| Tag | Content |
|---|
| CPLM ID | CPLM-023014 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Gamma-glutamyltransferase 7 |
Protein Synonyms/Alias | GGT 7; Gamma-glutamyltransferase-like 3; Gamma-glutamyltransferase-like 5; Gamma-glutamyltranspeptidase 7; Glutathione hydrolase 7; Gamma-glutamyltransferase 7 heavy chain; Gamma-glutamyltransferase 7 light chain |
Gene Name | GGT7 |
Gene Synonyms/Alias | GGTL3; GGTL5 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 225 | LQRSWETKPGLLVGV | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Cleaves glutathione conjugates (By similarity). |
Sequence Annotation | MOD_RES 83 83 Phosphoserine (By similarity).
CARBOHYD 198 198 N-linked (GlcNAc...) (Potential).
CARBOHYD 267 267 N-linked (GlcNAc...) (Potential).
CARBOHYD 283 283 N-linked (GlcNAc...) (Potential).
CARBOHYD 330 330 N-linked (GlcNAc...) (Potential).
CARBOHYD 353 353 N-linked (GlcNAc...) (Potential).
CARBOHYD 394 394 N-linked (GlcNAc...) (Potential).
CARBOHYD 452 452 N-linked (GlcNAc...) (Potential).
CARBOHYD 519 519 N-linked (GlcNAc...) (Potential).
CARBOHYD 523 523 N-linked (GlcNAc...) (Potential).
CARBOHYD 586 586 N-linked (GlcNAc...) (Potential). |
Keyword | Acyltransferase; Alternative splicing; Complete proteome; Glutathione biosynthesis; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 662 AA |
Protein Sequence | MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS 60
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG 120
VTVALVMQIY FGDPQIFQQG AVVTDAARCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH 180
SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREETLQR SWETKPGLLV GVPGMVKGLH 240
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLARALAEQL PPNMSERFRE TFLPSGRPPL 300
PGSLLHRPDL AEVLDVLGTS GPAAFYAGGN LTLEMVAEAQ HAGGVITEED FSNYSALVEK 360
PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS 420
RLGDPVYDST ITESMDDMLS KVEAAYLRGH INDSQAAPAP LLPVYELDGA PTAAQVLIMG 480
PDDFIVAMVS SLNQPFGSGL ITPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL 540
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL 600
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIAVKD PRSPDAAGAT 660
IL 662 |
Gene Ontology | GO:0031362; C:anchored to external side of plasma membrane; TAS:UniProtKB. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0003840; F:gamma-glutamyltransferase activity; TAS:UniProtKB. GO:0036374; F:glutathione hydrolase activity; IEA:EC. GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW. GO:0006749; P:glutathione metabolic process; TAS:UniProtKB. GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |