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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

PFKP

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.UniRule annotation

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, platelet type (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM)
  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 sitei34ATP; via amide nitrogenUniRule annotation1
Metal bindingi128Magnesium; catalyticUniRule annotation1
Active sitei175Proton acceptorUniRule annotation1
Binding sitei210Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei273SubstrateUniRule annotation1
Binding sitei301Substrate; shared with dimeric partnerUniRule annotation1
Binding sitei481Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei576Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei639Allosteric activator fructose 2,6-bisphosphateUniRule annotation1
Binding sitei665Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei744Allosteric activator fructose 2,6-bisphosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi97 – 98ATPUniRule annotation2
Nucleotide bindingi127 – 130ATPUniRule annotation4

GO - Molecular functioni

  • 6-phosphofructokinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein complex binding Source: MGI

GO - Biological processi

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:HS00894-MONOMER.
ZFISH:HS00894-MONOMER.
ReactomeiR-HSA-70171. Glycolysis.
SABIO-RKQ01813.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotation (EC:2.7.1.11UniRule annotation)
Short name:
ATP-PFKUniRule annotation
Short name:
PFK-P
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name:
PFK-C
PhosphohexokinaseUniRule annotation
Gene namesi
Name:PFKP
Synonyms:PFKF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:8878. PFKP.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi5214.
OpenTargetsiENSG00000067057.
PharmGKBiPA33217.

Polymorphism and mutation databases

BioMutaiPFKP.
DMDMi1346355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120241 – 784ATP-dependent 6-phosphofructokinase, platelet typeAdd BLAST784

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei6PhosphoserineCombined sources1
Modified residuei12PhosphoserineBy similarity1
Modified residuei21PhosphoserineCombined sources1
Modified residuei142PhosphoserineBy similarity1
Modified residuei386PhosphoserineCombined sources1
Modified residuei395N6-acetyllysineCombined sources1
Modified residuei486N6-acetyllysineCombined sources1
Glycosylationi540O-linked (GlcNAc)By similarity1
Modified residuei651PhosphotyrosineCombined sources1
Modified residuei688N6-acetyllysineCombined sources1
Modified residuei783PhosphoserineCombined sources1

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ01813.
MaxQBiQ01813.
PaxDbiQ01813.
PeptideAtlasiQ01813.
PRIDEiQ01813.

PTM databases

iPTMnetiQ01813.
PhosphoSitePlusiQ01813.
SwissPalmiQ01813.

Expressioni

Gene expression databases

BgeeiENSG00000067057.
CleanExiHS_PFKP.
ExpressionAtlasiQ01813. baseline and differential.
GenevisibleiQ01813. HS.

Organism-specific databases

HPAiHPA018257.
HPA056484.

Interactioni

Subunit structurei

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.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein complex binding Source: MGI

Protein-protein interaction databases

BioGridi111235. 75 interactors.
DIPiDIP-45850N.
IntActiQ01813. 31 interactors.
MINTiMINT-1159988.
STRINGi9606.ENSP00000370517.

