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P00558

- PGK1_HUMAN

UniProt

P00558 - PGK1_HUMAN

Protein

Phosphoglycerate kinase 1

Gene

PGK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).

    Catalytic activityi

    ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391Substrate
    Binding sitei123 – 1231Substrate
    Binding sitei171 – 1711Substrate
    Binding sitei220 – 2201ATP
    Binding sitei313 – 3131ATP; via carbonyl oxygen
    Binding sitei344 – 3441ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi373 – 3764ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. phosphoglycerate kinase activity Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. epithelial cell differentiation Source: UniProt
    3. gluconeogenesis Source: Reactome
    4. glucose metabolic process Source: Reactome
    5. glycolytic process Source: Reactome
    6. phosphorylation Source: UniProtKB
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02359-MONOMER.
    BRENDAi2.7.2.3. 2681.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RKP00558.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase 1 (EC:2.7.2.3)
    Alternative name(s):
    Cell migration-inducing gene 10 protein
    Primer recognition protein 2
    Short name:
    PRP 2
    Gene namesi
    Name:PGK1
    Synonyms:PGKA
    ORF Names:MIG10, OK/SW-cl.110
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8896. PGK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653]: A condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881L → P in PGK1D; with congenital non-spherocytic anemia; variant Matsue. 1 Publication
    VAR_006076
    Natural varianti158 – 1581G → V in PGK1D; with chronic hemolytic anemia; variant Shizuoka. 1 Publication
    VAR_006077
    Natural varianti164 – 1641D → V in PGK1D; with chronic hemolytic anemia and mental retardation; variant Amiens. 1 Publication
    VAR_006078
    Natural varianti191 – 1911Missing in PGK1D; with chronic hemolytic anemia; variant Alabama. 1 Publication
    VAR_006079
    Natural varianti206 – 2061R → P in PGK1D; with chronic hemolytic anemia; variant Uppsala. 1 Publication
    VAR_006080
    Natural varianti252 – 2521E → A in PGK1D; with chronic hemolytic anemia; variant Antwerp. 1 Publication
    VAR_006081
    Natural varianti266 – 2661V → M in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo. 1 Publication
    VAR_006082
    Natural varianti285 – 2851D → V in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity. 1 Publication
    VAR_006084
    Natural varianti315 – 3151D → N in PGK1D; with rhabdomyolysis; variant Creteil. 1 Publication
    VAR_006085
    Natural varianti316 – 3161C → R in PGK1D; with chronic hemolytic anemia; variant Michigan. 1 Publication
    VAR_006086

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi300653. phenotype.
    Orphaneti713. Glycogen storage disease due to phosphoglycerate kinase 1 deficiency.
    PharmGKBiPA33234.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 417416Phosphoglycerate kinase 1PRO_0000145831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei6 – 61N6-succinyllysineBy similarity
    Modified residuei11 – 111N6-acetyllysine1 Publication
    Modified residuei48 – 481N6-acetyllysine; alternate1 Publication
    Modified residuei48 – 481N6-succinyllysine; alternateBy similarity
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Modified residuei76 – 761PhosphotyrosineBy similarity
    Modified residuei86 – 861N6-acetyllysine1 Publication
    Modified residuei91 – 911N6-acetyllysineBy similarity
    Modified residuei97 – 971N6-acetyllysine1 Publication
    Modified residuei131 – 1311N6-acetyllysine; alternate1 Publication
    Modified residuei131 – 1311N6-malonyllysine; alternate1 Publication
    Modified residuei146 – 1461N6-acetyllysine1 Publication
    Modified residuei191 – 1911N6-succinyllysineBy similarity
    Modified residuei196 – 1961Phosphotyrosine1 Publication
    Modified residuei199 – 1991N6-acetyllysine1 Publication
    Modified residuei203 – 2031Phosphoserine3 Publications
    Modified residuei267 – 2671N6-acetyllysine1 Publication
    Modified residuei291 – 2911N6-acetyllysine1 Publication
    Modified residuei361 – 3611N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP00558.
    PaxDbiP00558.
    PeptideAtlasiP00558.
    PRIDEiP00558.

    2D gel databases

    DOSAC-COBS-2DPAGEP00558.
    OGPiP00558.
    REPRODUCTION-2DPAGEIPI00169383.
    P00558.
    UCD-2DPAGEP00558.

    PTM databases

    PhosphoSiteiP00558.

    Expressioni

    Gene expression databases

    ArrayExpressiP00558.
    BgeeiP00558.
    CleanExiHS_PGK1.
    GenevestigatoriP00558.

