CBLB_XENTR
ID CBLB_XENTR Reviewed; 982 AA.
AC Q6DFR2;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=E3 ubiquitin-protein ligase CBL-B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13191};
DE AltName: Full=RING-type E3 ubiquitin transferase CBL-B {ECO:0000305};
DE AltName: Full=SH3-binding protein CBL-B;
DE AltName: Full=Signal transduction protein CBL-B;
GN Name=cblb;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q13191}.
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:0000250|UniProtKB:Q13191};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with several SH3 domain-containing proteins and with
CC poly-ubiquitinated proteins. {ECO:0000250|UniProtKB:Q13191}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13191}.
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 -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250|UniProtKB:Q13191}.
CC -!- DOMAIN: The UBA domain interacts with poly-ubiquitinated proteins.
CC {ECO:0000250|UniProtKB:Q13191}.
CC -!- MISCELLANEOUS: This protein has one functional calcium-binding site.
CC {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; BC076671; AAH76671.1; -; mRNA.
DR RefSeq; NP_001006802.1; NM_001006801.1.
DR AlphaFoldDB; Q6DFR2; -.
DR BMRB; Q6DFR2; -.
DR SMR; Q6DFR2; -.
DR STRING; 8364.ENSXETP00000022441; -.
DR DNASU; 448509; -.
DR GeneID; 448509; -.
DR KEGG; xtr:448509; -.
DR CTD; 868; -.
DR Xenbase; XB-GENE-1018102; cblb.
DR InParanoid; Q6DFR2; -.
DR OrthoDB; 540689at2759; -.
DR Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000016127; Expressed in ovary and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:InterPro.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IBA:GO_Central.
DR GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd16709; RING-HC_Cbl-b; 1.
DR CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR Gene3D; 1.20.930.20; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.505.10; -; 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; IPR039520; CBL-B_RING-HC.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23007; PTHR23007; 1.
DR Pfam; PF02262; Cbl_N; 1.
DR Pfam; PF02761; Cbl_N2; 1.
DR Pfam; PF02762; Cbl_N3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47668; SSF47668; 1.
DR SUPFAM; SSF55550; SSF55550; 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; Cytoplasm; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..982
FT /note="E3 ubiquitin-protein ligase CBL-B"
FT /id="PRO_0000055865"
FT DOMAIN 46..354
FT /note="Cbl-PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00839"
FT DOMAIN 927..970
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 384..423
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..178
FT /note="4H"
FT REGION 179..251
FT /note="EF-hand-like"
FT REGION 252..354
FT /note="SH2-like"
FT REGION 355..383
FT /note="Linker"
FT REGION 480..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 297
FT /ligand="4-O-phospho-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:62338"
FT /evidence="ECO:0000250"
SQ SEQUENCE 982 AA; 110118 MW; B55D0D9C0F0658A1 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 QGDVIATSTV
PVPLPSARTS ARENHPHGSS LTRTPSDYDL LVPHPGEESF DSSPPSQPPP PPPARTCVPE
HAMPTASGCR PNSDVDLFLP HSDPCPEAPL PPARRGPGEA KSNRLSQEYD QLPSCPDCPQ
APARPPKPVP RRTAPEIHHR RHYNCDSLAE NVDAKIAKLM GEGFPFEEVK RALEIAQNNV
DVARSILREF AFPPPVCPRL HL
