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Database: UniProt
Entry: Q498E8_XENLA
LinkDB: Q498E8_XENLA
Original site: Q498E8_XENLA 
ID   Q498E8_XENLA            Unreviewed;       858 AA.
AC   Q498E8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Cullin 4B S homeolog {ECO:0000313|RefSeq:NP_001090088.1};
DE   SubName: Full=MGC115611 protein {ECO:0000313|EMBL:AAI00245.1};
GN   Name=cul4b.S {ECO:0000313|RefSeq:NP_001090088.1,
GN   ECO:0000313|Xenbase:XB-GENE-963634};
GN   Synonyms=cul4b {ECO:0000313|RefSeq:NP_001090088.1,
GN   ECO:0000313|Xenbase:XB-GENE-963634}, MGC115611
GN   {ECO:0000313|EMBL:AAI00245.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI00245.1};
RN   [1] {ECO:0000313|RefSeq:NP_001090088.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI00245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte {ECO:0000313|EMBL:AAI00245.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001090088.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC       {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC       ECO:0000256|RuleBase:RU003829}.
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DR   EMBL; BC100244; AAI00245.1; -; mRNA.
DR   RefSeq; NP_001090088.1; NM_001096619.1.
DR   DNASU; 735163; -.
DR   GeneID; 735163; -.
DR   KEGG; xla:735163; -.
DR   AGR; Xenbase:XB-GENE-963634; -.
DR   CTD; 735163; -.
DR   Xenbase; XB-GENE-963634; cul4b.S.
DR   OrthoDB; 21270at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 735163; Expressed in blastula and 19 other cell types or tissues.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR045093; Cullin.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR036317; Cullin_homology_sf.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11932; CULLIN; 1.
DR   PANTHER; PTHR11932:SF66; CULLIN-4B; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF74788; Cullin repeat-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   2: Evidence at transcript level;
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          503..731
FT                   /note="Cullin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50069"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  99075 MW;  EF9BBDAB0C643B62 CRC64;
     MKDLVASPSG QSKQGLSSPN PPAQEVRTEG NSTSKKRRLN ISSSDKDDLD PLSPARNSSS
     SSNHIQKKLR FEDTLDFLGL DVKMTEESSS SSSCSFSSTP QAVRSKNLLI SPVGVGHHAN
     GLTKASPVSS FANSKPGSAK KLVIKNFKDK PKLPENYTDE TWQKLKGTVE AIQNSTSIKY
     NLEELYQAVE NLCSYKISAN LYKQLRQICE DHIKAQIHQF REDSLDSVLF LKKIDKCWKD
     HCRQMIMIRS IFLFLDRTYV LQNSMLPSIW DMGLELFRTH IISDQKVQNK TIDGILLLIE
     RERNGEAIDR SLLRSLLSML SDLQIYQDSF EQRFLEETNR LYSAEGQRLM QEREVPEYLH
     HVNKRLEEEA DRVITYLDQS TQKPLIATVE KQLLGEHLTA TLQKGLNHLL DENRIQDLSL
     LYQLFSRVRG GVQVLLQHWI EYIKAFGSTI VINPEKDKTM VQELLDFKDK VDHVIDVCFL
     KNEKFVNAMK EAFETFINKR PNKPAELIAK HVDSKLRTGN KEATDEELEK MLDKIMIIFR
     FIYGKDVFEA FYKKDLAKRL LVGKSASVDA EKSMLSKLKH ECGAAFTSKL EGMFKDMELS
     KDIMVHFKQY MQNQNVPGNI ELTVNILTMG YWPTYVPMEV LLPPEMVKLQ EIFKTFYLGK
     HSGRKLQWQS TLGQCVLKAE FNEGRKELQV SLFQTLVLLM FNEGDEFSLE EIRQATGIED
     SELRRTLQSL ACGRARVLVK NPKSKDVDDG DKFTFNDDFR HQLFRIRINQ IQMKETVEEQ
     ASTTERVFQD RQYQIDAAIV RIMKMRKTLT HNLLVSEVYN QLKFPVKPAD LKKRIESLID
     RDYMERDKEN PNQYNYVA
//
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