WSB1_MOUSE
ID WSB1_MOUSE Reviewed; 421 AA.
AC O54927;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=WD repeat and SOCS box-containing protein 1;
DE Short=WSB-1;
GN Name=Wsb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss;
RX PubMed=9419338; DOI=10.1073/pnas.95.1.114;
RA Hilton D.J., Richardson R.T., Alexander W.S., Viney E.M., Willson T.A.,
RA Sprigg N.S., Starr R., Nicholson S.E., Metcalf D., Nicola N.A.;
RT "Twenty proteins containing a C-terminal SOCS box form five structural
RT classes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:114-119(1998).
RN [2]
RP INTERACTION WITH DIO2.
RX PubMed=15965468; DOI=10.1038/ncb1272;
RA Dentice M., Bandyopadhyay A., Gereben B., Callebaut I.,
RA Christoffolete M.A., Kim B.W., Nissim S., Mornon J.P., Zavacki A.M.,
RA Zeold A., Capelo L.P., Curcio-Morelli C., Ribeiro R., Harney J.W.,
RA Tabin C.J., Bianco A.C.;
RT "The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid
RT hormone activation and PTHrP secretion in the developing growth plate.";
RL Nat. Cell Biol. 7:698-705(2005).
CC -!- FUNCTION: Probable substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins. Recognizes type II iodothyronine deiodinase/DIO2.
CC Confers constitutive instability to HIPK2 through proteasomal
CC degradation (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DIO2. Component of the probable ECS(WSB1) E3
CC ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2,
CC Elongin BC complex and WSB1. Component of a probable ECS-like E3
CC ubiquitin-protein ligase complex which contains CUL5, RBX1, Elongin BC
CC complex and WSB1. Interacts with CUL5, RNF7, ELOB and ELOC. Binds to
CC HIPK2 through WD40 repeats (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin ligase
CC complexes. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF033186; AAB96647.1; -; mRNA.
DR CCDS; CCDS25118.1; -.
DR RefSeq; NP_062627.3; NM_019653.3.
DR AlphaFoldDB; O54927; -.
DR SMR; O54927; -.
DR BioGRID; 219684; 15.
DR IntAct; O54927; 7.
DR STRING; 10090.ENSMUSP00000017821; -.
DR iPTMnet; O54927; -.
DR PhosphoSitePlus; O54927; -.
DR PaxDb; O54927; -.
DR PRIDE; O54927; -.
DR ProteomicsDB; 299775; -.
DR Antibodypedia; 1139; 156 antibodies from 23 providers.
DR DNASU; 78889; -.
DR Ensembl; ENSMUST00000017821; ENSMUSP00000017821; ENSMUSG00000017677.
DR GeneID; 78889; -.
DR KEGG; mmu:78889; -.
DR UCSC; uc007kki.1; mouse.
DR CTD; 26118; -.
DR MGI; MGI:1926139; Wsb1.
DR VEuPathDB; HostDB:ENSMUSG00000017677; -.
DR eggNOG; KOG0266; Eukaryota.
DR GeneTree; ENSGT00890000139406; -.
DR HOGENOM; CLU_056876_0_0_1; -.
DR InParanoid; O54927; -.
DR OMA; YVWDPHT; -.
DR OrthoDB; 805365at2759; -.
DR PhylomeDB; O54927; -.
DR TreeFam; TF329216; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 78889; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Wsb1; mouse.
DR PRO; PR:O54927; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O54927; protein.
DR Bgee; ENSMUSG00000017677; Expressed in embryonic brain and 266 other tissues.
DR ExpressionAtlas; O54927; baseline and differential.
DR Genevisible; O54927; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0140454; P:protein aggregate center assembly; IDA:MGI.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF07525; SOCS_box; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50225; SOCS; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..421
FT /note="WD repeat and SOCS box-containing protein 1"
FT /id="PRO_0000051458"
FT REPEAT 124..165
FT /note="WD 1"
FT REPEAT 168..208
FT /note="WD 2"
FT REPEAT 212..251
FT /note="WD 3"
FT REPEAT 254..293
FT /note="WD 4"
FT REPEAT 309..346
FT /note="WD 5"
FT DOMAIN 372..421
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
SQ SEQUENCE 421 AA; 47065 MW; 4003D1FFE7A9A2EF CRC64;
MASFPPRVNE KEIVRSRTIG ELLAPAAPFD KKCGGENWTV AFAPDGSYFA WSQGYRIVKL
VPWSQCRKNF LLHGSKNVTN SSCLKLARQN SNGGQKNKPP EHVIDCGDIV WSLAFGSSVP
EKQSRCVNIE WHRFRFGQDQ LLLATGLNNG RIKIWDVYTG KLLLNLVDHI EMVRDLTFAP
DGSLLLVSAS RDKTLRVWDL KDDGNMVKVL RAHQNWVYSC AFSPDCSMLC SVGASKAVFL
WNMDKYTMIR KLEGHHHDVV ACDFSPDGAL LATASYDTRV YVWDPHNGDL LMEFGHLFPS
PTPIFAGGAN DRWVRAVSFS HDGLHVASLA DDKMVRFWRI DEDCPVQVAP LSNGLCCAFS
TDGSVLAAGT HDGSVYFWAT PRQVPSLQHI CRMSIRRVMS TQEVQKLPVP SKILAFLSYR
G
