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P48637

- GSHB_HUMAN

UniProt

P48637 - GSHB_HUMAN

Protein

Glutathione synthetase

Gene

GSS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.

    Cofactori

    Binds 1 magnesium ion per subunit.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei125 – 1251Substrate
    Metal bindingi144 – 1441Magnesium
    Binding sitei144 – 1441ATP
    Metal bindingi146 – 1461Magnesium
    Binding sitei220 – 2201Substrate
    Binding sitei305 – 3051ATP
    Metal bindingi368 – 3681Magnesium
    Binding sitei375 – 3751ATP
    Binding sitei425 – 4251ATP
    Binding sitei450 – 4501Substrate
    Binding sitei452 – 4521ATP
    Binding sitei458 – 4581ATP; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi364 – 37310ATP
    Nucleotide bindingi398 – 4014ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. glutathione binding Source: UniProtKB
    3. glutathione synthase activity Source: Reactome
    4. glycine binding Source: Ensembl
    5. magnesium ion binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular amino acid metabolic process Source: ProtInc
    3. glutathione biosynthetic process Source: Reactome
    4. glutathione derivative biosynthetic process Source: Reactome
    5. nervous system development Source: ProtInc
    6. response to amino acid Source: Ensembl
    7. response to cadmium ion Source: Ensembl
    8. response to nutrient levels Source: Ensembl
    9. response to oxidative stress Source: ProtInc
    10. response to tumor necrosis factor Source: Ensembl
    11. small molecule metabolic process Source: Reactome
    12. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Glutathione biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02174-MONOMER.
    ReactomeiREACT_6960. Glutathione synthesis and recycling.
    SABIO-RKP48637.
    UniPathwayiUPA00142; UER00210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione synthetase (EC:6.3.2.3)
    Short name:
    GSH synthetase
    Short name:
    GSH-S
    Alternative name(s):
    Glutathione synthase
    Gene namesi
    Name:GSS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:4624. GSS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Glutathione synthetase deficiency (GSS deficiency) [MIM:266130]: Severe form characterized by an increased rate of hemolysis and defective function of the central nervous system.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261A → D in GSS deficiency.
    VAR_003602
    Natural varianti188 – 1881L → P in GSS deficiency; 100-fold reduction of activity.
    VAR_003603
    Natural varianti219 – 2191D → A in GSS deficiency.
    VAR_003604
    Natural varianti219 – 2191D → G in GSS deficiency. 1 Publication
    Corresponds to variant rs28938472 [ dbSNP | Ensembl ].
    VAR_003605
    Natural varianti254 – 2541L → R in GSS deficiency.
    VAR_003606
    Natural varianti267 – 2671R → W in GSS deficiency. 1 Publication
    VAR_003607
    Natural varianti270 – 2701Y → C in GSS deficiency; 100-fold reduction of activity.
    VAR_003608
    Natural varianti270 – 2701Y → H in GSS deficiency; 100-fold reduction of activity.
    VAR_003609
    Natural varianti283 – 2831R → C in GSS deficiency; 10-fold reduction of activity. 1 Publication
    VAR_003610
    Natural varianti286 – 2861L → Q in GSS deficiency.
    VAR_003611
    Natural varianti330 – 3301R → C in GSS deficiency.
    Corresponds to variant rs148640446 [ dbSNP | Ensembl ].
    VAR_003612
    Natural varianti464 – 4641G → V in GSS deficiency.
    VAR_003613
    Natural varianti469 – 4691D → E in GSS deficiency.
    VAR_003614
    Glutathione synthetase deficiency of erythrocytes (GLUSYNDE) [MIM:231900]: Mild form causing hemolytic anemia.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi231900. phenotype.
    266130. phenotype.
    Orphaneti289846. Glutathione synthetase deficiency with 5-oxoprolinuria.
    289849. Glutathione synthetase deficiency without 5-oxoprolinuria.
    PharmGKBiPA29015.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 474473Glutathione synthetasePRO_0000211260Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48637.
    PaxDbiP48637.
    PeptideAtlasiP48637.
    PRIDEiP48637.

    2D gel databases

    OGPiP48637.
    REPRODUCTION-2DPAGEIPI00010706.

    PTM databases

    PhosphoSiteiP48637.

    Expressioni

    Gene expression databases

    ArrayExpressiP48637.
    BgeeiP48637.
    CleanExiHS_GSS.
    GenevestigatoriP48637.

