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P19157

- GSTP1_MOUSE

UniProt

P19157 - GSTP1_MOUSE

Protein

Glutathione S-transferase P 1

Gene

Gstp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration By similarity.By similarity

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Glutathione
    Binding sitei14 – 141Glutathione
    Binding sitei39 – 391Glutathione
    Binding sitei45 – 451Glutathione

    GO - Molecular functioni

    1. drug binding Source: BHF-UCL
    2. glutathione transferase activity Source: MGI
    3. JUN kinase binding Source: BHF-UCL
    4. kinase regulator activity Source: BHF-UCL

    GO - Biological processi

    1. cellular response to cell-matrix adhesion Source: BHF-UCL
    2. cellular response to epidermal growth factor stimulus Source: BHF-UCL
    3. cellular response to glucocorticoid stimulus Source: BHF-UCL
    4. cellular response to insulin stimulus Source: BHF-UCL
    5. cellular response to lipopolysaccharide Source: BHF-UCL
    6. common myeloid progenitor cell proliferation Source: BHF-UCL
    7. glutathione metabolic process Source: MGI
    8. negative regulation of acute inflammatory response Source: BHF-UCL
    9. negative regulation of apoptotic process Source: BHF-UCL
    10. negative regulation of biosynthetic process Source: BHF-UCL
    11. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    12. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    13. negative regulation of fibroblast proliferation Source: BHF-UCL
    14. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
    15. negative regulation of interleukin-1 beta production Source: BHF-UCL
    16. negative regulation of JUN kinase activity Source: BHF-UCL
    17. negative regulation of leukocyte proliferation Source: BHF-UCL
    18. negative regulation of MAP kinase activity Source: BHF-UCL
    19. negative regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
    20. negative regulation of neutrophil aggregation Source: BHF-UCL
    21. negative regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
    22. negative regulation of peroxidase activity Source: BHF-UCL
    23. negative regulation of stress-activated MAPK cascade Source: BHF-UCL
    24. negative regulation of tumor necrosis factor production Source: BHF-UCL
    25. oligodendrocyte development Source: BHF-UCL
    26. organ regeneration Source: BHF-UCL
    27. positive regulation of superoxide anion generation Source: BHF-UCL
    28. regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    29. regulation of stress-activated MAPK cascade Source: BHF-UCL
    30. response to amino acid Source: BHF-UCL
    31. response to estradiol Source: BHF-UCL
    32. response to ethanol Source: BHF-UCL
    33. response to L-ascorbic acid Source: BHF-UCL
    34. response to nutrient levels Source: BHF-UCL
    35. response to reactive oxygen species Source: BHF-UCL
    36. response to toxic substance Source: BHF-UCL
    37. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_215316. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase P 1 (EC:2.5.1.18)
    Short name:
    Gst P1
    Alternative name(s):
    GST YF-YF
    GST class-pi
    GST-piB
    Preadipocyte growth factor
    Gene namesi
    Name:Gstp1
    Synonyms:Gstpib
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:95865. Gstp1.

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity
    Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: BHF-UCL
    3. intracellular Source: BHF-UCL
    4. mitochondrion Source: UniProtKB-SubCell
    5. nucleus Source: BHF-UCL
    6. plasma membrane Source: BHF-UCL
    7. protein complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 210209Glutathione S-transferase P 1PRO_0000185903Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphotyrosine; by EGFRBy similarity
    Modified residuei103 – 1031N6-succinyllysine1 Publication
    Modified residuei116 – 1161N6-succinyllysine1 Publication
    Modified residuei128 – 1281N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP19157.
    PaxDbiP19157.
    PRIDEiP19157.

    2D gel databases

    REPRODUCTION-2DPAGEP19157.
    SWISS-2DPAGEP19157.

