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Q9ULV8

- CBLC_HUMAN

UniProt

Q9ULV8 - CBLC_HUMAN

Protein

E3 ubiquitin-protein ligase CBL-C

Gene

CBLC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival.5 Publications

    Enzyme regulationi

    Phosphorylation at Tyr-341 is necessary and sufficient for the activation of E3 activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei264 – 2641Phosphotyrosine

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi199 – 21012Add
    BLAST
    Zinc fingeri351 – 39040RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. epidermal growth factor receptor binding Source: BHF-UCL
    3. ligase activity Source: UniProtKB-KW
    4. phosphotyrosine binding Source: BHF-UCL
    5. SH3 domain binding Source: BHF-UCL
    6. signal transducer activity Source: InterPro
    7. ubiquitin-protein transferase activity Source: BHF-UCL
    8. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: InterPro
    2. negative regulation of epidermal growth factor-activated receptor activity Source: BHF-UCL
    3. negative regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
    4. negative regulation of MAP kinase activity Source: BHF-UCL
    5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9ULV8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase CBL-C (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 57
    SH3-binding protein CBL-3
    SH3-binding protein CBL-C
    Signal transduction protein CBL-C
    Gene namesi
    Name:CBLC
    Synonyms:CBL3, RNF57
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:15961. CBLC.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleus Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi244 – 2441Y → A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. 1 Publication
    Mutagenesisi244 – 2441Y → F: No effect on interaction with EGFR and SRC as well as on SRC ubiquitination. 1 Publication
    Mutagenesisi264 – 2641R → A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. 1 Publication
    Mutagenesisi265 – 2651P → L: Enhances interaction with EGFR and SRC as well as SRC ubiquitination. 1 Publication
    Mutagenesisi266 – 2661S → A: Decreases interactions with EGFR and SRC as well as SRC ubiquitination. 1 Publication
    Mutagenesisi268 – 2681T → A: Abolishes interaction with EGFR. Decreases interaction with and ubiquitination of SRC. 1 Publication
    Mutagenesisi276 – 2761G → E: No effect on interaction with RET. Binds slightly to SRC, this interaction is independent of SRC phosphorylation. Strongly decreases SRC ubiquitination. Abolishes interaction with EGFR. 3 Publications
    Mutagenesisi341 – 3411Y → E: Induces E3 activity and autoubiquitination. Releases ubiquitin-conjugating enzyme E2 UBE2D2 faster. 3 Publications
    Mutagenesisi341 – 3411Y → F: Abolishes activation by EGF stimulation and enhancement by TGFB1I1 of E3 activity. 3 Publications
    Mutagenesisi341 – 3411Missing: Abolishes E3 activity. 3 Publications
    Mutagenesisi351 – 3511C → A: No effect on TGFB1I1 and SRC interactions. Abolishes SRC ubiquitination. Abolishes interaction with TGFB1I1; when associated with A-366. Abolishes interaction with RET and inhibition of RET degradation. 3 Publications
    Mutagenesisi366 – 3661C → A: Abolishes interaction with TGFB1I1. Abolishes interaction with TGFB1I1; when associated with A-351. 1 Publication

    Organism-specific databases

    PharmGKBiPA26117.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 474474E3 ubiquitin-protein ligase CBL-CPRO_0000055866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei341 – 3411Phosphotyrosine; by SRC2 Publications

    Post-translational modificationi

    Phosphorylated on multiple tyrosine residues by SRC. Isoform 1, but not isoform 2, is phosphorylated on tyrosines by EGFR.
    Autoubiquitinated when phosphorylated at Tyr-341, enhanced by SRC; suggesting proteasomal degradation.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9ULV8.
    PaxDbiQ9ULV8.
    PRIDEiQ9ULV8.

    PTM databases

    PhosphoSiteiQ9ULV8.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ9ULV8.
    CleanExiHS_CBLC.
    GenevestigatoriQ9ULV8.

    Organism-specific databases

    HPAiCAB008087.

