`ACT_SITE`	`161 161`		`Potential.`
`ACT_SITE`	`259 259`		`Tele-phosphohistidine intermediate (By similarity).`
`ACT_SITE`	`328 328`		`Potential.`
`ACT_SITE`	`393 393`		`Proton donor (By similarity).`
`BINDING`	`105 105`		`Fructose-6-phosphate (By similarity).`
`BINDING`	`196 196`		`Fructose-6-phosphate (By similarity).`
`MOD_RES`	`33 33`		`Phosphoserine; by PKA (By similarity).`
`VAR_SEQ`	`1 33`		`MSREMGELTQTRLQKIWIPHSSSSSLLQRRRGS -> MEEKASKRAA (in isoform 2).`	`VSP_022168`
`CONFLICT`	`460 460`		`P -> A (in Ref. 3; CAA67353).`

Sequence information

Length: 471 AA [This is the length of the unprocessed precursor]

Molecular weight: 54849 Da [This is the MW of the unprocessed precursor]

CRC64: A8EA464FB4B2DA42 [This is a checksum on the sequence]

        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

P70266 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools