ID Q9VSK2_DROME Unreviewed; 878 AA.
AC Q9VSK2; Q9GV78;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 2.
DT 27-MAR-2024, entry version 202.
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:AAF50416.2,
GN ECO:0000313|FlyBase:FBgn0020224};
GN Synonyms=anon-WO0118547.68 {ECO:0000313|EMBL:AAF50416.2}, CBL
GN {ECO:0000313|EMBL:AAF50416.2}, cbl {ECO:0000313|EMBL:AAF50416.2},
GN CG7043 {ECO:0000313|EMBL:AAF50416.2}, D-Cbl
GN {ECO:0000313|EMBL:AAF50416.2}, D-cbl {ECO:0000313|EMBL:AAF50416.2},
GN d-cbl {ECO:0000313|EMBL:AAF50416.2}, D-Cbl L
GN {ECO:0000313|EMBL:AAF50416.2}, D-CblL {ECO:0000313|EMBL:AAF50416.2},
GN D-cblL {ECO:0000313|EMBL:AAF50416.2}, D-cblS
GN {ECO:0000313|EMBL:AAF50416.2}, DCbl {ECO:0000313|EMBL:AAF50416.2},
GN Dcbl {ECO:0000313|EMBL:AAF50416.2}, dCbl
GN {ECO:0000313|EMBL:AAF50416.2}, Dmel\CG7037
GN {ECO:0000313|EMBL:AAF50416.2}, Dv-Cbl {ECO:0000313|EMBL:AAF50416.2},
GN Dv-cbl {ECO:0000313|EMBL:AAF50416.2}, F165
GN {ECO:0000313|EMBL:AAF50416.2}, v-Cbl {ECO:0000313|EMBL:AAF50416.2};
GN ORFNames=CG7037 {ECO:0000313|EMBL:AAF50416.2,
GN ECO:0000313|FlyBase:FBgn0020224}, Dmel_CG7037
GN {ECO:0000313|EMBL:AAF50416.2};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF50416.2, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAG00952.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10918586; DOI=10.1038/sj.onc.1203624;
RA Robertson H., Hime G.R., Lada H., Bowtell D.D.;
RT "A Drosophila analogue of v-Cbl is a dominant-negative oncoprotein in
RT vivo.";
RL Oncogene 19:3299-3308(2000).
RN [2] {ECO:0000313|EMBL:AAF50416.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [4] {ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [6] {ECO:0000313|EMBL:AAF50416.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [7] {ECO:0000313|EMBL:AAF50416.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [8] {ECO:0000313|EMBL:AAF50416.2}
RP NUCLEOTIDE SEQUENCE.
RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA Svirskas R., Rubin G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|EMBL:AAF50416.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [10] {ECO:0000313|EMBL:AAF50416.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
RN [11] {ECO:0000313|EMBL:AAF50416.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109357; DOI=.1534/g3.115.018929;
RG FlyBase Consortium;
RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA Gelbart W.M., null;
RT "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT Throughput Data.";
RL G3 (Bethesda) 5:1721-1736(2015).
RN [12] {ECO:0000313|EMBL:AAF50416.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26109356; DOI=.1534/g3.115.018937;
RG FlyBase Consortium;
RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA null;
RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL G3 (Bethesda) 5:1737-1749(2015).
RN [13] {ECO:0000313|EMBL:AAF50416.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25589440;
RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA Karpen G.H., Celniker S.E.;
RT "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL Genome Res. 25:445-458(2015).
RN [14] {ECO:0000313|EMBL:AAF50416.2}
RP NUCLEOTIDE SEQUENCE.
RG Berkeley Drosophila Genome Project;
RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA Rubin G.;
RT "Drosophila melanogaster release 4 sequence.";
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN [15] {ECO:0000313|EMBL:AAF50416.2}
RP NUCLEOTIDE SEQUENCE.
RG FlyBase;
RL Submitted (NOV-2022) 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: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}.
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DR EMBL; AE014296; AAF50416.2; -; Genomic_DNA.
DR EMBL; AF273749; AAG00952.1; -; mRNA.
DR RefSeq; NP_648224.1; NM_139967.2.
DR AlphaFoldDB; Q9VSK2; -.
DR SMR; Q9VSK2; -.
DR IntAct; Q9VSK2; 1.
DR STRING; 7227.FBpp0076342; -.
DR PaxDb; 7227-FBpp0076342; -.
