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P09041

- PGK2_MOUSE

UniProt

P09041 - PGK2_MOUSE

Protein

Phosphoglycerate kinase 2

Gene

Pgk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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 – 2201ATP1 Publication
    Binding sitei313 – 3131ATP; via carbonyl oxygen1 Publication
    Binding sitei344 – 3441ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi373 – 3764ATP1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: MGI
    2. phosphorylation Source: UniProtKB
    3. sperm motility Source: MGI

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP09041.
    UniPathwayiUPA00109; UER00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglycerate kinase 2 (EC:2.7.2.3)
    Alternative name(s):
    Phosphoglycerate kinase, testis specific
    Gene namesi
    Name:Pgk2
    Synonyms:Pgk-2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:97563. Pgk2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cilium Source: MGI
    2. cytoplasm Source: UniProtKB-SubCell
    3. sperm fibrous sheath Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Phosphoglycerate kinase 2PRO_0000145836Add
    BLAST

    Proteomic databases

    MaxQBiP09041.
    PaxDbiP09041.
    PRIDEiP09041.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00555060.
    P09041.

    PTM databases

    PhosphoSiteiP09041.

    Expressioni

    Gene expression databases

    BgeeiP09041.
    CleanExiMM_PGK2.
    GenevestigatoriP09041.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP09041. 1 interaction.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Beta strandi18 – 225
    Beta strandi29 – 324
    Beta strandi33 – 353
    Helixi38 – 5215
    Beta strandi56 – 616
    Helixi73 – 764
    Helixi79 – 8911
    Beta strandi93 – 953
    Beta strandi99 – 1013
    Helixi102 – 1098
    Beta strandi115 – 1184
    Helixi122 – 1243
    Turni126 – 1305
    Beta strandi131 – 1333
    Beta strandi139 – 1413
    Helixi144 – 15512
    Beta strandi159 – 1635
    Helixi166 – 1683
    Helixi174 – 1774
    Beta strandi184 – 1863
    Helixi188 – 20215
    Beta strandi206 – 2138
    Helixi218 – 2203
    Helixi221 – 2277
    Turni228 – 2303
    Beta strandi232 – 2376
    Helixi240 – 24910
    Beta strandi253 – 2564
    Helixi260 – 2634
    Helixi266 – 27510
    Beta strandi279 – 2813
    Beta strandi284 – 29310
    Beta strandi298 – 3025
    Turni303 – 3053
    Beta strandi312 – 3165
    Helixi318 – 32912
    Beta strandi332 – 3387
    Helixi346 – 3483
    Helixi350 – 36415
    Beta strandi368 – 3714
    Helixi375 – 3828
    Turni386 – 3883
    Beta strandi389 – 3924
    Helixi396 – 4027
    Turni403 – 4053
    Helixi409 – 4124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P9QX-ray2.70A/B2-417[»]
    2P9TX-ray2.00A2-417[»]
    2PAAX-ray2.70A/B2-417[»]
    ProteinModelPortaliP09041.
    SMRiP09041. Positions 5-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09041.

    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.
    GeneTreeiENSGT00390000008820.
    HOGENOMiHOG000227107.
    HOVERGENiHBG008177.
    InParanoidiQ5RKV3.
    KOiK00927.
    OMAiVAKEFAP.
    OrthoDBiEOG74R1QN.
    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.

