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Q9WUA3

- PFKAP_MOUSE

UniProt

Q9WUA3 - PFKAP_MOUSE

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Protein
ATP-dependent 6-phosphofructokinase, platelet type
Gene
Pfkp, Pfkc
Organism
Mus musculus (Mouse)
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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATP; via amide nitrogen By similarity
Metal bindingi127 – 1271Magnesium; catalytic By similarity
Active sitei174 – 1741Proton acceptor By similarity
Binding sitei209 – 2091Substrate; shared with dimeric partner By similarity
Binding sitei272 – 2721Substrate By similarity
Binding sitei300 – 3001Substrate; shared with dimeric partner By similarity
Binding sitei480 – 4801Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei575 – 5751Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei638 – 6381Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei664 – 6641Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei743 – 7431Allosteric activator fructose 2,6-bisphosphate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 972ATP By similarity
Nucleotide bindingi126 – 1294ATP By similarity

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
Complete GO annotation...

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 6-phosphate metabolic process Source: InterPro
  3. glycolytic process Source: MGI
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

BRENDAi2.7.1.11. 3474.
SABIO-RKQ9WUA3.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, platelet type (EC:2.7.1.11)
Short name:
ATP-PFK
Short name:
PFK-P
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name:
PFK-C
Phosphohexokinase
Gene namesi
Name:Pfkp
Synonyms:Pfkc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1891833. Pfkp.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: MGI
  2. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 784784ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotation
PRO_0000112025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei394 – 3941N6-acetyllysine By similarity
Modified residuei485 – 4851N6-acetyllysine By similarity
Glycosylationi539 – 5391O-linked (GlcNAc) By similarity
Modified residuei650 – 6501Phosphotyrosine1 Publication
Modified residuei687 – 6871N6-acetyllysine1 Publication

Post-translational modificationi

GlcNAcylation decreases enzyme activity By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9WUA3.
PaxDbiQ9WUA3.
PRIDEiQ9WUA3.

PTM databases

PhosphoSiteiQ9WUA3.

Expressioni

Tissue specificityi

Expression is constant during tumor growth and markedly decreases when cell proliferation stops.1 Publication

Gene expression databases

ArrayExpressiQ9WUA3.
BgeeiQ9WUA3.
CleanExiMM_PFKP.
GenevestigatoriQ9WUA3.

Interactioni

Subunit structurei

Homo- and heterotetramers By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi207967. 3 interactions.
IntActiQ9WUA3. 5 interactions.
MINTiMINT-1676159.
STRINGi10090.ENSMUSP00000117030.

Structurei

3D structure databases

ProteinModelPortaliQ9WUA3.
SMRiQ9WUA3. Positions 21-764.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 398398N-terminal catalytic PFK domain 1UniRule annotation
Add
BLAST
Regioni172 – 1743Substrate binding By similarity
Regioni216 – 2183Substrate binding By similarity
Regioni306 – 3094Substrate binding By similarity
Regioni399 – 41012Interdomain linkerUniRule annotation
Add
BLAST
Regioni411 – 784374C-terminal regulatory PFK domain 2UniRule annotation
Add
BLAST
Regioni537 – 5415Allosteric activator fructose 2,6-bisphosphate binding By similarity
Regioni582 – 5843Allosteric activator fructose 2,6-bisphosphate binding By similarity
Regioni670 – 6734Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOVERGENiHBG000976.
InParanoidiQ9WUA3.
KOiK00850.
OMAiSAKAMQW.
OrthoDBiEOG7ZSHV5.
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: Q9WUA3-1) [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

MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI    50
YTGAKVYFIY EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF 100
RSREGRLKAA CNLARLGITN LCVIGGDGSL TGANLFRKEW SGLLEELARN 150
GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT DMTIGTDSAL HRIIEVVDAI 200
MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE SPPEEDWEEN 250
MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR 300
VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ 350
AVRLPLMECV QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL 400
PDEKIVKSNC NVAVINVGAP AAGMNAAVRS AVRVGIADGH KMFAIYDGFE 450
GFANGQIKEI GWADVGGWTG QGGSILGTKR TLPGKYLEKI AEQMHSHSIN 500
ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN NVPGSDFSIG 550
ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD 600
AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY 650
QLYSEEGKGV FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL 700
KGSQGTGKKF VSDDSICVLG ICKRDLLFQP VAELKKVTDF EHRIPKEQWW 750
LKLRPIMKIL AKYEASYDMS DSGKLESLQH HEEL 784
Length:784
Mass (Da):85,455
Last modified:November 1, 1999 - v1
Checksum:iE9C5AAABF26FCA65
GO
Isoform 2 (identifier: Q9WUA3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     457-496: IKEIGWADVG...LEKIAEQMHS → VSLPGVLGML...LVVGLYQILI
     497-784: Missing.

Note: May be due to intron retention. No experimental confirmation available.

Show »
Length:496
Mass (Da):53,682
Checksum:i22E3CB5080FD748C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041E → V in strain: NOD. 1 Publication
Natural varianti145 – 1451E → G in strain: C57BL/6J. 1 Publication
Natural varianti180 – 1801T → P in strain: C57BL/6. 1 Publication
Natural varianti261 – 2611R → Q in strain: LG/J and NOD. 2 Publications
Natural varianti292 – 2921V → M in strain: LG/J and NOD. 2 Publications
Natural varianti402 – 4021D → E in strain: C57BL/6J. 1 Publication
Natural varianti679 – 6791P → S in strain: C57BL/6J. 1 Publication
Natural varianti694 – 6941E → D in strain: LG/J and NOD. 2 Publications
Natural varianti696 – 6961I → F in strain: NOD. 1 Publication
Natural varianti777 – 7771S → P in strain: LG/J and NOD. 2 Publications
Natural varianti782 – 7821E → G in strain: LG/J and NOD. 2 Publications

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei457 – 49640IKEIG…EQMHS → VSLPGVLGMLKCYCIWGGHP PLTAPTKSRFLVVGLYQILI in isoform 2.
VSP_016664Add
BLAST
Alternative sequencei497 – 784288Missing in isoform 2.
VSP_016665Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y19008 mRNA. Translation: CAB64347.1.
AF123533 mRNA. Translation: AAD23571.1.
AF249893
, AF250369, AF250370, AF250371, AF250372, AF251021 Genomic DNA. Translation: AAF75700.1.
AY779275 mRNA. Translation: AAX11357.1.
AY779276 mRNA. Translation: AAX11358.1.
AK049841 mRNA. Translation: BAC33949.1.
AK078254 mRNA. Translation: BAC37195.1.
AK152670 mRNA. Translation: BAE31405.1.
AK154125 mRNA. Translation: BAE32390.1.
AK165422 mRNA. Translation: BAE38177.1.
AK165425 mRNA. Translation: BAE38180.1.
AK170624 mRNA. Translation: BAE41918.1.
AK171062 mRNA. Translation: BAE42221.1.
CT010268 mRNA. Translation: CAJ18476.1.
BC006926 mRNA. Translation: AAH06926.1.
CCDSiCCDS26230.1. [Q9WUA3-1]
RefSeqiNP_001278000.1. NM_001291071.1.
NP_062677.1. NM_019703.4. [Q9WUA3-1]
UniGeneiMm.273874.

