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P48507

- GSH0_HUMAN

UniProt

P48507 - GSH0_HUMAN

Protein

Glutamate--cysteine ligase regulatory subunit

Gene

GCLM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Pathwayi

    GO - Molecular functioni

    1. glutamate-cysteine ligase activity Source: Ensembl
    2. glutamate-cysteine ligase catalytic subunit binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: Ensembl
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. cysteine metabolic process Source: Ensembl
    4. glutamate metabolic process Source: UniProtKB
    5. glutathione biosynthetic process Source: UniProtKB
    6. glutathione derivative biosynthetic process Source: Reactome
    7. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    8. negative regulation of neuron apoptotic process Source: Ensembl
    9. positive regulation of glutamate-cysteine ligase activity Source: Ensembl
    10. regulation of blood vessel size Source: UniProtKB
    11. regulation of mitochondrial depolarization Source: Ensembl
    12. response to drug Source: UniProtKB
    13. response to nitrosative stress Source: Ensembl
    14. response to oxidative stress Source: UniProtKB
    15. small molecule metabolic process Source: Reactome
    16. sulfur amino acid metabolic process Source: Reactome
    17. xenobiotic metabolic process Source: Reactome

    Keywords - Biological processi

    Glutathione biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000023909-MONOMER.
    BRENDAi6.3.2.2. 2681.
    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_6960. Glutathione synthesis and recycling.
    UniPathwayiUPA00142; UER00209.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--cysteine ligase regulatory subunit
    Alternative name(s):
    GCS light chain
    Gamma-ECS regulatory subunit
    Gamma-glutamylcysteine synthetase regulatory subunit
    Glutamate--cysteine ligase modifier subunit
    Gene namesi
    Name:GCLM
    Synonyms:GLCLR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4312. GCLM.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. glutamate-cysteine ligase complex Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    MIMi601176. gene+phenotype.
    PharmGKBiPA28613.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 274274Glutamate--cysteine ligase regulatory subunitPRO_0000192573Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei263 – 2631N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48507.
    PaxDbiP48507.
    PeptideAtlasiP48507.
    PRIDEiP48507.

    2D gel databases

    OGPiP48507.

    PTM databases

    PhosphoSiteiP48507.

    Expressioni

    Tissue specificityi

    In all tissues examined. Highest levels in skeletal muscle.

    Gene expression databases

    ArrayExpressiP48507.
    BgeeiP48507.
    CleanExiHS_GCLM.
    GenevestigatoriP48507.

    Organism-specific databases

    HPAiCAB009568.
    CAB040554.
    HPA023696.
    HPA053656.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic heavy chain and a regulatory light chain.

    Protein-protein interaction databases

    BioGridi108992. 10 interactions.
    IntActiP48507. 3 interactions.
    STRINGi9606.ENSP00000359258.

    Structurei

    3D structure databases

    ProteinModelPortaliP48507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0656.
    HOGENOMiHOG000007111.
    HOVERGENiHBG005923.
    InParanoidiP48507.
    KOiK11205.
    OMAiWRLEWVL.
    OrthoDBiEOG7B5WWG.
    PhylomeDBiP48507.
    TreeFamiTF105986.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF51430. SSF51430. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P48507-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTDSRAAKA LLARARTLHL QTGNLLNWGR LRKKCPSTHS EELHDCIQKT    50
    LNEWSSQINP DLVREFPDVL ECTVSHAVEK INPDEREEMK VSAKLFIVES 100
    NSSSSTRSAV DMACSVLGVA QLDSVIIASP PIEDGVNLSL EHLQPYWEEL 150
    ENLVQSKKIV AIGTSDLDKT QLEQLYQWAQ VKPNSNQVNL ASCCVMPPDL 200
    TAFAKQFDIQ LLTHNDPKEL LSEASFQEAL QESIPDIQAH EWVPLWLLRY 250
    SVIVKSRGII KSKGYILQAK RRGS 274
    Length:274
    Mass (Da):30,727
    Last modified:February 1, 1996 - v1
    Checksum:i88F73E22322E40B2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091I → M.1 Publication
    Corresponds to variant rs17880087 [ dbSNP | Ensembl ].
    VAR_021063

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35546 mRNA. Translation: AAA65028.1.
    CR541833 mRNA. Translation: CAG46632.1.
    AY773965 Genomic DNA. Translation: AAV28733.1.
    AK290449 mRNA. Translation: BAF83138.1.
    AL049796, AL117351 Genomic DNA. Translation: CAI21813.1.
    AL117351, AL049796 Genomic DNA. Translation: CAI22976.1.
    CH471097 Genomic DNA. Translation: EAW73060.1.
    CH471097 Genomic DNA. Translation: EAW73061.1.
    BC041809 mRNA. Translation: AAH41809.1.
    CCDSiCCDS746.1.
    PIRiJC2474.
    RefSeqiNP_002052.1. NM_002061.2.
    UniGeneiHs.315562.