    Organism-specific databases

    HPAiCAB010065.
    HPA045385.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GAPDHP044062EBI-709599,EBI-354056

    Protein-protein interaction databases

    BioGridi111251. 51 interactions.
    IntActiP00558. 29 interactions.
    MINTiMINT-1131047.
    STRINGi9606.ENSP00000362413.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi9 – 113
    Beta strandi18 – 225
    Beta strandi29 – 324
    Beta strandi33 – 353
    Helixi38 – 5215
    Beta strandi56 – 616
    Helixi73 – 764
    Helixi79 – 8911
    Beta strandi94 – 974
    Beta strandi99 – 1013
    Helixi102 – 1098
    Beta strandi115 – 1184
    Helixi122 – 1243
    Turni126 – 1305
    Beta strandi131 – 1333
    Beta strandi135 – 1373
    Beta strandi139 – 1413
    Helixi144 – 15613
    Beta strandi159 – 1635
    Helixi166 – 1683
    Helixi174 – 1774
    Beta strandi184 – 1863
    Helixi188 – 20215
    Beta strandi206 – 2127
    Helixi217 – 2204
    Helixi221 – 2233
    Helixi224 – 2274
    Turni228 – 2303
    Beta strandi232 – 2365
    Helixi238 – 2403
    Helixi241 – 2499
    Helixi260 – 2634
    Helixi266 – 27510
    Beta strandi279 – 2813
    Beta strandi285 – 2939
    Beta strandi298 – 3025
    Turni303 – 3053
    Beta strandi312 – 3165
    Helixi318 – 33013
    Beta strandi332 – 3387
    Helixi346 – 3483
    Helixi350 – 36415
    Beta strandi368 – 3736
    Helixi376 – 3827
    Beta strandi388 – 3947
    Helixi397 – 4048
    Helixi409 – 4124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WZBX-ray1.47A2-417[»]
    2WZCX-ray1.50A2-417[»]
    2WZDX-ray1.56A1-417[»]
    2X13X-ray1.74A2-417[»]
    2X14X-ray1.90A2-417[»]
    2X15X-ray2.10A2-417[»]
    2XE6X-ray1.74A1-417[»]
    2XE7X-ray2.20A1-417[»]
    2XE8X-ray1.79A1-417[»]
    2Y3IX-ray2.90A/D1-416[»]
    2YBEX-ray2.00A1-417[»]
    2ZGVX-ray2.00A1-417[»]
    3C39X-ray1.85A/B1-417[»]
    3C3AX-ray2.30A/B1-417[»]
    3C3BX-ray1.80A/B1-417[»]
    3C3CX-ray2.40A/B1-417[»]
    3ZOZX-ray1.95A1-417[»]
    4AXXX-ray1.74A1-417[»]
    ProteinModelPortaliP00558.
    SMRiP00558. Positions 5-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00558.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 263Substrate binding
    Regioni63 – 664Substrate binding

    Sequence similaritiesi

    Belongs to the phosphoglycerate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0126.
    HOGENOMiHOG000227107.
    HOVERGENiHBG008177.
    InParanoidiP00558.
    KOiK00927.
    OMAiASCCAKW.
    PhylomeDBiP00558.
    TreeFamiTF300489.

    Family and domain databases

    Gene3Di3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPiMF_00145. Phosphoglyc_kinase.
    InterProiIPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view]
    PANTHERiPTHR11406. PTHR11406. 1 hit.
    PfamiPF00162. PGK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000724. Pgk. 1 hit.
    PRINTSiPR00477. PHGLYCKINASE.
    SUPFAMiSSF53748. SSF53748. 1 hit.
    PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00558-1) [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

    MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC    50
    LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV 100
    GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF 150
    RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA 200
    LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN 250
    MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ 300
    ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR 350
    GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL 400
    ELLEGKVLPG VDALSNI 417
    Length:417
    Mass (Da):44,615
    Last modified:January 23, 2007 - v3
    Checksum:iB5DFC7B5FA01767C
    GO
    Isoform 2 (identifier: P00558-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-28: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:389
    Mass (Da):41,429
    Checksum:i2A0D80F12CCEB825
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391Missing AA sequence (PubMed:7391027)Curated
    Sequence conflicti370 – 3701I → T in CAG32997. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881L → P in PGK1D; with congenital non-spherocytic anemia; variant Matsue. 1 Publication
    VAR_006076
    Natural varianti158 – 1581G → V in PGK1D; with chronic hemolytic anemia; variant Shizuoka. 1 Publication
    VAR_006077
    Natural varianti164 – 1641D → V in PGK1D; with chronic hemolytic anemia and mental retardation; variant Amiens. 1 Publication
    VAR_006078
    Natural varianti191 – 1911Missing in PGK1D; with chronic hemolytic anemia; variant Alabama. 1 Publication
    VAR_006079
    Natural varianti206 – 2061R → P in PGK1D; with chronic hemolytic anemia; variant Uppsala. 1 Publication
    VAR_006080
    Natural varianti252 – 2521E → A in PGK1D; with chronic hemolytic anemia; variant Antwerp. 1 Publication
    VAR_006081
    Natural varianti266 – 2661V → M in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo. 1 Publication
    VAR_006082
    Natural varianti268 – 2681D → N in Munchen; 21% of activity. 2 Publications
    VAR_006083
    Natural varianti285 – 2851D → V in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity. 1 Publication
    VAR_006084
    Natural varianti315 – 3151D → N in PGK1D; with rhabdomyolysis; variant Creteil. 1 Publication
    VAR_006085
    Natural varianti316 – 3161C → R in PGK1D; with chronic hemolytic anemia; variant Michigan. 1 Publication
    VAR_006086
    Natural varianti352 – 3521T → N.1 Publication
    VAR_006087

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 2. 1 PublicationVSP_056159Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00572 mRNA. Translation: CAA23835.1.
    L00160 mRNA. Translation: AAA60078.1.
    M11968
    , M11958, M11959, M11960, M11961, M11962, M11963, M11964, M11965, M11966, M11967 Genomic DNA. Translation: AAA60079.1.
    AY423725 mRNA. Translation: AAS00488.1.
    AB062432 mRNA. Translation: BAB93495.1.
    AK291081 mRNA. Translation: BAF83770.1.
    AK301740 mRNA. Translation: BAH13545.1.
    AK312280 mRNA. Translation: BAG35209.1.
    CR456716 mRNA. Translation: CAG32997.1.
    AL049589 Genomic DNA. Translation: CAI42951.1.
    CH471104 Genomic DNA. Translation: EAW98604.1.
    BC023234 mRNA. Translation: AAH23234.1.
    BC103752 mRNA. Translation: AAI03753.1.
    BC104837 mRNA. Translation: AAI04838.1.
    BC113568 mRNA. Translation: AAI13569.1.
    M34017 Genomic DNA. Translation: AAA60103.1.
    CCDSiCCDS14438.1.
    PIRiI59050. KIHUG.
    RefSeqiNP_000282.1. NM_000291.3.
    UniGeneiHs.78771.

    Genome annotation databases

    EnsembliENST00000373316; ENSP00000362413; ENSG00000102144.
    ENST00000537456; ENSP00000444708; ENSG00000102144.
    GeneIDi5230.
    KEGGihsa:5230.
    UCSCiuc004ecz.4. human.

    Polymorphism databases

    DMDMi52788229.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Phosphoglycerate kinase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00572 mRNA. Translation: CAA23835.1 .
    L00160 mRNA. Translation: AAA60078.1 .
    M11968
    , M11958 , M11959 , M11960 , M11961 , M11962 , M11963 , M11964 , M11965 , M11966 , M11967 Genomic DNA. Translation: AAA60079.1 .
    AY423725 mRNA. Translation: AAS00488.1 .
    AB062432 mRNA. Translation: BAB93495.1 .
    AK291081 mRNA. Translation: BAF83770.1 .
    AK301740 mRNA. Translation: BAH13545.1 .
    AK312280 mRNA. Translation: BAG35209.1 .
    CR456716 mRNA. Translation: CAG32997.1 .
    AL049589 Genomic DNA. Translation: CAI42951.1 .
    CH471104 Genomic DNA. Translation: EAW98604.1 .
    BC023234 mRNA. Translation: AAH23234.1 .
    BC103752 mRNA. Translation: AAI03753.1 .
    BC104837 mRNA. Translation: AAI04838.1 .
    BC113568 mRNA. Translation: AAI13569.1 .
    M34017 Genomic DNA. Translation: AAA60103.1 .
    CCDSi CCDS14438.1.
    PIRi I59050. KIHUG.
    RefSeqi NP_000282.1. NM_000291.3.
    UniGenei Hs.78771.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WZB X-ray 1.47 A 2-417 [» ]
    2WZC X-ray 1.50 A 2-417 [» ]
    2WZD X-ray 1.56 A 1-417 [» ]
    2X13 X-ray 1.74 A 2-417 [» ]
    2X14 X-ray 1.90 A 2-417 [» ]
    2X15 X-ray 2.10 A 2-417 [» ]
    2XE6 X-ray 1.74 A 1-417 [» ]
    2XE7 X-ray 2.20 A 1-417 [» ]
    2XE8 X-ray 1.79 A 1-417 [» ]
    2Y3I X-ray 2.90 A/D 1-416 [» ]
    2YBE X-ray 2.00 A 1-417 [» ]
    2ZGV X-ray 2.00 A 1-417 [» ]
    3C39 X-ray 1.85 A/B 1-417 [» ]
    3C3A X-ray 2.30 A/B 1-417 [» ]
    3C3B X-ray 1.80 A/B 1-417 [» ]
    3C3C X-ray 2.40 A/B 1-417 [» ]
    3ZOZ X-ray 1.95 A 1-417 [» ]
    4AXX X-ray 1.74 A 1-417 [» ]
    ProteinModelPortali P00558.
    SMRi P00558. Positions 5-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111251. 51 interactions.
    IntActi P00558. 29 interactions.
    MINTi MINT-1131047.
    STRINGi 9606.ENSP00000362413.