    PTM databases

    PhosphoSiteiP19157.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    BgeeiP19157.
    CleanExiMM_GSTP1.
    GenevestigatoriP19157.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CDK5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Prdx6O087092EBI-2309446,EBI-444895

    Protein-protein interaction databases

    BioGridi200101. 2 interactions.
    IntActiP19157. 5 interactions.
    MINTiMINT-1869068.
    STRINGi10090.ENSMUSP00000047790.

    Structurei

    Secondary structure

    1
    210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi10 – 123
    Helixi13 – 153
    Helixi16 – 249
    Beta strandi29 – 335
    Helixi36 – 405
    Beta strandi42 – 443
    Helixi45 – 473
    Beta strandi49 – 513
    Beta strandi55 – 584
    Beta strandi61 – 655
    Helixi66 – 7712
    Helixi84 – 11027
    Helixi112 – 13524
    Helixi138 – 1403
    Beta strandi144 – 1485
    Helixi151 – 16616
    Turni168 – 1736
    Helixi175 – 18612
    Helixi188 – 1958
    Helixi197 – 2004
    Beta strandi204 – 2085

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BAYX-ray2.00A/B2-210[»]
    1GLPX-ray1.90A/B2-210[»]
    1GLQX-ray1.80A/B2-210[»]
    1GSYX-ray2.44A/B2-210[»]
    1GTIX-ray3.00A/B/C/D/E/F2-210[»]
    2GLRX-ray2.20A/B2-210[»]
    2OA7X-ray2.20A/B2-210[»]
    2OACX-ray2.20A/B2-210[»]
    2OADX-ray2.50A/B2-210[»]
    3O76X-ray1.77A/B2-210[»]
    ProteinModelPortaliP19157.
    SMRiP19157. Positions 2-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19157.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8180GST N-terminalAdd
    BLAST
    Domaini83 – 204122GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 532Glutathione binding
    Regioni65 – 662Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Pi family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG05174.
    GeneTreeiENSGT00550000074559.
    HOGENOMiHOG000115733.
    HOVERGENiHBG108324.
    InParanoidiP19157.
    KOiK00799.
    OMAiLRCKYAT.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiP19157.
    TreeFamiTF105321.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01268. GSTRNSFRASEP.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19157-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPYTIVYFP VRGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY    50
    GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKNQREAAQM DMVNDGVEDL 100
    RGKYVTLIYT NYENGKNDYV KALPGHLKPF ETLLSQNQGG KAFIVGDQIS 150
    FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPEHV 200
    NRPINGNGKQ 210
    Length:210
    Mass (Da):23,609
    Last modified:January 23, 2007 - v2
    Checksum:iDAC7762F4E34FF27
    GO

    Mass spectrometryi

    Molecular mass is 23478.8±2 Da from positions 2 - 210. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53451 mRNA. Translation: CAA37529.1.
    X76143 Genomic DNA. No translation available.
    U15654 Genomic DNA. Translation: AAA64837.1.
    D30687 mRNA. Translation: BAA06349.1.
    BC002048 mRNA. Translation: AAH02048.1.
    BC061109 mRNA. Translation: AAH61109.1.
    AK079144 mRNA. Translation: BAC37560.1.
    CCDSiCCDS29411.1.
    PIRiS12709. B55140.
    RefSeqiNP_038569.1. NM_013541.1.
    UniGeneiMm.299292.

