SPOPL_HUMAN
ID SPOPL_HUMAN Reviewed; 392 AA.
AC Q6IQ16;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Speckle-type POZ protein-like;
DE AltName: Full=HIB homolog 2;
DE AltName: Full=Roadkill homolog 2;
GN Name=SPOPL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=16651542; DOI=10.1242/dev.02370;
RA Kent D., Bush E.W., Hooper J.E.;
RT "Roadkill attenuates Hedgehog responses through degradation of Cubitus
RT interruptus.";
RL Development 133:2001-2010(2006).
RN [3]
RP IDENTIFICATION.
RX PubMed=16740475; DOI=10.1016/j.devcel.2006.05.004;
RA Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.;
RT "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading
RT Ci/Gli transcription factor.";
RL Dev. Cell 10:719-729(2006).
RN [4]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH CUL3 AND MACROH2A1.
RX PubMed=22632832; DOI=10.1016/j.str.2012.04.009;
RA Errington W.J., Khan M.Q., Bueler S.A., Rubinstein J.L., Chakrabartty A.,
RA Prive G.G.;
RT "Adaptor protein self-assembly drives the control of a cullin-RING
RT ubiquitin ligase.";
RL Structure 20:1141-1153(2012).
CC -!- FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex that mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins, but with
CC relatively low efficiency. Cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complexes containing homodimeric SPOPL or the
CC heterodimer formed by SPOP and SPOPL are less efficient than ubiquitin
CC ligase complexes containing only SPOP. May function to down-regulate
CC the activity of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-
CC protein ligase complexes that contain SPOP.
CC {ECO:0000269|PubMed:22632832}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Heterodimer with SPOP. Component of cullin-RING-
CC based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC containing homodimeric SPOPL or the heterodimer formed by SPOP and
CC SPOPL. Interacts with CUL3 and MACROH2A1.
CC {ECO:0000269|PubMed:22632832}.
CC -!- INTERACTION:
CC Q6IQ16; P15336: ATF2; NbExp=3; IntAct=EBI-2822161, EBI-1170906;
CC Q6IQ16; Q02930-3: CREB5; NbExp=3; IntAct=EBI-2822161, EBI-10192698;
CC Q6IQ16; O15131: KPNA5; NbExp=4; IntAct=EBI-2822161, EBI-540602;
CC Q6IQ16; Q99836: MYD88; NbExp=3; IntAct=EBI-2822161, EBI-447677;
CC Q6IQ16; P28702: RXRB; NbExp=3; IntAct=EBI-2822161, EBI-748576;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR EMBL; BC071613; AAH71613.1; -; mRNA.
DR CCDS; CCDS33298.1; -.
DR RefSeq; NP_001001664.1; NM_001001664.2.
DR AlphaFoldDB; Q6IQ16; -.
DR SMR; Q6IQ16; -.
DR BioGRID; 130923; 15.
DR IntAct; Q6IQ16; 6.
DR STRING; 9606.ENSP00000280098; -.
DR iPTMnet; Q6IQ16; -.
DR PhosphoSitePlus; Q6IQ16; -.
DR BioMuta; SPOPL; -.
DR DMDM; 74736582; -.
DR EPD; Q6IQ16; -.
DR jPOST; Q6IQ16; -.
DR MassIVE; Q6IQ16; -.
DR MaxQB; Q6IQ16; -.
DR PaxDb; Q6IQ16; -.
DR PeptideAtlas; Q6IQ16; -.
DR PRIDE; Q6IQ16; -.
DR ProteomicsDB; 66471; -.
DR Antibodypedia; 33596; 139 antibodies from 21 providers.
DR DNASU; 339745; -.
DR Ensembl; ENST00000280098.9; ENSP00000280098.4; ENSG00000144228.9.
DR GeneID; 339745; -.
DR KEGG; hsa:339745; -.
DR MANE-Select; ENST00000280098.9; ENSP00000280098.4; NM_001001664.3; NP_001001664.1.
DR UCSC; uc002tvh.5; human.
DR CTD; 339745; -.
DR DisGeNET; 339745; -.
DR GeneCards; SPOPL; -.
DR HGNC; HGNC:27934; SPOPL.
DR HPA; ENSG00000144228; Low tissue specificity.
DR neXtProt; NX_Q6IQ16; -.
DR OpenTargets; ENSG00000144228; -.
DR PharmGKB; PA162404650; -.
DR VEuPathDB; HostDB:ENSG00000144228; -.
DR eggNOG; KOG1987; Eukaryota.
DR GeneTree; ENSGT00940000155953; -.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q6IQ16; -.
DR OMA; GAVMQSD; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; Q6IQ16; -.
DR TreeFam; TF313419; -.
DR PathwayCommons; Q6IQ16; -.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR SignaLink; Q6IQ16; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 339745; 13 hits in 1117 CRISPR screens.
DR ChiTaRS; SPOPL; human.
DR GenomeRNAi; 339745; -.
DR Pharos; Q6IQ16; Tdark.
DR PRO; PR:Q6IQ16; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6IQ16; protein.
DR Bgee; ENSG00000144228; Expressed in epithelial cell of pancreas and 190 other tissues.
DR ExpressionAtlas; Q6IQ16; baseline and differential.
DR Genevisible; Q6IQ16; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00917; MATH; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..392
FT /note="Speckle-type POZ protein-like"
FT /id="PRO_0000274588"
FT DOMAIN 31..161
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 200..267
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT VARIANT 45
FT /note="R -> Q (in dbSNP:rs36099753)"
FT /id="VAR_053719"
SQ SEQUENCE 392 AA; 44647 MW; CEB4243BD732DFEF CRC64;
MSREPTPPLP GDMSTGPIAE SWCYTQVKVV KFSYMWTINN FSFCREEMGE VLKSSTFSSG
PSDKMKWCLR VNPKGLDDES KDYLSLYLLL VSCPKSEVRA KFKFSLLNAK REETKAMESQ
RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGHTNTNTLK
VPECRLAEDL GNLWENTRFT DCSFFVRGQE FKAHKSVLAA RSPVFNAMFE HEMEESKKNR
VEINDLDPEV FKEMMRFIYT GRAPNLDKMA DNLLAAADKY ALERLKVMCE EALCSNLSVE
NVADTLVLAD LHSAEQLKAQ AIDFINRCSV LRQLGCKDGK NWNSNQATDI METSGWKSMI
QSHPHLVAEA FRALASAQCP QFGIPRKRLK QS
