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P16118

- F261_HUMAN

UniProt

P16118 - F261_HUMAN

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Protein
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Gene
PFKFB1, F6PK, PFRX
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.

Enzyme regulationi

Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Fructose 6-phosphate By similarity
Binding sitei105 – 1051Fructose 6-phosphate By similarity
Active sitei131 – 1311 Reviewed prediction
Binding sitei133 – 1331Fructose 6-phosphate By similarity
Binding sitei139 – 1391Fructose 6-phosphate By similarity
Active sitei161 – 1611 Reviewed prediction
Binding sitei175 – 1751Fructose 6-phosphate By similarity
Binding sitei196 – 1961Fructose 6-phosphate By similarity
Binding sitei200 – 2001Fructose 6-phosphate By similarity
Binding sitei258 – 2581Fructose 2,6-bisphosphate
Active sitei259 – 2591Tele-phosphohistidine intermediate By similarity
Binding sitei265 – 2651Fructose 2,6-bisphosphate
Binding sitei271 – 2711Fructose 2,6-bisphosphate; via amide nitrogen By similarity
Binding sitei308 – 3081Fructose 2,6-bisphosphate
Active sitei328 – 3281Proton donor/acceptor By similarity
Binding sitei339 – 3391Fructose 2,6-bisphosphate
Binding sitei353 – 3531Fructose 2,6-bisphosphate
Binding sitei357 – 3571Fructose 2,6-bisphosphate
Binding sitei368 – 3681Fructose 2,6-bisphosphate
Active sitei393 – 3931Proton donor/acceptor By similarity
Binding sitei394 – 3941Fructose 2,6-bisphosphate By similarity
Binding sitei398 – 3981Fructose 2,6-bisphosphate
Binding sitei430 – 4301ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATP
Nucleotide bindingi170 – 1756ATP
Nucleotide bindingi350 – 3534ATP By similarity
Nucleotide bindingi394 – 3985ATP By 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
  4. fructose-6-phosphate binding Source: Ensembl
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. dephosphorylation Source: GOC
  3. energy reserve metabolic process Source: Reactome
  4. fructose 2,6-bisphosphate metabolic process Source: UniProtKB
  5. fructose metabolic process Source: InterPro
  6. gluconeogenesis Source: UniProtKB
  7. glucose metabolic process Source: Reactome
  8. glycolytic process Source: UniProtKB
  9. intracellular signal transduction Source: Reactome
  10. organ regeneration Source: Ensembl
  11. positive regulation of glucokinase activity Source: Ensembl
  12. response to cAMP Source: Ensembl
  13. response to glucagon Source: Ensembl
  14. response to glucocorticoid Source: Ensembl
  15. response to insulin Source: Ensembl
  16. response to starvation Source: Ensembl
  17. 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

BRENDAi3.1.3.46. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
SABIO-RKP16118.

Names & Taxonomyi

Protein namesi
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:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:PFKFB1
Synonyms:F6PK, PFRX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8872. PFKFB1.

Subcellular locationi

GO - Cellular componenti

  1. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex Source: UniProtKB
  2. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
PRO_0000179960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei33 – 331Phosphoserine; by PKA By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP16118.
PRIDEiP16118.

PTM databases

PhosphoSiteiP16118.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

ArrayExpressiP16118.
BgeeiP16118.
CleanExiHS_PFKFB1.
GenevestigatoriP16118.

Organism-specific databases

HPAiHPA013959.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GCKP355572EBI-709807,EBI-709928

Protein-protein interaction databases

BioGridi111228. 6 interactions.
IntActiP16118. 3 interactions.
MINTiMINT-6772805.
STRINGi9606.ENSP00000364145.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 486
Helixi55 – 6814
Beta strandi73 – 775
Helixi78 – 836
Helixi91 – 944
Helixi99 – 12123
Beta strandi126 – 1327
Helixi137 – 15014
Beta strandi153 – 1608
Helixi164 – 17512
Helixi187 – 20115
Turni209 – 2146
Beta strandi217 – 2215
Turni222 – 2254
Beta strandi226 – 2305
Helixi235 – 24410
Beta strandi254 – 2585
Helixi263 – 2664
Helixi278 – 29316
Beta strandi300 – 3034
Helixi307 – 3148
Helixi324 – 3263
Helixi332 – 3343
Helixi339 – 3457
Helixi347 – 3559
Turni357 – 3593
Helixi368 – 38417
Beta strandi386 – 3927
Helixi394 – 40512
Turni409 – 4113
Helixi412 – 4143
Beta strandi421 – 4277
Beta strandi429 – 43810
Helixi460 – 4645

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K6MX-ray2.40A/B40-471[»]
ProteinModelPortaliP16118.
SMRiP16118. Positions 7-471.

Miscellaneous databases

EvolutionaryTraceiP16118.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2502496-phosphofructo-2-kinase
Add
BLAST
Regioni251 – 471221Fructose-2,6-bisphosphatase
Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0406.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP16118.
KOiK01103.
OMAiNIRGRIG.
OrthoDBiEOG7M3J03.
PhylomeDBiP16118.
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 (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P16118-1) [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

MSPEMGELTQ TRLQKIWIPH SSGSSRLQRR RGSSIPQFTN SPTMVIMVGL    50
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME 100
ALQIRKQCAL AALKDVHNYL SHEEGHVAVF DATNTTRERR SLILQFAKEH 150
GYKVFFIESI CNDPGIIAEN IRQVKLGSPD YIDCDREKVL EDFLKRIECY 200
EVNYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT VYYLMNIHVT 250
PRSIYLCRHG ESELNIRGRI GGDSGLSVRG KQYAYALANF IQSQGISSLK 300
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF 350
ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL 400
LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCKVESIYLN VEAVNTHREK 450
PENVDITREP EEALDTVPAH Y 471
Length:471
Mass (Da):54,681
Last modified:November 1, 1997 - v3
Checksum:iC4FF081A295FB7D3
GO
Isoform 2 (identifier: P16118-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MSPEMGELTQ...RYLNWIGTPT → MEEKTSRI

Show »
Length:406
Mass (Da):47,426
Checksum:i5D982E7DFBAC5CC1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373MSPEM…IGTPT → MEEKTSRI in isoform 2.
VSP_054795Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti305 – 3051H → R in CAA36861. 1 Publication
Sequence conflicti359 – 3591R → H in AAA35818. 1 Publication
Sequence conflicti397 – 3982MR → HA in AAA35818. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52638 mRNA. Translation: CAA36861.1.
AK314089 mRNA. Translation: BAG36785.1.
AK300724 mRNA. Translation: BAG62397.1.
AL049732, AL020991 Genomic DNA. Translation: CAI42048.1.
AL020991, AL049732 Genomic DNA. Translation: CAI43127.1.
BC096079 mRNA. Translation: AAH96079.1.
M19938 mRNA. Translation: AAA35818.1.
CCDSiCCDS14364.1. [P16118-1]
CCDS65273.1. [P16118-2]
PIRiS12732.
RefSeqiNP_001258733.1. NM_001271804.1.
NP_001258734.1. NM_001271805.1. [P16118-2]
NP_002616.2. NM_002625.3. [P16118-1]
UniGeneiHs.444304.

Genome annotation databases

EnsembliENST00000375006; ENSP00000364145; ENSG00000158571.
ENST00000545676; ENSP00000444074; ENSG00000158571.
GeneIDi5207.
KEGGihsa:5207.
UCSCiuc004dty.2. human. [P16118-1]

Polymorphism databases

DMDMi2507178.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52638 mRNA. Translation: CAA36861.1 .
AK314089 mRNA. Translation: BAG36785.1 .
AK300724 mRNA. Translation: BAG62397.1 .
AL049732 , AL020991 Genomic DNA. Translation: CAI42048.1 .
AL020991 , AL049732 Genomic DNA. Translation: CAI43127.1 .
BC096079 mRNA. Translation: AAH96079.1 .
M19938 mRNA. Translation: AAA35818.1 .
CCDSi CCDS14364.1. [P16118-1 ]
CCDS65273.1. [P16118-2 ]
PIRi S12732.
RefSeqi NP_001258733.1. NM_001271804.1.
NP_001258734.1. NM_001271805.1. [P16118-2 ]
NP_002616.2. NM_002625.3. [P16118-1 ]
UniGenei Hs.444304.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K6M X-ray 2.40 A/B 40-471 [» ]
ProteinModelPortali P16118.
SMRi P16118. Positions 7-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111228. 6 interactions.
IntActi P16118. 3 interactions.
MINTi MINT-6772805.
STRINGi 9606.ENSP00000364145.

PTM databases

PhosphoSitei P16118.

Polymorphism databases

DMDMi 2507178.

Proteomic databases

PaxDbi P16118.
PRIDEi P16118.

Protocols and materials databases

DNASUi 5207.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375006 ; ENSP00000364145 ; ENSG00000158571 .
ENST00000545676 ; ENSP00000444074 ; ENSG00000158571 .
GeneIDi 5207.
KEGGi hsa:5207.
UCSCi uc004dty.2. human. [P16118-1 ]

Organism-specific databases

CTDi 5207.
GeneCardsi GC0XM054976.
HGNCi HGNC:8872. PFKFB1.
HPAi HPA013959.
MIMi 311790. gene.
neXtProti NX_P16118.
PharmGKBi PA33211.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0406.
HOGENOMi HOG000181112.
HOVERGENi HBG005628.
InParanoidi P16118.
KOi K01103.
OMAi NIRGRIG.
OrthoDBi EOG7M3J03.
PhylomeDBi P16118.
TreeFami TF313541.

Enzyme and pathway databases

BRENDAi 3.1.3.46. 2681.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
SABIO-RK P16118.

Miscellaneous databases

EvolutionaryTracei P16118.
GenomeRNAii 5207.
NextBioi 20136.
PROi P16118.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16118.
Bgeei P16118.
CleanExi HS_PFKFB1.
Genevestigatori P16118.

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. "Sequence of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Lange A.J., Pilkis S.J.
    Nucleic Acids Res. 18:3652-3652(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "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 2).
    Tissue: Liver.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
  5. "Molecular cloning, sequence analysis, and expression of a human liver cDNA coding for fructose-6-P,2-kinase:fructose-2,6-bisphosphatase."
    Algaier J., Uyeda K.
    Biochem. Biophys. Res. Commun. 153:328-333(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-471.
    Tissue: Liver.
  6. "Tissue-specific structure/function differentiation of the liver isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Lee Y.H., Li Y., Uyeda K., Hasemann C.A.
    J. Biol. Chem. 278:523-530(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-471 IN COMPLEX WITH ATP ANALOG, SUBUNIT.

Entry informationi

Entry nameiF261_HUMAN
AccessioniPrimary (citable) accession number: P16118
Secondary accession number(s): B2RA88
, B4DUN5, Q5JXS5, Q99951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 158 of the entry and version 3 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 X
    Human chromosome X: 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

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