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Protein

Cystathionine gamma-lyase

Gene

CTH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 5'-phosphate3 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

    Pathway:iL-cysteine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Cystathionine beta-synthase (CBS)
    2. Cystathionine gamma-lyase (CTH)
    This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

    Sites

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

    GO - Molecular functioni

    • carbon-sulfur lyase activity Source: Reactome
    • cystathionine gamma-lyase activity Source: UniProtKB
    • homocysteine desulfhydrase activity Source: Reactome
    • L-cysteine desulfhydrase activity Source: Reactome
    • L-cystine L-cysteine-lyase (deaminating) Source: UniProtKB
    • pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    • cellular nitrogen compound metabolic process Source: Reactome
    • cysteine biosynthetic process Source: UniProtKB
    • cysteine metabolic process Source: ProtInc
    • endoplasmic reticulum unfolded protein response Source: UniProtKB
    • hydrogen sulfide biosynthetic process Source: UniProtKB
    • negative regulation of apoptotic signaling pathway Source: Ensembl
    • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    • positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    • protein homotetramerization Source: UniProtKB
    • protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine Source: UniProtKB
    • protein sulfhydration Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • sulfur amino acid catabolic process Source: Reactome
    • sulfur amino acid metabolic process Source: Reactome
    • transsulfuration Source: Reactome
    Complete GO annotation...

    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 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2501. CTH.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • nucleoplasm Source: HPA
    • nucleus Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Cystathioninuria (CSTNU)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAutosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.

    See also OMIM:219500
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671T → I in CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate. 2 Publications
    Corresponds to variant rs28941785 [ dbSNP | Ensembl ].
    VAR_015450
    Natural varianti240 – 2401Q → E in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate. 2 Publications
    Corresponds to variant rs28941786 [ dbSNP | Ensembl ].
    VAR_015451

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi219500. phenotype.
    Orphaneti212. Cystathioninuria.
    PharmGKBiPA27004.

    Chemistry

    DrugBankiDB00151. L-Cysteine.

    Polymorphism and mutation databases

    BioMutaiCTH.
    DMDMi27735163.

    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

    BgeeiP32929.
    CleanExiHS_CTH.
    GenevisibleiP32929. HS.

    Organism-specific databases

    HPAiHPA021591.
    HPA023300.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GUCD1Q96NT33EBI-749763,EBI-8293751
    RECKQ6P9E23EBI-749763,EBI-10253121
    WDYHV1Q96HA83EBI-749763,EBI-741158

    Protein-protein interaction databases

    BioGridi107873. 16 interactions.
    IntActiP32929. 5 interactions.
    MINTiMINT-1479767.
    STRINGi9606.ENSP00000359976.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 247Combined sources
    Helixi29 – 313Combined sources
    Beta strandi36 – 383Combined sources
    Turni61 – 633Combined sources
    Helixi66 – 7914Combined sources
    Beta strandi82 – 887Combined sources
    Helixi90 – 989Combined sources
    Beta strandi106 – 1127Combined sources
    Helixi115 – 1239Combined sources
    Helixi125 – 1284Combined sources
    Beta strandi131 – 1355Combined sources
    Helixi140 – 1467Combined sources
    Beta strandi151 – 1599Combined sources
    Turni161 – 1633Combined sources
    Helixi169 – 1768Combined sources
    Beta strandi178 – 1803Combined sources
    Beta strandi183 – 1875Combined sources
    Turni189 – 1913Combined sources
    Turni193 – 1953Combined sources
    Turni198 – 2025Combined sources
    Beta strandi204 – 2096Combined sources
    Turni210 – 2156Combined sources
    Beta strandi223 – 2275Combined sources
    Helixi230 – 24314Combined sources
    Helixi249 – 25911Combined sources
    Helixi262 – 28120Combined sources
    Beta strandi286 – 2905Combined sources
    Helixi300 – 3067Combined sources
    Beta strandi312 – 3209Combined sources
    Helixi322 – 33110Combined sources
    Beta strandi333 – 3375Combined sources
    Beta strandi342 – 3454Combined sources
    Beta strandi347 – 3493Combined sources
    Turni351 – 3588Combined sources
    Helixi361 – 3677Combined sources
    Beta strandi373 – 3775Combined sources
    Helixi383 – 39715Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    GeneTreeiENSGT00390000000312.
    HOGENOMiHOG000246415.
    HOVERGENiHBG005322.
    InParanoidiP32929.
    KOiK01758.
    OMAiEKHFENG.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG
    60 70 80 90 100
    APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL
    110 120 130 140 150
    LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE
    160 170 180 190 200
    TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA
    210 220 230 240 250
    LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI
    260 270 280 290 300
    DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH
    310 320 330 340 350
    ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL
    360 370 380 390 400
    PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP

    SGSHS
    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. 2 Publications
    Corresponds to variant rs28941785 [ dbSNP | Ensembl ].
    VAR_015450
    Natural varianti240 – 2401Q → E in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate. 2 Publications
    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:
    EMBLi
    GenBanki
    DDBJi
    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.
    ENST00000411986; ENSP00000413407; ENSG00000116761. [P32929-3]
    GeneIDi1491.
    KEGGihsa:1491.
    UCSCiuc001dfd.3. human. [P32929-1]
    uc001dfe.3. human. [P32929-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    BioGridi107873. 16 interactions.
    IntActiP32929. 5 interactions.
    MINTiMINT-1479767.
    STRINGi9606.ENSP00000359976.

    Chemistry

    BindingDBiP32929.
    DrugBankiDB00151. L-Cysteine.
    GuidetoPHARMACOLOGYi1444.

    PTM databases

    PhosphoSiteiP32929.

    Polymorphism and mutation databases

    BioMutaiCTH.
    DMDMi27735163.

    Proteomic databases

    MaxQBiP32929.
    PaxDbiP32929.
    PRIDEiP32929.

    Protocols and materials databases

    DNASUi1491.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi1491.
    GeneCardsiGC01P070876.
    HGNCiHGNC:2501. CTH.
    HPAiHPA021591.
    HPA023300.
    MIMi219500. phenotype.
    607657. gene.
    neXtProtiNX_P32929.
    Orphaneti212. Cystathioninuria.
    PharmGKBiPA27004.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0626.
    GeneTreeiENSGT00390000000312.
    HOGENOMiHOG000246415.
    HOVERGENiHBG005322.
    InParanoidiP32929.
    KOiK01758.
    OMAiEKHFENG.
    OrthoDBiEOG7NCV3J.
    PhylomeDBiP32929.
    TreeFamiTF300720.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSiCTH. human.
    EvolutionaryTraceiP32929.
    GenomeRNAii1491.
    NextBioi6127.
    PROiP32929.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP32929.
    CleanExiHS_CTH.
    GenevisibleiP32929. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "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.
    14. "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.
    15. "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: July 22, 2015
    This is version 160 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.