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P32929

- CGL_HUMAN

UniProt

P32929 - CGL_HUMAN

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Protein

Cystathionine gamma-lyase

Gene

CTH

Organism
Homo sapiens (Human)
Status
Reviewed - 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 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. 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
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: 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
Complete GO annotation...

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

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. 12 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.
GeneTreeiENSGT00390000000312.
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

        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. 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. 12 interactions.
IntActi P32929. 2 interactions.
MINTi MINT-1479767.
STRINGi 9606.ENSP00000359976.

Chemistry

DrugBanki DB00151. L-Cysteine.
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.
GeneTreei ENSGT00390000000312.
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

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

« 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. "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 29, 2014
This is version 152 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