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P00558

- PGK1_HUMAN

UniProt

P00558 - PGK1_HUMAN

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Protein
Phosphoglycerate kinase 1
Gene
PGK1, PGKA, MIG10, OK/SW-cl.110
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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).UniRule annotation

Catalytic activityi

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

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 – 3764ATPUniRule annotation

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
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
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 1UniRule annotation
PRO_0000145831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei6 – 61N6-succinyllysine By similarity
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei48 – 481N6-acetyllysine; alternate1 Publication
Modified residuei48 – 481N6-succinyllysine; alternate By similarity
Modified residuei75 – 751N6-acetyllysine1 Publication
Modified residuei76 – 761Phosphotyrosine By similarity
Modified residuei86 – 861N6-acetyllysine1 Publication
Modified residuei91 – 911N6-acetyllysine By 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-succinyllysine By 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-acetyllysine By 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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP00558.

Family & Domainsi

Region

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

Sequence similaritiesi

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]

Sequencei

Sequence statusi: Complete.

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

P00558-1 [UniParc]FASTAAdd to Basket

« 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

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

Sequence conflict

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

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.
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.
ENST00000597340; ENSP00000472461; ENSG00000269666.
GeneIDi5230.
KEGGihsa:5230.
UCSCiuc004ecz.4. human.

Polymorphism databases

DMDMi52788229.

Keywords - Coding sequence diversityi

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 .
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 .
ENST00000597340 ; ENSP00000472461 ; ENSG00000269666 .
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

« Hide 'large scale' publications
  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].
    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].
  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].
    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].
    Tissue: Cerebellum.
  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].
  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].
    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
, Q5J7W1, Q6IBT6, Q8NI87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 170 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

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