| IED ID | IndEnz0002001718 |
| Enzyme Type ID | protease001718 |
| Protein Name |
E3 ubiquitin-protein ligase RNF4 EC 2.3.2.27 RING finger protein 4 RING-type E3 ubiquitin transferase RNF4 Small nuclear ring finger protein Protein SNURF |
| Gene Name | RNF4 SNURF RES4-26 |
| 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 | MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI |
| Enzyme Length | 190 |
| Uniprot Accession Number | P78317 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. {ECO:0000269|PubMed:12885770, ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:19307308, ECO:0000269|PubMed:20026589, ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20943951}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein ubiquitination. |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (4); Chain (1); Compositional bias (1); Helix (2); Modified residue (2); Motif (4); Region (3); Turn (3); Zinc finger (1) |
| Keywords | 3D-structure;Activator;Alternative splicing;Cytoplasm;DNA-binding;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Transcription;Transcription regulation;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | P60709; Q02040; A6NKF2; P15336; Q07817; Q9H0C5; Q9Y2F9; Q9NWQ9; Q96B23; Q13554-3; Q13557-8; P13500; Q9Y281; P16220; Q9UER7; O00148; Q13838; P17661; Q6ICB0; Q08426; P11474; Q13158; Q9NWS6; Q8IZU1; O75344; Q96IK5; O14964; P07910; O60812; B2RXH8; P31943; P61978-2; Q13422-7; P20839-3; Q53G59; Q5T7P3; Q5T752; Q5T753; Q5T754; O14633; Q5TA81; Q5TA82; Q5TA77; Q5TCM9; Q9BS40; Q99836; Q99801; Q9HAN9; Q96HA8; O15381-5; P22234; P57721-2; P78364; O75360; P86480; Q9BQY4; Itself; Q06455-2; Q9UQR0; Q9UH03; O75971-2; P35711-4; O43805; Q16623; P32856-2; Q12846; P63165; Q92734; Q9NVV9; Q12933; Q13114; Q9BUZ4; O00463; O00635; Q9BYV2; Q15645; Q9UHF7; Q7KZS0; Q9UMX0; Q9UHD9; Q8WUN7; O95231; Q9HCK0; Q8NCN2; Q15916; Q96K80; Q9NP64; Q96MM3; Q9NSD4; Q9P2F9; Q9H7X3; Q3KQV3; O60232 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body. Nucleus, nucleoplasm. |
| Modified Residue | MOD_RES 94; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"; MOD_RES 95; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" |
| Post Translational Modification | PTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000250}.; PTM: Autoubiquitinated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (2) |
| Cross Reference PDB | 2EA6; 2XEU; 4PPE; |
| Mapped Pubmed ID | 12351196; 12646216; 12874792; 15231748; 16954532; 17762865; 19028597; 19380586; 19489725; 19524139; 19549727; 19874575; 20379614; 20696907; 20711500; 20936779; 21252943; 21857666; 22106342; 22493164; 22635276; 22661229; 22661230; 23211528; 23504328; 23602568; 24151981; 24656128; 24714598; 24907272; 24969970; 25260751; 25355316; 25588990; 25751062; 25895136; 25948581; 25960396; 25969536; 26299341; 26450775; 26766492; 27185577; 27312341; 27653698; 27678051; 28201649; 28275011; 28414785; 28620180; 29107745; 29180619; 29634367; 29695423; 30559154; 31048496; 32197837; 32295906; 32360601; 32722882; 32733036; |
| Motif | MOTIF 36..39; /note=SUMO interaction motif 1; /evidence=ECO:0000269|PubMed:18408734; MOTIF 46..49; /note=SUMO interaction motif 2; /evidence=ECO:0000269|PubMed:18408734; MOTIF 57..59; /note=SUMO interaction motif 3; /evidence=ECO:0000269|PubMed:18408734; MOTIF 67..70; /note=SUMO interaction motif 4; /evidence=ECO:0000269|PubMed:18408734 |
| Gene Encoded By | |
| Mass | 21,319 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |