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Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

PFKM

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

Functioni

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

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP)
  4. Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei25ATP; via amide nitrogenUniRule annotation1
Metal bindingi119Magnesium; catalyticUniRule annotation1
Active sitei166Proton acceptorUniRule annotation1
Binding sitei201Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Binding sitei292Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei471Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei566Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei629Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei655Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei735Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi88 – 89ATPUniRule annotation2
Nucleotide bindingi118 – 121ATPUniRule annotation4

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: UniProtKB
  • ATP binding Source: BHF-UCL
  • fructose binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
  • kinase binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: HGNC

GO - Biological processi

  • canonical glycolysis Source: Reactome
  • fructose 6-phosphate metabolic process Source: BHF-UCL
  • glucose homeostasis Source: Ensembl
  • glycogen catabolic process Source: Ensembl
  • glycolysis from storage polysaccharide through glucose-1-phosphate Source: Ensembl
  • glycolytic process Source: UniProtKB
  • muscle cell cellular homeostasis Source: BHF-UCL
  • positive regulation of insulin secretion Source: Ensembl
  • protein oligomerization Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07832-MONOMER.
ZFISH:HS07832-MONOMER.
ReactomeiR-HSA-70171. Glycolysis.
SABIO-RKP08237.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, muscle typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-M
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name:
PFK-A
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFKM
Synonyms:PFKX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:8877. PFKM.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • 6-phosphofructokinase complex Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • sperm principal piece Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 7 (GSD7)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic disorder characterized by exercise intolerance with associated nausea and vomiting, muscle cramping, exertional myopathy and compensated hemolysis. Short bursts of intense activity are particularly difficult. Severe muscle cramps and myoglobinuria develop after vigorous exercise.
See also OMIM:232800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00606339R → L in GSD7; Ashkenazi. Corresponds to variant rs121918193dbSNPEnsembl.1
Natural variantiVAR_00606439R → P in GSD7; Italian. 1 PublicationCorresponds to variant rs121918193dbSNPEnsembl.1
Natural variantiVAR_07223957G → V in GSD7; Italian. 1 Publication1
Natural variantiVAR_006065100R → Q in GSD7; Swiss. 1 PublicationCorresponds to variant rs2228500dbSNPEnsembl.1
Natural variantiVAR_072240180S → C in GSD7; Italian. 1 Publication1
Natural variantiVAR_006066209G → D in GSD7; French Canadian. 1 PublicationCorresponds to variant rs767265360dbSNPEnsembl.1
Natural variantiVAR_072241309D → G in GSD7; Spanish; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_006067543D → A in GSD7; Italian. 1 PublicationCorresponds to variant rs121918194dbSNPEnsembl.1
Natural variantiVAR_072242591D → A in GSD7; Italian. 1 Publication1
Natural variantiVAR_006068686W → C in GSD7; Japanese. 1 PublicationCorresponds to variant rs121918196dbSNPEnsembl.1
Natural variantiVAR_006069696R → H in GSD7; Swiss. 1 PublicationCorresponds to variant rs41291971dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

DisGeNETi5213.
MalaCardsiPFKM.
MIMi232800. phenotype.
OpenTargetsiENSG00000152556.
Orphaneti371. Glycogen storage disease due to muscle phosphofructokinase deficiency.
PharmGKBiPA33216.

Chemistry databases

ChEMBLiCHEMBL3291.

Polymorphism and mutation databases

BioMutaiPFKM.
DMDMi125126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001120162 – 780ATP-dependent 6-phosphofructokinase, muscle typeAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei133PhosphoserineBy similarity1
Modified residuei377PhosphoserineBy similarity1
Glycosylationi530O-linked (GlcNAc)By similarity1
Modified residuei667PhosphoserineCombined sources1
Modified residuei775PhosphoserineBy similarity1

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP08237.
MaxQBiP08237.
PaxDbiP08237.
PeptideAtlasiP08237.
PRIDEiP08237.

2D gel databases

UCD-2DPAGEP08237.

