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P22681

- CBL_HUMAN

UniProt

P22681 - CBL_HUMAN

Protein

E3 ubiquitin-protein ligase CBL

Gene

CBL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. 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. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3.9 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei294 – 2941PhosphotyrosineBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi227 – 24014Add
    BLAST
    Zinc fingeri381 – 42040RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. ephrin receptor binding Source: UniProtKB
    3. ligase activity Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc
    6. SH3 domain binding Source: BHF-UCL
    7. signal transducer activity Source: InterPro
    8. ubiquitin-protein transferase activity Source: HGNC
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: HGNC
    2. epidermal growth factor receptor signaling pathway Source: HGNC
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. negative regulation of apoptotic process Source: UniProtKB
    5. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    6. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    7. positive regulation of receptor-mediated endocytosis Source: HGNC
    8. protein ubiquitination Source: HGNC
    9. regulation of transcription, DNA-templated Source: GOC
    10. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111080. Spry regulation of FGF signaling.
    REACT_111184. Negative regulation of FGFR signaling.
    REACT_111225. Regulation of KIT signaling.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_12484. EGFR downregulation.
    REACT_23787. Regulation of signaling by CBL.
    REACT_27307. Interleukin-6 signaling.
    SignaLinkiP22681.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase CBL (EC:6.3.2.-)
    Alternative name(s):
    Casitas B-lineage lymphoma proto-oncogene
    Proto-oncogene c-Cbl
    RING finger protein 55
    Signal transduction protein CBL
    Gene namesi
    Name:CBL
    Synonyms:CBL2, RNF55
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1541. CBL.

    Subcellular locationi

    Cytoplasm. Cell membrane
    Note: Colocalizes with FGFR2 in lipid rafts at the cell membrane.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. flotillin complex Source: Ensembl
    4. nucleus Source: InterPro
    5. plasma membrane Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Noonan syndrome-like disorder with or without juvenile myelomonocytic leukemia (NSLL) [MIM:613563]: A syndrome characterized by a phenotype reminiscent of Noonan syndrome. Clinical features are highly variable, including facial dysmorphism, short neck, developmental delay, hyperextensible joints and thorax abnormalities with widely spaced nipples. The facial features consist of triangular face with hypertelorism, large low-set ears, ptosis, and flat nasal bridge. Some patients manifest cardiac defects. Some have an increased risk for certain malignancies, particularly juvenile myelomonocytic leukemia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti367 – 3671Q → P in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion. 1 Publication
    VAR_064332
    Natural varianti382 – 3821K → E in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion. 1 Publication
    VAR_064333
    Natural varianti390 – 3901D → Y in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion. 1 Publication
    VAR_064334
    Natural varianti420 – 4201R → Q in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion as well as constitutive ERK phosphorylation. 1 Publication
    VAR_064335

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801S → D: Abolishes interaction with ZAP70. 1 Publication
    Mutagenesisi82 – 821P → A: Abolishes interaction with ZAP70. 1 Publication
    Mutagenesisi229 – 2291D → Q: Abolishes interaction with ZAP70. 1 Publication
    Mutagenesisi240 – 2401E → S: Abolishes interaction with ZAP70. 1 Publication
    Mutagenesisi294 – 2941R → K: Abolishes interaction with ZAP70. 1 Publication
    Mutagenesisi306 – 3061G → E: Abolishes interaction with ZAP70 and EPHB1, but does not affect interaction with SLA. 2 Publications
    Mutagenesisi371 – 3711Y → F: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-700 and F-774. 1 Publication
    Mutagenesisi381 – 3811C → A: Loss of ubiquitin ligase activity. 1 Publication
    Mutagenesisi700 – 7001Y → F: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-774. 1 Publication
    Mutagenesisi731 – 7311Y → F: No effect on tyrosine phosphorylation by INSR. Loss of phosphorylation by SRC. Inhibition of bone resorption. Abolishes interaction with PIK3R1. 2 Publications
    Mutagenesisi774 – 7741Y → F: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-700. 1 Publication

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi613563. phenotype.
    Orphaneti86834. Juvenile myelomonocytic leukemia.
    363972. Noonan syndrome-like disorder with juvenile myelomonocytic leukemia.
    PharmGKBiPA26115.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 906906E3 ubiquitin-protein ligase CBLPRO_0000055858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei141 – 1411Phosphotyrosine
    Modified residuei371 – 3711Phosphotyrosine; by INSR1 Publication
    Modified residuei452 – 4521Phosphoserine1 Publication
    Modified residuei455 – 4551Phosphotyrosine
    Modified residuei552 – 5521Phosphotyrosine
    Modified residuei667 – 6671Phosphoserine
    Modified residuei668 – 6681PhosphoserineBy similarity
    Modified residuei669 – 6691Phosphoserine
    Modified residuei674 – 6741Phosphotyrosine1 Publication
    Modified residuei675 – 6751Phosphoserine
    Modified residuei700 – 7001Phosphotyrosine; by ABL13 Publications
    Modified residuei731 – 7311Phosphotyrosine; by SRC1 Publication
    Modified residuei774 – 7741Phosphotyrosine2 Publications
    Modified residuei900 – 9001Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues by ALK, EGFR, SYK, FYN and ZAP70 By similarity. Phosphorylated on tyrosine residues in response to FLT1 and KIT signaling. Phosphorylated on tyrosine residues by INSR and FGR. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Not phosphorylated at Tyr-731 by FGFR3. Phosphorylated on tyrosine residues by activated CSF1R, PDGFRA and PDGFRB. Phosphorylated on tyrosine residues by HCK.By similarity16 Publications
    Ubiquitinated, leading to its degradation via the proteasome.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP22681.
    PaxDbiP22681.
    PRIDEiP22681.

    PTM databases

    PhosphoSiteiP22681.

    Miscellaneous databases

    PMAP-CutDBP22681.

    Expressioni

    Gene expression databases

    BgeeiP22681.
    CleanExiHS_CBL.
    GenevestigatoriP22681.

    Organism-specific databases

    HPAiCAB004350.
    HPA027956.

    Interactioni

    Subunit structurei

    Interacts (phosphorylated at Tyr-731) with PIK3R1. Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Also interacts with SORBS1 and INPPL1/SHIP2. Interacts with phosphorylated LAT2. May interact with CBLB By similarity. Interacts with ALK, AXL, BLK, FGR and FGFR2. Interacts with CSF1R, EPHB1, FLT1, KDR, PDGFRA and PDGFRB; regulates receptor degradation through ubiquitination. Interacts with HCK and LYN. Interacts with TEK/TIE2 (tyrosine phosphorylated).By similarity28 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP0-23EBI-518228,EBI-7358775
    ARHGEF7Q141559EBI-518228,EBI-717515
    CD2APQ9Y5K64EBI-518228,EBI-298152
    CRKP461086EBI-518228,EBI-886
    CRKLP461092EBI-518228,EBI-910
    EGFRP0053317EBI-518228,EBI-297353
    F2RL1P550853EBI-518228,EBI-4303189
    FLT1P179482EBI-518228,EBI-1026718
    FynP396883EBI-518228,EBI-524514From a different organism.
    GRB2P629938EBI-518228,EBI-401755
    ITSN1Q1581112EBI-518228,EBI-602041
    MAPK8P459832EBI-518228,EBI-286483
    METP0858115EBI-518228,EBI-1039152
    NTRK1P046292EBI-518228,EBI-1028226
    PIK3R1P279865EBI-518228,EBI-79464
    PLCG1P084873EBI-518228,EBI-8013886From a different organism.
    SH2B2O144927EBI-518228,EBI-7507432
    SH3KBP1Q96B9718EBI-518228,EBI-346595
    SPRY2O4359717EBI-518228,EBI-742487
    SPRY4Q9C0049EBI-518228,EBI-354861
    SRCP129318EBI-518228,EBI-621482
    SYKP434052EBI-518228,EBI-78302
    YWHABP319463EBI-518228,EBI-359815
    YWHAQP273486EBI-518228,EBI-359854

    Protein-protein interaction databases

    BioGridi107315. 218 interactions.
    DIPiDIP-189N.
    IntActiP22681. 67 interactions.
    MINTiMINT-109040.
    STRINGi9606.ENSP00000264033.

