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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

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. 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 signaling pathway Source: Ensembl
  7. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  8. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  9. protein homotetramerization Source: UniProtKB
  10. protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine Source: UniProtKB
  11. protein sulfhydration Source: UniProtKB
  12. small molecule metabolic process Source: Reactome
  13. sulfur amino acid catabolic process Source: Reactome
  14. sulfur amino acid metabolic process Source: Reactome
  15. 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

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. 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.
GenevestigatoriP32929.

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. 17 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
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.
OMAiIVHKHGD.
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. [P32929-1]
ENST00000411986; ENSP00000413407; ENSG00000116761. [P32929-3]
GeneIDi1491.
KEGGihsa:1491.
UCSCiuc001dfd.3. human. [P32929-1]
uc001dfe.3. human. [P32929-2]

Polymorphism and mutation databases

BioMutaiCTH.

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. 17 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. [P32929-1]
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.
OMAiIVHKHGD.
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.
GenevestigatoriP32929.

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: April 29, 2015
This is version 157 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.