    Chemistry

    BindingDBi P00558.
    ChEMBLi CHEMBL2096677.

    PTM databases

    PhosphoSitei P00558.

    Polymorphism databases

    DMDMi 52788229.

    2D gel databases

    DOSAC-COBS-2DPAGE P00558.
    OGPi P00558.
    REPRODUCTION-2DPAGE IPI00169383.
    P00558.
    UCD-2DPAGE P00558.

    Proteomic databases

    MaxQBi P00558.
    PaxDbi P00558.
    PeptideAtlasi P00558.
    PRIDEi P00558.

    Protocols and materials databases

    DNASUi 5230.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373316 ; ENSP00000362413 ; ENSG00000102144 .
    ENST00000537456 ; ENSP00000444708 ; ENSG00000102144 .
    GeneIDi 5230.
    KEGGi hsa:5230.
    UCSCi uc004ecz.4. human.

    Organism-specific databases

    CTDi 5230.
    GeneCardsi GC0XP077246.
    HGNCi HGNC:8896. PGK1.
    HPAi CAB010065.
    HPA045385.
    MIMi 300653. phenotype.
    311800. gene.
    neXtProti NX_P00558.
    Orphaneti 713. Glycogen storage disease due to phosphoglycerate kinase 1 deficiency.
    PharmGKBi PA33234.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0126.
    HOGENOMi HOG000227107.
    HOVERGENi HBG008177.
    InParanoidi P00558.
    KOi K00927.
    OMAi ASCCAKW.
    PhylomeDBi P00558.
    TreeFami TF300489.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    BioCyci MetaCyc:HS02359-MONOMER.
    BRENDAi 2.7.2.3. 2681.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RK P00558.

    Miscellaneous databases

    ChiTaRSi PGK1. human.
    EvolutionaryTracei P00558.
    GeneWikii PGK1.
    GenomeRNAii 5230.
    NextBioi 20218.
    PROi P00558.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00558.
    Bgeei P00558.
    CleanExi HS_PGK1.
    Genevestigatori P00558.

