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P32929 (CGL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine gamma-lyase

EC=4.4.1.1
Alternative name(s):
Cysteine-protein sulfhydrase
Gamma-cystathionase
Gene names
Name:CTH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.12

Catalytic activity

L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate. Ref.8 Ref.12

Cofactor

Pyridoxal phosphate. Ref.8 Ref.12 Ref.14

Enzyme regulation

Inhibited by propargylglycine, trifluoroalanine and aminoethoxyvinylglycine. Ref.8 Ref.12

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 2/2.

Subunit structure

Homotetramer. Interacts with CALM in a calcium-dependent manner By similarity. Ref.8 Ref.12 Ref.14

Subcellular location

Cytoplasm.

Involvement in disease

Cystathioninuria (CSTNU) [MIM:219500]: Autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 mM for L-cystathionine Ref.8 Ref.14

KM=5.4 mM for homocysteine

KM=3.5 mM for cysteine

pH dependence:

Optimum pH is 8.2.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Cysteine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandCalmodulin-binding
Pyridoxal phosphate
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cysteine biosynthetic process

Inferred from direct assay Ref.8. Source: UniProtKB

cysteine metabolic process

Traceable author statement Ref.1. Source: ProtInc

endoplasmic reticulum unfolded protein response

Traceable author statement Ref.11. Source: UniProtKB

hydrogen sulfide biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from physical interaction Ref.12. Source: UniProtKB

protein sulfhydration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine

Inferred from direct assay Ref.12. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur amino acid catabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

transsulfuration

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionL-cysteine desulfhydrase activity

Traceable author statement. Source: Reactome

L-cystine L-cysteine-lyase (deaminating)

Inferred from mutant phenotype Ref.11. Source: UniProtKB

carbon-sulfur lyase activity

Traceable author statement. Source: Reactome

cystathionine gamma-lyase activity

Inferred from direct assay Ref.8Ref.12. Source: UniProtKB

homocysteine desulfhydrase activity

Traceable author statement. Source: Reactome

pyridoxal phosphate binding

Inferred from direct assay Ref.8Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32929-1)

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.
Isoform 2 (identifier: P32929-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-196: Missing.
Isoform 3 (identifier: P32929-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Cystathionine gamma-lyase
PRO_0000114749

Sites

Binding site621Substrate
Binding site1141Substrate
Binding site1191Substrate
Binding site3391Substrate

Amino acid modifications

Modified residue2121N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence85 – 11632Missing in isoform 3.
VSP_047274
Alternative sequence153 – 19644Missing in isoform 2.
VSP_006306
Natural variant671T → I in CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate. Ref.13 Ref.14
Corresponds to variant rs28941785 [ dbSNP | Ensembl ].
VAR_015450
Natural variant2401Q → E in CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate. Ref.13 Ref.14
Corresponds to variant rs28941786 [ dbSNP | Ensembl ].
VAR_015451
Natural variant4031S → I. Ref.1 Ref.3 Ref.4 Ref.13
Corresponds to variant rs1021737 [ dbSNP | Ensembl ].
VAR_015452

Secondary structure

........................................................................ 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 10, 2003. Version 3.
Checksum: 003246D7C1D16723

FASTA40544,508
        10         20         30         40         50         60 
MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY 

        70         80         90        100        110        120 
SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY 

       130        140        150        160        170        180 
FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG 

       190        200        210        220        230        240 
DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ 

       250        260        270        280        290        300 
NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH 

       310        320        330        340        350        360 
ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL 

       370        380        390        400 
KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS 

« Hide

Isoform 2 [UniParc].

Checksum: D6AE74B370664D23
Show »

FASTA36139,505
Isoform 3 [UniParc].

Checksum: 0A403F56C25EC633
Show »

FASTA37341,260

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC1362.
RefSeqNP_001177392.1. NM_001190463.1.
NP_001893.2. NM_001902.5.
NP_714964.2. NM_153742.4.
UniGeneHs.19904.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NMPX-ray2.60A/B/C/D1-402[»]
3COGX-ray2.00A/B/C/D1-402[»]
3ELPX-ray2.40A/B/C/D1-405[»]
ProteinModelPortalP32929.
SMRP32929. Positions 10-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107873. 8 interactions.
IntActP32929. 2 interactions.
MINTMINT-1479767.
STRING9606.ENSP00000359976.

Chemistry

DrugBankDB00151. L-Cysteine.
DB00114. Pyridoxal Phosphate.
GuidetoPHARMACOLOGY1444.

PTM databases

PhosphoSiteP32929.

Polymorphism databases

DMDM27735163.

Proteomic databases

PaxDbP32929.
PRIDEP32929.

Protocols and materials databases

DNASU1491.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346806; ENSP00000311554; ENSG00000116761. [P32929-2]
ENST00000370938; ENSP00000359976; ENSG00000116761. [P32929-1]
ENST00000411986; ENSP00000413407; ENSG00000116761. [P32929-3]
GeneID1491.
KEGGhsa:1491.
UCSCuc001dfd.3. human. [P32929-1]
uc001dfe.3. human. [P32929-2]

Organism-specific databases

CTD1491.
GeneCardsGC01P070876.
HGNCHGNC:2501. CTH.
HPAHPA021591.
HPA023300.
MIM219500. phenotype.
607657. gene.
neXtProtNX_P32929.
Orphanet212. Cystathioninuria.
PharmGKBPA27004.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0626.
HOGENOMHOG000246415.
HOVERGENHBG005322.
InParanoidP32929.
KOK01758.
OMAMQTKLIH.
OrthoDBEOG7NCV3J.
PhylomeDBP32929.
TreeFamTF300720.

Enzyme and pathway databases

BioCycMetaCyc:HS04050-MONOMER.
BRENDA4.4.1.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP32929.
UniPathwayUPA00136; UER00202.

Gene expression databases

ArrayExpressP32929.
BgeeP32929.
CleanExHS_CTH.
GenevestigatorP32929.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32929.
GenomeRNAi1491.
NextBio6127.
PROP32929.
SOURCESearch...

Entry information

Entry nameCGL_HUMAN
AccessionPrimary (citable) accession number: P32929
Secondary accession number(s): B4E1R2 expand/collapse secondary AC list , E9PDV0, Q53FB3, Q53Y79, Q9H4W7, Q9H4W8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 10, 2003
Last modified: April 16, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM