ID Q9I9L2_XENLA Unreviewed; 565 AA.
AC Q9I9L2;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
DE Flags: Fragment;
GN Name=Cbl {ECO:0000313|EMBL:AAF43710.1};
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:AAF43710.1};
RN [1] {ECO:0000313|EMBL:AAF43710.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10967110; DOI=10.1074/jbc.M005424200;
RA Adler C.E., Miyoshi-Akiyama T., Aleman L.M., Tanaka M., Smith J.M.,
RA Mayer B.J.;
RT "Abl family kinases and Cbl cooperate with the Nck adaptor to modulate
RT Xenopus development.";
RL J. Biol. Chem. 275:36472-36478(2000).
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|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|RuleBase:RU367001};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU367001}.
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 EMBL; AF237765; AAF43710.1; -; mRNA.
DR AlphaFoldDB; Q9I9L2; -.
DR UniPathway; UPA00143; -.
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: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; cd14393; UBA_c-Cbl; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024162; Adaptor_Cbl.
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:SF5; E3 UBIQUITIN-PROTEIN LIGASE CBL; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|RuleBase:RU367001};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367001};
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 40..79
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 515..554
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 137..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAF43710.1"
SQ SEQUENCE 565 AA; 61478 MW; D3F9C7BA84BEA63F CRC64;
GRNQNPDRTG LCEPTPQDHI KVTQEQYELY CEMGSTFQLC KICAENDKDV KIEPCGHLMC
TSCLTSWQES EGQGCPFCRC EIKGTEPIVV DPFDPRCGAM AELLRQCMDG TPSPCYDDDD
DDEVELTLSF VMKELAGSKV ERPPSPLSVT PQASLPPVPP RLDLLQQRTP NQSGACSPAT
SSKASSSSHH KDKPLPVPPT LRDLPPPPPP DRPHSIASES RPQRRPLPST PAEKPLLLPT
NRPGETWHPR AVPKAPATNL TPGDPWTGGR ELTNRHSLPF TLPSHIDERR DRHGSTQSLD
NTGISATTEL FGGLDNDDAK MKPSSSANAI YSLATRPFPV PPVGDHVDSG DESEYMCPSS
RPLIPAPVAK TEARRPLETV PSLWPPDQQT ERESYETMYN IQCQATTPVV VEPSREGAET
NSAIANNGPE DDDNEDDGYD IPKPHLPMAI ARRTLSDAPN ATPAFCPGTI SRDSGAGLPE
SSQVPERPPK PFPRRMNSER RPVVGGGFGD APPAPLSSEI ESLLSQGYSQ QDVNKALLIA
RNNIEMARNI LREFVAIPSP AHVAT
//