    Interactioni

    Subunit structurei

    Interacts with ubiquitin-conjugating enzyme E2 UBE2D2 and UBE2D3. Isoform 1 interacts with EGFR (tyrosine phosphorylated). Interacts with the SH3 domain proteins LYN and CRK. Interacts (via RING-type zinc finger) with TGFB1I1 (via LIM zinc-binding domain 2); the interaction is direct and enhances the E3 activity. Interacts directly with RET (inactive) and CD2AP; dissociates from RET upon RET activation by GDNF which also increases the interaction with CD2AP suggesting dissociation as CBLC:CD2AP complex. Interacts with SRC; the interaction is enhanced when SRC is phosphorylated at 'Tyr-419'.7 Publications

    Protein-protein interaction databases

    BioGridi117156. 35 interactions.
    IntActiQ9ULV8. 18 interactions.
    MINTiMINT-247027.
    STRINGi9606.ENSP00000270279.

    Structurei

    Secondary structure

    1
    474
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 3119
    Beta strandi40 – 423
    Helixi44 – 6219
    Beta strandi64 – 663
    Helixi76 – 9722
    Beta strandi100 – 1023
    Helixi108 – 1114
    Helixi116 – 13823
    Helixi140 – 1423
    Turni146 – 1483
    Helixi154 – 16411
    Beta strandi168 – 1714
    Helixi172 – 1798
    Turni180 – 1823
    Helixi189 – 19810
    Beta strandi203 – 2075
    Helixi208 – 21710
    Helixi221 – 2233
    Helixi224 – 2329
    Beta strandi238 – 2414
    Helixi244 – 2518
    Helixi252 – 2543
    Beta strandi260 – 2656
    Beta strandi267 – 2693
    Beta strandi273 – 2786
    Beta strandi284 – 2874
    Helixi294 – 30310
    Helixi320 – 3234

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OP0X-ray2.52A/B9-323[»]
    3VRNX-ray1.64A1-323[»]
    3VROX-ray1.80A1-323[»]
    3VRPX-ray1.52A1-323[»]
    3VRQX-ray2.39A/B1-323[»]
    3VRRX-ray2.00A1-323[»]
    ProteinModelPortaliQ9ULV8.
    SMRiQ9ULV8. Positions 10-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 321315Cbl-PTBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 1451394HAdd
    BLAST
    Regioni146 – 21873EF-hand-likeAdd
    BLAST
    Regioni219 – 321103SH2-likeAdd
    BLAST
    Regioni322 – 35029LinkerAdd
    BLAST
    Regioni351 – 474124Interaction with RETAdd
    BLAST

    Domaini

    EF-hand-like and Sh2-like domains are required for N-terminal inhibition of E3 activity.1 Publication
    The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.1 PublicationPROSITE-ProRule annotation
    The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.By similarity

    Sequence similaritiesi

    Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri351 – 39040RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, SH3-binding, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG318595.
    HOGENOMiHOG000294176.
    HOVERGENiHBG005255.
    InParanoidiQ9ULV8.
    KOiK04707.
    OMAiWQHSDSQ.
    OrthoDBiEOG73BVCF.
    PhylomeDBiQ9ULV8.
    TreeFamiTF314210.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.20.930.20. 1 hit.
    3.30.40.10. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR024162. Adaptor_Cbl.
    IPR014741. Adaptor_Cbl_EF_hand-like.
    IPR003153. Adaptor_Cbl_N_hlx.
    IPR014742. Adaptor_Cbl_SH2-like.
    IPR024159. Cbl_PTB.
    IPR011992. EF-hand-dom_pair.
    IPR000980. SH2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PANTHERiPTHR23007. PTHR23007. 1 hit.
    PfamiPF02262. Cbl_N. 1 hit.
    PF02761. Cbl_N2. 1 hit.
    PF02762. Cbl_N3. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47668. SSF47668. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS51506. CBL_PTB. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ULV8-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALAVAPWGR QWEEARALGR AVRMLQRLEE QCVDPRLSVS PPSLRDLLPR    50
    TAQLLREVAH SRRAAGGGGP GGPGGSGDFL LIYLANLEAK SRQVAALLPP 100
    RGRRSANDEL FRAGSRLRRQ LAKLAIIFSH MHAELHALFP GGKYCGHMYQ 150
    LTKAPAHTFW RESCGARCVL PWAEFESLLG TCHPVEPGCT ALALRTTIDL 200
    TCSGHVSIFE FDVFTRLFQP WPTLLKNWQL LAVNHPGYMA FLTYDEVQER 250
    LQACRDKPGS YIFRPSCTRL GQWAIGYVSS DGSILQTIPA NKPLSQVLLE 300
    GQKDGFYLYP DGKTHNPDLT ELGQAEPQQR IHVSEEQLQL YWAMDSTFEL 350
    CKICAESNKD VKIEPCGHLL CSCCLAAWQH SDSQTCPFCR CEIKGWEAVS 400
    IYQFHGQATA EDSGNSSDQE GRELELGQVP LSAPPLPPRP DLPPRKPRNA 450
    QPKVRLLKGN SPPAALGPQD PAPA 474
    Length:474
    Mass (Da):52,456
    Last modified:February 6, 2007 - v3
    Checksum:i202634AEDE434544
    GO
    Isoform 2 (identifier: Q9ULV8-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         261-306: Missing.

