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P09411

- PGK1_MOUSE

UniProt

P09411 - PGK1_MOUSE

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Protein
Phosphoglycerate kinase 1
Gene
Pgk1, Pgk-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 By similarity
Binding sitei123 – 1231Substrate By similarity
Binding sitei171 – 1711Substrate By similarity
Binding sitei220 – 2201ATP By similarity
Binding sitei313 – 3131ATP; via carbonyl oxygen By similarity
Binding sitei344 – 3441ATP By similarity

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. phosphoglycerate kinase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP09411.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase 1 (EC:2.7.2.3)
Gene namesi
Name:Pgk1
Synonyms:Pgk-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:97555. Pgk1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 417416Phosphoglycerate kinase 1UniRule annotation
PRO_0000145835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei6 – 61N6-succinyllysine1 Publication
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei48 – 481N6-acetyllysine; alternate By similarity
Modified residuei48 – 481N6-succinyllysine; alternate1 Publication
Modified residuei75 – 751N6-acetyllysine By similarity
Modified residuei76 – 761Phosphotyrosine1 Publication
Modified residuei86 – 861N6-acetyllysine By similarity
Modified residuei91 – 911N6-acetyllysine1 Publication
Modified residuei97 – 971N6-acetyllysine By similarity
Modified residuei131 – 1311N6-acetyllysine; alternate By similarity
Modified residuei131 – 1311N6-malonyllysine; alternate By similarity
Modified residuei146 – 1461N6-acetyllysine By similarity
Modified residuei191 – 1911N6-succinyllysine1 Publication
Modified residuei196 – 1961Phosphotyrosine By similarity
Modified residuei199 – 1991N6-acetyllysine By similarity
Modified residuei203 – 2031Phosphoserine2 Publications
Modified residuei267 – 2671N6-acetyllysine By similarity
Modified residuei291 – 2911N6-acetyllysine1 Publication
Modified residuei361 – 3611N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09411.
PaxDbiP09411.
PRIDEiP09411.

2D gel databases

COMPLUYEAST-2DPAGEP09411.
REPRODUCTION-2DPAGEIPI00555069.
P09411.
SWISS-2DPAGEP09411.

PTM databases

PhosphoSiteiP09411.

Expressioni

Gene expression databases

BgeeiP09411.
CleanExiMM_PGK1.
GenevestigatoriP09411.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi202133. 3 interactions.
IntActiP09411. 7 interactions.
MINTiMINT-1854650.

Structurei

3D structure databases

ProteinModelPortaliP09411.
SMRiP09411. Positions 5-417.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0126.
GeneTreeiENSGT00390000008820.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP09411.
KOiK00927.
OMAiASCCAKW.
OrthoDBiEOG74R1QN.
PhylomeDBiP09411.
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.

P09411-1 [UniParc]FASTAAdd to Basket

« Hide

MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC    50
LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV 100
GPEVENACAN PAAGTVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIDAF 150
RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA 200
LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN 250
MEIGTSLYDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ 300
ATVASGIPAG WMGLDCGTES SKKYAEAVGR AKQIVWNGPV GVFEWEAFAR 350
GTKSLMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL 400
ELLEGKVLPG VDALSNV 417
Length:417
Mass (Da):44,550
Last modified:May 1, 2007 - v4
Checksum:i5E2EE194FF9D8CEE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561K → N in AAA70267. 1 Publication
Sequence conflicti184 – 1841K → R in BAE26693. 1 Publication
Sequence conflicti265 – 2651I → V in BAE37790. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15668 mRNA. Translation: AAA70267.1.
AK145846 mRNA. Translation: BAE26693.1.
AK167710 mRNA. Translation: BAE39754.1.
AK167459 mRNA. Translation: BAE39544.1.
AK167441 mRNA. Translation: BAE39527.1.
AK133877 mRNA. Translation: BAE21906.1.
AK164440 mRNA. Translation: BAE37790.1.
BX469914 Genomic DNA. Translation: CAM17784.1.
BC083355 mRNA. Translation: AAH83355.1.
BC108372 mRNA. Translation: AAI08373.1.
M18735 Genomic DNA. Translation: AAA39919.1.
X55309 Genomic DNA. Translation: CAA39013.1.
X15339 Genomic DNA. Translation: CAA33391.1.
CCDSiCCDS30339.1.
PIRiA25567.
RefSeqiNP_032854.2. NM_008828.3.
UniGeneiMm.316355.
Mm.336204.
Mm.336205.