PTM databases

iPTMnetiP08237.
PhosphoSitePlusiP08237.

Miscellaneous databases

PMAP-CutDBP08237.

Expressioni

Gene expression databases

BgeeiENSG00000152556.
CleanExiHS_PFKM.
ExpressionAtlasiP08237. baseline and differential.
GenevisibleiP08237. HS.

Organism-specific databases

HPAiHPA002117.

Interactioni

Subunit structurei

Homo- and heterotetramers. Muscle is M4, liver is L4, and red cell is M3L, M2L2, or ML3. Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-514788,EBI-514788
PFKLP178586EBI-514788,EBI-487243
SIAH1Q8IUQ43EBI-514788,EBI-747107

GO - Molecular functioni

  • identical protein binding Source: BHF-UCL
  • kinase binding Source: BHF-UCL
  • protein C-terminus binding Source: HGNC

Protein-protein interaction databases

BioGridi111234. 62 interactors.
IntActiP08237. 23 interactors.
MINTiMINT-5005297.
STRINGi9606.ENSP00000345771.

Chemistry databases

BindingDBiP08237.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OMTX-ray6.00A1-780[»]
ProteinModelPortaliP08237.
SMRiP08237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 390N-terminal catalytic PFK domain 1Add BLAST389
Regioni164 – 166Substrate bindingUniRule annotation3
Regioni208 – 210Substrate bindingUniRule annotation3
Regioni298 – 301Substrate bindingUniRule annotation4
Regioni391 – 401Interdomain linkerAdd BLAST11
Regioni402 – 780C-terminal regulatory PFK domain 2Add BLAST379
Regioni528 – 532Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni573 – 575Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni661 – 664Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP08237.
KOiK00850.
OMAiIFIPEMP.
OrthoDBiEOG091G01YN.
PhylomeDBiP08237.
TreeFamiTF300411.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08237-1) [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
MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF
60 70 80 90 100
VHEGYQGLVD GGDHIKEATW ESVSMMLQLG GTVIGSARCK DFREREGRLR
110 120 130 140 150
AAYNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITDEEA
160 170 180 190 200
TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIMEIVD AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET
260 270 280 290 300
RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME
360 370 380 390 400
CVQVTKDVTK AMDEKKFDEA LKLRGRSFMN NWEVYKLLAH VRPPVSKSGS
410 420 430 440 450
HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE
460 470 480 490 500
AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE
510 520 530 540 550
AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC
560 570 580 590 600
TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
610 620 630 640 650
TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG
660 670 680 690 700
IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI
710 720 730 740 750
FANTPDSGCV LGMRKRALVF QPVAELKDQT DFEHRIPKEQ WWLKLRPILK
760 770 780
ILAKYEIDLD TSDHAHLEHI TRKRSGEAAV
Length:780
Mass (Da):85,183
Last modified:January 23, 2007 - v2
Checksum:i769A2C01F97D1122
GO
Isoform 2 (identifier: P08237-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     282-312: Missing.

Show »
Length:749
Mass (Da):81,776
Checksum:iFA4B5D6B077EDC8B
GO
Isoform 3 (identifier: P08237-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHKDEFHLKFFMCVIQSRQLVRTPQRTAGEASTSSMLIPKPPPKTDILKSLDTMDDPDTVGSIPVFKTEWIM

