ubiquitin-like protein ATG12 [Mus musculus]
ubiquitin-like protein ATG12( domain architecture ID 10108002)
ubiquitin-like protein ATG12 is involved in autophagy vesicle formation and is localized at the developing autophagosome
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Ubl_ATG12 | cd01612 | ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ... |
55-140 | 7.11e-55 | |||
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like (Ubl) proteins such as ATG12 protein have a conserved Ubl fold structure and undergo a unique Ubl conjugation, a process essential for autophagosome formation. ATG12 is conjugated to ATG5 by multistep modifications of the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG10. The ATG12-ATG5 conjugate facilitates the lipidation of ATG8 and directs its correct subcellular localization. ATG12 is localized at the developing autophagosome. : Pssm-ID: 340454 Cd Length: 86 Bit Score: 166.54 E-value: 7.11e-55
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Ubl_ATG12 | cd01612 | ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ... |
55-140 | 7.11e-55 | |||
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like (Ubl) proteins such as ATG12 protein have a conserved Ubl fold structure and undergo a unique Ubl conjugation, a process essential for autophagosome formation. ATG12 is conjugated to ATG5 by multistep modifications of the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG10. The ATG12-ATG5 conjugate facilitates the lipidation of ATG8 and directs its correct subcellular localization. ATG12 is localized at the developing autophagosome. Pssm-ID: 340454 Cd Length: 86 Bit Score: 166.54 E-value: 7.11e-55
|
|||||||
APG12 | pfam04110 | Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ... |
55-141 | 2.43e-53 | |||
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy. Pssm-ID: 397985 Cd Length: 87 Bit Score: 162.97 E-value: 2.43e-53
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Ubl_ATG12 | cd01612 | ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an ... |
55-140 | 7.11e-55 | |||
ubiquitin-like (Ubl) domain found in autophagy-related protein 12 (ATG12); Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like (Ubl) proteins such as ATG12 protein have a conserved Ubl fold structure and undergo a unique Ubl conjugation, a process essential for autophagosome formation. ATG12 is conjugated to ATG5 by multistep modifications of the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG10. The ATG12-ATG5 conjugate facilitates the lipidation of ATG8 and directs its correct subcellular localization. ATG12 is localized at the developing autophagosome. Pssm-ID: 340454 Cd Length: 86 Bit Score: 166.54 E-value: 7.11e-55
|
|||||||
APG12 | pfam04110 | Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of ... |
55-141 | 2.43e-53 | |||
Ubiquitin-like autophagy protein Apg12; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. The Apg12 system is one of the ubiquitin-like protein conjugation systems conserved in eukaryotes. It was first discovered in yeast during systematic analyses of the apg mutants defective in autophagy. Covalent attachment of Apg12-Apg5 is essential for autophagy. Pssm-ID: 397985 Cd Length: 87 Bit Score: 162.97 E-value: 2.43e-53
|
|||||||
Ubl_Autophagy_like | cd01611 | ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein; Autophagy is an ... |
55-136 | 6.83e-37 | |||
ubiquitin-like (Ubl) domain found in autophagy-related ubiquitin-like protein; Autophagy is an essential intracellular process that targets large protein complexes, bacterial pathogens, and organelles for degradation. The autophagy-related ubiquitin-like proteins, such as Saccharomyces cerevisiae Atg8p, undergo a unique ubiquitin-like (Ubl) conjugation, a process essential for autophagosome formation. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. ATG8 family proteins undergo multistep modifications by the E1-like (ubiquitin activating) enzyme ATG7, and the E2-like (ubiquitin conjugating) enzyme ATG3. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa). Pssm-ID: 340453 Cd Length: 84 Bit Score: 121.00 E-value: 6.83e-37
|
|||||||
Ubl_ATG8_like | cd16108 | ubiquitin-like (Ubl) domain found in autophagy-related 8 (ATG8) and similar proteins; The ATG8 ... |
65-135 | 9.31e-04 | |||
ubiquitin-like (Ubl) domain found in autophagy-related 8 (ATG8) and similar proteins; The ATG8 family of proteins constitute a single member in Saccharomyces cerevisiae, Atg8p, and multiple homologs in higher eukaryotes, they are multifunctional ubiquitin-like (Ubl) key regulators of autophagy. The ATG8 system is a Ubl conjugation system that is essential for autophagosome formation. In the ATG8 system, a cysteine protease (ATG4) cleaves a C-terminal arginine from ATG8, and then the exposed C-terminal glycine is conjugated to phosphatidylethanolamine (PE) by ATG7, an E1-like enzyme, and ATG3, an E2-like enzyme. The mammalian ATG8 family is classified into three subfamilies: i) MAP1LC3 (microtubule associated protein 1 light chain 3) which includes MAP1LC3A, MAP1LC3B, MAP1LC3B2, and MAP1LC3C, ii) GABARAP (GABA type A receptor associated protein) which includes GABARAP, GABARAPL1, and GABARAPL3, and iii) GABARAPL2 (GABA type A receptor associated protein like 2), also known as GATE-16 (golgi-associated adenosine triphosphatase enhancer of 16 kDa). Pssm-ID: 340525 Cd Length: 85 Bit Score: 36.02 E-value: 9.31e-04
|
|||||||
ATG8 | pfam02991 | Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a ... |
58-141 | 1.35e-03 | |||
Autophagy protein Atg8 ubiquitin like; Light chain 3 is proposed to function primarily as a subunit of microtubule associated proteins 1A and 1B and that its expression may regulate microtubule binding activity. Autophagy is generally known as a process involved in the degradation of bulk cytoplasmic components that are non-specifically sequestered into an autophagosome, where they are sequestered into double-membrane vesicles and delivered to the degradative organelle, the lysosome/vacuole, for breakdown and eventual recycling of the resulting macromolecules. The yeast proteins are involved in the autophagosome, and Atg8 binds Atg19, via its N-terminus and the C-terminus of Atg19. Pssm-ID: 281049 Cd Length: 104 Bit Score: 36.18 E-value: 1.35e-03
|
|||||||
Blast search parameters | ||||
|