Genome annotation databases

EnsembliENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
ENSMUST00000085735; ENSMUSP00000136544; ENSMUSG00000066632.
GeneIDi18655.
KEGGimmu:18655.
UCSCiuc009ubo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15668 mRNA. Translation: AAA70267.1 .
AK145846 mRNA. Translation: BAE26693.1 .
AK167710 mRNA. Translation: BAE39754.1 .
AK167459 mRNA. Translation: BAE39544.1 .
AK167441 mRNA. Translation: BAE39527.1 .
AK133877 mRNA. Translation: BAE21906.1 .
AK164440 mRNA. Translation: BAE37790.1 .
BX469914 Genomic DNA. Translation: CAM17784.1 .
BC083355 mRNA. Translation: AAH83355.1 .
BC108372 mRNA. Translation: AAI08373.1 .
M18735 Genomic DNA. Translation: AAA39919.1 .
X55309 Genomic DNA. Translation: CAA39013.1 .
X15339 Genomic DNA. Translation: CAA33391.1 .
CCDSi CCDS30339.1.
PIRi A25567.
RefSeqi NP_032854.2. NM_008828.3.
UniGenei Mm.316355.
Mm.336204.
Mm.336205.

3D structure databases

ProteinModelPortali P09411.
SMRi P09411. Positions 5-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202133. 3 interactions.
IntActi P09411. 7 interactions.
MINTi MINT-1854650.

PTM databases

PhosphoSitei P09411.

2D gel databases

COMPLUYEAST-2DPAGE P09411.
REPRODUCTION-2DPAGE IPI00555069.
P09411.
SWISS-2DPAGE P09411.

Proteomic databases

MaxQBi P09411.
PaxDbi P09411.
PRIDEi P09411.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081593 ; ENSMUSP00000080302 ; ENSMUSG00000062070 .
ENSMUST00000085735 ; ENSMUSP00000136544 ; ENSMUSG00000066632 .
GeneIDi 18655.
KEGGi mmu:18655.
UCSCi uc009ubo.1. mouse.

Organism-specific databases

CTDi 5230.
MGIi MGI:97555. Pgk1.

Phylogenomic databases

eggNOGi COG0126.
GeneTreei ENSGT00390000008820.
HOGENOMi HOG000227107.
HOVERGENi HBG008177.
InParanoidi P09411.
KOi K00927.
OMAi ASCCAKW.
OrthoDBi EOG74R1QN.
PhylomeDBi P09411.
TreeFami TF300489.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00185 .
SABIO-RK P09411.

Miscellaneous databases

ChiTaRSi PGK1. mouse.
NextBioi 294662.
PROi P09411.
SOURCEi Search...

Gene expression databases

Bgeei P09411.
CleanExi MM_PGK1.
Genevestigatori P09411.

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. "The nucleotide sequence of a cDNA clone containing the entire coding region for mouse X-chromosome-linked phosphoglycerate kinase."
    Mori N., Singer-Sam J., Lee C.-Y., Riggs A.D.
    Gene 45:275-280(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye and Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: 129 and C57BL/6.
    Tissue: Brain and Mammary tumor.
  5. "Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence of its promoter."
    Adra C.N., Boer P.H., McBurney M.W.
    Gene 60:65-74(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  6. "Selective activation of testis-specific genes in cultured rat spermatogenic cells."
    Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.
    Biochim. Biophys. Acta 1049:331-338(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  7. "Polymorphisms in the coding and noncoding regions of murine Pgk-1 alleles."
    Boer P.H., Potten H., Adra C.N., Jardine K., Mullhofer G., McBurney M.W.
    Biochem. Genet. 28:299-308(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  8. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-30; 76-86; 98-123; 157-184; 193-216; 247-264; 280-297; 333-350 AND 389-417, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  9. "Evolutionary conservation of the substrate-binding cleft of phosphoglycerate kinases."
    Mori N., Singer-Sam J., Riggs A.D.
    FEBS Lett. 204:313-317(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-11; LYS-91; LYS-291 AND LYS-361, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-48 AND LYS-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiPGK1_MOUSE
AccessioniPrimary (citable) accession number: P09411
Secondary accession number(s): Q3TPE6, Q3UKV8, Q5XJE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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