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IID00151
 UniprotP49792
ProteinE3 SUMO-protein ligase RanBP2
GeneRANBP2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
3224
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-145 Monomer :
 Evidence X-RAY 4ga0 A Reference
       Region 4ga0 A 1-2 disorder
       Region 4ga0 A 3-145 order
Seq 1155-1321 Hetero dimer : IID00162Complex
 Evidence X-RAY 1rrp D Reference
       Region 1rrp D 1171-1304 order
 Evidence X-RAY 1rrp B Reference
       Region 1rrp B 1171-1304 order
 Evidence X-RAY 5clq D Reference
       Region 5clq D 1155-1175 disorder
       Region 5clq D 1176-1306 order
       Region 5clq D 1307-1321 disorder
 Evidence X-RAY 5clq B Reference
       Region 5clq B 1155-1172 disorder
       Region 5clq B 1173-1306 order
       Region 5clq B 1307-1321 disorder
 Evidence X-RAY 5cll D Reference
       Region 5cll D 1155-1168 disorder
       Region 5cll D 1169-1307 order
       Region 5cll D 1308-1321 disorder
 Evidence X-RAY 5cll B Reference
       Region 5cll B 1155-1168 disorder
       Region 5cll B 1169-1307 order
       Region 5cll B 1308-1321 disorder
Seqdisorder 1171-1190
 Evidence NMR Reference
       Region 1171-1190 disorder
Seqdisorder 1996-2027
 Evidence NMR Reference
       Region 1996-2027 disorder
Seq 2028-2154 Monomer :
 Evidence NMR 1xke A Reference
       Region 1xke A 2028-2154 order
       Region 1xke A 2028-2028 high_rmsd
       Region 1xke A 2152-2154 high_rmsd
Seq 2629-2695 Hetero tetramer : IID00376Complex,P63279
 Evidence X-RAY 3uio D Reference
       Region 3uio D 2631-2694 order
       Region 3uio D 2695-2695 disorder
 Evidence X-RAY 3uin D Reference
       Region 3uin D 2629-2693 order
       Region 3uin D 2694-2695 disorder
Seq 2631-2711 Hetero tetramer : IID00378Complex,P63279
 Evidence X-RAY 1z5s D Reference
       Region 1z5s D 2631-2693 order
       Region 1z5s D 2694-2711 disorder
 Evidence X-RAY 3uip D Reference
       Region 3uip D 2631-2690 order
       Region 3uip D 2691-2695 disorder
Seq 2705-2717 Hetero dimer : IID00378Complex
 Evidence NMR 2las B Reference
       Region 2las B 2705-2717 order
       Region 2las B 2705-2705 high_rmsd
Seq 2907-3050 Monomer :
 Evidence X-RAY 4l6e A Reference
       Region 4l6e A 2907-2924 disorder
       Region 4l6e A 2925-3048 order
       Region 4l6e A 3049-3050 disorder
Seq 3057-3224 Hetero dimer : P12497
 Evidence X-RAY 4lqw B Reference
       Region 4lqw B 3057-3224 order
 Evidence X-RAY 4lqw A Reference
       Region 4lqw A 3057-3224 order
Seq 3062-3224 Monomer :
 Evidence X-RAY 4i9y F Reference
       Region 4i9y F 3062-3224 order
 Evidence X-RAY 4i9y E Reference
       Region 4i9y E 3062-3224 order
 Evidence X-RAY 4i9y D Reference
       Region 4i9y D 3062-3224 order
 Evidence X-RAY 4i9y C Reference
       Region 4i9y C 3062-3224 order
 Evidence X-RAY 4i9y B Reference
       Region 4i9y B 3062-3224 order
 Evidence X-RAY 4i9y A Reference
       Region 4i9y A 3062-3224 order