Note: No experimental confirmation available.Curated
Show »
Length:851
Mass (Da):93,254
Checksum:iA09ABE529E682EC4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti670P → S in BAC86498 (PubMed:14702039).Curated1
Isoform 3 (identifier: P08237-3)
Sequence conflicti2H → L in BAC86498 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00606339R → L in GSD7; Ashkenazi. Corresponds to variant rs121918193dbSNPEnsembl.1
Natural variantiVAR_00606439R → P in GSD7; Italian. 1 PublicationCorresponds to variant rs121918193dbSNPEnsembl.1
Natural variantiVAR_07223957G → V in GSD7; Italian. 1 Publication1
Natural variantiVAR_006065100R → Q in GSD7; Swiss. 1 PublicationCorresponds to variant rs2228500dbSNPEnsembl.1
Natural variantiVAR_072240180S → C in GSD7; Italian. 1 Publication1
Natural variantiVAR_006066209G → D in GSD7; French Canadian. 1 PublicationCorresponds to variant rs767265360dbSNPEnsembl.1
Natural variantiVAR_072241309D → G in GSD7; Spanish; complete loss of enzyme activity. 1 Publication1
Natural variantiVAR_006067543D → A in GSD7; Italian. 1 PublicationCorresponds to variant rs121918194dbSNPEnsembl.1
Natural variantiVAR_072242591D → A in GSD7; Italian. 1 Publication1
Natural variantiVAR_006068686W → C in GSD7; Japanese. 1 PublicationCorresponds to variant rs121918196dbSNPEnsembl.1
Natural variantiVAR_006069696R → H in GSD7; Swiss. 1 PublicationCorresponds to variant rs41291971dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0461251M → MHKDEFHLKFFMCVIQSRQL VRTPQRTAGEASTSSMLIPK PPPKTDILKSLDTMDDPDTV GSIPVFKTEWIM in isoform 3. 1 Publication1
Alternative sequenceiVSP_004667282 – 312Missing in isoform 2. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59741
, M59720, M59721, M59722, M59723, M59724, M59725, M59726, M59727, M59728, M59729, M59730, M59731, M59732, M59733, M59734, M59735, M59736, M59737, M59738, M59739, M59740 Genomic DNA. Translation: AAA82938.1.
M26066 mRNA. Translation: AAA60068.1.
Y00698 mRNA. Translation: CAA68692.1.
AK126229 mRNA. Translation: BAC86498.1.
AC004801 Genomic DNA. No translation available.
AC074029 Genomic DNA. No translation available.
BC000534 mRNA. Translation: AAH00534.1.
BC012799 mRNA. Translation: AAH12799.1.
BC013298 mRNA. Translation: AAH13298.1.
BC021203 mRNA. Translation: AAH21203.1.
J05533 mRNA. Translation: AAA79220.1.
M24925 Genomic DNA. Translation: AAA36436.1.
CCDSiCCDS53786.1. [P08237-3]
CCDS8760.1. [P08237-1]
PIRiA91605. KIHUFM.
RefSeqiNP_000280.1. NM_000289.5. [P08237-1]
NP_001160158.1. NM_001166686.1. [P08237-3]
NP_001160159.1. NM_001166687.1. [P08237-1]
NP_001160160.1. NM_001166688.1. [P08237-1]
XP_005269034.1. XM_005268977.1. [P08237-3]
XP_005269035.1. XM_005268978.2. [P08237-3]
XP_005269036.1. XM_005268979.1. [P08237-3]
XP_011536790.1. XM_011538488.2. [P08237-1]
XP_016874957.1. XM_017019468.1. [P08237-3]
UniGeneiHs.75160.

