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P32929

- CGL_HUMAN

UniProt

P32929 - CGL_HUMAN

Protein

Cystathionine gamma-lyase

Gene

CTH

Organism
Homo sapiens (Human)
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 3 (10 Jan 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function.3 Publications

    Catalytic activityi

    L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate.2 Publications

    Cofactori

    Pyridoxal phosphate.3 Publications

    Enzyme regulationi

    Inhibited by propargylglycine, trifluoroalanine and aminoethoxyvinylglycine.2 Publications

    Kineticsi

    1. KM=0.5 mM for L-cystathionine2 Publications
    2. KM=5.4 mM for homocysteine2 Publications
    3. KM=3.5 mM for cysteine2 Publications

    pH dependencei

    Optimum pH is 8.2.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621Substrate
    Binding sitei114 – 1141Substrate
    Binding sitei119 – 1191Substrate
    Binding sitei339 – 3391Substrate

    GO - Molecular functioni

    1. carbon-sulfur lyase activity Source: Reactome
    2. cystathionine gamma-lyase activity Source: UniProtKB
    3. homocysteine desulfhydrase activity Source: Reactome
    4. L-cysteine desulfhydrase activity Source: Reactome
    5. L-cystine L-cysteine-lyase (deaminating) Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. cysteine biosynthetic process Source: UniProtKB
    3. cysteine metabolic process Source: ProtInc
    4. endoplasmic reticulum unfolded protein response Source: UniProtKB
    5. hydrogen sulfide biosynthetic process Source: UniProtKB
    6. negative regulation of apoptotic process Source: Ensembl
    7. negative regulation of apoptotic signaling pathway Source: Ensembl
    8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    9. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    10. protein homotetramerization Source: UniProtKB
    11. protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine Source: UniProtKB
    12. protein sulfhydration Source: UniProtKB
    13. small molecule metabolic process Source: Reactome
    14. sulfur amino acid catabolic process Source: Reactome
    15. sulfur amino acid metabolic process Source: Reactome
    16. transsulfuration Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis

    Keywords - Ligandi

    Calmodulin-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04050-MONOMER.
    BRENDAi4.4.1.1. 2681.
    ReactomeiREACT_115589. Cysteine formation from homocysteine.
    REACT_115654. Degradation of cysteine and homocysteine.
    SABIO-RKP32929.
    UniPathwayiUPA00136; UER00202.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cystathionine gamma-lyase (EC:4.4.1.1)
    Alternative name(s):
    Cysteine-protein sulfhydrase
    Gamma-cystathionase
    Gene namesi
    Name:CTH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2501. CTH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Cystathioninuria (CSTNU) [MIM:219500]: Autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671T → I in CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate. 1 Publication
    Corresponds to variant rs28941785 [ dbSNP | Ensembl ].
    VAR_015450
    Natural varianti240 – 2401Q → E in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate. 1 Publication
    Corresponds to variant rs28941786 [ dbSNP | Ensembl ].
    VAR_015451

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi219500. phenotype.
    Orphaneti212. Cystathioninuria.
    PharmGKBiPA27004.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405Cystathionine gamma-lyasePRO_0000114749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei212 – 2121N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    MaxQBiP32929.
    PaxDbiP32929.
    PRIDEiP32929.

    PTM databases

    PhosphoSiteiP32929.

    Expressioni

    Gene expression databases

    ArrayExpressiP32929.
    BgeeiP32929.
    CleanExiHS_CTH.
    GenevestigatoriP32929.

    Organism-specific databases

    HPAiHPA021591.
    HPA023300.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with CALM in a calcium-dependent manner By similarity.By similarity

    Protein-protein interaction databases

    BioGridi107873. 8 interactions.
    IntActiP32929. 2 interactions.
    MINTiMINT-1479767.
    STRINGi9606.ENSP00000359976.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 247
    Helixi29 – 313
    Beta strandi36 – 383
    Helixi66 – 7914
    Beta strandi82 – 887
    Helixi90 – 989
    Beta strandi106 – 1127
    Helixi115 – 1239
    Helixi125 – 1284
    Beta strandi131 – 1355
    Helixi140 – 1467
    Beta strandi151 – 1599
    Turni161 – 1633
    Helixi169 – 1768
    Beta strandi178 – 1803
    Beta strandi183 – 1875
    Turni189 – 1913
    Turni193 – 1953
    Turni198 – 2025
    Beta strandi204 – 2096
    Turni210 – 2156
    Beta strandi223 – 2275
    Helixi230 – 24314
    Helixi249 – 25911
    Helixi262 – 28120
    Beta strandi286 – 2905
    Helixi300 – 3067
    Beta strandi312 – 3209
    Helixi322 – 33110
    Beta strandi333 – 3375
    Beta strandi342 – 3454
    Beta strandi347 – 3493
    Turni351 – 3588
    Helixi361 – 3677
    Beta strandi373 – 3775
    Helixi383 – 39715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NMPX-ray2.60A/B/C/D1-402[»]
    3COGX-ray2.00A/B/C/D1-402[»]
    3ELPX-ray2.40A/B/C/D1-405[»]
    ProteinModelPortaliP32929.
    SMRiP32929. Positions 10-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32929.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the trans-sulfuration enzymes family.Curated

