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Q16875

- F263_HUMAN

UniProt

Q16875 - F263_HUMAN

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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Gene

PFKFB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751Fructose 6-phosphate1 Publication
Binding sitei99 – 991Fructose 6-phosphate1 Publication
Active sitei125 – 1251Sequence Analysis
Binding sitei127 – 1271Fructose 6-phosphate1 Publication
Binding sitei133 – 1331Fructose 6-phosphate1 Publication
Active sitei155 – 1551Sequence Analysis
Binding sitei169 – 1691Fructose 6-phosphate1 Publication
Binding sitei190 – 1901Fructose 6-phosphate1 Publication
Binding sitei194 – 1941Fructose 6-phosphate1 Publication
Binding sitei253 – 2531Fructose 2,6-bisphosphate
Active sitei254 – 2541Tele-phosphohistidine intermediateBy similarity
Binding sitei260 – 2601Fructose 2,6-bisphosphateBy similarity
Binding sitei266 – 2661Fructose 2,6-bisphosphate; via amide nitrogen
Active sitei323 – 3231Proton donor/acceptorCurated
Binding sitei334 – 3341Fructose 2,6-bisphosphate
Binding sitei348 – 3481Fructose 2,6-bisphosphate
Binding sitei352 – 3521Fructose 2,6-bisphosphate
Binding sitei363 – 3631Fructose 2,6-bisphosphate
Active sitei388 – 3881Proton donor/acceptorBy similarity
Binding sitei389 – 3891Fructose 2,6-bisphosphate
Binding sitei393 – 3931Fructose 2,6-bisphosphate
Binding sitei425 – 4251ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 509ATP
Nucleotide bindingi164 – 1696ATP
Nucleotide bindingi345 – 3484ATPBy similarity
Nucleotide bindingi389 – 3935ATPBy similarity

GO - Molecular functioni

  1. 6-phosphofructo-2-kinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. carbohydrate phosphorylation Source: GOC
  3. fructose 2,6-bisphosphate metabolic process Source: InterPro
  4. fructose metabolic process Source: InterPro
  5. glucose metabolic process Source: Reactome
  6. glycolytic process Source: Reactome
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.105. 2681.
ReactomeiREACT_1383. Glycolysis.
SABIO-RKQ16875.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
Short name:
6PF-2-K/Fru-2,6-P2ase 3
Short name:
PFK/FBPase 3
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme
Renal carcinoma antigen NY-REN-56
iPFK-2
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:PFKFB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:8874. PFKFB3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: HPA
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5205206-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3PRO_0000179968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei461 – 4611Phosphoserine; by AMPK4 Publications
Modified residuei463 – 4631Phosphothreonine1 Publication
Modified residuei467 – 4671Phosphoserine3 Publications
Modified residuei471 – 4711Phosphothreonine; by PKCBy similarity

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16875.
PaxDbiQ16875.
PRIDEiQ16875.

PTM databases

PhosphoSiteiQ16875.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ16875.
CleanExiHS_PFKFB3.
ExpressionAtlasiQ16875. baseline and differential.
GenevestigatoriQ16875.

Organism-specific databases

HPAiCAB020795.
HPA008266.
HPA043889.

Interactioni

Protein-protein interaction databases

BioGridi111230. 9 interactions.
DIPiDIP-33964N.
IntActiQ16875. 5 interactions.
STRINGi9606.ENSP00000369100.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73
Turni9 – 113
Beta strandi14 – 163
Beta strandi36 – 416
Beta strandi44 – 474
Helixi48 – 6114
Beta strandi66 – 705
Helixi71 – 799
Helixi85 – 884
Helixi93 – 11624
Beta strandi121 – 1266
Helixi131 – 14313
Beta strandi147 – 1548
Helixi158 – 16811
Turni169 – 1713
Helixi173 – 1753
Helixi180 – 19516
Turni203 – 2097
Beta strandi210 – 2167
Turni217 – 2204
Beta strandi221 – 2255
Helixi230 – 23910
Beta strandi249 – 2535
Helixi258 – 2625
Helixi273 – 28917
Beta strandi295 – 2984
Helixi302 – 3098
Turni310 – 3123
Beta strandi315 – 3173
Helixi319 – 3213
Helixi327 – 3293
Helixi334 – 3407
Helixi342 – 3509
Turni352 – 3543
Helixi363 – 37917
Beta strandi381 – 3877
Helixi389 – 39911
Turni404 – 4063
Helixi407 – 4093
Beta strandi416 – 4238
Beta strandi426 – 4338
Helixi442 – 4465
Helixi455 – 4573