SeqProS verified 1171-1190 Hetero dimer : IID00162Complex
       Region 1rrp B 1171-1304 order
       Region 1rrp D 1171-1304 order
       Region 1171-1190 disorder
Seqphosphorylation
    3207-3207 Phosphoserine
    2900-2900 Phosphoserine
    2805-2805 Phosphoserine
    2741-2741 Phosphoserine
    2743-2743 Phosphothreonine
    2668-2668 Phosphoserine
    2666-2666 Phosphotyrosine
    2613-2613 Phosphothreonine
    2526-2526 Phosphoserine
    2510-2510 Phosphoserine
    2462-2462 Phosphoserine
    2493-2493 Phosphoserine
    2297-2297 Phosphoserine
    2293-2293 Phosphothreonine
    2290-2290 Phosphoserine
    2280-2280 Phosphoserine
    2246-2246 Phosphoserine
    2251-2251 Phosphoserine
    2270-2270 Phosphoserine
    2153-2153 Phosphothreonine
    2005-2005 Phosphothreonine
    2008-2008 Phosphoserine
    1871-1871 Phosphoserine
    1835-1835 Phosphoserine
    1869-1869 Phosphoserine
    1573-1573 Phosphoserine
    1833-1833 Phosphoserine
    1520-1520 Phosphoserine
    1509-1509 Phosphoserine
    1450-1450 Phosphoserine
    1456-1456 Phosphoserine
    1412-1412 Phosphothreonine
    1443-1443 Phosphoserine
    1396-1396 Phosphothreonine
    1249-1249 Phosphoserine
    1160-1160 Phosphoserine
    1110-1110 Phosphoserine
    1144-1144 Phosphothreonine
    1107-1107 Phosphoserine
    1103-1103 Phosphoserine
    1098-1098 Phosphothreonine
    955-955 Phosphoserine
    948-948 Phosphoserine
    837-837 Phosphoserine
    788-788 Phosphoserine
    781-781 Phosphoserine
    779-779 Phosphothreonine
    21-21 Phosphoserine
    19-19 Phosphothreonine
Seqacetylation
    1977-1977 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-6,504-508,695-701,747-803,832-879,914-1170,1307-2020,2148-2306,2444-2908,3047-3071,3207-3211
Order 7-503,509-690,702-746,804-831,880-888,895-906,1171-1306,2021-2147,2307-2443,2909-3046,3072-3206,3212-3224
ProS 1-6,504-508,695-701,747-762,775-787,795-803,832-833,840-869,876-879,914-914,936-948,955-965,1032-1036,1129-1136,1166-1170,1354-1364,1418-1426,1469-1492,1497-1504,1546-1556,1563-1571,1606-1619,1624-1629,1668-1678,1685-1692,1717-1721,1726-1750,1776-1794,1799-1807,1957-1961,2008-2020,2213-2216,2223-2229,2267-2272,2476-2489,2505-2508,2608-2611,2630-2642,2655-2668,2674-2680,2686-2692,2727-2752,2848-2851,2870-2878,3047-3055,3062-3071,3207-3211
Pfam Hmmer
PF00515 60-93 9.7e-08
PF00638 1183-1304 5.1e-91
PF00641 1351-1381 2e-09
PF00641 1415-1444 1.7e-11
PF00641 1479-1508 4.5e-13
PF00641 1543-1572 1.2e-12
PF00641 1606-1635 1.5e-13
PF00641 1665-1694 1.5e-13
PF00641 1724-1753 1.6e-11
PF00641 1781-1810 2.2e-13
PF00638 2024-2145 1.4e-88
PF00638 2321-2442 1.5e-86
PF00638 2922-3043 9.6e-93
PF00160 3065-3224 5.6e-96
SEG 235-247 ,607-619 ,785-801 ,1157-1169 ,1572-1583 ,2198-2210 ,2232-2253 ,2269-2284 ,2311-2322 ,2492-2504 ,2614-2631 ,2669-2678 ,2798-2810 ,2839-2850 ,2891-2905 ,2920-2931
Function
Function in SwissProt
E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:22194619, PubMed:15931224). Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830).