CBLBB_XENLA
ID CBLBB_XENLA Reviewed; 764 AA.
AC Q6NRE7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=E3 ubiquitin-protein ligase CBL-B-B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13191};
DE AltName: Full=RING-type E3 ubiquitin transferase CBL-B-B {ECO:0000305};
DE AltName: Full=SH3-binding protein CBL-B-B;
DE AltName: Full=Signal transduction protein CBL-B-B;
GN Name=cblb-b;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-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; BC070806; AAH70806.1; -; mRNA.
DR RefSeq; NP_001084790.1; NM_001091321.1.
DR AlphaFoldDB; Q6NRE7; -.
DR BMRB; Q6NRE7; -.
DR SMR; Q6NRE7; -.
DR PRIDE; Q6NRE7; -.
DR GeneID; 431829; -.
DR KEGG; xla:431829; -.
DR CTD; 431829; -.
DR Xenbase; XB-GENE-6251770; cblb.S.
DR OrthoDB; 234717at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 431829; Expressed in spleen 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..764
FT /note="E3 ubiquitin-protein ligase CBL-B-B"
FT /id="PRO_0000055864"
FT DOMAIN 48..356
FT /note="Cbl-PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00839"
FT ZN_FING 386..425
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 48..180
FT /note="4H"
FT REGION 181..253
FT /note="EF-hand-like"
FT REGION 254..356
FT /note="SH2-like"
FT REGION 357..385
FT /note="Linker"
FT REGION 482..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P22681"
FT BINDING 299
FT /ligand="4-O-phospho-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:62338"
FT /evidence="ECO:0000250"
SQ SEQUENCE 764 AA; 86210 MW; 4FFD300CEE119F76 CRC64;
MASSSSSSSN SSTSSSALSG RLPGARSANP RKARILGLFD AIQDAVGPPK QAAADRRTVE
KTWKLMDKVV RLCQNPKLQL KNSPPYILDI LPDTYQHLRL ILSKYDDNQK LAQLSENEYF
KIYIDSLMKK SKRAIRLFKE GKERMYEEQS QERRNLTKLS LIFSHMLAEI KAIFPSGQFQ
GDTFRITKAD AAEFWRKFFG ERTIVPWKIF RQCLHEVQQI SSGLEAMALK STIDLTCNDY
ISVFEFDIFA RLFQPWSSIL RNWNFLAVTH PGYMAFLTYD EVKARLQKYS LKHGSYIFRL
SCTRLGQWAI GYVTAGGNIL QTIPHNKPLF QALIDGSREG FYLYPDGRSY NPDLTDLCEP
TPHDHIKVTQ EQYELYCEMG STFQLCKICA ENDKDVKIEP CGHLMCTSCL TSWQESDGQG
CPFCRCEIKG TEPIIVDPFD PRDENRCCSF NDSLCTPMFD FDDDDLREEC LIMNRLASLR
KMNERQNSPV TSPGSSPLLQ RRKTPPDPVQ IPHLNLPPVP PRLDLIQRGL ARSPCASPTG
SPKSSPCMAR KQDKPLPAPP PPLREPPPPP ERPPPIPPDS RTCRHLHHAE NVPCRDQSTP
NEAWCTRDLS GGNQPSVCRV THDGSPKLGV SSSVLNGRHS RVSTEAGFMR HKHHKRRESP
LETHRVYNGL SGNEEYDVPP RLSPPPPTIT IHPTVICPLL ANSASDKVRN SAEEDDSEYK
IPSSHPVSSR LPLHCHSIKH FPRLCENGQC LSNGAHNGIS EIKN