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AXNX-ray2.10A1-520[»]
2DWOX-ray2.25A1-520[»]
2DWPX-ray2.70A1-520[»]
2I1VX-ray2.50B1-520[»]
3QPUX-ray2.30A1-520[»]
3QPVX-ray2.50A1-520[»]
3QPWX-ray2.25A1-520[»]
4MA4X-ray2.23A1-520[»]
ProteinModelPortaliQ16875.
SMRiQ16875. Positions 4-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16875.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2452456-phosphofructo-2-kinaseAdd
BLAST
Regioni246 – 520275Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0406.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ16875.
KOiK01103.
OrthoDBiEOG7M3J03.
PhylomeDBiQ16875.
TreeFamiTF313541.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16875-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPLELTQSRV QKIWVPVDHR PSLPRSCGPK LTNSPTVIVM VGLPARGKTY
60 70 80 90 100
ISKKLTRYLN WIGVPTKVFN VGEYRREAVK QYSSYNFFRP DNEEAMKVRK
110 120 130 140 150
QCALAALRDV KSYLAKEGGQ IAVFDATNTT RERRHMILHF AKENDFKAFF
160 170 180 190 200
IESVCDDPTV VASNIMEVKI SSPDYKDCNS AEAMDDFMKR ISCYEASYQP
210 220 230 240 250
LDPDKCDRDL SLIKVIDVGR RFLVNRVQDH IQSRIVYYLM NIHVQPRTIY
260 270 280 290 300
LCRHGENEHN LQGRIGGDSG LSSRGKKFAS ALSKFVEEQN LKDLRVWTSQ
310 320 330 340 350
LKSTIQTAEA LRLPYEQWKA LNEIDAGVCE ELTYEEIRDT YPEEYALREQ
360 370 380 390 400
DKYYYRYPTG ESYQDLVQRL EPVIMELERQ ENVLVICHQA VLRCLLAYFL
410 420 430 440 450
DKSAEEMPYL KCPLHTVLKL TPVAYGCRVE SIYLNVESVC THRERSEDAK
460 470 480 490 500
KGPNPLMRRN SVTPLASPEP TKKPRINSFE EHVASTSAAL PSCLPPEVPT
510 520
QLPGQNMKGS RSSADSSRKH
Length:520
Mass (Da):59,609
Last modified:November 1, 1996 - v1
Checksum:iA7675A4ADC376879
GO
Isoform 2 (identifier: Q16875-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     506-520: NMKGSRSSADSSRKH → PLLGQACLT

Show »
Length:514
Mass (Da):58,876
Checksum:i18FD1D267306853D
GO
Isoform 3 (identifier: Q16875-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MPLELTQSRVQKIWVPVDHRPSLPRS → MPFRKA

Note: Gene prediction based on EST data.

Show »
Length:500
Mass (Da):57,287
Checksum:i32D2924D3D207C17
GO
Isoform 4 (identifier: Q16875-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MPLELTQSRVQKIWVPVDHRPSLPRS → MGEGGQKEGDSQQAGALPLLCQLDTFSPKATVFGVSINPA

Note: No experimental confirmation available.

