SPOP
entrez
8405
canonical
uniprot
O43791
canonical
ensembl
ENSG00000121067
resolver
ensp
ENSP00000240327
resolver
ensp
ENSP00000377001
resolver
ensp
ENSP00000420908
resolver
ensp
ENSP00000424119
resolver
ensp
ENSP00000425905
resolver
ensp
ENSP00000426986
resolver
ensp
ENSP00000499562
resolver
ensp
ENSP00000524728
resolver
ensp
ENSP00000524729
resolver
ensp
ENSP00000524730
resolver
ensp
ENSP00000524731
resolver
ensp
ENSP00000524732
resolver
ensp
ENSP00000524733
resolver
ensp
ENSP00000600059
resolver
ensp
ENSP00000640811
resolver
ensp
ENSP00000640812
resolver
ensp
ENSP00000640813
resolver
ensp
ENSP00000640814
resolver
ensp
ENSP00000640815
resolver
ensp
ENSP00000640817
resolver
ensp
ENSP00000640818
resolver
ensp
ENSP00000640819
resolver
ensp
ENSP00000640820
resolver
ensp
ENSP00000640821
resolver
ensp
ENSP00000640822
resolver
ensp
ENSP00000640823
resolver
ensp
ENSP00000640824
resolver
ensp
ENSP00000640825
resolver
ensp
ENSP00000640826
resolver
ensp
ENSP00000640827
resolver
ensp
ENSP00000640828
resolver
ensp
ENSP00000640829
resolver
ensp
ENSP00000640830
resolver
ensp
ENSP00000640831
resolver
ensp
ENSP00000640832
resolver
ensp
ENSP00000640833
resolver
enst
ENST00000347630
resolver
enst
ENST00000393328
resolver
enst
ENST00000503676
resolver
enst
ENST00000504102
resolver
enst
ENST00000509079
resolver
enst
ENST00000514121
resolver
enst
ENST00000665825
resolver
enst
ENST00000854669
resolver
enst
ENST00000854670
resolver
enst
ENST00000854671
resolver
enst
ENST00000854672
resolver
enst
ENST00000854673
resolver
enst
ENST00000854674
resolver
enst
ENST00000930000
resolver
enst
ENST00000970752
resolver
enst
ENST00000970753
resolver
enst
ENST00000970754
resolver
enst
ENST00000970755
resolver
enst
ENST00000970756
resolver
enst
ENST00000970758
resolver
enst
ENST00000970759
resolver
enst
ENST00000970760
resolver
enst
ENST00000970761
resolver
enst
ENST00000970762
resolver
enst
ENST00000970763
resolver
enst
ENST00000970764
resolver
enst
ENST00000970765
resolver
enst
ENST00000970766
resolver
enst
ENST00000970767
resolver
enst
ENST00000970768
resolver
enst
ENST00000970769
resolver
enst
ENST00000970770
resolver
enst
ENST00000970771
resolver
enst
ENST00000970772
resolver
enst
ENST00000970773
resolver
enst
ENST00000970774
resolver
genesymbol
SPOP
resolver
hgnc
HGNC:11254
resolver
uniprot
B2R6S3
resolver
uniprot
D3DTW7
resolver
uniprot
Q53HJ1
resolver
uniprot_entry
SPOP_HUMAN
resolver
uniprot_sec
B2R6S3
resolver
uniprot_sec
D3DTW7
resolver
uniprot_sec
Q53HJ1
resolver
amino_acid_sequence
MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS
uniprot
proteins
disease_involvement
DISEASE: Nabais Sa-de Vries syndrome 1 (NSDVS1) [MIM:618828]: An autosomal dominant disorder characterized by global developmental delay, impaired intellectual development, speech delay, and variable behavioral abnormalities. Affected individuals show congenital microcephaly and dysmorphic facial features, including round face, small palpebral fissures, highly arched eyebrows, and short nose. {ECO:0000269|PubMed:32109420}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Nabais Sa-de Vries syndrome 2 (NSDVS2) [MIM:618829]: An autosomal dominant disorder characterized by global developmental delay apparent from birth, impaired intellectual development, speech delay, dysmorphic facial features, and additional anomalies including congenital heart defects, sleep disturbances, hypotonia, and variable endocrine abnormalities. {ECO:0000269|PubMed:32109420}. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability (PubMed:32109420). Plays an essential role for proper translation, but not for their degradation, of critical DNA replication licensing factors CDT1 and CDC6, thereby participating in DNA synthesis and cell proliferation (PubMed:36791496). Regulates interferon regulatory factor 1/IRF1 proteasomal turnover by targeting S/T-rich degrons in IRF1 (PubMed:37622993). Facilitates the lysosome-dependent degradation of enterovirus EV71 protease 2A by inducing its 'Lys-48'-linked polyubiquitination, which ultimately restricts EV71 replication (PubMed:37796126). Acts as an antiviral factor also against hepatitis B virus/HBV by promoting ubiquitination and subsequent degradation of HNF1A (PubMed:38018242). In turn, inhibits HBV transcription and replication by preventing HNF1A stimulating activity of HBV preS1 promoter and enhancer II (PubMed:38018242). Involved in ubiquitination of BRDT and promotes its degradation, thereby regulates histone removal in early condensing spermatids prior to histone-to-protamine exchange (By similarity). {ECO:0000250|UniProtKB:Q6ZWS8, ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:19818708, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:32109420, ECO:0000269|PubMed:37622993, ECO:0000269|PubMed:37796126, ECO:0000269|PubMed:38018242}.
uniprot
proteins
mass_dalton
42132
uniprot
proteins
mutagenesis
MUTAGEN 87; /note="Y->A: Strongly reduced affinity for substrate proteins."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 123; /note="Y->A: Strongly reduced affinity for substrate proteins."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 130; /note="D->A: Strongly reduced affinity for substrate proteins."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 131; /note="W->A: Strongly reduced affinity for substrate proteins."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 133; /note="F->A: Strongly reduced affinity for substrate proteins."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 186; /note="L->D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 190; /note="L->D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 193; /note="L->D: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex."; /evidence="ECO:0000269|PubMed:19818708"; MUTAGEN 217; /note="I->K: Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex."; /evidence="ECO:0000269|PubMed:19818708
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:19818708, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:32109420}.
uniprot
proteins
protein_family
Tdpoz family
uniprot
proteins
pubmed
14528312
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15240113
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15897469
uniprot
proteins
pubmed
16524876
uniprot
proteins
pubmed
16651542
uniprot
proteins
pubmed
16740475
uniprot
proteins
pubmed
19818708
uniprot
proteins
pubmed
22085717
uniprot
proteins
pubmed
22632832
uniprot
proteins
pubmed
32109420
uniprot
proteins
pubmed
36791496
uniprot
proteins
pubmed
37622993
uniprot
proteins
pubmed
37796126
uniprot
proteins
pubmed
38018242
uniprot
proteins
pubmed
9414087
uniprot
proteins
sequence_length
374
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:37622993, ECO:0000269|PubMed:38018242}. Nucleus speckle {ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9414087}. Cytoplasm {ECO:0000269|PubMed:38018242}.
uniprot
proteins