Q01813 (K6PP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phosphofructokinase type C
EC=2.7.1.11

Alternative name(s):
6-phosphofructokinase, platelet type
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphofructokinase 1
Phosphohexokinase

Gene names

Name:	PFKP
Synonyms:	PFKF

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.
Catalytic activity	ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.
Cofactor	Magnesium.
Enzyme regulation	Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subunit structure	Tetramer. 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.
Post-translational modification	GlcNAcylation decreases enzyme activity By similarity.
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 family. Two domains subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Non-traceable author statement. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	6-phosphofructokinase complex Non-traceable author statement. Source: UniProtKB
Molecular_function	6-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
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 784	784	6-phosphofructokinase type C		PRO_0000112024
Regions
	Nucleotide binding	44 – 48	5	ATP By similarity
	Nucleotide binding	202 – 206	5	ATP By similarity
	Nucleotide binding	219 – 235	17	ATP By similarity
Sites
	Active site	175	1	Proton acceptor By similarity
	Metal binding	233	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	210	1	Substrate By similarity
	Binding site	301	1	Substrate By similarity
	Binding site	307	1	Substrate By similarity
	Binding site	310	1	Substrate By similarity
Amino acid modifications
	Modified residue	12	1	Phosphoserine By similarity
	Modified residue	386	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.12 Ref.14
	Modified residue	395	1	N6-acetyllysine Ref.11
	Modified residue	486	1	N6-acetyllysine Ref.11
	Modified residue	651	1	Phosphotyrosine Ref.6
	Modified residue	688	1	N6-acetyllysine Ref.11
	Modified residue	783	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
	Glycosylation	540	1	O-linked (GlcNAc...) By similarity
Natural variations
	Alternative sequence	1 – 87	87	MDADD…SSILQ → MCGYERCRPCRGAHGYLRGG QGVLHLRGLPGHGGRRLKHR RGRLGECLQHPASGAVRGDW REKPGCWSHRFPCPGRHAL in isoform 2.		VSP_046416
Experimental info
	Sequence conflict	484 – 485	2	PG → IP Ref.5
	Sequence conflict	498	1	Missing in AAA36435. Ref.5
	Sequence conflict	655	1	S → P in BAG52577. Ref.2
	Sequence conflict	699	1	A → E in AAA36435. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 22522E77E9AF80F6	FASTA	784	85,596
	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
	Isoform 2 [UniParc]. Checksum: 649595FEDE1A9187	FASTA	776	85,316
	10 20 30 40 50 60 MCGYERCRPC RGAHGYLRGG QGVLHLRGLP GHGGRRLKHR RGRLGECLQH PASGAVRGDW 70 80 90 100 110 120 REKPGCWSHR FPCPGRHALV GGTIIGSARC QAFRTREGRL KAACNLLQRG ITNLCVIGGD 130 140 150 160 170 180 GSLTGANLFR KEWSGLLEEL ARNGQIDKEA VQKYAYLNVV GMVGSIDNDF CGTDMTIGTD 190 200 210 220 230 240 SALHRIIEVV DAIMTTAQSH QRTFVLEVMG RHCGYLALVS ALACGADWVF LPESPPEEGW 250 260 270 280 290 300 EEQMCVKLSE NRARKKRLNI IIVAEGAIDT QNKPITSEKI KELVVTQLGY DTRVTILGHV 310 320 330 340 350 360 QRGGTPSAFD RILASRMGVE AVIALLEATP DTPACVVSLN GNHAVRLPLM ECVQMTQDVQ 370 380 390 400 410 420 KAMDERRFQD AVRLRGRSFA GNLNTYKRLA IKLPDDQIPK TNCNVAVINV GAPAAGMNAA 430 440 450 460 470 480 VRSAVRVGIA DGHRMLAIYD GFDGFAKGQI KEIGWTDVGG WTGQGGSILG TKRVLPGKYL 490 500 510 520 530 540 EEIATQMRTH SINALLIIGG FEAYLGLLEL SAAREKHEEF CVPMVMVPAT VSNNVPGSDF 550 560 570 580 590 600 SIGADTALNT ITDTCDRIKQ SASGTKRRVF IIETMGGYCG YLANMGGLAA GADAAYIFEE 610 620 630 640 650 660 PFDIRDLQSN VEHLTEKMKT TIQRGLVLRN ESCSENYTTD FIYQLYSEEG KGVFDCRKNV 670 680 690 700 710 720 LGHMQQGGAP SPFDRNFGTK ISARAMEWIT AKLKEARGRG KKFTTDDSIC VLGISKRNVI 730 740 750 760 770 FQPVAELKKQ TDFEHRIPKE QWWLKLRPLM KILAKYKASY DVSDSGQLEH VQPWSV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY.
[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-386 AND SER-783, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00009790. IPI00643196.
PIR	JC2055.
RefSeq	NP_001229268.1. NM_001242339.1. NP_002618.1. NM_002627.4.
UniGene	Hs.26010.
3D structure databases
ProteinModelPortal	Q01813.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01813. 10 interactions.
MINT	MINT-1159988.
STRING	9606.ENSP00000370517.
PTM databases
PhosphoSite	Q01813.
Polymorphism databases
DMDM	1346355.
Proteomic databases
PaxDb	Q01813.
PeptideAtlas	Q01813.
PRIDE	Q01813.
Protocols and materials databases
DNASU	5214.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000381075; ENSP00000370465; ENSG00000067057. ENST00000381125; ENSP00000370517; ENSG00000067057.
GeneID	5214.
KEGG	hsa:5214.
UCSC	uc001igp.3. human. uc001igq.3. human.
Organism-specific databases
CTD	5214.
GeneCards	GC10P003109.
HGNC	HGNC:8878. PFKP.
HPA	HPA018257.
MIM	171840. gene.
neXtProt	NX_Q01813.
PharmGKB	PA33217.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0205.
HOGENOM	HOG000200154.
HOVERGEN	HBG000976.
InParanoid	Q01813.
KO	K00850.
OMA	YLANMGA.
OrthoDB	EOG4NS39Z.
PhylomeDB	Q01813.
Enzyme and pathway databases
BioCyc	MetaCyc:HS00894-MONOMER.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q01813.
UniPathway	UPA00109; UER00182.
Gene expression databases
ArrayExpress	Q01813.
Bgee	Q01813.
CleanEx	HS_PFKP.
Genevestigator	Q01813.
GermOnline	ENSG00000067057. Homo sapiens.
Family and domain databases
InterPro	IPR009161. 6-phosphofructokinase_euk. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view]
Pfam	PF00365. PFK. 2 hits. [Graphical view]
PIRSF	PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTS	PR00476. PHFRCTKINASE.
SUPFAM	SSF53784. Ppfruckinase. 2 hits.
TIGRFAMs	TIGR02478. 6PF1K_euk. 1 hit.
PROSITE	PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q01813.
ChEMBL	CHEMBL2972.
ChiTaRS	PFKP. human.
GenomeRNAi	5214.
NextBio	20168.
SOURCE	Search...

Entry information

Entry name

K6PP_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 143 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.