Gamma-glutamylaminecyclotransferase
Details
- Name
- Gamma-glutamylaminecyclotransferase
- Kind
- protein
- Synonyms
- 4.3.2.8
- A2LD1
- AIG2-like domain-containing protein 1
- Gamma-glutamylamine cyclotransferase
- GGACT
- Gene Name
- GGACT
- UniProtKB Entry
- Q9BVM4Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0009542|Gamma-glutamylaminecyclotransferase MALVFVYGTLKRGQPNHRVLRDGAHGSAAFRARGRTLEPYPLVIAGEHNIPWLLHLPGSG RLVEGEVYAVDERMLRFLDDFESCPALYQRTVLRVQLLEDRAPGAEEPPAPTAVQCFVYS RATFPPEWAQLPHHDSYDSEGPHGLRYNPRENR
- Number of residues
- 153
- Molecular Weight
- 17328.44
- Theoretical pI
- Not Available
- GO Classification
- Functionsgamma-glutamylaminecyclotransferase activityComponentscytosol
- General Function
- Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine
- Specific Function
- Gamma-glutamylaminecyclotransferase activity
- Pfam Domain Function
- GGACT (PF06094)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0013222|Gamma-glutamylaminecyclotransferase (GGACT) ATGGCCCTAGTCTTCGTGTACGGCACCCTGAAGCGGGGTCAGCCCAACCACAGGGTCCTG CGGGACGGCGCCCACGGCTCCGCAGCCTTTCGGGCGCGCGGCCGCACGCTGGAGCCCTAC CCGTTGGTGATCGCGGGGGAGCACAACATCCCGTGGCTGCTGCACCTGCCCGGCTCGGGG CGCCTCGTGGAGGGCGAGGTCTACGCGGTAGACGAGCGGATGCTGCGCTTTCTGGATGAC TTCGAGAGTTGCCCGGCCCTGTACCAGCGCACGGTGCTGCGGGTACAGCTGCTGGAGGAC CGGGCCCCGGGCGCAGAGGAGCCGCCAGCGCCCACCGCGGTGCAGTGCTTCGTGTACAGC AGGGCCACCTTCCCGCCGGAGTGGGCCCAGCTCCCGCACCATGACAGCTACGACTCCGAG GGGCCGCACGGGCTGCGCTACAACCCCCGGGAGAACAGATAA
- Chromosome Location
- 13
- Locus
- 13q32.3
- External Identifiers
Resource Link UniProtKB ID Q9BVM4 UniProtKB Entry Name GGACT_HUMAN GeneCard ID GGACT HGNC ID HGNC:25100 PDB ID(s) 3JUB, 3JUC, 3JUD KEGG ID hsa:87769 NCBI Gene ID 87769 - General References
- 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
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- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Oakley AJ, Coggan M, Board PG: Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism. J Biol Chem. 2010 Mar 26;285(13):9642-8. doi: 10.1074/jbc.M109.082099. Epub 2010 Jan 28. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Formic acid experimental, investigational unknown target Details