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Q16875 (F263_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 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:

  1. 6-phosphofructo-2-kinase
    EC=2.7.1.105
  2. Fructose-2,6-bisphosphatase
    EC=3.1.3.46
Gene names
Name:PFKFB3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
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.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylation by AMPK stimulates activity.

Sequence similarities

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16875-1)

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: Q16875-2)

The sequence of this isoform differs from the canonical sequence as follows:
     506-520: NMKGSRSSADSSRKH → PLLGQACLT
Isoform 3 (identifier: Q16875-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MPLELTQSRVQKIWVPVDHRPSLPRS → MPFRKA
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5205206-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
PRO_0000179968

Regions

Nucleotide binding42 – 509ATP
Nucleotide binding164 – 1696ATP
Nucleotide binding345 – 3484ATP By similarity
Nucleotide binding389 – 3935ATP By similarity
Region1 – 2452456-phosphofructo-2-kinase
Region246 – 520275Fructose-2,6-bisphosphatase

Sites

Active site1251 Potential
Active site1551 Potential
Active site2541Tele-phosphohistidine intermediate By similarity
Active site3231Proton donor/acceptor Probable
Active site3881Proton donor/acceptor By similarity
Binding site751Fructose 6-phosphate
Binding site991Fructose 6-phosphate
Binding site1271Fructose 6-phosphate
Binding site1331Fructose 6-phosphate
Binding site1691Fructose 6-phosphate
Binding site1901Fructose 6-phosphate
Binding site1941Fructose 6-phosphate
Binding site2531Fructose 2,6-bisphosphate
Binding site2601Fructose 2,6-bisphosphate By similarity
Binding site2661Fructose 2,6-bisphosphate; via amide nitrogen
Binding site3341Fructose 2,6-bisphosphate
Binding site3481Fructose 2,6-bisphosphate
Binding site3521Fructose 2,6-bisphosphate
Binding site3631Fructose 2,6-bisphosphate
Binding site3891Fructose 2,6-bisphosphate
Binding site3931Fructose 2,6-bisphosphate
Binding site4251ATP

Amino acid modifications

Modified residue4611Phosphoserine; by AMPK Ref.11 Ref.12 Ref.13 Ref.14
Modified residue4631Phosphothreonine Ref.12
Modified residue4671Phosphoserine Ref.12 Ref.13 Ref.14
Modified residue4711Phosphothreonine; by PKC By similarity

Natural variations

Alternative sequence1 – 2626MPLEL…SLPRS → MPFRKA in isoform 3.
VSP_047165
Alternative sequence506 – 52015NMKGS…SSRKH → PLLGQACLT in isoform 2.
VSP_004680

Experimental info

Sequence conflict1361M → V in AAB99795. Ref.4
Sequence conflict1411A → G in AAC62000. Ref.5

Secondary structure

............................................................................... 520
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: A7675A4ADC376879

FASTA52059,609
        10         20         30         40         50         60 
MPLELTQSRV QKIWVPVDHR PSLPRSCGPK LTNSPTVIVM VGLPARGKTY ISKKLTRYLN 

        70         80         90        100        110        120 
WIGVPTKVFN VGEYRREAVK QYSSYNFFRP DNEEAMKVRK QCALAALRDV KSYLAKEGGQ 

       130        140        150        160        170        180 
IAVFDATNTT RERRHMILHF AKENDFKAFF IESVCDDPTV VASNIMEVKI SSPDYKDCNS 

       190        200        210        220        230        240 
AEAMDDFMKR ISCYEASYQP LDPDKCDRDL SLIKVIDVGR RFLVNRVQDH IQSRIVYYLM 

       250        260        270        280        290        300 
NIHVQPRTIY LCRHGENEHN LQGRIGGDSG LSSRGKKFAS ALSKFVEEQN LKDLRVWTSQ 

       310        320        330        340        350        360 
LKSTIQTAEA LRLPYEQWKA LNEIDAGVCE ELTYEEIRDT YPEEYALREQ DKYYYRYPTG 

       370        380        390        400        410        420 
ESYQDLVQRL EPVIMELERQ ENVLVICHQA VLRCLLAYFL DKSAEEMPYL KCPLHTVLKL 

       430        440        450        460        470        480 
TPVAYGCRVE SIYLNVESVC THRERSEDAK KGPNPLMRRN SVTPLASPEP TKKPRINSFE 

       490        500        510        520 
EHVASTSAAL PSCLPPEVPT QLPGQNMKGS RSSADSSRKH 

« Hide

Isoform 2 [UniParc].

Checksum: 18FD1D267306853D
Show »

FASTA51458,876
Isoform 3 [UniParc].

Checksum: 32D2924D3D207C17
Show »

FASTA50057,287

References

« Hide 'large scale' references
[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. 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 1).
[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. expand/collapse author list , 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]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].
[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]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
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]"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-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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49817 mRNA. Translation: BAA08624.1.
L77662 mRNA. Translation: AAL40083.1.
AF109735 mRNA. Translation: AAD08818.1.
AF041831 expand/collapse EMBL AC list , AF041823, AF041824, AF041825, AF041826, AF041827, AF041828, AF041829, AF041830 Genomic DNA. Translation: AAB99795.1.
AF056320 mRNA. Translation: AAC62000.1.
AK291263 mRNA. Translation: BAF83952.1.
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.
PIRJC4626.
RefSeqNP_001138915.1. NM_001145443.1.
NP_001269559.1. NM_001282630.1.
NP_004557.1. NM_004566.3.
XP_005252520.1. XM_005252463.1.
UniGeneHs.195471.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ16875.
SMRQ16875. Positions 4-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111230. 7 interactions.
DIPDIP-33964N.
IntActQ16875. 5 interactions.
STRING9606.ENSP00000369100.

Chemistry

ChEMBLCHEMBL2331053.

PTM databases

PhosphoSiteQ16875.

Polymorphism databases

DMDM3023733.

Proteomic databases

PaxDbQ16875.
PRIDEQ16875.

Protocols and materials databases

DNASU5209.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360521; ENSP00000353712; ENSG00000170525. [Q16875-2]
ENST00000379775; ENSP00000369100; ENSG00000170525. [Q16875-1]
ENST00000379789; ENSP00000369115; ENSG00000170525. [Q16875-3]
GeneID5209.
KEGGhsa:5209.
UCSCuc001ije.3. human. [Q16875-1]
uc001ijf.3. human. [Q16875-2]

Organism-specific databases

CTD5209.
GeneCardsGC10P006186.
HGNCHGNC:8874. PFKFB3.
HPACAB020795.
HPA008266.
HPA043889.
MIM605319. gene.
neXtProtNX_Q16875.
PharmGKBPA33213.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0406.
HOGENOMHOG000181112.
HOVERGENHBG005628.
KOK01103.
OrthoDBEOG7M3J03.
PhylomeDBQ16875.
TreeFamTF313541.

Enzyme and pathway databases

BRENDA2.7.1.105. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ16875.

Gene expression databases

ArrayExpressQ16875.
BgeeQ16875.
CleanExHS_PFKFB3.
GenevestigatorQ16875.

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

ChiTaRSPfkfb3. human.
EvolutionaryTraceQ16875.
GeneWikiPFKFB3.
GenomeRNAi5209.
NextBio20146.
PROQ16875.
SOURCESearch...

Entry information

Entry nameF263_HUMAN
AccessionPrimary (citable) accession number: Q16875
Secondary accession number(s): O43622 expand/collapse secondary AC list , O75902, Q5VX15, Q5VX18, Q5VX19
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 146 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM