P08237 · PFKAM_HUMAN
- ProteinATP-dependent 6-phosphofructokinase, muscle type
- GenePFKM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids780 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Catalytic activity
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H+
Cofactor
Activity regulation
Pathway
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 25 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 88-89 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 118-121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 119 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 164-166 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 166 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 201 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 208-210 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 264 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 292 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 298-301 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 471 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 528-532 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TVSNN | ||||||
Binding site | 566 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 573-575 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 629 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 655 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 661-664 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 735 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent 6-phosphofructokinase, muscle type
- EC number
- Short namesATP-PFK ; PFK-M
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08237
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Glycogen storage disease 7 (GSD7)
- Note
- 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 alsoMIM:232800
Natural variants in GSD7
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_006063 | 39 | R>L | in GSD7; Ashkenazi; dbSNP:rs121918193 | |
VAR_006064 | 39 | R>P | in GSD7; Italian; dbSNP:rs121918193 | |
VAR_072239 | 57 | G>V | in GSD7; Italian | |
VAR_072240 | 180 | S>C | in GSD7; Italian | |
VAR_006066 | 209 | G>D | in GSD7; loss of activity shown by complementation assays in yeast; dbSNP:rs767265360 | |
VAR_072241 | 309 | D>G | in GSD7; Spanish; complete loss of enzyme activity; dbSNP:rs1169383137 | |
VAR_006067 | 543 | D>A | in GSD7; Italian; dbSNP:rs121918194 | |
VAR_072242 | 591 | D>A | in GSD7; Italian | |
VAR_006068 | 686 | W>C | in GSD7; Japanese; dbSNP:rs121918196 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_006063 | 39 | in GSD7; Ashkenazi; dbSNP:rs121918193 | |||
Sequence: R → L | ||||||
Natural variant | VAR_006064 | 39 | in GSD7; Italian; dbSNP:rs121918193 | |||
Sequence: R → P | ||||||
Natural variant | VAR_072239 | 57 | in GSD7; Italian | |||
Sequence: G → V | ||||||
Natural variant | VAR_006065 | 100 | in dbSNP:rs2228500 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_072240 | 180 | in GSD7; Italian | |||
Sequence: S → C | ||||||
Natural variant | VAR_006066 | 209 | in GSD7; loss of activity shown by complementation assays in yeast; dbSNP:rs767265360 | |||
Sequence: G → D | ||||||
Natural variant | VAR_072241 | 309 | in GSD7; Spanish; complete loss of enzyme activity; dbSNP:rs1169383137 | |||
Sequence: D → G | ||||||
Natural variant | VAR_006067 | 543 | in GSD7; Italian; dbSNP:rs121918194 | |||
Sequence: D → A | ||||||
Natural variant | VAR_072242 | 591 | in GSD7; Italian | |||
Sequence: D → A | ||||||
Natural variant | VAR_006068 | 686 | in GSD7; Japanese; dbSNP:rs121918196 | |||
Sequence: W → C | ||||||
Natural variant | VAR_006069 | 696 | in dbSNP:rs41291971 | |||
Sequence: R → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 783 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylthreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000112016 | 2-780 | UniProt | ATP-dependent 6-phosphofructokinase, muscle type | |||
Sequence: THEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 133 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 377 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 398 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 477 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 530 | UniProt | O-linked (GlcNAc) serine | ||||
Sequence: S | |||||||
Modified residue | 557 | UniProt | N6-(2-hydroxyisobutyryl)lysine | ||||
Sequence: K | |||||||
Modified residue | 667 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 667 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 775 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Phosphofructokinase (PFK) enzyme functions as a tetramer composed of different combinations of 3 types of subunits, called PFKM (where M stands for Muscle), PFKL (Liver) and PFKP (Platelet). The composition of the PFK tetramer differs according to the tissue type it is present in. In muscles, it is composed of 4 PFKM subunits (also called M4). In the liver, the predominant form is a tetramer of PFKL subunits (L4). In erythrocytes, both PFKM and PFKL subunits randomly tetramerize to form M4, L4 and other combinations (ML3, M2L2, M3L). The kinetic and regulatory properties of the tetrameric enzyme are dependent on the subunit composition, hence can vary across tissues (Probable). Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific region) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08237 | PFKL P17858 | 6 | EBI-514788, EBI-487243 | |
BINARY | P08237 | PFKM P08237 | 3 | EBI-514788, EBI-514788 | |
BINARY | P08237 | PFKP Q01813 | 2 | EBI-514788, EBI-359022 | |
BINARY | P08237 | SIAH1 Q8IUQ4 | 3 | EBI-514788, EBI-747107 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-390 | N-terminal catalytic PFK domain 1 | ||||
Sequence: THEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKKFDEALKLRGRSFMNNWEVYKLLAH | ||||||
Region | 391-401 | Interdomain linker | ||||
Sequence: VRPPVSKSGSH | ||||||
Region | 402-780 | C-terminal regulatory PFK domain 2 | ||||
Sequence: TVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P08237-1
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.
