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Q01813 (PFKAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. 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:
ATP-dependent 6-phosphofructokinase, platelet type

Short name=ATP-PFK
Short name=PFK-P
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphohexokinase
Gene names
Name:PFKP
Synonyms:PFKF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. HAMAP-Rule MF_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium.

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homo- and heterotetramers. Muscle is M4, liver is L4, and red cell is M3L, M2L2, or ML3. A subunit composition with a higher proportion of platelet type subunits is found in platelets, brain and fibroblasts.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_03184

Miscellaneous

In human PFK exists as a system of 3 types of subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet) isoenzymes.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

carbohydrate phosphorylation

Inferred from sequence or structural similarity. Source: GOC

fructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glucose metabolic process

Traceable author statement. Source: Reactome

glycolytic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_function6-phosphofructokinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex binding

Inferred from direct assay PubMed 23209302. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01813-1)

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: Q01813-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: MDADDSRAPK...DWESVSSILQ → MCGYERCRPC...RFPCPGRHAL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784ATP-dependent 6-phosphofructokinase, platelet type HAMAP-Rule MF_03184
PRO_0000112024

Regions

Nucleotide binding97 – 982ATP By similarity
Nucleotide binding127 – 1304ATP By similarity
Region1 – 399399N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region173 – 1753Substrate binding By similarity
Region217 – 2193Substrate binding By similarity
Region307 – 3104Substrate binding By similarity
Region400 – 41112Interdomain linker HAMAP-Rule MF_03184
Region412 – 784373C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region538 – 5425Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region583 – 5853Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region671 – 6744Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1751Proton acceptor By similarity
Metal binding1281Magnesium; catalytic By similarity
Binding site341ATP; via amide nitrogen By similarity
Binding site2101Substrate; shared with dimeric partner By similarity
Binding site2731Substrate By similarity
Binding site3011Substrate; shared with dimeric partner By similarity
Binding site4811Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6391Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7441Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue121Phosphoserine By similarity
Modified residue3861Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13 Ref.15
Modified residue3951N6-acetyllysine Ref.12
Modified residue4861N6-acetyllysine Ref.12
Modified residue6511Phosphotyrosine Ref.6
Modified residue6881N6-acetyllysine Ref.12
Modified residue7831Phosphoserine Ref.8 Ref.9 Ref.11 Ref.13
Glycosylation5401O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence1 – 8787MDADD…SSILQ → MCGYERCRPCRGAHGYLRGG QGVLHLRGLPGHGGRRLKHR RGRLGECLQHPASGAVRGDW REKPGCWSHRFPCPGRHAL in isoform 2.
VSP_046416

Experimental info

Sequence conflict484 – 4852PG → IP Ref.5
Sequence conflict4981Missing in AAA36435. Ref.5
Sequence conflict6551S → P in BAG52577. Ref.2
Sequence conflict6991A → E in AAA36435. Ref.5

Sequences

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

Last modified February 1, 1996. Version 2.
Checksum: 22522E77E9AF80F6

FASTA78485,596
        10         20         30         40         50         60 
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVYFI 

        70         80         90        100        110        120 
YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA FRTREGRLKA ACNLLQRGIT 

       130        140        150        160        170        180 
NLCVIGGDGS LTGANLFRKE WSGLLEELAR NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG 

       190        200        210        220        230        240 
TDMTIGTDSA LHRIIEVVDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP 

       250        260        270        280        290        300 
ESPPEEGWEE QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT 

       310        320        330        340        350        360 
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN HAVRLPLMEC 

       370        380        390        400        410        420 
VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK LPDDQIPKTN CNVAVINVGA 

       430        440        450        460        470        480 
PAAGMNAAVR SAVRVGIADG HRMLAIYDGF DGFAKGQIKE IGWTDVGGWT GQGGSILGTK 

       490        500        510        520        530        540 
RVLPGKYLEE IATQMRTHSI NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS 

       550        560        570        580        590        600 
NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA 

       610        620        630        640        650        660 
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGKG 

       670        680        690        700        710        720 
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK LKEARGRGKK FTTDDSICVL 

       730        740        750        760        770        780 
GISKRNVIFQ PVAELKKQTD FEHRIPKEQW WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ 


PWSV 

« Hide

Isoform 2 [UniParc].

