IED ID | IndEnz0002007195 |
Enzyme Type ID | protease007195 |
Protein Name |
Protein DDI1 homolog 1 EC 3.4.23.- |
Gene Name | DDI1 |
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 | MLITVYCVRRDLSEVTFSLQVSPDFELRNFKVLCEAESRVPVEEIQIIHMERLLIEDHCSLGSYGLKDGDIVVLLQKDNVGPRAPGRAPNQPRVDFSGIAVPGTSSSRPQHPGQQQQRTPAAQRSQGLASGEKVAGLQGLGSPALIRSMLLSNPHDLSLLKERNPPLAEALLSGSLETFSQVLMEQQREKALREQERLRLYTADPLDREAQAKIEEEIRQQNIEENMNIAIEEAPESFGQVTMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGVAKGVGTQRIIGRVHLAQIQIEGDFLQCSFSILEDQPMDMLLGLDMLRRHQCSIDLKKNVLVIGTTGTQTYFLPEGELPLCSRMVSGQDESSDKEITHSVMDSGRKEH |
Enzyme Length | 396 |
Uniprot Accession Number | Q8WTU0 |
Absorption | |
Active Site | ACT_SITE 260; /evidence=ECO:0000305 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by the proteinase inhibitors amprenavir, indinavir, lopinavir, isovaleryl pepstatin, ritonavir and saquinavir. {ECO:0000269|PubMed:21266539}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: Probable aspartic protease (Probable). Seems to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2 (Probable). Required, with DDI2, for cellular survival following replication stress. Together or redudantly with DDI2, removes RTF2 from stalled forks to allow cell cycle progression after replication stress and maintains genome integrity (PubMed:29290612). {ECO:0000269|PubMed:29290612, ECO:0000305|PubMed:21266539, ECO:0000305|PubMed:29290612}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (9); Chain (1); Compositional bias (2); Domain (1); Helix (5); Natural variant (3); Region (2); Sequence conflict (4); Turn (2) |
Keywords | 3D-structure;Aspartyl protease;Hydrolase;Protease;Reference proteome |
Interact With | Q9NRJ3; Q8WWM9; O14645; Q96MY7; O95872; O14901; Q9P2K6; Q6ZVX7; P20618; A0A087WYA8; Q9BUL9; P20132; Q9BXF9; Q12933; P61086; O75604 |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 3S8I; |
Mapped Pubmed ID | 16189514; 19913121; 20628086; 21516116; 25416956; 26496610; 29788202; |
Motif | |
Gene Encoded By | |
Mass | 44,124 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |