Reviewed,
UniProtKB/Swiss-Prot P49792 (RBP2_HUMAN)
Last modified
November 25, 2008.
Version 99.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: E3 SUMO-protein ligase RanBP2 Alternative name(s): Ran-binding protein 2 Nuclear pore complex protein Nup358 Nucleoporin Nup358 358 kDa nucleoporin p270 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 3224 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. 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. Could also have isomerase or chaperone activity and may bind RNA or DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. |
| Pathway | |
| Subunit structure | Forms a tight complex with RANBP1 and UBE2I. Interacts with SUMO1 but not SUMO2. Interacts with PARK2. Interacts with sumoylated RANGAP1. |
| Subcellular location | Nucleus › nuclear pore complex. Note= Cytoplasmic filaments. |
| Domain | Contains F-X-F-G repeats. |
| Post-translational modification | Polyubiquitinated by PARK2, which leads to proteasomal degradation. |
| Sequence similarities | Contains 1 PPIase cyclophilin-type domain. Contains 4 RanBD1 domains. Contains 8 RanBP2-type zinc fingers. Contains 1 TPR repeat. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PARK2 | O60260 | 6 | EBI-973138,EBI-716346 | |
| TOP2A | P11388 | 1 | EBI-973138,EBI-539628 | |
| Top2a | Q01320 | 1 | EBI-973138,EBI-642809 | From a different organism. |
| UBE2I | P63279 | 1 | EBI-973138,EBI-80168 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3224 | 3224 | E3 SUMO-protein ligase RanBP2 | PRO_0000204913 | |||||
Regions | |||||||||
| Repeat | 60 – 93 | 34 | TPR | ||||||
| Domain | 1171 – 1307 | 137 | RanBD1 1 | ||||||
| Domain | 2012 – 2148 | 137 | RanBD1 2 | ||||||
| Domain | 2309 – 2445 | 137 | RanBD1 3 | ||||||
| Repeat | 2633 – 2685 | 53 | 1 | ||||||
| Repeat | 2711 – 2761 | 51 | 2 | ||||||
| Domain | 2911 – 3046 | 136 | RanBD1 4 | ||||||
| Domain | 3067 – 3223 | 157 | PPIase cyclophilin-type | ||||||
| Zinc finger | 1351 – 1381 | 31 | RanBP2-type 1 | ||||||
| Zinc finger | 1415 – 1444 | 30 | RanBP2-type 2 | ||||||
| Zinc finger | 1479 – 1508 | 30 | RanBP2-type 3 | ||||||
| Zinc finger | 1543 – 1572 | 30 | RanBP2-type 4 | ||||||
| Zinc finger | 1606 – 1635 | 30 | RanBP2-type 5 | ||||||
| Zinc finger | 1665 – 1694 | 30 | RanBP2-type 6 | ||||||
| Zinc finger | 1724 – 1753 | 30 | RanBP2-type 7 | ||||||
| Zinc finger | 1781 – 1810 | 30 | RanBP2-type 8 | ||||||
| Region | 2631 – 2635 | 5 | Interaction with sumoylated RANGAP1 | ||||||
| Region | 2633 – 2761 | 129 | 2 X 50 AA approximate repeats | ||||||
| Region | 2633 – 2710 | 78 | Required for E3 SUMO-ligase activity | ||||||
| Region | 2633 – 2685 | 53 | Interaction with UBE2I | ||||||
| Region | 2686 – 2761 | 76 | Interaction with SUMO1 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 19 | 1 | Phosphothreonine | ||||||
| Modified residue | 21 | 1 | Phosphoserine | ||||||
| Modified residue | 394 | 1 | Phosphoserine | ||||||
| Modified residue | 779 | 1 | Phosphothreonine | ||||||
| Modified residue | 781 | 1 | Phosphoserine | ||||||
| Modified residue | 788 | 1 | Phosphoserine | ||||||
| Modified residue | 796 | 1 | Phosphoserine | ||||||
| Modified residue | 799 | 1 | Phosphothreonine | ||||||
| Modified residue | 948 | 1 | Phosphoserine | ||||||
| Modified residue | 955 | 1 | Phosphoserine | ||||||
| Modified residue | 1110 | 1 | Phosphoserine | ||||||
| Modified residue | 1144 | 1 | Phosphothreonine | ||||||
| Modified residue | 1160 | 1 | Phosphoserine | ||||||
| Modified residue | 1396 | 1 | Phosphothreonine | ||||||
| Modified residue | 1399 | 1 | Phosphothreonine | ||||||
| Modified residue | 1400 | 1 | Phosphoserine | ||||||
| Modified residue | 1412 | 1 | Phosphothreonine | ||||||
| Modified residue | 1443 | 1 | Phosphoserine | ||||||
| Modified residue | 1447 | 1 | Phosphoserine | ||||||
| Modified residue | 1456 | 1 | Phosphoserine | ||||||
| Modified residue | 1509 | 1 | Phosphoserine | ||||||
| Modified residue | 1573 | 1 | Phosphoserine | ||||||
| Modified residue | 1731 | 1 | Phosphoserine | ||||||
| Modified residue | 1869 | 1 | Phosphoserine | ||||||
| Modified residue | 2128 | 1 | Phosphothreonine | ||||||
| Modified residue | 2153 | 1 | Phosphothreonine | ||||||
| Modified residue | 2246 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2251 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2270 | 1 | Phosphoserine | ||||||
| Modified residue | 2276 | 1 | Phosphoserine | ||||||
| Modified residue | 2280 | 1 | Phosphoserine | ||||||
| Modified residue | 2290 | 1 | Phosphoserine | ||||||
| Modified residue | 2293 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2297 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2447 | 1 | Phosphoserine | ||||||
| Modified residue | 2450 | 1 | Phosphothreonine | ||||||
| Modified residue | 2454 | 1 | Phosphoserine | ||||||
| Modified residue | 2510 | 1 | Phosphoserine | ||||||
| Modified residue | 2518 | 1 | Phosphoserine | ||||||
| Modified residue | 2613 | 1 | Phosphothreonine | ||||||
| Modified residue | 2668 | 1 | Phosphoserine | ||||||
| Modified residue | 2741 | 1 | Phosphoserine | ||||||
| Modified residue | 2743 | 1 | Phosphothreonine | ||||||
| Modified residue | 2807 | 1 | Phosphoserine | ||||||
| Modified residue | 2900 | 1 | Phosphoserine | ||||||
| Modified residue | 3207 | 1 | Phosphoserine | ||||||
| Cross-link | 2592 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | |||||||
Natural variations | |||||||||
| Natural variant | 548 | 1 | V → L: dbSNP rs1057954. | VAR_029765 | |||||
| Natural variant | 580 | 1 | E → K: dbSNP rs4012065. | VAR_029766 | |||||
| Natural variant | 581 | 1 | C → Y: dbSNP rs1057957. | VAR_029767 | |||||
| Natural variant | 784 | 1 | R → K: dbSNP rs2912838. | VAR_023939 | |||||
| Natural variant | 1870 | 1 | P → L: dbSNP rs2889846. | VAR_029768 | |||||
| Natural variant | 1892 | 1 | P → A: dbSNP rs12770. | VAR_014886 | |||||
Experimental info | |||||||||
| Mutagenesis | 2632 | 1 | V → K: Abolishes interaction with sumoylated RANGAP1 | ||||||
| Mutagenesis | 2634 | 1 | I → K: Abolishes interaction with sumoylated RANGAP1 | ||||||
| Mutagenesis | 2635 | 1 | V → K: Abolishes interaction with sumoylated RANGAP1 | ||||||
| Mutagenesis | 2640 | 1 | P → A: No effect on SUMO E3 ligase activity | ||||||
| Mutagenesis | 2645 | 1 | K → A: No effect on SUMO E3 ligase activity | ||||||
| Mutagenesis | 2651 | 1 | L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity | ||||||
| Mutagenesis | 2652 | 1 | K → A: No effect on SUMO E3 ligase activity | ||||||
| Mutagenesis | 2653 | 1 | L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity | ||||||
| Mutagenesis | 2654 | 1 | P → A: Impairs SUMO E3 ligase activity | ||||||
| Mutagenesis | 2655 | 1 | P → A: No effect on SUMO E3 ligase activity | ||||||
| Mutagenesis | 2656 | 1 | T → A: Impairs SUMO E3 ligase activity | ||||||
| Mutagenesis | 2657 | 1 | F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity | ||||||
| Mutagenesis | 2658 | 1 | F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity | ||||||
| Mutagenesis | 2659 | 1 | C → S or A: Impairs SUMO E3 ligase activity | ||||||
| Mutagenesis | 2676 | 1 | D → A: Impairs SUMO E3 ligase activity | ||||||
| Mutagenesis | 2677 | 1 | F → A: Impairs SUMO E3 ligase activity | ||||||
| Mutagenesis | 2689 | 1 | Y → A: Impairs SUMO E3 ligase activity | ||||||
| Sequence conflict | 777 | 1 | H → R in AAC41758. Ref.1 | ||||||
| Sequence conflict | 2207 | 1 | S → A in AAA85838. Ref.5 | ||||||

Clusters with