    Genome annotation databases

    EnsembliENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
    ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.
    GeneIDi14870.
    KEGGimmu:14870.
    UCSCiuc008fyf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53451 mRNA. Translation: CAA37529.1 .
    X76143 Genomic DNA. No translation available.
    U15654 Genomic DNA. Translation: AAA64837.1 .
    D30687 mRNA. Translation: BAA06349.1 .
    BC002048 mRNA. Translation: AAH02048.1 .
    BC061109 mRNA. Translation: AAH61109.1 .
    AK079144 mRNA. Translation: BAC37560.1 .
    CCDSi CCDS29411.1.
    PIRi S12709. B55140.
    RefSeqi NP_038569.1. NM_013541.1.
    UniGenei Mm.299292.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BAY X-ray 2.00 A/B 2-210 [» ]
    1GLP X-ray 1.90 A/B 2-210 [» ]
    1GLQ X-ray 1.80 A/B 2-210 [» ]
    1GSY X-ray 2.44 A/B 2-210 [» ]
    1GTI X-ray 3.00 A/B/C/D/E/F 2-210 [» ]
    2GLR X-ray 2.20 A/B 2-210 [» ]
    2OA7 X-ray 2.20 A/B 2-210 [» ]
    2OAC X-ray 2.20 A/B 2-210 [» ]
    2OAD X-ray 2.50 A/B 2-210 [» ]
    3O76 X-ray 1.77 A/B 2-210 [» ]
    ProteinModelPortali P19157.
    SMRi P19157. Positions 2-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200101. 2 interactions.
    IntActi P19157. 5 interactions.
    MINTi MINT-1869068.
    STRINGi 10090.ENSMUSP00000047790.

    PTM databases

    PhosphoSitei P19157.

    2D gel databases

    REPRODUCTION-2DPAGE P19157.
    SWISS-2DPAGE P19157.

    Proteomic databases

    MaxQBi P19157.
    PaxDbi P19157.
    PRIDEi P19157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169613 ; ENSMUSP00000129565 ; ENSMUSG00000060803 .
    ENSMUST00000180480 ; ENSMUSP00000138073 ; ENSMUSG00000097830 .
    GeneIDi 14870.
    KEGGi mmu:14870.
    UCSCi uc008fyf.1. mouse.

    Organism-specific databases

    CTDi 2950.
    MGIi MGI:95865. Gstp1.

    Phylogenomic databases

    eggNOGi NOG05174.
    GeneTreei ENSGT00550000074559.
    HOGENOMi HOG000115733.
    HOVERGENi HBG108324.
    InParanoidi P19157.
    KOi K00799.
    OMAi LRCKYAT.
    OrthoDBi EOG7KH9M3.
    PhylomeDBi P19157.
    TreeFami TF105321.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_215316. Glutathione conjugation.

    Miscellaneous databases

    EvolutionaryTracei P19157.
    NextBioi 287133.
    PROi P19157.
    SOURCEi Search...

    Gene expression databases

    Bgeei P19157.
    CleanExi MM_GSTP1.
    Genevestigatori P19157.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01268. GSTRNSFRASEP.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cDNA sequence coding a class pi glutathione S-transferase of mouse."
      Hatayama I., Satoh K., Sato K.
      Nucleic Acids Res. 18:4606-4606(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "Isolation and characterization of two mouse PI class glutathione S-transferase genes."
      Bammler T.K., Smith C.A.D., Wolf R.C.
      Biochem. J. 298:385-390(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Two murine GSTpi genes are arranged in tandem and are differentially expressed."
      Xu X., Stambrook P.J.
      J. Biol. Chem. 269:30268-30273(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
      Tissue: Liver.
    4. "Molecular cloning of mouse preadipocyte growth factor."
      Kawada T., Aoki N., Kamei Y., Sugimoto E.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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].
    6. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    7. "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] OF 9-210.
      Strain: C57BL/6J.
      Tissue: Embryo.
    8. "Purification, mass spectrometric characterization, and covalent modification of murine glutathione S-transferases."
      Mitchell A.E., Morin D., Lame M.W., Jones A.D.
      Chem. Res. Toxicol. 8:1054-1062(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
      Strain: CD-1.
      Tissue: Liver.
    9. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors."
      Garcia-Saez I., Parraga A., Phillips M.F., Mantle T.J., Coll M.
      J. Mol. Biol. 237:298-314(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOGS.
    11. "The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region."
      Vega M.C., Walsh S.B., Mantle T.J., Coll M.
      J. Biol. Chem. 273:2844-2850(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    Entry informationi

    Entry nameiGSTP1_MOUSE
    AccessioniPrimary (citable) accession number: P19157
    Secondary accession number(s): Q8BNY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3