Genome annotation databases

EnsembliENST00000312352; ENSP00000309438; ENSG00000152556. [P08237-1]
ENST00000340802; ENSP00000345771; ENSG00000152556. [P08237-3]
ENST00000359794; ENSP00000352842; ENSG00000152556. [P08237-1]
ENST00000547587; ENSP00000449426; ENSG00000152556. [P08237-1]
ENST00000551804; ENSP00000448177; ENSG00000152556. [P08237-2]
GeneIDi5213.
KEGGihsa:5213.
UCSCiuc001rrb.3. human. [P08237-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59741
, M59720, M59721, M59722, M59723, M59724, M59725, M59726, M59727, M59728, M59729, M59730, M59731, M59732, M59733, M59734, M59735, M59736, M59737, M59738, M59739, M59740 Genomic DNA. Translation: AAA82938.1.
M26066 mRNA. Translation: AAA60068.1.
Y00698 mRNA. Translation: CAA68692.1.
AK126229 mRNA. Translation: BAC86498.1.
AC004801 Genomic DNA. No translation available.
AC074029 Genomic DNA. No translation available.
BC000534 mRNA. Translation: AAH00534.1.
BC012799 mRNA. Translation: AAH12799.1.
BC013298 mRNA. Translation: AAH13298.1.
BC021203 mRNA. Translation: AAH21203.1.
J05533 mRNA. Translation: AAA79220.1.
M24925 Genomic DNA. Translation: AAA36436.1.
CCDSiCCDS53786.1. [P08237-3]
CCDS8760.1. [P08237-1]
PIRiA91605. KIHUFM.
RefSeqiNP_000280.1. NM_000289.5. [P08237-1]
NP_001160158.1. NM_001166686.1. [P08237-3]
NP_001160159.1. NM_001166687.1. [P08237-1]
NP_001160160.1. NM_001166688.1. [P08237-1]
XP_005269034.1. XM_005268977.1. [P08237-3]
XP_005269035.1. XM_005268978.2. [P08237-3]
XP_005269036.1. XM_005268979.1. [P08237-3]
XP_011536790.1. XM_011538488.2. [P08237-1]
XP_016874957.1. XM_017019468.1. [P08237-3]
UniGeneiHs.75160.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OMTX-ray6.00A1-780[»]
ProteinModelPortaliP08237.
SMRiP08237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111234. 62 interactors.
IntActiP08237. 23 interactors.
MINTiMINT-5005297.
STRINGi9606.ENSP00000345771.

Chemistry databases

BindingDBiP08237.
ChEMBLiCHEMBL3291.

PTM databases

iPTMnetiP08237.
PhosphoSitePlusiP08237.

Polymorphism and mutation databases

BioMutaiPFKM.
DMDMi125126.

2D gel databases

UCD-2DPAGEP08237.

Proteomic databases

EPDiP08237.
MaxQBiP08237.
PaxDbiP08237.
PeptideAtlasiP08237.
PRIDEiP08237.

Protocols and materials databases

DNASUi5213.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312352; ENSP00000309438; ENSG00000152556. [P08237-1]
ENST00000340802; ENSP00000345771; ENSG00000152556. [P08237-3]
ENST00000359794; ENSP00000352842; ENSG00000152556. [P08237-1]
ENST00000547587; ENSP00000449426; ENSG00000152556. [P08237-1]
ENST00000551804; ENSP00000448177; ENSG00000152556. [P08237-2]
GeneIDi5213.
KEGGihsa:5213.
UCSCiuc001rrb.3. human. [P08237-1]

Organism-specific databases

CTDi5213.
DisGeNETi5213.
GeneCardsiPFKM.
HGNCiHGNC:8877. PFKM.
HPAiHPA002117.
MalaCardsiPFKM.
MIMi232800. phenotype.
610681. gene.
neXtProtiNX_P08237.
OpenTargetsiENSG00000152556.
Orphaneti371. Glycogen storage disease due to muscle phosphofructokinase deficiency.
PharmGKBiPA33216.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiP08237.
KOiK00850.
OMAiIFIPEMP.
OrthoDBiEOG091G01YN.
PhylomeDBiP08237.
TreeFamiTF300411.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciMetaCyc:HS07832-MONOMER.
ZFISH:HS07832-MONOMER.
ReactomeiR-HSA-70171. Glycolysis.
SABIO-RKP08237.

Miscellaneous databases

ChiTaRSiPFKM. human.
GeneWikiiPFKM.
GenomeRNAii5213.
PMAP-CutDBP08237.
PROiP08237.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000152556.
CleanExiHS_PFKM.
ExpressionAtlasiP08237. baseline and differential.
GenevisibleiP08237. HS.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E. 1 hit.
InterProiIPR009161. 6-Pfructokinase_euk.
IPR022953. ATP_PFK.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPFKAM_HUMAN
AccessioniPrimary (citable) accession number: P08237
Secondary accession number(s): J3KNX3
, Q16814, Q16815, Q6ZTT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 192 of the entry and version 2 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

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.