ID B3DLI0_XENTR Unreviewed; 888 AA. AC B3DLI0; DT 22-JUL-2008, integrated into UniProtKB/TrEMBL. DT 22-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001}; DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001}; GN Name=cbl {ECO:0000313|EMBL:AAI67455.1, GN ECO:0000313|RefSeq:NP_001122110.1, GN ECO:0000313|Xenbase:XB-GENE-6258452}; GN Synonyms=c-cbl {ECO:0000313|RefSeq:NP_001122110.1}, rnf55 GN {ECO:0000313|RefSeq:NP_001122110.1}; 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|EMBL:AAI67455.1}; RN [1] {ECO:0000313|RefSeq:NP_001122110.1} 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:AAI67455.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testes {ECO:0000313|EMBL:AAI67455.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|RefSeq:NP_001122110.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (NOV-2023) 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|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 -!- 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}. 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; BC167455; AAI67455.1; -; mRNA. DR RefSeq; NP_001122110.1; NM_001128638.1. DR GeneID; 594900; -. DR KEGG; xtr:594900; -. DR AGR; Xenbase:XB-GENE-6258452; -. DR CTD; 867; -. DR Xenbase; XB-GENE-6258452; cbl. DR HOGENOM; CLU_013535_3_0_1; -. DR OrthoDB; 1123734at2759; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000008143; Chromosome 7. 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: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; cd14393; UBA_c-Cbl; 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:SF5; E3 UBIQUITIN-PROTEIN LIGASE CBL; 1. DR Pfam; PF02262; Cbl_N; 1. DR Pfam; PF02761; Cbl_N2; 1. DR Pfam; PF02762; Cbl_N3; 1. DR Pfam; PF00627; UBA; 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 2: Evidence at transcript level; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367001}; 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 29..333 FT /note="Cbl-PTB" FT /evidence="ECO:0000259|PROSITE:PS51506" FT DOMAIN 363..402 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 838..877 FT /note="UBA" FT /evidence="ECO:0000259|PROSITE:PS50030" FT REGION 461..624 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 660..715 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 736..840 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..486 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 492..507 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 520..538 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 604..618 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 888 AA; 98562 MW; FEE51C20A0F5847E CRC64; MATNLRKGGG LIGLVKDAFQ PHHHHPTAQP GAVDRKTVEK CWKLMDKVVR LCQNQRLALK NSPPYILDLL PDTYQHLRTI MSRYEGKMEI LGENEYFRVF MENLLKKTKQ TISLFKEGKE RMYEENSQPR RNLTKLSLIF SHMLAELKAI FPNGQFQGDS FRITKADAAE FWRKAFGEKT IVPWKIFRLA LHDVHPISSG LEAMALKSTI DLTCNDYISV FEFDIFTRLF QPWSSLLRNW NSLAVTHPGY MAFLTYDEVK ARLQKFIHKP GSYIFRLSCT RLGQWAIGYV TGDGNILQTI PHNKPLFQAL IDGFREGFYL FPDGRNQNPD LTGLCEPTPQ DHIKVTQEQY ELYCEMGSTF QLCKICAEND KDVKIEPCGH LMCTSCLTSW QESEGQGCPF CRCEIKGTEP IVVDPFDPRG GGMAELLRHC MDGTPSPCYD DDDDDSGNDS IFVMKELAGA KVERPPSPLS ATPQASLPPV PPRLDLLPQR APNQSGACSP ATSSKASSSS HHKDKPLPVP PTLRDLPPPP PPDRPHSMPC ESRPQRRPLP STPAEKPLPL PTNRPGETWH PRAVPKAPAS NLTPGDPWTG GRELTNRHSL PFTLPSHIDE RRDRHGSTQS LDNTGISATT ELFGGLDNDD AKMKPSSSAN AIYSLATRPF PVSKPPTGDH VDSGDESEYM CPSSRPLIPA AVPKSEARRP LETLPGLRPP DQQTERESYE TMYNIQCQAT NPVVVEPSRE EETNSAIANN GPENDDNEED GYDIPKPHLP MAPARRTMSD APNATPAFCS GAIGRDSGAG LLESSQVPER PPKPFPRRMN SERRSVVGGG SGDAPPAPLS SEIESLLSQG YSQQDVNKAL LIAHNNIEMA RNILREFVSI PSPAHVAT //