CBLBA_XENLA
ID CBLBA_XENLA Reviewed; 918 AA.
AC Q6GQL0;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=E3 ubiquitin-protein ligase CBL-B-A;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13191};
DE AltName: Full=RING-type E3 ubiquitin transferase CBL-B-A {ECO:0000305};
DE AltName: Full=SH3-binding protein CBL-B-A;
DE AltName: Full=Signal transduction protein CBL-B-A;
GN Name=cblb-a;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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 -!- MISCELLANEOUS: This protein has one functional calcium-binding site.
CC {ECO:0000250}.
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DR EMBL; BC072732; AAH72732.1; -; mRNA.
DR RefSeq; NP_001085428.1; NM_001091959.1.
DR AlphaFoldDB; Q6GQL0; -.
DR SMR; Q6GQL0; -.
DR MaxQB; Q6GQL0; -.
DR PRIDE; Q6GQL0; -.
DR DNASU; 443854; -.
DR GeneID; 443854; -.
DR KEGG; xla:443854; -.
DR CTD; 443854; -.
DR Xenbase; XB-GENE-6251733; cblb.L.
DR OrthoDB; 540689at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 443854; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:InterPro.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; ISS:UniProtKB.
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; 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 SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47668; SSF47668; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51506; CBL_PTB; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Immunity; Metal-binding; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..918
FT /note="E3 ubiquitin-protein ligase CBL-B-A"
FT /id="PRO_0000055863"
FT DOMAIN 46..354
FT /note="Cbl-PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00839"
FT ZN_FING 384..423
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..27
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 481..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..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 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 918 AA; 102831 MW; 5CEB1FDCBCE9D572 CRC64;
MASGSGSSSS TSSSALSGRL PGSRSANPRK ARILGLFDAI QDAVGPPKQA AADRRTVEKT
WKLMDKVVRL CQNPKLQLKN SPPYILDILP DTYQHLRLIL SKYDDNQKLA QLSENEYFKI
YIDSLIKKSK RAMRLFKEGK ERMYEEQSQE RRNLTKLSLI FSHMLAEIKA IFPSGQFQGD
NFRITKADAA EFWRKFFGER TIVPWKIFRQ CLHEVHQISS GLEAMALKST IDLTCNDYIS
VFEFDIFTRL FQPWGSILRN WNFLAVTHPG YMAFLTYDEV KARLQKYSLK PGSYIFRLSC
TRLGQWAIGY VTADGNILQT IPHNKPLFQA LIDGSREGFY LYPDGRSYNP DLTGLCEPTP
HDHIKVTQEQ YELYCEMGST FQLCKICAEN DKDVKIEPCG HLMCTSCLTS WQESDGQGCP
FCRCEIKGME PIIVDPFDPR DESRCFSFSD SLCTPMLDFD DDDLREECLI MNRLAALRKM
NERQNSPVTS PGSSPLSQRR KTPPEPLQIP HLNLPPVPPR LDLIQKGLAR SPCASPTGSP
KSSPCMVRKQ DKPLPAPPPL LREPPPPPER PPPIPPDSRT CRHLHHADNV PCRDQSTPHE
AWCTRDLSGG NPASVCRVTH DGSPKLGVPS SSVLNGRHSR MSTEAGFMRH KHHKRRESPL
ETLRVYNGLS GNEEYDVPPR LSPPTITIHP IVKCPVLVNS VSDKVRNSAE EDDCEYKIPS
SHPVSSRLPL HCHSIKHFPR LCENGQCLSN GTHNGISEIK KLKPPDQGDV IATSTVPIHF
PPARTSAREN HPHGSSLTRT PSDYDLLVPH PGEESFDISP PSQPPPPPPA RTCVTEHVMP
TALGSRPNSD VDLFLPHSDP CPEAPLPPAR RGPGEVKSNR LSQEYDQLPS CPGKGQEKAS
NTKGELLLPN QNLIMRPT
