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IID00191
 UniprotO95071
ProteinE3 ubiquitin-protein ligase UBR5
GeneUBR5
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
2799
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 180-230 Hetero dimer : P0CH28
 Evidence X-RAY 2qho H Reference
       Region 2qho H 180-226 order
       Region 2qho H 227-230 disorder
 Evidence X-RAY 2qho F Reference
       Region 2qho F 180-228 order
       Region 2qho F 229-230 disorder
 Evidence X-RAY 2qho D Reference
       Region 2qho D 180-226 order
       Region 2qho D 227-230 disorder
 Evidence X-RAY 2qho B Reference
       Region 2qho B 180-225 order
       Region 2qho B 226-230 disorder
Seq 2393-2453 Monomer :
 Evidence X-RAY 1i2t A Reference
       Region 1i2t A 2393-2453 order
Seq 2687-2799 Monomer :
 Evidence X-RAY 3pt3 B Reference
       Region 3pt3 B 2687-2737 order
       Region 3pt3 B 2738-2747 disorder
       Region 3pt3 B 2748-2792 order
       Region 3pt3 B 2793-2799 disorder
 Evidence X-RAY 3pt3 A Reference
       Region 3pt3 A 2687-2692 disorder
       Region 3pt3 A 2693-2737 order
       Region 3pt3 A 2738-2749 disorder
       Region 3pt3 A 2750-2792 order
       Region 3pt3 A 2793-2799 disorder
Seqphosphorylation
    2486-2486 Phosphoserine
    2484-2484 Phosphoserine
    2469-2469 Phosphoserine
    2289-2289 Phosphoserine
    2241-2241 Phosphoserine
    2213-2213 Phosphothreonine
    2076-2076 Phosphoserine
    2030-2030 Phosphothreonine
    2028-2028 Phosphoserine
    2026-2026 Phosphoserine
    1990-1990 Phosphoserine
    1969-1969 Phosphothreonine
    1780-1780 Phosphoserine
    1746-1746 Phosphotyrosine
    1741-1741 Phosphoserine
    1736-1736 Phosphothreonine
    1549-1549 Phosphoserine
    1481-1481 Phosphoserine
    1375-1375 Phosphoserine
    1355-1355 Phosphoserine
    1308-1308 Phosphoserine
    1227-1227 Phosphoserine
    1135-1135 Phosphothreonine
    1115-1115 Phosphothreonine
    1018-1018 Phosphoserine
    928-928 Phosphoserine
    808-808 Phosphoserine
    637-637 Phosphothreonine
    612-612 Phosphoserine
    578-578 Phosphoserine
    352-352 Phosphoserine
    327-327 Phosphoserine
    110-110 Phosphoserine
Seqacetylation
    2-2 N-acetylthreonine
 
Prediction
NeProc
Disorder 79-180,228-244,250-261,267-350,512-526,582-647,692-696,936-1072,1287-1318,1357-1360,1444-1453,1503-1782,1863-1918,1971-2019,2065-2180,2312-2388,2427-2434,2442-2496
Order 1-78,181-227,245-249,262-266,351-511,527-577,648-684,701-852,858-935,1073-1142,1150-1286,1319-1351,1361-1443,1454-1498,1783-1811,1814-1862,1919-1970,2020-2064,2181-2311,2389-2426,2435-2441,2497-2799
ProS 79-83,162-168,240-244,250-261,267-282,290-337,953-958,985-997,1025-1040,1287-1296,1314-1318,1503-1518,1641-1655,1688-1701,1707-1720,1741-1753,1775-1782,1863-1871,1912-1918,1971-1987,2065-2073,2091-2109,2312-2319,2357-2375,2427-2434,2442-2469
AlphaFold
Disorder 1-1,12-12,32-35,79-180,182-182,198-199,225-352,365-367,513-527,552-554,579-646,661-665,684-704,720-728,805-808,825-828,852-862,902-904,936-1079,1144-1148,1226-1227,1295-1313,1318-1318,1346-1376,1392-1394,1444-1453,1489-1490,1493-1493,1501-1501,1515-1775,1814-1814,1848-1849,1851-1852,1855-1913,1915-1916,1923-1924,1926-1944,1961-2016,2031-2037,2062-2062,2068-2184,2187-2187,2198-2199,2201-2202,2205-2209,2213-2216,2266-2270,2285-2286,2316-2367,2379-2390,2453-2499,2794-2799
Order 2-11,13-31,36-78,181-181,183-197,200-224,353-364,368-512,528-551,555-578,647-660,666-683,705-719,729-804,809-824,829-851,863-901,905-935,1080-1143,1149-1225,1228-1294,1314-1317,1319-1345,1377-1391,1395-1443,1454-1488,1491-1492,1494-1500,1502-1514,1776-1813,1815-1847,1850-1850,1853-1854,1914-1914,1917-1922,1925-1925,1945-1960,2017-2030,2038-2061,2063-2067,2185-2186,2188-2197,2200-2200,2203-2204,2210-2212,2217-2265,2271-2284,2287-2315,2368-2378,2391-2452,2500-2793
Pfam Hmmer
PF02207 1177-1244 7.1e-26
PF00658 2375-2449 5.4e-25
PF00632 2486-2799 3.3e-105
SEG 129-156 ,213-224 ,227-236 ,282-323 ,614-628 ,933-950 ,970-999 ,1138-1151 ,1396-1405 ,1524-1537 ,1567-1602 ,1641-1657 ,1662-1687 ,1726-1742 ,1759-1789 ,1879-1890 ,1972-1983 ,1986-1999 ,2076-2081 ,2329-2366 ,2420-2438 ,2489-2500 ,2776-2794
Function
Function in SwissProt
E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.