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Q5NVN0

- KPYM_PONAB

UniProt

Q5NVN0 - KPYM_PONAB

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Protein

Pyruvate kinase PKM

Gene

PKM

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 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).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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701SerineBy similarity
Binding sitei73 – 731SubstrateBy similarity
Metal bindingi75 – 751PotassiumBy similarity
Metal bindingi77 – 771PotassiumBy similarity
Binding sitei106 – 1061SerineBy similarity
Metal bindingi113 – 1131PotassiumBy similarity
Metal bindingi114 – 1141Potassium; via carbonyl oxygenBy similarity
Sitei270 – 2701Transition state stabilizerBy similarity
Metal bindingi272 – 2721MagnesiumBy similarity
Binding sitei295 – 2951Substrate; via amide nitrogenBy similarity
Metal bindingi296 – 2961MagnesiumBy similarity
Binding sitei296 – 2961Substrate; via amide nitrogenBy similarity
Binding sitei328 – 3281SubstrateBy similarity
Binding sitei464 – 4641SerineBy similarity
Binding sitei482 – 4821D-fructose 1,6-bisphosphate; part of allosteric siteBy similarity
Binding sitei489 – 4891D-fructose 1,6-bisphosphate; part of allosteric siteBy 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-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 531530Pyruvate kinase PKMPRO_0000112090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei62 – 621N6-acetyllysineBy similarity
Modified residuei66 – 661N6-succinyllysineBy similarity
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei105 – 1051PhosphotyrosineBy similarity
Modified residuei148 – 1481PhosphotyrosineBy similarity
Modified residuei166 – 1661N6-acetyllysine; alternateBy similarity
Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
Modified residuei175 – 1751PhosphotyrosineBy similarity
Modified residuei195 – 1951PhosphothreonineBy similarity
Modified residuei266 – 2661N6-acetyllysineBy similarity
Modified residuei270 – 2701N6-acetyllysineBy similarity
Modified residuei305 – 3051N6-acetyllysineBy similarity
Modified residuei322 – 3221N6-acetyllysine; alternateBy similarity
Modified residuei322 – 3221N6-succinyllysine; alternateBy similarity
Modified residuei475 – 4751N6-acetyllysineBy similarity
Modified residuei498 – 4981N6-succinyllysineBy 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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5NVN0.
SMRiQ5NVN0. Positions 13-531.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 531225Interaction with POU5F1By similarityAdd
BLAST
Regioni389 – 43345Intersubunit contactAdd
BLAST
Regioni432 – 4376D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity
Regioni514 – 5218D-fructose 1,6-bisphosphate binding; part of allosteric siteBy similarity

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

HOVERGENiHBG000941.
InParanoidiQ5NVN0.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT
60 70 80 90 100
IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS
110 120 130 140 150
DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME
160 170 180 190 200
KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLLTEVENG
210 220 230 240 250
GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD
260 270 280 290 300
VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
310 320 330 340 350
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSGVAN
360 370 380 390 400
AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR
410 420 430 440 450
ASSHSTDLME AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI
460 470 480 490 500
IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR
510 520 530
GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
Length:531
Mass (Da):58,018
Last modified:January 23, 2007 - v3
Checksum:i86BDD4AEF68B5510
GO

Experimental Info

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

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.
InParanoidi Q5NVN0.
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: October 29, 2014
This is version 75 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