    Genome annotation databases

    EnsembliENST00000370238; ENSP00000359258; ENSG00000023909.
    GeneIDi2730.
    KEGGihsa:2730.
    UCSCiuc001dqg.1. human.

    Polymorphism databases

    DMDMi1346188.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35546 mRNA. Translation: AAA65028.1 .
    CR541833 mRNA. Translation: CAG46632.1 .
    AY773965 Genomic DNA. Translation: AAV28733.1 .
    AK290449 mRNA. Translation: BAF83138.1 .
    AL049796 , AL117351 Genomic DNA. Translation: CAI21813.1 .
    AL117351 , AL049796 Genomic DNA. Translation: CAI22976.1 .
    CH471097 Genomic DNA. Translation: EAW73060.1 .
    CH471097 Genomic DNA. Translation: EAW73061.1 .
    BC041809 mRNA. Translation: AAH41809.1 .
    CCDSi CCDS746.1.
    PIRi JC2474.
    RefSeqi NP_002052.1. NM_002061.2.
    UniGenei Hs.315562.

    3D structure databases

    ProteinModelPortali P48507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108992. 10 interactions.
    IntActi P48507. 3 interactions.
    STRINGi 9606.ENSP00000359258.

    Chemistry

    DrugBanki DB00151. L-Cysteine.
    DB00142. L-Glutamic Acid.

    PTM databases

    PhosphoSitei P48507.

    Polymorphism databases

    DMDMi 1346188.

    2D gel databases

    OGPi P48507.

    Proteomic databases

    MaxQBi P48507.
    PaxDbi P48507.
    PeptideAtlasi P48507.
    PRIDEi P48507.

    Protocols and materials databases

    DNASUi 2730.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370238 ; ENSP00000359258 ; ENSG00000023909 .
    GeneIDi 2730.
    KEGGi hsa:2730.
    UCSCi uc001dqg.1. human.

    Organism-specific databases

    CTDi 2730.
    GeneCardsi GC01M094351.
    HGNCi HGNC:4312. GCLM.
    HPAi CAB009568.
    CAB040554.
    HPA023696.
    HPA053656.
    MIMi 601176. gene+phenotype.
    neXtProti NX_P48507.
    PharmGKBi PA28613.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOGENOMi HOG000007111.
    HOVERGENi HBG005923.
    InParanoidi P48507.
    KOi K11205.
    OMAi WRLEWVL.
    OrthoDBi EOG7B5WWG.
    PhylomeDBi P48507.
    TreeFami TF105986.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00209 .
    BioCyci MetaCyc:ENSG00000023909-MONOMER.
    BRENDAi 6.3.2.2. 2681.
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_6960. Glutathione synthesis and recycling.

    Miscellaneous databases

    ChiTaRSi GCLM. human.
    GeneWikii GCLM.
    GenomeRNAii 2730.
    NextBioi 10760.
    PROi P48507.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48507.
    Bgeei P48507.
    CleanExi HS_GCLM.
    Genevestigatori P48507.

    Family and domain databases

    Gene3Di 3.20.20.100. 1 hit.
    InterProi IPR023210. NADP_OxRdtase_dom.
    [Graphical view ]
    Pfami PF00248. Aldo_ket_red. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51430. SSF51430. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of the cDNA for the light subunit of human liver gamma-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues."
      Gipp J.J., Bailey H.H., Mulcahy R.T.
      Biochem. Biophys. Res. Commun. 206:584-589(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "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].
    3. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-209.
    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].
      Tissue: Brain.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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.
    8. "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-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGSH0_HUMAN
    AccessioniPrimary (citable) accession number: P48507
    Secondary accession number(s): A8K334
    , D3DT45, Q6FHC1, Q9NPX9, Q9NU74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 128 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3