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Q5NVN0

- KPYM_PONAB

UniProt

Q5NVN0 - KPYM_PONAB

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Protein
Pyruvate kinase PKM
Gene
PKM, PKM2
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation By similarity.

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium By similarity.
Potassium By similarity.

Enzyme regulationi

Allosterically activated by D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric form is inhibited by PML. Selective binding to tyrosine-phosphorylated peptides releases the allosteric activator FBP, leading to inhibition of PKM enzymatic activity, this diverts glucose metabolites from energy production to anabolic processes when cells are stimulated by certain growth factors. Glycolytic flux are highly dependent on de novo biosynthesis of serine and glycine, and serine is a natural ligand and allosteric activator By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Serine By similarity
Binding sitei73 – 731Substrate By similarity
Metal bindingi75 – 751Potassium By similarity
Metal bindingi77 – 771Potassium By similarity
Binding sitei106 – 1061Serine By similarity
Metal bindingi113 – 1131Potassium By similarity
Metal bindingi114 – 1141Potassium; via carbonyl oxygen By similarity
Sitei270 – 2701Transition state stabilizer By similarity
Metal bindingi272 – 2721Magnesium By similarity
Binding sitei295 – 2951Substrate; via amide nitrogen By similarity
Metal bindingi296 – 2961Magnesium By similarity
Binding sitei296 – 2961Substrate; via amide nitrogen By similarity
Binding sitei328 – 3281Substrate By similarity
Binding sitei464 – 4641Serine By similarity
Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric site By similarity
Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric site By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase PKM (EC:2.7.1.40)
Alternative name(s):
Pyruvate kinase muscle isozyme
Gene namesi
Name:PKM
Synonyms:PKM2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 531530Pyruvate kinase PKM
PRO_0000112090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei37 – 371Phosphoserine By similarity
Modified residuei62 – 621N6-acetyllysine By similarity
Modified residuei66 – 661N6-succinyllysine By similarity
Modified residuei89 – 891N6-acetyllysine By similarity
Modified residuei105 – 1051Phosphotyrosine By similarity
Modified residuei148 – 1481Phosphotyrosine By similarity
Modified residuei166 – 1661N6-acetyllysine; alternate By similarity
Modified residuei166 – 1661N6-succinyllysine; alternate By similarity
Modified residuei175 – 1751Phosphotyrosine By similarity
Modified residuei195 – 1951Phosphothreonine By similarity
Modified residuei266 – 2661N6-acetyllysine By similarity
Modified residuei270 – 2701N6-acetyllysine By similarity
Modified residuei305 – 3051N6-acetyllysine By similarity
Modified residuei322 – 3221N6-acetyllysine; alternate By similarity
Modified residuei322 – 3221N6-succinyllysine; alternate By similarity
Modified residuei475 – 4751N6-acetyllysine By similarity
Modified residuei498 – 4981N6-succinyllysine By similarity

Post-translational modificationi

ISGylated By similarity.
Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ5NVN0.

Interactioni

Subunit structurei

Monomer and homotetramer. Exists as a monomer in the absence of FBP, and reversibly associates to form a homotetramer in the presence of FBP. The monomeric form binds T3. Tetramer formation induces pyruvate kinase activity. Interacts with HERC1 POU5F1 and PML By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5NVN0.
SMRiQ5NVN0. Positions 13-531.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 531225Interaction with POU5F1 By similarity
Add
BLAST
Regioni389 – 43345Intersubunit contact
Add
BLAST
Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric site By similarity
Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric site By similarity

Sequence similaritiesi

Belongs to the pyruvate kinase family.

Phylogenomic databases

HOVERGENiHBG000941.
KOiK00873.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5NVN0-1 [UniParc]FASTAAdd to Basket

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MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT    50
IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS 100
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME 150
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLLTEVENG 200
GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD 250
VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE 300
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSGVAN 350
AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR 400
ASSHSTDLME AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI 450
IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR 500
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P 531
Length:531
Mass (Da):58,018
Last modified:January 23, 2007 - v3
Checksum:i86BDD4AEF68B5510
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531D → G in CAH93166. 1 Publication
Sequence conflicti329 – 3291Q → R in CAH93166. 1 Publication
Sequence conflicti347 – 3471G → D in CAH93166. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR861086 mRNA. Translation: CAH93166.1.
CR925988 mRNA. Translation: CAI29633.1.
RefSeqiNP_001127083.1. NM_001133611.1.

Genome annotation databases

GeneIDi100174114.
KEGGipon:100174114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR861086 mRNA. Translation: CAH93166.1 .
CR925988 mRNA. Translation: CAI29633.1 .
RefSeqi NP_001127083.1. NM_001133611.1.

3D structure databases

ProteinModelPortali Q5NVN0.
SMRi Q5NVN0. Positions 13-531.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5NVN0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100174114.
KEGGi pon:100174114.

Organism-specific databases

CTDi 396456.

Phylogenomic databases

HOVERGENi HBG000941.
KOi K00873.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiKPYM_PONAB
AccessioniPrimary (citable) accession number: Q5NVN0
Secondary accession number(s): Q5R500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 4 isozymes of pyruvate kinase in mammals (L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R isozymes are generated from the PKLR by differential splicing of RNA; the M1 and M2 forms are produced from the PKM gene by differential splicing. L type is major isozyme in the liver, R is found in red cells, M1 is the main form in muscle, heart and brain, and M2 is found in early fetal tissues as well as in most cancer cells.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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