Structurei

Secondary structure

1784
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni17 – 19Combined sources3
Beta strandi26 – 31Combined sources6
Helixi39 – 53Combined sources15
Beta strandi56 – 60Combined sources5
Helixi63 – 69Combined sources7
Helixi71 – 73Combined sources3
Beta strandi74 – 76Combined sources3
Helixi79 – 81Combined sources3
Turni83 – 87Combined sources5
Beta strandi88 – 90Combined sources3
Helixi100 – 102Combined sources3
Helixi104 – 116Combined sources13
Beta strandi119 – 126Combined sources8
Helixi128 – 139Combined sources12
Helixi140 – 142Combined sources3
Helixi143 – 149Combined sources7
Beta strandi150 – 152Combined sources3
Helixi155 – 160Combined sources6
Turni161 – 163Combined sources3
Beta strandi166 – 171Combined sources6
Beta strandi179 – 183Combined sources5
Helixi187 – 208Combined sources22
Beta strandi210 – 217Combined sources8
Helixi223 – 232Combined sources10
Beta strandi235 – 238Combined sources4
Beta strandi240 – 242Combined sources3
Helixi248 – 261Combined sources14
Beta strandi266 – 272Combined sources7
Beta strandi278 – 280Combined sources3
Helixi285 – 296Combined sources12
Beta strandi300 – 304Combined sources5
Helixi306 – 310Combined sources5
Helixi316 – 335Combined sources20
Beta strandi338 – 340Combined sources3
Beta strandi343 – 348Combined sources6
Beta strandi351 – 356Combined sources6
Helixi357 – 373Combined sources17
Helixi376 – 383Combined sources8
Helixi385 – 398Combined sources14
Helixi403 – 405Combined sources3
Beta strandi412 – 420Combined sources9
Helixi425 – 438Combined sources14
Beta strandi442 – 446Combined sources5
Helixi449 – 454Combined sources6
Beta strandi458 – 460Combined sources3
Turni463 – 468Combined sources6
Beta strandi474 – 477Combined sources4
Helixi484 – 487Combined sources4
Helixi488 – 497Combined sources10
Beta strandi500 – 508Combined sources9
Helixi509 – 520Combined sources12
Turni521 – 524Combined sources4
Helixi526 – 528Combined sources3
Beta strandi532 – 540Combined sources9
Helixi552 – 568Combined sources17
Beta strandi570 – 573Combined sources4
Beta strandi576 – 582Combined sources7
Helixi589 – 598Combined sources10
Beta strandi601 – 604Combined sources4
Beta strandi606 – 608Combined sources3
Helixi612 – 625Combined sources14
Beta strandi632 – 638Combined sources7
Beta strandi643 – 645Combined sources3
Helixi647 – 657Combined sources11
Turni658 – 661Combined sources4
Beta strandi663 – 668Combined sources6
Helixi670 – 673Combined sources4
Helixi680 – 702Combined sources23
Helixi714 – 716Combined sources3
Beta strandi717 – 723Combined sources7
Beta strandi726 – 731Combined sources6
Helixi732 – 735Combined sources4
Helixi736 – 738Combined sources3
Turni741 – 744Combined sources4
Beta strandi745 – 748Combined sources4
Helixi750 – 755Combined sources6
Helixi756 – 761Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RH3X-ray3.02A/B/C/D26-762[»]
4U1RX-ray2.80A/B/C/D26-762[»]
4WL0X-ray2.89A/B/C/D26-762[»]
4XYJX-ray3.10A/B/C/D/E/F/G/H1-784[»]
4XYKX-ray3.40A/B/C/D1-784[»]
4XZ2X-ray2.67A/B/C/D26-762[»]
ProteinModelPortaliQ01813.
SMRiQ01813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 399N-terminal catalytic PFK domain 1Add BLAST399
Regioni173 – 175Substrate bindingUniRule annotation3
Regioni217 – 219Substrate bindingUniRule annotation3
Regioni307 – 310Substrate bindingUniRule annotation4
Regioni400 – 411Interdomain linkerAdd BLAST12
Regioni412 – 784C-terminal regulatory PFK domain 2Add BLAST373
Regioni538 – 542Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation5
Regioni583 – 585Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation3
Regioni671 – 674Allosteric 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.
InParanoidiQ01813.
KOiK00850.
OMAiKMCQKLS.
OrthoDBiEOG091G01YN.
PhylomeDBiQ01813.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q01813-1) [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
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG
60 70 80 90 100
IYVGAKVYFI YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA
110 120 130 140 150
FRTREGRLKA ACNLLQRGIT NLCVIGGDGS LTGANLFRKE WSGLLEELAR
160 170 180 190 200
NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG TDMTIGTDSA LHRIIEVVDA
210 220 230 240 250
IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE
260 270 280 290 300
QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT
310 320 330 340 350
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN
360 370 380 390 400
HAVRLPLMEC VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK
410 420 430 440 450
LPDDQIPKTN CNVAVINVGA PAAGMNAAVR SAVRVGIADG HRMLAIYDGF
460 470 480 490 500
DGFAKGQIKE IGWTDVGGWT GQGGSILGTK RVLPGKYLEE IATQMRTHSI
510 520 530 540 550
NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS NNVPGSDFSI
560 570 580 590 600
GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
610 620 630 640 650
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI
660 670 680 690 700
YQLYSEEGKG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK
710 720 730 740 750
LKEARGRGKK FTTDDSICVL GISKRNVIFQ PVAELKKQTD FEHRIPKEQW
760 770 780
WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ PWSV
Length:784
Mass (Da):85,596
Last modified:February 1, 1996 - v2
Checksum:i22522E77E9AF80F6
GO
Isoform 2 (identifier: Q01813-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: MDADDSRAPK...DWESVSSILQ → MCGYERCRPC...RFPCPGRHAL

Note: No experimental confirmation available.
Show »
Length:776
Mass (Da):85,316
Checksum:i649595FEDE1A9187
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti484 – 485PG → IP (PubMed:1834056).Curated2
Sequence conflicti498Missing in AAA36435 (PubMed:1834056).Curated1
Sequence conflicti655S → P in BAG52577 (PubMed:14702039).Curated1
Sequence conflicti699A → E in AAA36435 (PubMed:1834056).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0464161 – 87MDADD…SSILQ → MCGYERCRPCRGAHGYLRGG QGVLHLRGLPGHGGRRLKHR RGRLGECLQHPASGAVRGDW REKPGCWSHRFPCPGRHAL in isoform 2. 1 PublicationAdd BLAST87

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55698.1. [Q01813-2]
CCDS7059.1. [Q01813-1]
PIRiJC2055.
RefSeqiNP_001229268.1. NM_001242339.1. [Q01813-2]
NP_002618.1. NM_002627.4. [Q01813-1]
UniGeneiHs.26010.

Genome annotation databases

EnsembliENST00000381075; ENSP00000370465; ENSG00000067057. [Q01813-2]
ENST00000381125; ENSP00000370517; ENSG00000067057. [Q01813-1]
GeneIDi5214.
KEGGihsa:5214.
UCSCiuc001igp.4. human. [Q01813-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55698.1. [Q01813-2]
CCDS7059.1. [Q01813-1]
PIRiJC2055.
RefSeqiNP_001229268.1. NM_001242339.1. [Q01813-2]
NP_002618.1. NM_002627.4. [Q01813-1]
UniGeneiHs.26010.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RH3X-ray3.02A/B/C/D26-762[»]
4U1RX-ray2.80A/B/C/D26-762[»]
4WL0X-ray2.89A/B/C/D26-762[»]
4XYJX-ray3.10A/B/C/D/E/F/G/H1-784[»]
4XYKX-ray3.40A/B/C/D1-784[»]
4XZ2X-ray2.67A/B/C/D26-762[»]
ProteinModelPortaliQ01813.
SMRiQ01813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111235. 75 interactors.
DIPiDIP-45850N.
IntActiQ01813. 31 interactors.
MINTiMINT-1159988.
STRINGi9606.ENSP00000370517.

PTM databases

iPTMnetiQ01813.
PhosphoSitePlusiQ01813.
SwissPalmiQ01813.

Polymorphism and mutation databases

BioMutaiPFKP.
DMDMi1346355.

Proteomic databases

EPDiQ01813.
MaxQBiQ01813.
PaxDbiQ01813.
PeptideAtlasiQ01813.
PRIDEiQ01813.

Protocols and materials databases

DNASUi5214.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381075; ENSP00000370465; ENSG00000067057. [Q01813-2]
ENST00000381125; ENSP00000370517; ENSG00000067057. [Q01813-1]
GeneIDi5214.
KEGGihsa:5214.
UCSCiuc001igp.4. human. [Q01813-1]

Organism-specific databases

CTDi5214.
DisGeNETi5214.
GeneCardsiPFKP.
HGNCiHGNC:8878. PFKP.
HPAiHPA018257.
HPA056484.
MIMi171840. gene.
neXtProtiNX_Q01813.
OpenTargetsiENSG00000067057.
PharmGKBiPA33217.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2440. Eukaryota.
COG0205. LUCA.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiQ01813.
KOiK00850.
OMAiKMCQKLS.
OrthoDBiEOG091G01YN.
PhylomeDBiQ01813.
TreeFamiTF300411.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00182.
BioCyciMetaCyc:HS00894-MONOMER.
ZFISH:HS00894-MONOMER.
ReactomeiR-HSA-70171. Glycolysis.
SABIO-RKQ01813.

Miscellaneous databases

ChiTaRSiPFKP. human.
GeneWikiiPFKP.
GenomeRNAii5214.
PROiQ01813.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000067057.
CleanExiHS_PFKP.
ExpressionAtlasiQ01813. baseline and differential.
GenevisibleiQ01813. 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 nameiPFKAP_HUMAN
AccessioniPrimary (citable) accession number: Q01813
Secondary accession number(s): B3KS15, Q5VSR7, Q5VSR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 180 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.