about
Glutaredoxin 5POP5 homolog, ribonuclease P/MRP subunitNADH:ubiquinone oxidoreductase subunit AB1Lipoic acid synthetaseLipoyl(octanoyl) transferase 2Lipoyltransferase 1Glycine cleavage system protein HNeuronatinLipoyl synthase CTL0821Lipoyl synthase CT_558Glutaredoxin 5NADH:ubiquinone oxidoreductase subunit AB1Lipoyl synthase BU269Lipoyltransferase BU268Lipoate-protein ligase B FTT_1031Lipoate-protein ligase A FTT_0690cLipoyl synthase FTT_0653Lipoyl synthase PA3996Lipoyl synthase TTHA0239Lipoate-protein ligase B TTHA0240Glycine cleavage system protein H (aminomethyl carrier)Lipoyltransferase 1Lipoyl(octanoyl) transferase 2 (putative)Lipoic acid synthetaseProcessing of precursor 5, ribonuclease P/MRP family (S. cerevisiae)Lipoate-protein ligase A ECIAI39_4918Lipoyl synthase ECIAI39_0603Lipoate-protein ligase B ECIAI39_0605lipoyl synthase Rv2218octanoyltransferase Rv2217Lipoyl synthase NGO0793Lipoate-protein ligase B NMB1217Lipoyl synthase NMB1216Lipoyl synthase TDE1575Lipoyltransferase and lipoate-protein ligase TDE1551Lipoyltransferase and lipoate-protein ligase TDE2647Octanoyltransferase PP_4801Lipoyltransferase lpg1511Lipoyl synthase lpg0745lipoate-protein ligase B FTT_1031
P682
Cloning of human neuronatin gene and its localization to chromosome-20q 11.2-12: the deduced protein is a novel "proteolipid'The glycine cleavage system: structure of a cDNA encoding human H-protein, and partial characterization of its gene in patients with hyperglycinemiasVariant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5
P921
Q21103167-10706504-F2FD-40FB-8472-FB9713273807Q21114130-39AFFE6C-3F2D-42D1-9806-8120C0D3F3C7Q21115295-EC432B1A-7DAB-40F7-826B-C177C7D41F10Q21118637-B82B26E6-DC7D-4318-94D9-9AD8D1BEB39EQ21118637-D3F58762-46D1-4DE4-8127-79EAC517680DQ21120776-307B2647-5393-4D27-ADD2-3FE6180611CDQ21120788-238FCA3E-5455-4F02-A440-5BB965BF3BB7Q21120788-FD3619AC-18FB-453A-8BD0-01BCB763020EQ21131508-BB7BD6D2-1A5A-4667-A493-9964B9846CB1Q21133213-3E3CE32F-F6B3-417A-A26D-67A4A8FFFA64Q21172461-C206B21A-F65B-4DF3-A75A-302F1789447BQ21174487-0B93E89B-E4EB-4972-B10A-C9B337C2D52AQ21174487-1FA5B7D4-EFC9-44B7-B9DF-025FA2AED80EQ21174487-42E7BA2F-D649-4453-BADA-F5EADCD43F69Q21495762-59EA338C-039B-4C74-88BA-B7EC1617D5A4Q21498792-2EC1664A-784C-4932-9B20-9D7CDC91036BQ21599534-15EBB640-18F3-45E9-A2E6-4E52C0613EFCQ21599904-9433AA17-301E-4463-97FA-1E3776E71DA8Q21630303-1D04B0D7-12EC-4DAE-88A9-B62BF5DDF695Q21630596-9A578368-BE2E-4F07-BE5C-67D0D40DAA32Q21631801-6CD699D5-4FEE-492C-A1FE-858054238DA1Q21762820-54B52EE9-F9A0-46BD-A6F2-5ADFE970AAC2Q21762820-D7AF1AED-3DD5-4F72-A7C9-221CC812DDDAQ21762820-DDFBEEBB-DFF1-408E-82C1-FA5B984055C3Q21766803-D4659007-6D0C-487F-B6A2-78BE5F898A8BQ21766966-545A194D-B6F1-430C-B9C0-E047F9E1580FQ21984261-3DEECCC9-BA7F-474A-86EF-5F8C3C33D576Q21984644-4BFA2E77-A43A-47B7-B937-979FEF8D9FE8Q21984644-E369B9C7-21CD-4890-90F4-E91ECD8023CBQ21984645-86F8ED05-FE67-4FF8-9709-6FBF54FABBC3Q21985099-BE248A8F-9617-468D-85B8-BCF9604FE539Q21985099-EBE09BFB-1562-4FE9-8A7F-5C0F150B078EQ21989386-B69EF255-96FC-4782-BE0E-5677249C0676Q22136211-174E6208-183E-48DF-BB72-0D57178749DFQ22136612-DD1F6983-48B0-48C7-9DA6-E9396043C1ACQ22162080-BC761139-4ED3-430D-814B-5E0C34940B0FQ22233429-486C8FA0-AC99-46A4-8E92-3309E21D880CQ22233429-94A7A084-106B-446B-9FFD-73598CFB2A66Q22233429-F2D20AF9-ED80-440B-9648-24F4B06B1A80Q22234964-961F0B0D-0FD0-454B-A881-52B177BEB810
P682
description
The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine.
@en
biologisch proces
@nl
name
protein lipoylation
@en
type
label
protein lipoylation
@en
altLabel
GO:0009249
@en
peptidyl-lysine lipoylation
@en
protein-lipoic acid cofactor linkage
@en
prefLabel
protein lipoylation
@en
P279
P2888
P686
GO:0009249