Show »
Length:534
Mass (Da):60,602
Checksum:iFB3222408A8BC7EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361M → V in AAB99795. 1 PublicationCurated
Sequence conflicti141 – 1411A → G in AAC62000. (PubMed:10077634)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MPLEL…SLPRS → MPFRKA in isoform 3. CuratedVSP_047165Add
BLAST
Alternative sequencei1 – 2626MPLEL…SLPRS → MGEGGQKEGDSQQAGALPLL CQLDTFSPKATVFGVSINPA in isoform 4. 1 PublicationVSP_054549Add
BLAST
Alternative sequencei506 – 52015NMKGS…SSRKH → PLLGQACLT in isoform 2. 1 PublicationVSP_004680Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D49817 mRNA. Translation: BAA08624.1.
L77662 mRNA. Translation: AAL40083.1.
AF109735 mRNA. Translation: AAD08818.1.
AF041831
, AF041823, AF041824, AF041825, AF041826, AF041827, AF041828, AF041829, AF041830 Genomic DNA. Translation: AAB99795.1.
AF056320 mRNA. Translation: AAC62000.1.
AK291263 mRNA. Translation: BAF83952.1.
AK304450 mRNA. Translation: BAH14191.1.
AL359960, AL157395 Genomic DNA. Translation: CAH72163.1.
AL157395, AL359960 Genomic DNA. Translation: CAH73606.1.
CH471072 Genomic DNA. Translation: EAW86398.1.
CH471072 Genomic DNA. Translation: EAW86399.1.
BC040482 mRNA. Translation: AAH40482.1.
CCDSiCCDS44353.1. [Q16875-3]
CCDS60479.1. [Q16875-4]
CCDS7078.1. [Q16875-1]
PIRiJC4626.
RefSeqiNP_001138915.1. NM_001145443.1. [Q16875-3]
NP_001269559.1. NM_001282630.1. [Q16875-4]
NP_004557.1. NM_004566.3. [Q16875-1]
XP_005252520.1. XM_005252463.1. [Q16875-2]
UniGeneiHs.195471.

Genome annotation databases

EnsembliENST00000360521; ENSP00000353712; ENSG00000170525. [Q16875-2]
ENST00000379775; ENSP00000369100; ENSG00000170525. [Q16875-1]
ENST00000379789; ENSP00000369115; ENSG00000170525. [Q16875-3]
ENST00000536985; ENSP00000443319; ENSG00000170525. [Q16875-4]
GeneIDi5209.
KEGGihsa:5209.
UCSCiuc001ije.3. human. [Q16875-1]
uc001ijf.3. human. [Q16875-2]
uc010qaw.2. human.

Polymorphism databases

DMDMi3023733.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D49817 mRNA. Translation: BAA08624.1 .
L77662 mRNA. Translation: AAL40083.1 .
AF109735 mRNA. Translation: AAD08818.1 .
AF041831
, AF041823 , AF041824 , AF041825 , AF041826 , AF041827 , AF041828 , AF041829 , AF041830 Genomic DNA. Translation: AAB99795.1 .
AF056320 mRNA. Translation: AAC62000.1 .
AK291263 mRNA. Translation: BAF83952.1 .
AK304450 mRNA. Translation: BAH14191.1 .
AL359960 , AL157395 Genomic DNA. Translation: CAH72163.1 .
AL157395 , AL359960 Genomic DNA. Translation: CAH73606.1 .
CH471072 Genomic DNA. Translation: EAW86398.1 .
CH471072 Genomic DNA. Translation: EAW86399.1 .
BC040482 mRNA. Translation: AAH40482.1 .
CCDSi CCDS44353.1. [Q16875-3 ]
CCDS60479.1. [Q16875-4 ]
CCDS7078.1. [Q16875-1 ]
PIRi JC4626.
RefSeqi NP_001138915.1. NM_001145443.1. [Q16875-3 ]
NP_001269559.1. NM_001282630.1. [Q16875-4 ]
NP_004557.1. NM_004566.3. [Q16875-1 ]
XP_005252520.1. XM_005252463.1. [Q16875-2 ]
UniGenei Hs.195471.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AXN X-ray 2.10 A 1-520 [» ]
2DWO X-ray 2.25 A 1-520 [» ]
2DWP X-ray 2.70 A 1-520 [» ]
2I1V X-ray 2.50 B 1-520 [» ]
3QPU X-ray 2.30 A 1-520 [» ]
3QPV X-ray 2.50 A 1-520 [» ]
3QPW X-ray 2.25 A 1-520 [» ]
4MA4 X-ray 2.23 A 1-520 [» ]
ProteinModelPortali Q16875.
SMRi Q16875. Positions 4-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111230. 9 interactions.
DIPi DIP-33964N.
IntActi Q16875. 5 interactions.
STRINGi 9606.ENSP00000369100.

Chemistry

ChEMBLi CHEMBL2331053.

PTM databases

PhosphoSitei Q16875.

Polymorphism databases

DMDMi 3023733.

Proteomic databases

MaxQBi Q16875.
PaxDbi Q16875.
PRIDEi Q16875.