    Family and domain databases

    Gene3Di 3.40.50.1260. 1 hit.
    3.40.50.1270. 1 hit.
    HAMAPi MF_00145. Phosphoglyc_kinase.
    InterProi IPR001576. Phosphoglycerate_kinase.
    IPR015901. Phosphoglycerate_kinase_C.
    IPR015911. Phosphoglycerate_kinase_CS.
    IPR015824. Phosphoglycerate_kinase_N.
    [Graphical view ]
    PANTHERi PTHR11406. PTHR11406. 1 hit.
    Pfami PF00162. PGK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000724. Pgk. 1 hit.
    PRINTSi PR00477. PHGLYCKINASE.
    SUPFAMi SSF53748. SSF53748. 1 hit.
    PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and DNA sequence of a full-length cDNA clone for human X chromosome-encoded phosphoglycerate kinase."
      Michelson A.M., Markham A.F., Orkin S.H.
      Proc. Natl. Acad. Sci. U.S.A. 80:472-476(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Structure of the human phosphoglycerate kinase gene and the intron-mediated evolution and dispersal of the nucleotide-binding domain."
      Michelson A.M., Blake C.C., Evans S.T., Orkin S.H.
      Proc. Natl. Acad. Sci. U.S.A. 82:6965-6969(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Identification of a human migration-inducing gene 10 (MIG10)."
      Kim J.W.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    5. "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: Cerebellum and Testis.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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, Skin and Uterus.
    10. "Sequence of the promoter region of the gene for human X-linked 3-phosphoglycerate kinase]."
      Singer-Sam J., Keith D.H., Tani K., Simmer R.L., Shively L., Lindsay S., Yoshida A., Riggs A.D.
      Gene 32:409-417(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    11. "Genomic sequencing and methylation analysis by ligation mediated PCR."
      Pfeifer G.P., Steigerwald S.D., Mueller P.R., Wold B., Riggs A.D.
      Science 246:810-813(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
    12. "Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence."
      Huang I.-Y., Welch C.D., Yoshida A.
      J. Biol. Chem. 255:6412-6420(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-417.
      Tissue: Erythrocyte.
    13. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 23-30; 76-86; 107-123; 157-171; 200-216; 221-264; 280-297; 333-350; 366-382 AND 389-417, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    14. "Functional identity of a primer recognition protein as phosphoglycerate kinase."
      Jindal H.K., Vishwanatha J.K.
      J. Biol. Chem. 265:6540-6543(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Placenta.
    15. "Hematologically important mutations: molecular abnormalities of phosphoglycerate kinase."
      Yoshida A.
      Blood Cells Mol. Dis. 22:265-267(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    16. "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-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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-11; LYS-48; LYS-75; LYS-86; LYS-97; LYS-131; LYS-146; LYS-199; LYS-267 AND LYS-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: MALONYLATION AT LYS-131.
    23. "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-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    25. "Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase."
      Gondeau C., Chaloin L., Lallemand P., Roy B., Perigaud C., Barman T., Varga A., Vas M., Lionne C., Arold S.T.
      Nucleic Acids Res. 36:3620-3629(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PHOSPHOGLYCERATE; L-ADP; D-ADP; L-CDP AND D-CDP, SUBSTRATE-BINDING SITES.
    26. "Molecular abnormality of a phosphoglycerate kinase variant (PGK-Alabama)."
      Yoshida A., Twele T.W., Dave V., Beutler E.
      Blood Cells Mol. Dis. 21:179-181(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D LYS-191 DEL.
    27. "Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes: PGK Creteil and PGK Amiens."
      Cohen-Solal M., Valentin C., Plassa F., Guillemin G., Danze F., Jaisson F., Rosa R.
      Blood 84:898-903(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PGK1D VAL-164 AND ASN-315.
    28. "Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant."
      Ookawara T., Dave V., Willems P., Martin J.J., de Barsy T., Matthys E., Yoshida A.
      Arch. Biochem. Biophys. 327:35-40(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D ALA-252.
    29. "A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish patient with isolated chronic hemolytic anemia: mechanism of mutation and structure-function relationships."
      Valentin C., Birgens H., Craescu C.T., Broedum-Nielsen K., Cohen-Solal M.
      Hum. Mutat. 12:280-287(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D VAL-285.
    30. "Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue) associated with hemolytic anemia: Leu-->Pro substitution caused by T/A-->C/G transition in exon 3."
      Maeda M., Yoshida A.
      Blood 77:1348-1352(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D PRO-88.
    31. "Molecular abnormalities of a phosphoglycerate kinase variant generated by spontaneous mutation."
      Maeda M., Bawle E.V., Kulkarni R., Beutler E., Yoshida A.
      Blood 79:2759-2762(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D ARG-316.
    32. "A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK Munchen) associated with enzyme deficiency."
      Fujii H., Krietsch W.K.G., Yoshida A.
      J. Biol. Chem. 255:6421-6423(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MUNCHEN ASN-268.
    33. "Structure and function of normal and variant human phosphoglycerate kinase."
      Huang I.-Y., Fujii H., Yoshida A.
      Hemoglobin 4:601-609(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MUNCHEN ASN-268, VARIANT ASN-352.
    34. "A single amino acid substitution (157 Gly-->Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria."
      Fujii H., Kanno H., Hirono A., Shiomura T., Miwa S.
      Blood 79:1582-1585(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D VAL-158.
    35. "Use of cultured lymphoblastoid cells for the study of abnormal enzymes: molecular abnormality of a phosphoglycerate kinase variant associated with hemolytic anemia."
      Fujii H., Chen S.-H., Akatsuka J., Miwa S., Yoshida A.
      Proc. Natl. Acad. Sci. U.S.A. 78:2587-2590(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D MET-266.
    36. "Molecular abnormality of phosphoglycerate kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia."
      Fujii H., Yoshida A.
      Proc. Natl. Acad. Sci. U.S.A. 77:5461-5465(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PGK1D PRO-206.

    Entry informationi

    Entry nameiPGK1_HUMAN
    AccessioniPrimary (citable) accession number: P00558
    Secondary accession number(s): A8K4W6
    , B7Z7A9, Q5J7W1, Q6IBT6, Q8NI87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 171 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3