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IID50007
UniprotP32499
ProteinNucleoporin NUP2
GeneNUP2
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
720
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-51 Hetero dimer : IID50012Complex
 Evidence X-RAY 2c1t D Reference
       Region 2c1t D 1-1 disorder
       Region 2c1t D 2-18 order
       Region 2c1t D 19-24 disorder
       Region 2c1t D 25-46 order
       Region 2c1t D 47-51 disorder
 Evidence X-RAY 2c1t C Reference
       Region 2c1t C 1-1 disorder
       Region 2c1t C 2-18 order
       Region 2c1t C 19-27 disorder
       Region 2c1t C 28-46 order
       Region 2c1t C 47-51 disorder
Seq 1-51 Hetero dimer : IID50012Complex
 Evidence X-RAY 1un0 D Reference
       Region 1un0 D 1-35 disorder
       Region 1un0 D 36-51 order
 Evidence X-RAY 1un0 C Reference
       Region 1un0 C 1-35 disorder
       Region 1un0 C 36-51 order
Seqdisorder 1-720
 Evidence CD¸FTIR spectroscopy¸protease sensitivity¸ gel filtration¸ sedimentation velocity Reference
       Region 1-720 disorder
SeqProS verified 2-18,25-46 These regions bind to Kap60 (yeast importin alpha) competing with NLS Hetero dimer : IID50012Complex
       Region 2c1t C 2-18 order
       Region 2c1t D 2-18 order
       Region 2c1t C 28-46 order
       Region 2c1t D 25-46 order
       Region 1-720 disorder
SeqProS verified 36-51 This region binds to Kap60 (yeast importin alpha) competing with NLS Hetero dimer : IID50012Complex
       Region 1un0 C 36-51 order
       Region 1un0 D 36-51 order
       Region 1-720 disorder
Seqphosphorylation
    590-590 Phosphothreonine
    581-581 Phosphoserine
    361-361 Phosphothreonine
    351-351 Phosphoserine
    348-348 Phosphoserine
    205-205 Phosphoserine
    203-203 Phosphoserine
    165-165 Phosphoserine
    137-137 Phosphoserine
    20-20 Phosphoserine
    17-17 Phosphoserine
 
Prediction
NeProc
Disorder 1-606
Order 607-672,677-720
ProS 1-17,40-45,117-128,568-586
AlphaFold
Disorder 1-29,31-31,39-86,133-177,179-179,181-211,216-216,221-225,227-553,555-594
Order 30-30,32-38,87-132,178-178,180-180,212-215,217-220,226-226,554-554,595-720
Pfam Hmmer
PF00638 598-718 3.7e-73
SEG 153-172 ,331-360 ,425-435 ,479-495 ,534-548
Function
Function in SwissProt
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading.