ID A0A6I8Q566_XENTR Unreviewed; 891 AA.
AC A0A6I8Q566;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN Name=cblb {ECO:0000313|Ensembl:ENSXETP00000067627,
GN ECO:0000313|RefSeq:XP_012812208.1,
GN ECO:0000313|Xenbase:XB-GENE-1018102};
GN Synonyms=cblb-a {ECO:0000313|RefSeq:XP_012812208.1}, cblb-b
GN {ECO:0000313|RefSeq:XP_012812208.1}, rnf56
GN {ECO:0000313|RefSeq:XP_012812208.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000067627};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000067627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000067627};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000067627}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2020) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_012812208.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012812208.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012812208.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC specific E2 ubiquitin-conjugating enzymes, and transfers it to
CC substrates, generally promoting their degradation by the proteasome.
CC {ECO:0000256|ARBA:ARBA00003573, ECO:0000256|RuleBase:RU367001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367001};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367001}.
CC -!- SUBUNIT: Interacts with several SH3 domain-containing proteins and with
CC poly-ubiquitinated proteins. {ECO:0000256|ARBA:ARBA00064467}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB)
CC domain, a short linker region and the RING-type zinc finger. The PTB
CC domain, which is also called TKB (tyrosine kinase binding) domain, is
CC composed of three different subdomains: a four-helix bundle (4H), a
CC calcium-binding EF hand and a divergent SH2 domain.
CC {ECO:0000256|RuleBase:RU367001}.
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DR RefSeq; XP_012812208.1; XM_012956754.3.
DR DNASU; 448509; -.
DR Ensembl; ENSXETT00000066610; ENSXETP00000067627; ENSXETG00000016127.
DR GeneID; 448509; -.
DR AGR; Xenbase:XB-GENE-1018102; -.
DR CTD; 868; -.
DR Xenbase; XB-GENE-1018102; cblb.
DR OrthoDB; 7237699at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Bgee; ENSXETG00000016127; Expressed in ovary and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR CDD; cd16708; RING-HC_Cbl; 1.
DR CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR CDD; cd14392; UBA_Cbl-b; 1.
DR FunFam; 1.10.238.10:FF:000022; E3 ubiquitin-protein ligase CBL; 1.
DR FunFam; 1.20.930.20:FF:000001; E3 ubiquitin-protein ligase CBL; 1.
DR FunFam; 3.30.40.10:FF:000015; E3 ubiquitin-protein ligase CBL; 1.
DR FunFam; 3.30.505.10:FF:000154; E3 ubiquitin-protein ligase CBL; 1.
DR FunFam; 1.10.8.10:FF:000037; E3 ubiquitin-protein ligase CBL-B isoform B; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024162; Adaptor_Cbl.
DR InterPro; IPR014741; Adaptor_Cbl_EF_hand-like.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR003153; Adaptor_Cbl_N_hlx.
DR InterPro; IPR014742; Adaptor_Cbl_SH2-like.
DR InterPro; IPR024159; Cbl_PTB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23007; CBL; 1.
DR PANTHER; PTHR23007:SF3; E3 UBIQUITIN-PROTEIN LIGASE CBL-B; 1.
DR Pfam; PF02262; Cbl_N; 1.
DR Pfam; PF02761; Cbl_N2; 1.
DR Pfam; PF02762; Cbl_N3; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF47668; N-terminal domain of cbl (N-cbl); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51506; CBL_PTB; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367001};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367001};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367001};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367001};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367001};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 46..354
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT DOMAIN 384..423
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 836..879
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..14
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 100567 MW; D048696C8033B3CE CRC64;
MASSSSSSSS TNSSAVTGRL PGARSANPRK ARILGLFDAI QDAVGPPKQA AADRRTVEKT
WKLMDKVVRL CQNPKLQLKN SPPYILDILP DTYQHLRLIL SKYDDNQKLA QLSENEYFKI
YIDSLMKKSK RAIRLFKEGK ERMYEEQSQE RRNLTKLSLI FSHMLAEIKA IFPSGQFQGD
NFRITKADAA EFWRKFFGER TIVPWKIFRQ CLHEVHQISS GLEAMALKST IDLTCNDYIS
VFEFDIFTRL FQPWTSILRN WNFLAVTHPG YMAFLTYDEV KARLQKYSTK PGSYIFRLSC
TRLGQWAIGY VTADGNILQT IPHNKPLFQA LIDGSREGFY LYPDGRSYNP DLTDLCEPTP
HDHIKVTQEQ YELYCEMGST FQLCKICAEN DKDVKIEPCG HLMCTSCLTS WQESDGQGCP
FCRCEIKGTE PIVVDPFDPR DENRCCSFND SLCTPMLDFD DDDLREECLI MNRLASLRKM
NERQNSPVTS PGSSPLSQRR KTPPDPLQIP HLNLPPVPPR LDLIQKGLAR SPCASPTGSP
KSSPCMVRKQ DKPLPAPPPP LREPPPPPER PPPIPPDSRT CRHLHHTENV PCRDQSTQHD
AWCTRDISGA SQPSICRVAH DGSPKLGVPS SSVLNGRHSR MSTEAGFIRH KHHKRRESPL
ETIRVYNGLS GNEEYDVPPR LSPPPPPPTI TIHPAIKCPL LVNSVSDKVR NSAEEDDSEY
KIPSSHPVSS RLPLHCHSIK HFPRLCENGQ CLSNGTHNGI SEIKKLKQPD QDPCPEAPLP
PARRGPGEAK SNRLSQEYDQ LPSCPDCPQA PARPPKPVPR RTAPEIHHRR HYNCDSLAEN
VDAKIAKLMG EGFPFEEVKR ALEIAQNNVD VARSILREFA FPPPVCPRLH L
//