    Show »
    Length:428
    Mass (Da):47,418
    Checksum:i7070EDF530032CA0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2341N → T in BAA86298. (PubMed:10571044)Curated
    Sequence conflicti413 – 4131S → P in AAH28915. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti405 – 4051H → Y.2 Publications
    Corresponds to variant rs3208856 [ dbSNP | Ensembl ].
    VAR_018298

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei261 – 30646Missing in isoform 2. 1 PublicationVSP_005732Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028645 mRNA. Translation: BAA86298.1.
    AF117646 mRNA. Translation: AAD34341.1.
    AF117647 mRNA. Translation: AAD34342.1.
    BC028915 mRNA. Translation: AAH28915.1.
    CCDSiCCDS12643.1. [Q9ULV8-1]
    CCDS46109.1. [Q9ULV8-2]
    RefSeqiNP_001124324.1. NM_001130852.1. [Q9ULV8-2]
    NP_036248.3. NM_012116.3. [Q9ULV8-1]
    UniGeneiHs.466907.

    Genome annotation databases

    EnsembliENST00000270279; ENSP00000270279; ENSG00000142273. [Q9ULV8-1]
    ENST00000341505; ENSP00000340250; ENSG00000142273. [Q9ULV8-2]
    GeneIDi23624.
    KEGGihsa:23624.
    UCSCiuc002ozs.3. human. [Q9ULV8-1]
    uc010ejt.3. human. [Q9ULV8-2]

    Polymorphism databases

    DMDMi125987803.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028645 mRNA. Translation: BAA86298.1 .
    AF117646 mRNA. Translation: AAD34341.1 .
    AF117647 mRNA. Translation: AAD34342.1 .
    BC028915 mRNA. Translation: AAH28915.1 .
    CCDSi CCDS12643.1. [Q9ULV8-1 ]
    CCDS46109.1. [Q9ULV8-2 ]
    RefSeqi NP_001124324.1. NM_001130852.1. [Q9ULV8-2 ]
    NP_036248.3. NM_012116.3. [Q9ULV8-1 ]
    UniGenei Hs.466907.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OP0 X-ray 2.52 A/B 9-323 [» ]
    3VRN X-ray 1.64 A 1-323 [» ]
    3VRO X-ray 1.80 A 1-323 [» ]
    3VRP X-ray 1.52 A 1-323 [» ]
    3VRQ X-ray 2.39 A/B 1-323 [» ]
    3VRR X-ray 2.00 A 1-323 [» ]
    ProteinModelPortali Q9ULV8.
    SMRi Q9ULV8. Positions 10-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117156. 35 interactions.
    IntActi Q9ULV8. 18 interactions.
    MINTi MINT-247027.
    STRINGi 9606.ENSP00000270279.

    PTM databases

    PhosphoSitei Q9ULV8.

    Polymorphism databases

    DMDMi 125987803.

    Proteomic databases

    MaxQBi Q9ULV8.
    PaxDbi Q9ULV8.
    PRIDEi Q9ULV8.

