| IED ID | IndEnz0002013296 |
| Enzyme Type ID | protease013296 |
| Protein Name |
Ubiquitin thioesterase ZRANB1 EC 3.4.19.12 TRAF-binding domain-containing protein hTrabid Zinc finger Ran-binding domain-containing protein 1 |
| Gene Name | ZRANB1 TRABID |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSVCTYENWAKAKRCVVCDHPRPNNIEAIELAETEEASSIINEQDRARWRGSCSSGNSQRRSPPATKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE |
| Enzyme Length | 708 |
| Uniprot Accession Number | Q9UGI0 |
| Absorption | |
| Active Site | ACT_SITE 443; /note=Nucleophile; /evidence=ECO:0000269|PubMed:22157957; ACT_SITE 585; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q6GQQ9 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:33637724}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (PubMed:22157957, PubMed:23827681, PubMed:25752573, PubMed:25752577). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (PubMed:18281465). Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription (PubMed:18281465). Acts as a regulator of autophagy by mediating deubiquitination of PIK3C3/VPS34, thereby promoting autophagosome maturation (PubMed:33637724). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987). Required in the stress fiber dynamics and cell migration (PubMed:21834987). {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22157957, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:33637724}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (13); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Helix (21); Metal binding (12); Mutagenesis (16); Region (3); Repeat (2); Sequence conflict (3); Turn (6); Zinc finger (3) |
| Keywords | 3D-structure;ANK repeat;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation pathway;Wnt signaling pathway;Zinc;Zinc-finger |
| Interact With | X5D778; Q9BXS5; Q12774; Q8TBH0; Q96B67; Q8TBE0; O95696; Q13895; Q9H257-2; O95931; Q9HC52; Q96HB5; Q8IYE1; Q8N715; Q9UK58; O75419; Q99459; Q07002; Q8IVW4; Q8NE01; Q9UBL6-2; Q2TBE0; O43602-2; P26196; P59910; O60941-5; Q9UII6; Q08426; O15371; Q9H0I2; P50548; Q9NVQ4-2; Q9H5Z6-2; Q3B820; Q96MY7; Q7L5A3; Q9Y247; O95363; Q9BVV2; Q8TAE8; Q8NHY3; P55040; Q9BZE0; O95872; Q92917; P09067; P31273; Q14005-2; Q9C086; Q96PC2; Q8NA54; O75564-2; Q63ZY3; Q9HAQ2; Q9BVG8-5; Q96BZ8; Q8TAP4-4; Q8TBB1; O15481; P61326; Q96EZ8; P53582; Q8WXB1; P55081; Q8IVT4; Q9UJV3-2; Q9BU76; O15442-2; Q9P2K5-2; Q9HC98-4; Q9BRJ7; O43809; P30039; O43189; Q5T6S3; Q16512; Q494U1-3; Q96PV4; Q8WUT1; Q9UGP5-2; O15160; Q6NYC8; Q99633; O43395; Q8WWY3; Q8WXF1-2; P47897; Q86YV0; O94955; Q15287; O00560; Q96FJ0; B7ZLI8; O43463; Q9BSW7; Q96C24; Q9Y2I9-2; A6NER0; Q6DHY5; Q15560; Q8N8B7-2; Q9BT49; P35590; Q08117-2; Q8IZW8; Q9H0E2; Q9Y228; Q9BUZ4; Q9Y4K3; P0DI81-3; Q3SY00; Q9UJ04; Q5T7W7; P57075-2; P0CG48; O75604; Q9UKW4; Q14119; P19544-6; P13010; O43167; Q9UFB7; Q15973; P17021; P15622-3; Q9H9D4; Q8TAU3; Q7Z4V0; Q9ULM2; Q6ZNH5; Q9H707; Q86XF7; Q9P0T4; Q96SQ5; Q96NL3; Q9UEG4; Q5T619; Q96H86; Q96BV0; Q3KQV3; Q96EG3; P0DTD1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:25752577}. Nucleus {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:25752577}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:25752577}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3ZRH; 5AF6; |
| Mapped Pubmed ID | 15334086; 19373254; 19615732; 20711500; 22028648; 29669287; 29748601; 30686098; 33853758; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,967 |
| Kinetics | |
| Metal Binding | METAL 10; /note="Zinc 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322, ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"; METAL 13; /note="Zinc 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322, ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"; METAL 24; /note="Zinc 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322, ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"; METAL 27; /note="Zinc 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322, ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"; METAL 90; /note="Zinc 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 93; /note="Zinc 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 104; /note="Zinc 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 107; /note="Zinc 2"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 155; /note="Zinc 3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 158; /note="Zinc 3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 169; /note="Zinc 3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"; METAL 172; /note="Zinc 3"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" |
| Rhea ID | |
| Cross Reference Brenda |