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Q01813

- PFKAP_HUMAN

UniProt

Q01813 - PFKAP_HUMAN

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Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

PFKP

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Magnesium.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341ATP; via amide nitrogenUniRule annotation
Metal bindingi128 – 1281Magnesium; catalyticUniRule annotation
Active sitei175 – 1751Proton acceptorUniRule annotation
Binding sitei210 – 2101Substrate; shared with dimeric partnerUniRule annotation
Binding sitei273 – 2731SubstrateUniRule annotation
Binding sitei301 – 3011Substrate; shared with dimeric partnerUniRule annotation
Binding sitei481 – 4811Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei576 – 5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei639 – 6391Allosteric activator fructose 2,6-bisphosphateUniRule annotation
Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
Binding sitei744 – 7441Allosteric activator fructose 2,6-bisphosphateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi97 – 982ATPUniRule annotation
Nucleotide bindingi127 – 1304ATPUniRule annotation

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein complex binding Source: MGI

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. carbohydrate phosphorylation Source: GOC
  3. fructose 6-phosphate metabolic process Source: InterPro
  4. glucose metabolic process Source: Reactome
  5. glycolytic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
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.
ReactomeiREACT_1383. 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
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:8878. PFKP.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 784784ATP-dependent 6-phosphofructokinase, platelet typePRO_0000112024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei386 – 3861Phosphoserine5 Publications
Modified residuei395 – 3951N6-acetyllysine1 Publication
Modified residuei486 – 4861N6-acetyllysine1 Publication
Glycosylationi540 – 5401O-linked (GlcNAc)By similarity
Modified residuei651 – 6511Phosphotyrosine1 Publication
Modified residuei688 – 6881N6-acetyllysine1 Publication
Modified residuei783 – 7831Phosphoserine4 Publications

Post-translational modificationi

GlcNAcylation decreases enzyme activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ01813.
PaxDbiQ01813.
PeptideAtlasiQ01813.
PRIDEiQ01813.

PTM databases

PhosphoSiteiQ01813.

Expressioni

Gene expression databases

BgeeiQ01813.
CleanExiHS_PFKP.
ExpressionAtlasiQ01813. baseline and differential.
GenevestigatoriQ01813.

Organism-specific databases

HPAiHPA018257.

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.

Protein-protein interaction databases

BioGridi111235. 38 interactions.
IntActiQ01813. 17 interactions.
MINTiMINT-1159988.
STRINGi9606.ENSP00000370517.

Structurei

3D structure databases

ProteinModelPortaliQ01813.
SMRiQ01813. Positions 22-764.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 399399N-terminal catalytic PFK domain 1Add
BLAST
Regioni173 – 1753Substrate bindingUniRule annotation
Regioni217 – 2193Substrate bindingUniRule annotation
Regioni307 – 3104Substrate bindingUniRule annotation
Regioni400 – 41112Interdomain linkerAdd
BLAST
Regioni412 – 784373C-terminal regulatory PFK domain 2Add
BLAST
Regioni538 – 5425Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni583 – 5853Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
Regioni671 – 6744Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

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

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiQ01813.
KOiK00850.
OMAiSAKAMQW.
OrthoDBiEOG7ZSHV5.
PhylomeDBiQ01813.
TreeFamiTF300411.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti484 – 4852PG → IP(PubMed:1834056)Curated
Sequence conflicti498 – 4981Missing in AAA36435. (PubMed:1834056)Curated
Sequence conflicti655 – 6551S → P in BAG52577. (PubMed:14702039)Curated
Sequence conflicti699 – 6991A → E in AAA36435. (PubMed:1834056)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8787MDADD…SSILQ → MCGYERCRPCRGAHGYLRGG QGVLHLRGLPGHGGRRLKHR RGRLGECLQHPASGAVRGDW REKPGCWSHRFPCPGRHAL in isoform 2. 1 PublicationVSP_046416Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [Q01813-1]

Polymorphism databases

DMDMi1346355.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS55698.1. [Q01813-2 ]
CCDS7059.1. [Q01813-1 ]
PIRi JC2055.
RefSeqi NP_001229268.1. NM_001242339.1. [Q01813-2 ]
NP_002618.1. NM_002627.4. [Q01813-1 ]
UniGenei Hs.26010.

3D structure databases

ProteinModelPortali Q01813.
SMRi Q01813. Positions 22-764.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111235. 38 interactions.
IntActi Q01813. 17 interactions.
MINTi MINT-1159988.
STRINGi 9606.ENSP00000370517.

Chemistry

BindingDBi Q01813.

PTM databases

PhosphoSitei Q01813.

Polymorphism databases

DMDMi 1346355.

Proteomic databases

MaxQBi Q01813.
PaxDbi Q01813.
PeptideAtlasi Q01813.
PRIDEi Q01813.

Protocols and materials databases

DNASUi 5214.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381075 ; ENSP00000370465 ; ENSG00000067057 . [Q01813-2 ]
ENST00000381125 ; ENSP00000370517 ; ENSG00000067057 . [Q01813-1 ]
GeneIDi 5214.
KEGGi hsa:5214.
UCSCi uc001igp.3. human. [Q01813-1 ]

Organism-specific databases

CTDi 5214.
GeneCardsi GC10P003109.
HGNCi HGNC:8878. PFKP.
HPAi HPA018257.
MIMi 171840. gene.
neXtProti NX_Q01813.
PharmGKBi PA33217.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0205.
GeneTreei ENSGT00390000013209.
HOGENOMi HOG000200154.
HOVERGENi HBG000976.
InParanoidi Q01813.
KOi K00850.
OMAi SAKAMQW.
OrthoDBi EOG7ZSHV5.
PhylomeDBi Q01813.
TreeFami TF300411.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BioCyci MetaCyc:HS00894-MONOMER.
Reactomei REACT_1383. Glycolysis.
SABIO-RK Q01813.

Miscellaneous databases

ChiTaRSi PFKP. human.
GeneWikii PFKP.
GenomeRNAii 5214.
NextBioi 20168.
PROi Q01813.
SOURCEi Search...

Gene expression databases

Bgeei Q01813.
CleanExi HS_PFKP.
ExpressionAtlasi Q01813. baseline and differential.
Genevestigatori Q01813.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 2 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. 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. 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].

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: October 29, 2014
This is version 158 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3