    Organism-specific databases

    HPAiHPA051186.
    HPA054508.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109192. 27 interactions.
    IntActiP48637. 2 interactions.
    MINTiMINT-5001027.
    STRINGi9606.ENSP00000216951.

    Structurei

    Secondary structure

    1
    474
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94
    Helixi12 – 2817
    Beta strandi32 – 343
    Beta strandi43 – 475
    Beta strandi50 – 534
    Beta strandi56 – 583
    Helixi59 – 679
    Helixi69 – 8113
    Helixi83 – 919
    Helixi93 – 964
    Helixi98 – 11316
    Beta strandi119 – 13214
    Beta strandi134 – 1363
    Beta strandi138 – 1469
    Helixi153 – 1586
    Helixi160 – 16910
    Helixi173 – 1764
    Helixi184 – 19916
    Beta strandi205 – 2095
    Helixi217 – 22812
    Turni229 – 2313
    Beta strandi234 – 2374
    Helixi239 – 2457
    Beta strandi246 – 2483
    Beta strandi254 – 2563
    Beta strandi259 – 26810
    Helixi272 – 2743
    Helixi277 – 28812
    Beta strandi289 – 2957
    Helixi297 – 3015
    Helixi305 – 3106
    Helixi316 – 3205
    Helixi325 – 3339
    Beta strandi338 – 3403
    Beta strandi342 – 3443
    Helixi345 – 35612
    Helixi358 – 3603
    Beta strandi361 – 3666
    Beta strandi369 – 3713
    Helixi376 – 38611
    Helixi390 – 3945
    Beta strandi395 – 3995
    Beta strandi406 – 4116
    Beta strandi418 – 43518
    Beta strandi438 – 45316
    Turni461 – 4644
    Beta strandi467 – 4693
    Beta strandi472 – 4743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HGSX-ray2.10A1-474[»]
    ProteinModelPortaliP48637.
    SMRiP48637. Positions 3-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48637.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni148 – 1514Substrate binding
    Regioni214 – 2163Substrate binding
    Regioni267 – 2704Substrate binding
    Regioni461 – 4622Substrate binding

    Sequence similaritiesi

    Belongs to the eukaryotic GSH synthase family.Curated

    Phylogenomic databases

    eggNOGiNOG329040.
    HOGENOMiHOG000172641.
    HOVERGENiHBG002458.
    InParanoidiP48637.
    KOiK01920.
    OMAiGWLLRSK.
    OrthoDBiEOG757CXD.
    PhylomeDBiP48637.
    TreeFamiTF105187.

    Family and domain databases

    Gene3Di1.10.1080.10. 2 hits.
    3.30.1490.50. 1 hit.
    3.30.1490.80. 2 hits.
    3.40.50.1760. 1 hit.
    InterProiIPR004887. Glutathione_synth_subst-bd_euk.
    IPR014042. Glutathione_synthase_a-hlx_euk.
    IPR014709. Glutathione_synthase_dom.
    IPR005615. Glutathione_synthase_euk.
    IPR014049. Glutathione_synthase_N_euk.
    IPR016185. PreATP-grasp_dom.
    [Graphical view]
    PANTHERiPTHR11130. PTHR11130. 1 hit.
    PfamiPF03917. GSH_synth_ATP. 1 hit.
    PF03199. GSH_synthase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001558. GSHase. 1 hit.
    SUPFAMiSSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.

    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: P48637-1) [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

    MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF    50
    TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT 100
    ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA 150
    SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG 200
    SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE DISEKGSLDQ 250
    DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ 300
    LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA 350
    IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK 400
    IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR 450
    TKAIEHADGG VAAGVAVLDN PYPV 474
    Length:474
    Mass (Da):52,385
    Last modified:February 1, 1996 - v1
    Checksum:i3C25EF7072EFE058
    GO
    Isoform 2 (identifier: P48637-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-203: Missing.

    Note: Detected in colon, kidney, lung, liver, placenta, peripheral blood and uterus, but not in heart, skeletal muscle and spleen.

    Show »
    Length:363
    Mass (Da):40,349
    Checksum:i931DA0F137EE1634
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261A → D in GSS deficiency.
    VAR_003602
    Natural varianti188 – 1881L → P in GSS deficiency; 100-fold reduction of activity.
    VAR_003603
    Natural varianti219 – 2191D → A in GSS deficiency.
    VAR_003604
    Natural varianti219 – 2191D → G in GSS deficiency. 1 Publication
    Corresponds to variant rs28938472 [ dbSNP | Ensembl ].
    VAR_003605
    Natural varianti236 – 2361R → Q.1 Publication
    Corresponds to variant rs34239729 [ dbSNP | Ensembl ].
    VAR_025047
    Natural varianti254 – 2541L → R in GSS deficiency.
    VAR_003606
    Natural varianti267 – 2671R → W in GSS deficiency. 1 Publication
    VAR_003607
    Natural varianti270 – 2701Y → C in GSS deficiency; 100-fold reduction of activity.
    VAR_003608
    Natural varianti270 – 2701Y → H in GSS deficiency; 100-fold reduction of activity.
    VAR_003609
    Natural varianti283 – 2831R → C in GSS deficiency; 10-fold reduction of activity. 1 Publication
    VAR_003610
    Natural varianti286 – 2861L → Q in GSS deficiency.
    VAR_003611
    Natural varianti330 – 3301R → C in GSS deficiency.
    Corresponds to variant rs148640446 [ dbSNP | Ensembl ].
    VAR_003612
    Natural varianti437 – 4371K → E.2 Publications
    Corresponds to variant rs34852238 [ dbSNP | Ensembl ].
    VAR_025048
    Natural varianti464 – 4641G → V in GSS deficiency.
    VAR_003613
    Natural varianti469 – 4691D → E in GSS deficiency.
    VAR_003614

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei93 – 203111Missing in isoform 2. 1 PublicationVSP_047617Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42531 mRNA. Translation: AAA69492.1.
    AB459500 mRNA. Translation: BAG75452.1.
    U34683 mRNA. Translation: AAB62390.1.
    AK312492 mRNA. Translation: BAG35394.1.
    DQ074975 Genomic DNA. Translation: AAY57328.1.
    AL133324 Genomic DNA. Translation: CAB93423.1.
    CH471077 Genomic DNA. Translation: EAW76239.1.
    CH471077 Genomic DNA. Translation: EAW76240.1.
    BC007927 mRNA. Translation: AAH07927.1.
    CCDSiCCDS13245.1. [P48637-1]
    PIRiS56748.
    RefSeqiNP_000169.1. NM_000178.2. [P48637-1]
    XP_005260463.1. XM_005260406.2. [P48637-1]
    UniGeneiHs.82327.

    Genome annotation databases

    EnsembliENST00000216951; ENSP00000216951; ENSG00000100983. [P48637-1]
    ENST00000451957; ENSP00000407517; ENSG00000100983. [P48637-2]
    GeneIDi2937.
    KEGGihsa:2937.
    UCSCiuc002xbg.3. human. [P48637-1]

    Polymorphism databases

    DMDMi1346191.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42531 mRNA. Translation: AAA69492.1 .
    AB459500 mRNA. Translation: BAG75452.1 .
    U34683 mRNA. Translation: AAB62390.1 .
    AK312492 mRNA. Translation: BAG35394.1 .
    DQ074975 Genomic DNA. Translation: AAY57328.1 .
    AL133324 Genomic DNA. Translation: CAB93423.1 .
    CH471077 Genomic DNA. Translation: EAW76239.1 .
    CH471077 Genomic DNA. Translation: EAW76240.1 .
    BC007927 mRNA. Translation: AAH07927.1 .
    CCDSi CCDS13245.1. [P48637-1 ]
    PIRi S56748.
    RefSeqi NP_000169.1. NM_000178.2. [P48637-1 ]
    XP_005260463.1. XM_005260406.2. [P48637-1 ]
    UniGenei Hs.82327.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HGS X-ray 2.10 A 1-474 [» ]
    ProteinModelPortali P48637.
    SMRi P48637. Positions 3-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109192. 27 interactions.
    IntActi P48637. 2 interactions.
    MINTi MINT-5001027.
    STRINGi 9606.ENSP00000216951.

    Chemistry

    DrugBanki DB00143. Glutathione.
    DB00145. Glycine.
    DB00151. L-Cysteine.

    PTM databases

    PhosphoSitei P48637.

    Polymorphism databases

    DMDMi 1346191.

    2D gel databases

    OGPi P48637.
    REPRODUCTION-2DPAGE IPI00010706.

    Proteomic databases

    MaxQBi P48637.
    PaxDbi P48637.
    PeptideAtlasi P48637.
    PRIDEi P48637.

