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O60825 (F262_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. 6-phosphofructo-2-kinase
    EC=2.7.1.105
  2. Fructose-2,6-bisphosphatase
    EC=3.1.3.46
Gene names
Name:PFKFB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 the activation of the kinase activity.

Subunit structure

Homodimer By similarity.

Tissue specificity

Heart.

Post-translational modification

Phosphorylation by AMPK stimulates activity.

Sequence similarities

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

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

carbohydrate phosphorylation

Inferred from direct assay Ref.8. Source: GOC

fructose 2,6-bisphosphate metabolic process

Inferred from electronic annotation. Source: InterPro

fructose metabolic process

Traceable author statement Ref.1. Source: ProtInc

glucose metabolic process

Traceable author statement. Source: Reactome

glycolysis

Inferred from direct assay Ref.8. Source: UniProtKB

lactate metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucokinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

pyruvate metabolic process

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_function6-phosphofructo-2-kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fructose-2,6-bisphosphate 2-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60825-1)

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: O60825-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 5055046-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
PRO_0000179964

Regions

Nucleotide binding45 – 539ATP By similarity
Nucleotide binding167 – 1726ATP By similarity
Nucleotide binding348 – 3514ATP By similarity
Nucleotide binding392 – 3965ATP By similarity
Region2 – 2482476-phosphofructo-2-kinase
Region249 – 505257Fructose-2,6-bisphosphatase

Sites

Active site1281 Potential
Active site1581 Potential
Active site2571Tele-phosphohistidine intermediate By similarity
Active site3261Proton donor/acceptor By similarity
Active site3911Proton donor/acceptor By similarity
Binding site781Fructose 6-phosphate By similarity
Binding site1021Fructose 6-phosphate By similarity
Binding site1301Fructose 6-phosphate By similarity
Binding site1361Fructose 6-phosphate By similarity
Binding site1721Fructose 6-phosphate By similarity
Binding site1931Fructose 6-phosphate By similarity
Binding site1971Fructose 6-phosphate By similarity
Binding site2561Fructose 2,6-bisphosphate By similarity
Binding site2631Fructose 2,6-bisphosphate By similarity
Binding site2691Fructose 2,6-bisphosphate; via amide nitrogen By similarity
Binding site3061Fructose 2,6-bisphosphate By similarity
Binding site3371Fructose 2,6-bisphosphate By similarity
Binding site3511Fructose 2,6-bisphosphate By similarity
Binding site3551Fructose 2,6-bisphosphate By similarity
Binding site3661Fructose 2,6-bisphosphate By similarity
Binding site3921Fructose 2,6-bisphosphate By similarity
Binding site3961Fructose 2,6-bisphosphate By similarity
Binding site4281ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.14
Modified residue291Phosphoserine; by PKA By similarity
Modified residue4661Phosphoserine; by AMPK Ref.8 Ref.9 Ref.12 Ref.13
Modified residue4681Phosphothreonine Ref.9
Modified residue4751Phosphothreonine; by PKC By similarity
Modified residue4831Phosphoserine Ref.9 Ref.12
Modified residue4931Phosphoserine Ref.9 Ref.12

Natural variations

Alternative sequence451 – 50555NNFPK…QEGAD → AAETTLAVRRRPSAASLMLP C in isoform 2.
VSP_004675

Experimental info

Mutagenesis4661S → E: Constitutively active mutant that cannot be phosphorylated and further activated by AMPK. Ref.8
Sequence conflict281Missing in CAA06605. Ref.1
Sequence conflict303 – 3042QL → HV in CAA06606. Ref.1
Sequence conflict3721R → L in CAA06606. Ref.1
Sequence conflict3961R → H in CAA06606. Ref.1
Sequence conflict4061G → D in CAA06606. Ref.1
Sequence conflict4271A → T in CAA06606. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 5CD6A933A7EBF604

FASTA50558,477
        10         20         30         40         50         60 
MSGASSSEQN NNSYETKTPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG KTYVSKKLTR 

        70         80         90        100        110        120 
YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK IRKQCALVAL EDVKAYLTEE 

       130        140        150        160        170        180 
NGQIAVFDAT NTTRERRDMI LNFAEQNSFK VFFVESVCDD PDVIAANILE VKVSSPDYPE 

       190        200        210        220        230        240 
RNRENVMEDF LKRIECYKVT YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY 

       250        260        270        280        290        300 
YLMNIHVQPR TIYLCRHGES EFNLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW 

       310        320        330        340        350        360 
TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL RDQEKYLYRY 

       370        380        390        400        410        420 
PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA YFLDKGADEL PYLRCPLHTI 

       430        440        450        460        470        480 
FKLTPVAYGC KVETIKLNVE AVNTHRDKPT NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR 

       490        500 
NYSVGSRPLK PLSPLRAQDM QEGAD 

« Hide

Isoform 2 [UniParc].

Checksum: 2B9C8957889F4D61
Show »

FASTA47154,406

References

« Hide 'large scale' references
[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]"Isolation of novel heart-specific genes using the BodyMap database."
Soejima H., Kawamoto S., Akai J., Miyoshi O., Arai Y., Morohka T., Matsuo S., Niikawa N., Kimura A., Okubo K., Mukai T.
Genomics 74:115-120(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001018063.1. NM_001018053.1.
NP_006203.2. NM_006212.2.
UniGeneHs.282702.

3D structure databases

ProteinModelPortalO60825.
SMRO60825. Positions 37-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111229. 6 interactions.
IntActO60825. 4 interactions.
MINTMINT-3000455.
STRING9606.ENSP00000356047.

PTM databases

PhosphoSiteO60825.

Proteomic databases

PaxDbO60825.
PRIDEO60825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367079; ENSP00000356046; ENSG00000123836. [O60825-2]
ENST00000367080; ENSP00000356047; ENSG00000123836. [O60825-1]
GeneID5208.
KEGGhsa:5208.
UCSCuc001hfg.3. human. [O60825-1]
uc001hfh.3. human. [O60825-2]

Organism-specific databases

CTD5208.
GeneCardsGC01P207226.
HGNCHGNC:8873. PFKFB2.
HPAHPA049975.
MIM171835. gene.
neXtProtNX_O60825.
PharmGKBPA33212.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0406.
HOGENOMHOG000181112.
HOVERGENHBG005628.
InParanoidO60825.
KOK01103.
OMAHPRTIYL.
OrthoDBEOG7M3J03.
PhylomeDBO60825.
TreeFamTF313541.

Enzyme and pathway databases

BRENDA3.1.3.46. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKO60825.

Gene expression databases

ArrayExpressO60825.
BgeeO60825.
CleanExHS_PFKFB2.
GenevestigatorO60825.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERPTHR10606. PTHR10606. 1 hit.
PfamPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PIRSFPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSPR00991. 6PFRUCTKNASE.
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPFKFB2. human.
GeneWikiPFKFB2.
GenomeRNAi5208.
NextBio20140.
PROO60825.
SOURCESearch...

Entry information

Entry nameF262_HUMAN
AccessionPrimary (citable) accession number: O60825
Secondary accession number(s): O60824 expand/collapse secondary AC list , Q5VVQ3, Q5VVQ4, Q9H3P1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM