Search Keyword:


Search option:


IID01032
 UniprotQ9Y2U9
ProteinKelch domain-containing protein 2
GeneKLHDC2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
406
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-362 Hetero tetramer : Q9BQE4
 Evidence X-RAY 6do4 A Reference
       Region 6do4 A 1-26 disorder
       Region 6do4 A 27-52 order
       Region 6do4 A 53-60 disorder
       Region 6do4 A 61-125 order
       Region 6do4 A 126-127 disorder
       Region 6do4 A 128-167 order
       Region 6do4 A 168-169 disorder
       Region 6do4 A 170-183 order
       Region 6do4 A 184-185 disorder
       Region 6do4 A 186-359 order
       Region 6do4 A 360-362 disorder
 Evidence X-RAY 6do4 B Reference
       Region 6do4 B 1-26 disorder
       Region 6do4 B 27-52 order
       Region 6do4 B 53-60 disorder
       Region 6do4 B 61-124 order
       Region 6do4 B 125-128 disorder
       Region 6do4 B 129-183 order
       Region 6do4 B 184-186 disorder
       Region 6do4 B 187-359 order
       Region 6do4 B 360-362 disorder
Seq 1-362 Hetero tetramer : Q9Y6D0
 Evidence X-RAY 6do3 A Reference
       Region 6do3 A 1-26 disorder
       Region 6do3 A 27-52 order
       Region 6do3 A 53-60 disorder
       Region 6do3 A 61-123 order
       Region 6do3 A 124-129 disorder
       Region 6do3 A 130-184 order
       Region 6do3 A 185-186 disorder
       Region 6do3 A 187-359 order
       Region 6do3 A 360-362 disorder
 Evidence X-RAY 6do3 B Reference
       Region 6do3 B 1-27 disorder
       Region 6do3 B 28-52 order
       Region 6do3 B 53-60 disorder
       Region 6do3 B 61-123 order
       Region 6do3 B 124-129 disorder
       Region 6do3 B 130-185 order
       Region 6do3 B 186-186 disorder
       Region 6do3 B 187-359 order
       Region 6do3 B 360-362 disorder
Seq 1-362 Hetero tetramer : O94782
 Evidence X-RAY 6do5 A Reference
       Region 6do5 A 1-26 disorder
       Region 6do5 A 27-52 order
       Region 6do5 A 53-60 disorder
       Region 6do5 A 61-125 order
       Region 6do5 A 126-127 disorder
       Region 6do5 A 128-167 order
       Region 6do5 A 168-169 disorder
       Region 6do5 A 170-183 order
       Region 6do5 A 184-185 disorder
       Region 6do5 A 186-359 order
       Region 6do5 A 360-362 disorder
 Evidence X-RAY 6do5 B Reference
       Region 6do5 B 1-26 disorder
       Region 6do5 B 27-52 order
       Region 6do5 B 53-60 disorder
       Region 6do5 B 61-73 order
       Region 6do5 B 74-74 disorder
       Region 6do5 B 75-124 order
       Region 6do5 B 125-127 disorder
       Region 6do5 B 128-167 order
       Region 6do5 B 168-169 disorder
       Region 6do5 B 170-183 order
       Region 6do5 B 184-186 disorder
       Region 6do5 B 187-359 order
       Region 6do5 B 360-362 disorder
Seq 1-362 Homo dimer :
 Evidence X-RAY 8pif A Reference
       Region 8pif A 1-27 disorder
       Region 8pif A 28-52 order
       Region 8pif A 53-60 disorder
       Region 8pif A 61-124 order
       Region 8pif A 125-127 disorder
       Region 8pif A 128-167 order
       Region 8pif A 168-169 disorder
       Region 8pif A 170-183 order
       Region 8pif A 184-186 disorder
       Region 8pif A 187-359 order
       Region 8pif A 360-362 disorder
 Evidence X-RAY 8pif B Reference
       Region 8pif B 1-26 disorder
       Region 8pif B 27-52 order
       Region 8pif B 53-60 disorder
       Region 8pif B 61-124 order
       Region 8pif B 125-127 disorder
       Region 8pif B 128-167 order
       Region 8pif B 168-170 disorder
       Region 8pif B 171-183 order
       Region 8pif B 184-186 disorder
       Region 8pif B 187-359 order
       Region 8pif B 360-362 disorder
Seq 1-406 Hetero hexamer : Q15369,Q15370
 Evidence X-RAY 8ebn A Reference
       Region 8ebn A 1-26 disorder
       Region 8ebn A 27-53 order
       Region 8ebn A 54-59 disorder
       Region 8ebn A 60-379 order
       Region 8ebn A 380-391 disorder
       Region 8ebn A 392-406 order
 Evidence X-RAY 8ebn B Reference
       Region 8ebn B 1-26 disorder
       Region 8ebn B 27-122 order
       Region 8ebn B 123-128 disorder
       Region 8ebn B 129-167 order
       Region 8ebn B 168-171 disorder
       Region 8ebn B 172-178 order
       Region 8ebn B 179-187 disorder
       Region 8ebn B 188-236 order
       Region 8ebn B 237-240 disorder
       Region 8ebn B 241-406 order
Seq 15-361 Hetero tetramer : IID00933Complex
 Evidence X-RAY 8ebl A Reference
       Region 8ebl A 15-24 disorder
       Region 8ebl A 25-359 order
       Region 8ebl A 360-361 disorder
 Evidence X-RAY 8ebl B Reference
       Region 8ebl B 15-26 disorder
       Region 8ebl B 27-359 order
       Region 8ebl B 360-361 disorder
Seq 15-361 Hetero tetramer :
 Evidence X-RAY 8ebm A Reference
       Region 8ebm A 15-26 disorder
       Region 8ebm A 27-53 order
       Region 8ebm A 54-60 disorder
       Region 8ebm A 61-124 order
       Region 8ebm A 125-127 disorder
       Region 8ebm A 128-359 order
       Region 8ebm A 360-361 disorder
 Evidence X-RAY 8ebm B Reference
       Region 8ebm B 15-26 disorder
       Region 8ebm B 27-53 order
       Region 8ebm B 54-60 disorder
       Region 8ebm B 61-359 order
       Region 8ebm B 360-361 disorder
SeqProS predicted 404-406 This region is predicted to be disordered by NeProc and AlphaFold (pLDDT < 68.5). Hetero hexamer : Q15369,Q15370
       Region 8ebn A 392-406 order
       Region 8ebn B 241-406 order
 
Prediction
NeProc
Disorder 1-5,404-406
Order 6-403
ProS 1-5,404-406
AlphaFold
Disorder 1-26,54-59,399-406
Order 27-53,60-398
Function
Function in SwissProt
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948, PubMed:29775578, PubMed:30526872). The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms (PubMed:29779948, PubMed:29775578, PubMed:30526872). The CRL2(KLHDC2) complex specifically recognizes proteins with a diglycine (Gly-Gly) at the C-terminus, leading to their ubiquitination and degradation (PubMed:29779948, PubMed:29775578, PubMed:30526872). The CRL2(KLHDC2) complex mediates ubiquitination and degradation of truncated SELENOK and SELENOS selenoproteins produced by failed UGA/Sec decoding, which end with a diglycine (PubMed:26138980, PubMed:30526872). The CRL2(KLHDC2) complex also recognizes proteolytically cleaved proteins ending with Gly-Gly, such as the N-terminal fragment of USP1, leading to their degradation (PubMed:29775578, PubMed:30526872). May also act as an indirect repressor of CREB3-mediated transcription by interfering with CREB3-DNA-binding (PubMed:11384994).