- Name1
- Length780
- Mass (Da)85,183
- Last updated2007-01-23 v2
- Checksum769A2C01F97D1122
P08237-2
- Name2
- Differences from canonical
- 282-312: Missing
P08237-3
- Name3
- Differences from canonical
- 1-1: M → MHKDEFHLKFFMCVIQSRQLVRTPQRTAGEASTSSMLIPKPPPKTDILKSLDTMDDPDTVGSIPVFKTEWIM
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y891 | A0A2R8Y891_HUMAN | PFKM | 883 | ||
H0YHB8 | H0YHB8_HUMAN | PFKM | 41 | ||
F8VZI0 | F8VZI0_HUMAN | PFKM | 694 | ||
F8VZQ1 | F8VZQ1_HUMAN | PFKM | 161 | ||
F8VZ53 | F8VZ53_HUMAN | PFKM | 59 | ||
F8VX13 | F8VX13_HUMAN | PFKM | 156 | ||
F8VYK8 | F8VYK8_HUMAN | PFKM | 149 | ||
F8VVE3 | F8VVE3_HUMAN | PFKM | 165 | ||
F8VW30 | F8VW30_HUMAN | PFKM | 116 | ||
F8VUB8 | F8VUB8_HUMAN | PFKM | 141 | ||
F8VTQ3 | F8VTQ3_HUMAN | PFKM | 854 | ||
F8VTT5 | F8VTT5_HUMAN | PFKM | 176 | ||
F8VSF7 | F8VSF7_HUMAN | PFKM | 102 | ||
F8VSF5 | F8VSF5_HUMAN | PFKM | 73 | ||
F8VP00 | F8VP00_HUMAN | PFKM | 176 | ||
F8VNZ1 | F8VNZ1_HUMAN | PFKM | 125 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046125 | 1 | in isoform 3 | |||
Sequence: M → MHKDEFHLKFFMCVIQSRQLVRTPQRTAGEASTSSMLIPKPPPKTDILKSLDTMDDPDTVGSIPVFKTEWIM | ||||||
Sequence conflict | 2 | In isoform P08237-3; in Ref. 4; BAC86498 | ||||
Sequence: H → L | ||||||
Alternative sequence | VSP_004667 | 282-312 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 670 | in Ref. 4; BAC86498 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M59741 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59720 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59721 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59722 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59723 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59724 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59725 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59726 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59727 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59728 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59729 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59730 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59731 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59732 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59733 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59734 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59735 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59736 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59737 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59738 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59739 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M59740 EMBL· GenBank· DDBJ | AAA82938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M26066 EMBL· GenBank· DDBJ | AAA60068.1 EMBL· GenBank· DDBJ | mRNA | ||
Y00698 EMBL· GenBank· DDBJ | CAA68692.1 EMBL· GenBank· DDBJ | mRNA | ||
AK126229 EMBL· GenBank· DDBJ | BAC86498.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004801 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC074029 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000534 EMBL· GenBank· DDBJ | AAH00534.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012799 EMBL· GenBank· DDBJ | AAH12799.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013298 EMBL· GenBank· DDBJ | AAH13298.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021203 EMBL· GenBank· DDBJ | AAH21203.1 EMBL· GenBank· DDBJ | mRNA | ||
J05533 EMBL· GenBank· DDBJ | AAA79220.1 EMBL· GenBank· DDBJ | mRNA | ||
M24925 EMBL· GenBank· DDBJ | AAA36436.1 EMBL· GenBank· DDBJ | Genomic DNA |