Checksum: 649595FEDE1A9187
Show »

FASTA77685,316

References

« Hide 'large scale' references
[1]"Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet."
Eto K., Sakura H., Yasuda K., Hayakawa T., Kawasaki E., Moriuchi R., Nagataki S., Yazaki Y., Kadowaki T.
Biochem. Biophys. Res. Commun. 198:990-998(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Pancreatic islet.
[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. 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] (ISOFORMS 1 AND 2).
Tissue: Prostate.
[3]"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].
[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).
Tissue: Brain and Placenta.
[5]"Isolation and sequence of a cDNA encoding human platelet phosphofructokinase."
Simpson C.J., Fothergill-Gilmore L.A.
Biochem. Biophys. Res. Commun. 180:197-203(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 484-784 (ISOFORM 1).
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-386 AND SER-783, 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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-395; LYS-486 AND LYS-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-386 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D25328 mRNA. Translation: BAA04998.1.
AK092597 mRNA. Translation: BAG52577.1.
AK291841 mRNA. Translation: BAF84530.1.
AL731533, AL451164 Genomic DNA. Translation: CAH69851.1.
AL451164, AL731533 Genomic DNA. Translation: CAI39999.1.
BC002536 mRNA. Translation: AAH02536.1.
BC029138 mRNA. Translation: AAH29138.1.
M64784 mRNA. Translation: AAA36435.1.
CCDSCCDS55698.1. [Q01813-2]
CCDS7059.1. [Q01813-1]
PIRJC2055.
RefSeqNP_001229268.1. NM_001242339.1. [Q01813-2]
NP_002618.1. NM_002627.4. [Q01813-1]
UniGeneHs.26010.

3D structure databases

ProteinModelPortalQ01813.
SMRQ01813. Positions 22-765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111235. 37 interactions.
IntActQ01813. 16 interactions.
MINTMINT-1159988.
STRING9606.ENSP00000370517.

Chemistry

BindingDBQ01813.

PTM databases

PhosphoSiteQ01813.

Polymorphism databases

DMDM1346355.

Proteomic databases

MaxQBQ01813.
PaxDbQ01813.
PeptideAtlasQ01813.
PRIDEQ01813.

Protocols and materials databases

DNASU5214.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381075; ENSP00000370465; ENSG00000067057. [Q01813-2]
ENST00000381125; ENSP00000370517; ENSG00000067057. [Q01813-1]
GeneID5214.
KEGGhsa:5214.
UCSCuc001igp.3. human. [Q01813-1]

Organism-specific databases

CTD5214.
GeneCardsGC10P003109.
HGNCHGNC:8878. PFKP.
HPAHPA018257.
MIM171840. gene.
neXtProtNX_Q01813.
PharmGKBPA33217.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidQ01813.
KOK00850.
OMASAKAMQW.
OrthoDBEOG7ZSHV5.
PhylomeDBQ01813.
TreeFamTF300411.

Enzyme and pathway databases

BioCycMetaCyc:HS00894-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ01813.
UniPathwayUPA00109; UER00182.

Gene expression databases

ArrayExpressQ01813.
BgeeQ01813.
CleanExHS_PFKP.
GenevestigatorQ01813.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPFKP. human.
GeneWikiPFKP.
GenomeRNAi5214.
NextBio20168.
PROQ01813.
SOURCESearch...

Entry information

Entry namePFKAP_HUMAN
AccessionPrimary (citable) accession number: Q01813
Secondary accession number(s): B3KS15, Q5VSR7, Q5VSR8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 155 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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