    Phylogenomic databases

    eggNOGiCOG0626.
    HOGENOMiHOG000246415.
    HOVERGENiHBG005322.
    InParanoidiP32929.
    KOiK01758.
    OMAiKTHIGHE.
    OrthoDBiEOG7NCV3J.
    PhylomeDBiP32929.
    TreeFamiTF300720.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11808. PTHR11808. 1 hit.
    PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001434. CGS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P32929-1) [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

    MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG    50
    APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL 100
    LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE 150
    TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA 200
    LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI 250
    DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH 300
    ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL 350
    PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP 400
    SGSHS 405
    Length:405
    Mass (Da):44,508
    Last modified:January 10, 2003 - v3
    Checksum:i003246D7C1D16723
    GO
    Isoform 2 (identifier: P32929-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-196: Missing.

    Show »
    Length:361
    Mass (Da):39,505
    Checksum:iD6AE74B370664D23
    GO
    Isoform 3 (identifier: P32929-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-116: Missing.

    Show »
    Length:373
    Mass (Da):41,260
    Checksum:i0A403F56C25EC633
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671T → I in CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate. 1 Publication
    Corresponds to variant rs28941785 [ dbSNP | Ensembl ].
    VAR_015450
    Natural varianti240 – 2401Q → E in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate. 1 Publication
    Corresponds to variant rs28941786 [ dbSNP | Ensembl ].
    VAR_015451
    Natural varianti403 – 4031S → I.4 Publications
    Corresponds to variant rs1021737 [ dbSNP | Ensembl ].
    VAR_015452

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei85 – 11632Missing in isoform 3. 1 PublicationVSP_047274Add
    BLAST
    Alternative sequencei153 – 19644Missing in isoform 2. 1 PublicationVSP_006306Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S52784 mRNA. Translation: AAB24700.1.
    S52028 mRNA. Translation: AAB24699.1.
    BT006882 mRNA. Translation: AAP35528.1.
    AK303946 mRNA. Translation: BAG64874.1.
    AK223376 mRNA. Translation: BAD97096.1.
    AL354872 Genomic DNA. Translation: CAC12901.1.
    AL354872 Genomic DNA. Translation: CAC12902.1.
    CH471059 Genomic DNA. Translation: EAX06450.1.
    BC015807 mRNA. Translation: AAH15807.1.
    CCDSiCCDS53333.1. [P32929-3]
    CCDS650.1. [P32929-1]
    CCDS651.1. [P32929-2]
    PIRiJC1362.
    RefSeqiNP_001177392.1. NM_001190463.1. [P32929-3]
    NP_001893.2. NM_001902.5. [P32929-1]
    NP_714964.2. NM_153742.4. [P32929-2]
    UniGeneiHs.19904.

    Genome annotation databases

    EnsembliENST00000346806; ENSP00000311554; ENSG00000116761. [P32929-2]
    ENST00000370938; ENSP00000359976; ENSG00000116761. [P32929-1]
    ENST00000411986; ENSP00000413407; ENSG00000116761. [P32929-3]
    GeneIDi1491.
    KEGGihsa:1491.
    UCSCiuc001dfd.3. human. [P32929-1]
    uc001dfe.3. human. [P32929-2]

    Polymorphism databases

    DMDMi27735163.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S52784 mRNA. Translation: AAB24700.1 .
    S52028 mRNA. Translation: AAB24699.1 .
    BT006882 mRNA. Translation: AAP35528.1 .
    AK303946 mRNA. Translation: BAG64874.1 .
    AK223376 mRNA. Translation: BAD97096.1 .
    AL354872 Genomic DNA. Translation: CAC12901.1 .
    AL354872 Genomic DNA. Translation: CAC12902.1 .
    CH471059 Genomic DNA. Translation: EAX06450.1 .
    BC015807 mRNA. Translation: AAH15807.1 .
    CCDSi CCDS53333.1. [P32929-3 ]
    CCDS650.1. [P32929-1 ]
    CCDS651.1. [P32929-2 ]
    PIRi JC1362.
    RefSeqi NP_001177392.1. NM_001190463.1. [P32929-3 ]
    NP_001893.2. NM_001902.5. [P32929-1 ]
    NP_714964.2. NM_153742.4. [P32929-2 ]
    UniGenei Hs.19904.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NMP X-ray 2.60 A/B/C/D 1-402 [» ]
    3COG X-ray 2.00 A/B/C/D 1-402 [» ]
    3ELP X-ray 2.40 A/B/C/D 1-405 [» ]
    ProteinModelPortali P32929.
    SMRi P32929. Positions 10-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107873. 8 interactions.
    IntActi P32929. 2 interactions.
    MINTi MINT-1479767.
    STRINGi 9606.ENSP00000359976.