    Protocols and materials databases

    DNASUi 2937.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216951 ; ENSP00000216951 ; ENSG00000100983 . [P48637-1 ]
    ENST00000451957 ; ENSP00000407517 ; ENSG00000100983 . [P48637-2 ]
    GeneIDi 2937.
    KEGGi hsa:2937.
    UCSCi uc002xbg.3. human. [P48637-1 ]

    Organism-specific databases

    CTDi 2937.
    GeneCardsi GC20M033517.
    HGNCi HGNC:4624. GSS.
    HPAi HPA051186.
    HPA054508.
    MIMi 231900. phenotype.
    266130. phenotype.
    601002. gene.
    neXtProti NX_P48637.
    Orphaneti 289846. Glutathione synthetase deficiency with 5-oxoprolinuria.
    289849. Glutathione synthetase deficiency without 5-oxoprolinuria.
    PharmGKBi PA29015.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329040.
    HOGENOMi HOG000172641.
    HOVERGENi HBG002458.
    InParanoidi P48637.
    KOi K01920.
    OMAi GWLLRSK.
    OrthoDBi EOG757CXD.
    PhylomeDBi P48637.
    TreeFami TF105187.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00210 .
    BioCyci MetaCyc:HS02174-MONOMER.
    Reactomei REACT_6960. Glutathione synthesis and recycling.
    SABIO-RK P48637.

    Miscellaneous databases

    ChiTaRSi GSS. human.
    EvolutionaryTracei P48637.
    GenomeRNAii 2937.
    NextBioi 11639.
    PROi P48637.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48637.
    Bgeei P48637.
    CleanExi HS_GSS.
    Genevestigatori P48637.

    Family and domain databases

    Gene3Di 1.10.1080.10. 2 hits.
    3.30.1490.50. 1 hit.
    3.30.1490.80. 2 hits.
    3.40.50.1760. 1 hit.
    InterProi IPR004887. Glutathione_synth_subst-bd_euk.
    IPR014042. Glutathione_synthase_a-hlx_euk.
    IPR014709. Glutathione_synthase_dom.
    IPR005615. Glutathione_synthase_euk.
    IPR014049. Glutathione_synthase_N_euk.
    IPR016185. PreATP-grasp_dom.
    [Graphical view ]
    PANTHERi PTHR11130. PTHR11130. 1 hit.
    Pfami PF03917. GSH_synth_ATP. 1 hit.
    PF03199. GSH_synthase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001558. GSHase. 1 hit.
    SUPFAMi SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR01986. glut_syn_euk. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing and expression of a cDNA for human glutathione synthetase."
      Gali R.R., Board P.G.
      Biochem. J. 310:353-358(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Alternative RNA splicing in expression of the glutathione synthetase gene in human cells."
      Uchida M., Sugaya M., Kanamaru T., Hisatomi H.
      Mol. Biol. Rep. 37:2105-2109(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. Shi Z.-Z., Galang R.L., Habib G.M., Lebovitz R.M., Lieberman M.W.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    4. "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] (ISOFORM 1), VARIANT GLU-437.
      Tissue: Substantia nigra.
    5. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-236 AND GLU-437.
    6. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lung.
    9. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 26-34; 113-125; 142-158; 222-230; 254-267; 274-283; 294-305; 419-434 AND 453-474, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Molecular basis of glutathione synthetase deficiency and a rare gene permutation event."
      Polekhina G., Board P.G., Gali R.R., Rossjohn J., Parker M.W.
      EMBO J. 18:3204-3213(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-474 IN COMPLEX WITH ADP AND GLUTATHIONE, COFACTOR, SUBUNIT.
    15. "Mutations in the glutathione synthetase gene cause 5-oxoprolinuria."
      Shi Z.-Z., Habib G.M., Rhead W.J., Gahl W.A., He X., Sazer S., Lieberman M.W.
      Nat. Genet. 14:361-365(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSS DEFICIENCY GLY-219; TRP-267 AND CYS-283.
    16. "Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction."
      Dahl N., Pigg M., Ristoff E., Gali R., Carlsson B., Mannervik B., Larsson A., Board P.
      Hum. Mol. Genet. 6:1147-1152(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSS DEFICIENCY.

    Entry informationi

    Entry nameiGSHB_HUMAN
    AccessioniPrimary (citable) accession number: P48637
    Secondary accession number(s): B2R697
    , B6F210, E1P5P9, Q4TTD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 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 20
      Human chromosome 20: 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