    P09041-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSAKLTLD KVDLKGKRVI MRVDFNVPMK NNQITNNQRI KAAIPSIKHC    50
    LDNGAKSVVL MSHLGRPDGI PMPDKYSLEP VADELKSLLN KDVIFLKDCV 100
    GPEVEQACAN PDNGSIILLE NLRFHVEEEG KGKDSSGKKI SADPAKVEAF 150
    QASLSKLGDV YVNDAFGTAH RAHSSTVGVN LPQKASGFLM KKELDYFSKA 200
    LEKPERPFLA ILGGAKVKDK IQLIKNMLDK VNFMIIGGGM AYTFLKELKN 250
    MQIGASLFDE EGATIVKEIM EKAEKNGVKI VFPVDFVTGD KFDENAKVGQ 300
    ATIESGIPSG WMGLDCGPES IKINAQIVAQ AKLIVWNGPI GVFEWDAFAK 350
    GTKALMDEVV KATSNGCVTI IGGGDTATCC AKWGTEDKVS HVSTGGGASL 400
    ELLEGKILPG VEALSNM 417
    Length:417
    Mass (Da):44,853
    Last modified:July 27, 2011 - v4
    Checksum:iBC3FACE559798B53
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511Q → R in AAA39920. (PubMed:2823118)Curated
    Sequence conflicti176 – 1761T → M in AAA39920. (PubMed:2823118)Curated
    Sequence conflicti176 – 1761T → M in AAA39921. (PubMed:2823118)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17299 Genomic DNA. Translation: AAA39920.1.
    M18654 mRNA. Translation: AAA39921.1.
    AK133436 mRNA. Translation: BAE21656.1.
    CH466559 Genomic DNA. Translation: EDL23381.1.
    BC052343 mRNA. Translation: AAH52343.1.
    BC061054 mRNA. Translation: AAH61054.1.
    X55310 Genomic DNA. Translation: CAA39014.1.
    CCDSiCCDS28782.1.
    PIRiA27775.
    RefSeqiNP_112467.2. NM_031190.2.
    UniGeneiMm.717.

    Genome annotation databases

    EnsembliENSMUST00000033585; ENSMUSP00000033585; ENSMUSG00000031233.
    GeneIDi18663.
    KEGGimmu:18663.
    UCSCiuc008cof.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17299 Genomic DNA. Translation: AAA39920.1 .
    M18654 mRNA. Translation: AAA39921.1 .
    AK133436 mRNA. Translation: BAE21656.1 .
    CH466559 Genomic DNA. Translation: EDL23381.1 .
    BC052343 mRNA. Translation: AAH52343.1 .
    BC061054 mRNA. Translation: AAH61054.1 .
    X55310 Genomic DNA. Translation: CAA39014.1 .
    CCDSi CCDS28782.1.
    PIRi A27775.
    RefSeqi NP_112467.2. NM_031190.2.
    UniGenei Mm.717.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P9Q X-ray 2.70 A/B 2-417 [» ]
    2P9T X-ray 2.00 A 2-417 [» ]
    2PAA X-ray 2.70 A/B 2-417 [» ]
    ProteinModelPortali P09041.
    SMRi P09041. Positions 5-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P09041. 1 interaction.

    PTM databases

    PhosphoSitei P09041.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00555060.
    P09041.

    Proteomic databases

    MaxQBi P09041.
    PaxDbi P09041.
    PRIDEi P09041.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033585 ; ENSMUSP00000033585 ; ENSMUSG00000031233 .
    GeneIDi 18663.
    KEGGi mmu:18663.
    UCSCi uc008cof.2. mouse.

    Organism-specific databases

    CTDi 5232.
    MGIi MGI:97563. Pgk2.

    Phylogenomic databases

    eggNOGi COG0126.
    GeneTreei ENSGT00390000008820.
    HOGENOMi HOG000227107.
    HOVERGENi HBG008177.
    InParanoidi Q5RKV3.
    KOi K00927.
    OMAi VAKEFAP.
    OrthoDBi EOG74R1QN.
    TreeFami TF300489.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00185 .
    SABIO-RK P09041.

    Miscellaneous databases

    EvolutionaryTracei P09041.
    NextBioi 294668.
    PROi P09041.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09041.
    CleanExi MM_PGK2.
    Genevestigatori P09041.

    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. "The testis-specific phosphoglycerate kinase gene pgk-2 is a recruited retroposon."
      Boer P.H., Adra C.N., Lau Y.-F.C., McBurney M.W.
      Mol. Cell. Biol. 7:3107-3112(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / 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: Testis.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Testis.
    5. "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 1-6.
    6. "X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from Mus musculus."
      Sawyer G.M., Monzingo A.F., Poteet E.C., O'Brien D.A., Robertus J.D.
      Proteins 71:1134-1144(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-417 ALONE AND IN COMPLEX WITH PHOSPHOGLYCERATE AND ATP, SUBUNIT, SUBSTRATE-BINDING SITES.

    Entry informationi

    Entry nameiPGK2_MOUSE
    AccessioniPrimary (citable) accession number: P09041
    Secondary accession number(s): Q5RKV3, Q6P8V2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3