    Chemistry

    DrugBanki DB00151. L-Cysteine.
    DB00114. Pyridoxal Phosphate.
    GuidetoPHARMACOLOGYi 1444.

    PTM databases

    PhosphoSitei P32929.

    Polymorphism databases

    DMDMi 27735163.

    Proteomic databases

    MaxQBi P32929.
    PaxDbi P32929.
    PRIDEi P32929.

    Protocols and materials databases

    DNASUi 1491.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346806 ; ENSP00000311554 ; ENSG00000116761 . [P32929-2 ]
    ENST00000370938 ; ENSP00000359976 ; ENSG00000116761 . [P32929-1 ]
    ENST00000411986 ; ENSP00000413407 ; ENSG00000116761 . [P32929-3 ]
    GeneIDi 1491.
    KEGGi hsa:1491.
    UCSCi uc001dfd.3. human. [P32929-1 ]
    uc001dfe.3. human. [P32929-2 ]

    Organism-specific databases

    CTDi 1491.
    GeneCardsi GC01P070876.
    HGNCi HGNC:2501. CTH.
    HPAi HPA021591.
    HPA023300.
    MIMi 219500. phenotype.
    607657. gene.
    neXtProti NX_P32929.
    Orphaneti 212. Cystathioninuria.
    PharmGKBi PA27004.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0626.
    HOGENOMi HOG000246415.
    HOVERGENi HBG005322.
    InParanoidi P32929.
    KOi K01758.
    OMAi KTHIGHE.
    OrthoDBi EOG7NCV3J.
    PhylomeDBi P32929.
    TreeFami TF300720.

    Enzyme and pathway databases

    UniPathwayi UPA00136 ; UER00202 .
    BioCyci MetaCyc:HS04050-MONOMER.
    BRENDAi 4.4.1.1. 2681.
    Reactomei REACT_115589. Cysteine formation from homocysteine.
    REACT_115654. Degradation of cysteine and homocysteine.
    SABIO-RK P32929.

    Miscellaneous databases

    EvolutionaryTracei P32929.
    GenomeRNAii 1491.
    NextBioi 6127.
    PROi P32929.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32929.
    Bgeei P32929.
    CleanExi HS_CTH.
    Genevestigatori P32929.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11808. PTHR11808. 1 hit.
    Pfami PF01053. Cys_Met_Meta_PP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001434. CGS. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00868. CYS_MET_METAB_PP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase."
      Lu Y., O'Dowd B.F., Orrego H., Israel Y.
      Biochem. Biophys. Res. Commun. 189:749-758(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-403.
      Tissue: Liver.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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 3), VARIANT ILE-403.
      Tissue: Trachea.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-403.
      Tissue: Kidney.
    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] (ISOFORM 1).
      Tissue: Skin.
    8. "Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration."
      Steegborn C., Clausen T., Sondermann P., Jacob U., Worbs M., Marinkovic S., Huber R., Wahl M.C.
      J. Biol. Chem. 274:12675-12684(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia."
      Chiku T., Padovani D., Zhu W., Singh S., Vitvitsky V., Banerjee R.
      J. Biol. Chem. 284:11601-11612(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "H2s-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response."
      Krishnan N., Fu C., Pappin D.J., Tonks N.K.
      Sci. Signal. 4:RA86-RA86(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CYSTEINE-PROTEIN SULFHYDRASE.
    12. "Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S."
      Sun Q., Collins R., Huang S., Holmberg-Schiavone L., Anand G.S., Tan C.-H., van-den-Berg S., Deng L.-W., Moore P.K., Karlberg T., Sivaraman J.
      J. Biol. Chem. 284:3076-3085(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-402 IN COMPLEXES WITH PYRODOXAL PHOSPHATE; NITRATE AND PROPARGYLGLYCINE, FUNCTION, SUBUNIT, ENZYME REGULATION, CATALYTIC ACTIVITY, COFACTOR.
    13. "Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)."
      Wang J., Hegele R.A.
      Hum. Genet. 112:404-408(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CSTNU ILE-67 AND GLU-240, VARIANT ILE-403.
    14. "Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase."
      Zhu W., Lin A., Banerjee R.
      Biochemistry 47:6226-6232(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CSTNU ILE-67 AND GLU-240, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiCGL_HUMAN
    AccessioniPrimary (citable) accession number: P32929
    Secondary accession number(s): B4E1R2
    , E9PDV0, Q53FB3, Q53Y79, Q9H4W7, Q9H4W8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 10, 2003
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3