Genome annotation databases

EnsembliENSMUST00000138703; ENSMUSP00000117030; ENSMUSG00000021196. [Q9WUA3-1]
GeneIDi56421.
KEGGimmu:56421.
UCSCiuc007pjz.1. mouse. [Q9WUA3-1]
uc007pkc.1. mouse. [Q9WUA3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y19008 mRNA. Translation: CAB64347.1 .
AF123533 mRNA. Translation: AAD23571.1 .
AF249893
, AF250369 , AF250370 , AF250371 , AF250372 , AF251021 Genomic DNA. Translation: AAF75700.1 .
AY779275 mRNA. Translation: AAX11357.1 .
AY779276 mRNA. Translation: AAX11358.1 .
AK049841 mRNA. Translation: BAC33949.1 .
AK078254 mRNA. Translation: BAC37195.1 .
AK152670 mRNA. Translation: BAE31405.1 .
AK154125 mRNA. Translation: BAE32390.1 .
AK165422 mRNA. Translation: BAE38177.1 .
AK165425 mRNA. Translation: BAE38180.1 .
AK170624 mRNA. Translation: BAE41918.1 .
AK171062 mRNA. Translation: BAE42221.1 .
CT010268 mRNA. Translation: CAJ18476.1 .
BC006926 mRNA. Translation: AAH06926.1 .
CCDSi CCDS26230.1. [Q9WUA3-1 ]
RefSeqi NP_001278000.1. NM_001291071.1.
NP_062677.1. NM_019703.4. [Q9WUA3-1 ]
UniGenei Mm.273874.

3D structure databases

ProteinModelPortali Q9WUA3.
SMRi Q9WUA3. Positions 21-764.
ModBasei Search...

Protein-protein interaction databases

BioGridi 207967. 3 interactions.
IntActi Q9WUA3. 5 interactions.
MINTi MINT-1676159.
STRINGi 10090.ENSMUSP00000117030.

PTM databases

PhosphoSitei Q9WUA3.

Proteomic databases

MaxQBi Q9WUA3.
PaxDbi Q9WUA3.
PRIDEi Q9WUA3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000138703 ; ENSMUSP00000117030 ; ENSMUSG00000021196 . [Q9WUA3-1 ]
GeneIDi 56421.
KEGGi mmu:56421.
UCSCi uc007pjz.1. mouse. [Q9WUA3-1 ]
uc007pkc.1. mouse. [Q9WUA3-2 ]

Organism-specific databases

CTDi 5214.
MGIi MGI:1891833. Pfkp.

Phylogenomic databases

eggNOGi COG0205.
GeneTreei ENSGT00390000013209.
HOVERGENi HBG000976.
InParanoidi Q9WUA3.
KOi K00850.
OMAi SAKAMQW.
OrthoDBi EOG7ZSHV5.
TreeFami TF300411.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
BRENDAi 2.7.1.11. 3474.
SABIO-RK Q9WUA3.

Miscellaneous databases

NextBioi 312572.
PROi Q9WUA3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9WUA3.
Bgeei Q9WUA3.
CleanExi MM_PFKP.
Genevestigatori Q9WUA3.

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. "Phosphofructokinase C isozyme from ascites tumor cells: cloning, expression, and properties."
    Sanchez-Martinez C., Estevez A.M., Aragon J.J.
    Biochem. Biophys. Res. Commun. 271:635-640(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Ascitic tumor.
  2. "Genomic organization, 5'flanking region and tissue-specific expression of mouse phosphofructokinase C gene."
    Gunasekera D., Kemp R.G.
    Gene 260:103-112(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PRO-180.
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x SM/J murine model of obesity."
    Ehrich T.H., Hrbek T., Kenney-Hunt J.P., Pletscher L.S., Wang B., Semenkovich C.F., Cheverud J.M.
    Diabetes 54:1863-1872(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-261; MET-292; ASP-694; PRO-777 AND GLY-782.
    Strain: LG/J and SM/J.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-104; GLY-145; GLN-261; MET-292; GLU-402; SER-679; ASP-694; PHE-696; PRO-777 AND GLY-782.
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Hippocampus, Kidney and Olfactory bulb.
  5. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "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).
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPFKAP_MOUSE
AccessioniPrimary (citable) accession number: Q9WUA3
Secondary accession number(s): Q3TNA9
, Q3U4P1, Q3U7G4, Q4KUG1, Q543K8, Q8C5I6, Q9JI86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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