DR DNASU; 38961; -.
DR EnsemblMetazoa; FBtr0076615; FBpp0076342; FBgn0020224.
DR GeneID; 38961; -.
DR KEGG; dme:Dmel_CG7037; -.
DR UCSC; CG7037-RB; d. melanogaster.
DR AGR; FB:FBgn0020224; -.
DR CTD; 867; -.
DR FlyBase; FBgn0020224; Cbl.
DR VEuPathDB; VectorBase:FBgn0020224; -.
DR eggNOG; KOG1785; Eukaryota.
DR GeneTree; ENSGT00940000168289; -.
DR HOGENOM; CLU_013535_3_1_1; -.
DR InParanoid; Q9VSK2; -.
DR OMA; CGTVPYE; -.
DR OrthoDB; 1123734at2759; -.
DR Reactome; R-DME-1295596; Spry regulation of FGF signaling.
DR Reactome; R-DME-1433559; Regulation of KIT signaling.
DR Reactome; R-DME-182971; EGFR downregulation.
DR Reactome; R-DME-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-DME-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-DME-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-DME-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-DME-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-DME-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-912631; Regulation of signaling by CBL.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 38961; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38961; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020224; Expressed in cleaving embryo and 29 other cell types or tissues.
DR ExpressionAtlas; Q9VSK2; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
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:UniProtKB-UniRule.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISM:FlyBase.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:FlyBase.
DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0001754; P:eye photoreceptor cell differentiation; IDA:FlyBase.
DR GO; GO:0048134; P:germ-line cyst formation; IGI:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR GO; GO:0032353; P:negative regulation of hormone biosynthetic process; IMP:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:FlyBase.
DR GO; GO:0006513; P:protein monoubiquitination; IMP:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IDA:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:FlyBase.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:FlyBase.
DR CDD; cd16708; RING-HC_Cbl; 1.
DR CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR CDD; cd14318; UBA_Cbl_like; 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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23007; CBL; 1.
DR PANTHER; PTHR23007:SF11; 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; PF13920; zf-C3HC4_3; 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:UP000000803};
KW Transferase {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 35..339
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT DOMAIN 369..409
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 832..872
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 422..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 94788 MW; C92DA7BBE6A2586D CRC64;
MATRGSGTRV QSQPKIFPSL LSKLHGAISE ACVSQRLSTD KKTLEKTWKL MDKVVKLCQQ
PKMNLKNSPP FILDILPDTY QRLRLIYSKN EDQMHLLHAN EHFNVFINNL MRKCKQAIKL
FKEGKEKMFD ENSHYRRNLT KLSLVFSHML SELKAIFPNG VFAGDQFRIT KADAADFWKS
NFGNSTLVPW KIFRQELNKV HPIISGLEAM ALKTTIDLTC NDFISNFEFD VFTRLFQPWV
TLLRNWQILA VTHPGYVAFL TYDEVKARLQ RYILKAGSYV FRLSCTRLGQ WAIGYVTAEG
EILQTIPQNK SLCQALLDGH REGFYLYPDG QAYNPDLSSA VQSPTEDHIT VTQEQYELYC
EMGSTFQLCK ICAENDKDIR IEPCGHLLCT PCLTSWQVDS EGQGCPFCRA EIKGTEQIVV
DAFDPRKQHN RNVTNGRQQQ QEEDDTEDIG DFNIATSSLH ALSTSSTVAA EKHSPHTSPR
LGRRSTTPSL MAVQNDLYAG GTPTLSLPSS SCSSIAAAST SSSSSLASVA TVAASTSSSQ
HQQPQPSAPP ASAVLSNGGG GGGGGGASSS QKNTNRMSAP LIGSCVANST YGQKLPQNCS
HSSTSSSSDN ASSSSSYAIL QNLHDTGTPA TAAAVVAPPL PPRKSSPGVE TPSKATAPPP
PSSSKSIDNI QCSLDNVPPQ TTAPPIPPHV SPSVDTLAED LMRQQLIATS TTSPVLSLLD
EDIVEVGPAE TISGVIDTRP LEARGVTLCR QDSASSHYTQ LCTTSSGGSA AALANGKKAN
SAKQSQATTT TSAAAAAATA GNGSNPGQQS QPLLYANVTI NQKDCGTVPY ENINLEYIAR
LMNAGYSKEN AITALGISRN NIEMAGDILR EFVSKNSA
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