    Protocols and materials databases

    DNASUi 23624.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270279 ; ENSP00000270279 ; ENSG00000142273 . [Q9ULV8-1 ]
    ENST00000341505 ; ENSP00000340250 ; ENSG00000142273 . [Q9ULV8-2 ]
    GeneIDi 23624.
    KEGGi hsa:23624.
    UCSCi uc002ozs.3. human. [Q9ULV8-1 ]
    uc010ejt.3. human. [Q9ULV8-2 ]

    Organism-specific databases

    CTDi 23624.
    GeneCardsi GC19P045281.
    H-InvDB HIX0202847.
    HGNCi HGNC:15961. CBLC.
    HPAi CAB008087.
    MIMi 608453. gene.
    neXtProti NX_Q9ULV8.
    PharmGKBi PA26117.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG318595.
    HOGENOMi HOG000294176.
    HOVERGENi HBG005255.
    InParanoidi Q9ULV8.
    KOi K04707.
    OMAi WQHSDSQ.
    OrthoDBi EOG73BVCF.
    PhylomeDBi Q9ULV8.
    TreeFami TF314210.

    Enzyme and pathway databases

    SignaLinki Q9ULV8.

    Miscellaneous databases

    GeneWikii CBLC.
    GenomeRNAii 23624.
    NextBioi 46378.
    PROi Q9ULV8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ULV8.
    CleanExi HS_CBLC.
    Genevestigatori Q9ULV8.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.20.930.20. 1 hit.
    3.30.40.10. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR024162. Adaptor_Cbl.
    IPR014741. Adaptor_Cbl_EF_hand-like.
    IPR003153. Adaptor_Cbl_N_hlx.
    IPR014742. Adaptor_Cbl_SH2-like.
    IPR024159. Cbl_PTB.
    IPR011992. EF-hand-dom_pair.
    IPR000980. SH2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    PANTHERi PTHR23007. PTHR23007. 1 hit.
    Pfami PF02262. Cbl_N. 1 hit.
    PF02761. Cbl_N2. 1 hit.
    PF02762. Cbl_N3. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47668. SSF47668. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS51506. CBL_PTB. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a novel cbl-family gene, cbl-c."
      Kim M., Tezuka T., Suzuki Y., Sugano S., Hirai M., Yamamoto T.
      Gene 239:145-154(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TYR-405.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT TYR-405, FUNCTION AS EGF SIGNALING NEGATIVE REGULATOR, PHOSPHORYLATION BY EGFR (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH CRK AND LYN.
      Tissue: Pancreatic adenocarcinoma.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Skin.
    4. "Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation."
      Kim M., Tezuka T., Tanaka K., Yamamoto T.
      Oncogene 23:1645-1655(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH SRC, AUTOUBIQUITINATION, MUTAGENESIS OF GLY-276; TYR-341 AND CYS-351.
    5. "CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation of ret signal transduction."
      Tsui C.C., Pierchala B.A.
      J. Neurosci. 28:8789-8800(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RET STABILITY, INTERACTION WITH RET, MUTAGENESIS OF GLY-276 AND CYS-351.
    6. "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme."
      Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.
      J. Biol. Chem. 285:23687-23698(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, DOMAIN, INTERACTION WITH UBE2D2 AND UBE2D3, PHOSPHORYLATION AT TYR-341, MUTAGENESIS OF TYR-341.
    7. "Cbl-c ubiquitin ligase activity is increased via the interaction of its RING finger domain with a LIM domain of the paxillin homolog, Hic 5."
      Ryan P.E., Kales S.C., Yadavalli R., Nau M.M., Zhang H., Lipkowitz S.
      PLoS ONE 7:E49428-E49428(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, PHOSPHORYLATION AT TYR-341, INTERACTION WITH TGFB1I1, MUTAGENESIS OF TYR-341; CYS-351 AND CYS-366.
    8. "Crystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGFR py1069 peptide."
      Structural genomics consortium (SGC)
      Submitted (OCT-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 9-323 IN COMPLEX WITH EGFR PEPTIDE.
    9. "Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c."
      Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., Yamanashi Y., Yamamoto T., Nakagawa A.
      J. Biochem. 152:487-495(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1-323 IN COMPLEX WITH CALCIUM; SRC AND EGFR PEPTIDES, CALCIUM-BINDING, INTERACTION WITH EGFR AND SRC, MUTAGENESIS OF TYR-244; ARG-264; PRO-265; SER-266; THR-268 AND GLY-276.

    Entry informationi

    Entry nameiCBLC_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULV8
    Secondary accession number(s): Q8N1E5, Q9Y5Z2, Q9Y5Z3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    This protein has one functional calcium-binding site.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3