    Structurei

    Secondary structure

    1
    906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi53 – 7018
    Helixi73 – 753
    Beta strandi79 – 824
    Helixi84 – 10118
    Turni102 – 1043
    Helixi106 – 1116
    Helixi113 – 13624
    Helixi137 – 1415
    Helixi146 – 16823
    Helixi170 – 1723
    Helixi176 – 1783
    Helixi184 – 19411
    Beta strandi198 – 2014
    Helixi202 – 21211
    Helixi218 – 22811
    Beta strandi233 – 2375
    Helixi238 – 24710
    Helixi251 – 2533
    Helixi254 – 2618
    Turni262 – 2643
    Beta strandi268 – 2714
    Helixi274 – 2818
    Helixi282 – 2843
    Beta strandi290 – 2956
    Beta strandi297 – 2993
    Beta strandi302 – 3087
    Turni310 – 3123
    Beta strandi314 – 3174
    Beta strandi320 – 3223
    Helixi324 – 33310
    Turni350 – 3534
    Beta strandi354 – 3563
    Beta strandi360 – 3623
    Helixi365 – 3739
    Turni374 – 3763
    Beta strandi377 – 3804
    Turni382 – 3843
    Beta strandi385 – 3884
    Beta strandi391 – 3944
    Beta strandi398 – 4003
    Helixi402 – 41110
    Turni417 – 4193
    Beta strandi425 – 4284
    Beta strandi430 – 4323
    Helixi856 – 86611
    Helixi871 – 88010
    Turni881 – 8833
    Helixi885 – 89511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B47X-ray2.20A/B/C47-350[»]
    1FBVX-ray2.90A47-434[»]
    1YVHX-ray2.05A25-351[»]
    2CBLX-ray2.10A47-351[»]
    2JUJNMR-A851-906[»]
    2K4DNMR-A358-437[»]
    2OO9X-ray2.10A/B/C856-895[»]
    2Y1MX-ray2.67A/B/C/D/E/F47-435[»]
    2Y1NX-ray2.00A/C47-435[»]
    3BUMX-ray2.00B25-351[»]
    3BUNX-ray2.00B25-351[»]
    3BUOX-ray2.60B/D25-351[»]
    3BUWX-ray1.45B/D25-351[»]
    3BUXX-ray1.35B/D25-351[»]
    3OB1X-ray2.20B25-351[»]
    3OB2X-ray2.10B25-351[»]
    3PLFX-ray1.92B/D25-351[»]
    4A49X-ray2.21A354-435[»]
    4A4BX-ray2.79A47-435[»]
    4A4CX-ray2.70A47-435[»]
    4GPLX-ray3.00B47-351[»]
    ProteinModelPortaliP22681.
    SMRiP22681. Positions 48-435, 851-906.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22681.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 351305Cbl-PTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini856 – 89540UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 357357Sufficient for interaction with EPHB1Add
    BLAST
    Regioni47 – 1751294HAdd
    BLAST
    Regioni176 – 24873EF-hand-likeAdd
    BLAST
    Regioni249 – 351103SH2-likeAdd
    BLAST
    Regioni352 – 38029LinkerAdd
    BLAST
    Regioni648 – 906259Interaction with CD2APAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi357 – 476120Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi477 – 688212Pro-richAdd
    BLAST
    Compositional biasi689 – 834146Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
    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.