Protocols and materials databases

DNASUi 5209.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360521 ; ENSP00000353712 ; ENSG00000170525 . [Q16875-2 ]
ENST00000379775 ; ENSP00000369100 ; ENSG00000170525 . [Q16875-1 ]
ENST00000379789 ; ENSP00000369115 ; ENSG00000170525 . [Q16875-3 ]
ENST00000536985 ; ENSP00000443319 ; ENSG00000170525 . [Q16875-4 ]
GeneIDi 5209.
KEGGi hsa:5209.
UCSCi uc001ije.3. human. [Q16875-1 ]
uc001ijf.3. human. [Q16875-2 ]
uc010qaw.2. human.

Organism-specific databases

CTDi 5209.
GeneCardsi GC10P006186.
HGNCi HGNC:8874. PFKFB3.
HPAi CAB020795.
HPA008266.
HPA043889.
MIMi 605319. gene.
neXtProti NX_Q16875.
PharmGKBi PA33213.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0406.
GeneTreei ENSGT00390000018751.
HOGENOMi HOG000181112.
HOVERGENi HBG005628.
InParanoidi Q16875.
KOi K01103.
OrthoDBi EOG7M3J03.
PhylomeDBi Q16875.
TreeFami TF313541.

Enzyme and pathway databases

BRENDAi 2.7.1.105. 2681.
Reactomei REACT_1383. Glycolysis.
SABIO-RK Q16875.

Miscellaneous databases

ChiTaRSi Pfkfb3. human.
EvolutionaryTracei Q16875.
GeneWikii PFKFB3.
GenomeRNAii 5209.
NextBioi 20146.
PROi Q16875.
SOURCEi Search...

Gene expression databases

Bgeei Q16875.
CleanExi HS_PFKFB3.
ExpressionAtlasi Q16875. baseline and differential.
Genevestigatori Q16875.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view ]
PANTHERi PTHR10606. PTHR10606. 1 hit.
Pfami PF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSi PR00991. 6PFRUCTKNASE.
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta."
    Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.
    J. Biochem. 119:506-511(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "The third human isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3) map position 10p14-p15."
    Nicholl J., Hamilton J.A., Sutherland G.R., Sutherland R.L., Watts C.K.
    Chromosome Res. 5:150-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/ fructose-2, 6-bisphosphatase gene (PFKFB3)."
    Manzano A., Rosa J.L., Ventura F., Perez J.X., Nadal M., Estivill X., Ambrosio S., Gil J., Bartrons R.
    Cytogenet. Cell Genet. 83:214-217(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    El-Maghrabi M.R.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Brain.
  5. "An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect."
    Chesney J., Mitchell R.A., Benigni F., Bacher M., Spiegel L., Al-Abed Y., Han J.H., Metz C., Bucala R.
    Proc. Natl. Acad. Sci. U.S.A. 96:3047-3052(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Skeletal muscle.
  6. "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.
    , 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] (ISOFORMS 1 AND 4).
    Tissue: Trachea.
  7. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Testis.
  10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  11. "The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase."
    Marsin A.S., Bouzin C., Bertrand L., Hue L.
    J. Biol. Chem. 277:30778-30783(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-461.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-463 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-461 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3): a possible new target for cancer therapy."
    Kim S.G., Manes N.P., El-Maghrabi M.R., Lee Y.H.
    J. Biol. Chem. 281:2939-2944(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ADP AND FRUCTOSE 6-PHOSPHATE.
  16. "A direct substrate-substrate interaction found in the kinase domain of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Kim S.G., Cavalier M., El-Maghrabi M.R., Lee Y.H.
    J. Mol. Biol. 370:14-26(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEXES WITH ADP; ATP; FRUCTOSE 6-PHOSPHATE; FRUCTOSE-2,6-BISPHOSPHATE AND PHOSPHOENOLPYRUVATE.
  17. "Molecular basis of the fructose-2,6-bisphosphatase reaction of PFKFB3: transition state and the C-terminal function."
    Cavalier M.C., Kim S.G., Neau D., Lee Y.H.
    Proteins 80:1143-1153(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Entry informationi

Entry nameiF263_HUMAN
AccessioniPrimary (citable) accession number: Q16875
Secondary accession number(s): B7Z955
, O43622, O75902, Q5VX15, Q5VX18, Q5VX19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3