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Database: UniProt
Entry: A0A3Q1LPD2_BOVIN
LinkDB: A0A3Q1LPD2_BOVIN
Original site: A0A3Q1LPD2_BOVIN 
ID   A0A3Q1LPD2_BOVIN        Unreviewed;       935 AA.
AC   A0A3Q1LPD2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN   Name=CBLB {ECO:0000313|Ensembl:ENSBTAP00000061928.1,
GN   ECO:0000313|VGNC:VGNC:26809};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000061928.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000061928.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000061928.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000061928.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000061928.1};
RG   Ensembl;
RL   Submitted (JUL-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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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   AlphaFoldDB; A0A3Q1LPD2; -.
DR   Ensembl; ENSBTAT00000078595.1; ENSBTAP00000061928.1; ENSBTAG00000013057.6.
DR   VEuPathDB; HostDB:ENSBTAG00000013057; -.
DR   VGNC; VGNC:26809; CBLB.
DR   GeneTree; ENSGT00940000156631; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000013057; Expressed in intramuscular adipose tissue and 110 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1LPD2; baseline and differential.
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; cd16709; RING-HC_Cbl-b; 1.
DR   CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR   CDD; cd14392; UBA_Cbl-b; 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; 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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23007; CBL; 1.
DR   PANTHER; PTHR23007:SF3; E3 UBIQUITIN-PROTEIN LIGASE CBL-B; 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   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   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367001};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367001};
KW   Ubl conjugation pathway {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          1..295
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000259|PROSITE:PS51506"
FT   DOMAIN          325..364
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          884..923
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          418..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..521
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..785
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  104269 MW;  954D33B0F197E3A7 CRC64;
     MWVQVLAKVR LCQNPKLQLK NSPPYILDIL PDTYQHLRLI LSKYDDNQKL AQLSENEYFK
     IYIDSLMKKS KRAIRLFKEG KERMYEEQSQ DRRNLTKLSL IFSHMLAEIK AIFPNGQFQG
     DNFRITKADA AEFWRKFFGD KTIVPWKVFR QCLHEVHQIS SGLEAMALKS TIDLTCNDYI
     SVFEFDIFTR LFQPWGSILR NWNFLAVTHP GYMAFLTYDE VKARLQKYST KPGSYIFRLS
     CTRLGQWAIG YVTGDGNILQ TIPHNKPLFQ ALIDGSREGF YLYPDGRSYN PDLTGLCEPT
     PHDHIKVTQE QYELYCEMGS TFQLCKICAE NDKDVKIEPC GHLMCTSCLT AWQESDGQGC
     PFCRCEIKGT EPIIVDPFDP RDEGSRCCSI IDPFGMPMLD LDDDDDREES LMMNRLANVR
     KCTDRQNSPV TSPGSSPLAQ RRKPHPDPLQ IPHLSLPPVP PRLDLIQKGI VRSPCGSPTG
     SPKSSPCMVR KQDKPLPAPP PPLRDPPPPP PERPPPVPPD NRLSRHFHHV ESVPSRDQPM
     PLEAWCPRDV LGTNQSVGCR LLGDGSPKPG ITASSNANGR HSRMGSDPVL LRKHRRNDLP
     LEGAKVFSNG HLGSEEYDVP PRLSPPPPAA TLLPSIKCTG PLANSLSEKT RDPVEEDDDE
     YKVPSSHPVS LSSQPSHCHN VKPPPRSCDN GHCILNGTHG TSSEMKKSNI PELGIYLKGD
     VFDSASDPVP LPPARPPTRD NPKHGSSLNR TPSDYDLLIP PLGEDAFDAL PPSLPPPPPP
     ARHSLIEHSK PPGSGSRPSS GQDLFLLPSD PFFDPASGQV PLPPARRLPG ENVKSNRASQ
     DYDPLPSSSD GSQAPARPPK PRPRRTAPEI HHRKPHGPEA ALENVDAKIA KLMGEGYAFE
     EVKRALEIAQ NNVEVARSIL REFAFPPPVS PRLNL
//
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