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri381 – 42040RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG242251.
    HOGENOMiHOG000294176.
    HOVERGENiHBG005255.
    InParanoidiP22681.
    KOiK04707.
    OMAiMEPRADV.
    OrthoDBiEOG7M0NQX.
    PhylomeDBiP22681.
    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.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR018957. Znf_C3HC4_RING-type.
    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.
    PF00627. UBA. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF47668. SSF47668. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS51506. CBL_PTB. 1 hit.
    PS50030. UBA. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22681-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGNVKKSSG AGGGSGSGGS GSGGLIGLMK DAFQPHHHHH HHLSPHPPGT    50
    VDKKMVEKCW KLMDKVVRLC QNPKLALKNS PPYILDLLPD TYQHLRTILS 100
    RYEGKMETLG ENEYFRVFME NLMKKTKQTI SLFKEGKERM YEENSQPRRN 150
    LTKLSLIFSH MLAELKGIFP SGLFQGDTFR ITKADAAEFW RKAFGEKTIV 200
    PWKSFRQALH EVHPISSGLE AMALKSTIDL TCNDYISVFE FDIFTRLFQP 250
    WSSLLRNWNS LAVTHPGYMA FLTYDEVKAR LQKFIHKPGS YIFRLSCTRL 300
    GQWAIGYVTA DGNILQTIPH NKPLFQALID GFREGFYLFP DGRNQNPDLT 350
    GLCEPTPQDH IKVTQEQYEL YCEMGSTFQL CKICAENDKD VKIEPCGHLM 400
    CTSCLTSWQE SEGQGCPFCR CEIKGTEPIV VDPFDPRGSG SLLRQGAEGA 450
    PSPNYDDDDD ERADDTLFMM KELAGAKVER PPSPFSMAPQ ASLPPVPPRL 500
    DLLPQRVCVP SSASALGTAS KAASGSLHKD KPLPVPPTLR DLPPPPPPDR 550
    PYSVGAESRP QRRPLPCTPG DCPSRDKLPP VPSSRLGDSW LPRPIPKVPV 600
    SAPSSSDPWT GRELTNRHSL PFSLPSQMEP RPDVPRLGST FSLDTSMSMN 650
    SSPLVGPECD HPKIKPSSSA NAIYSLAARP LPVPKLPPGE QCEGEEDTEY 700
    MTPSSRPLRP LDTSQSSRAC DCDQQIDSCT YEAMYNIQSQ APSITESSTF 750
    GEGNLAAAHA NTGPEESENE DDGYDVPKPP VPAVLARRTL SDISNASSSF 800
    GWLSLDGDPT TNVTEGSQVP ERPPKPFPRR INSERKAGSC QQGSGPAASA 850
    ATASPQLSSE IENLMSQGYS YQDIQKALVI AQNNIEMAKN ILREFVSISS 900
    PAHVAT 906
    Length:906
    Mass (Da):99,633
    Last modified:July 7, 2009 - v2
    Checksum:i1AA6BF67377322CA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151S → T in CAA40393. (PubMed:2030914)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti287 – 2871K → R Found in patients with acute myeloid leukemia; unknown pathological significance. 1 Publication
    VAR_071040
    Natural varianti365 – 3651Q → QSK Found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis.
    VAR_071041
    Natural varianti367 – 3671Q → P in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion. 1 Publication
    VAR_064332
    Natural varianti371 – 3711Y → H Found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis. 1 Publication
    Corresponds to variant rs267606706 [ dbSNP | Ensembl ].
    VAR_071042
    Natural varianti382 – 3821K → E in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion. 1 Publication
    VAR_064333
    Natural varianti390 – 3901D → Y in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion. 1 Publication
    VAR_064334
    Natural varianti420 – 4201R → Q in NSLL; causes impaired CBL-mediated degradation of cell-surface receptors in a dominant-negative fashion as well as constitutive ERK phosphorylation. 1 Publication
    VAR_064335
    Natural varianti499 – 4991R → L Found in patients with acute myeloid leukemia; unknown pathological significance. 1 Publication
    VAR_071043
    Natural varianti620 – 6201L → F.
    Corresponds to variant rs2227988 [ dbSNP | Ensembl ].
    VAR_057211
    Natural varianti782 – 7821P → L.
    Corresponds to variant rs2229073 [ dbSNP | Ensembl ].
    VAR_057212
    Natural varianti904 – 9041V → I.
    Corresponds to variant rs17122769 [ dbSNP | Ensembl ].
    VAR_057213

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57110 mRNA. Translation: CAA40393.1.
    AP002956 Genomic DNA. No translation available.
    BC132733 mRNA. Translation: AAI32734.1.
    BC136463 mRNA. Translation: AAI36464.1.
    CCDSiCCDS8418.1.
    PIRiA43817.
    RefSeqiNP_005179.2. NM_005188.3.
    UniGeneiHs.504096.

    Genome annotation databases

    EnsembliENST00000264033; ENSP00000264033; ENSG00000110395.
    GeneIDi867.
    KEGGihsa:867.
    UCSCiuc001pwe.4. human.

    Polymorphism databases

    DMDMi251757253.

    Keywords - Coding sequence diversityi

    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
    X57110 mRNA. Translation: CAA40393.1 .
    AP002956 Genomic DNA. No translation available.
    BC132733 mRNA. Translation: AAI32734.1 .
    BC136463 mRNA. Translation: AAI36464.1 .
    CCDSi CCDS8418.1.
    PIRi A43817.
    RefSeqi NP_005179.2. NM_005188.3.
    UniGenei Hs.504096.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B47 X-ray 2.20 A/B/C 47-350 [» ]
    1FBV X-ray 2.90 A 47-434 [» ]
    1YVH X-ray 2.05 A 25-351 [» ]
    2CBL X-ray 2.10 A 47-351 [» ]
    2JUJ NMR - A 851-906 [» ]
    2K4D NMR - A 358-437 [» ]
    2OO9 X-ray 2.10 A/B/C 856-895 [» ]
    2Y1M X-ray 2.67 A/B/C/D/E/F 47-435 [» ]
    2Y1N X-ray 2.00 A/C 47-435 [» ]
    3BUM X-ray 2.00 B 25-351 [» ]
    3BUN X-ray 2.00 B 25-351 [» ]
    3BUO X-ray 2.60 B/D 25-351 [» ]
    3BUW X-ray 1.45 B/D 25-351 [» ]
    3BUX X-ray 1.35 B/D 25-351 [» ]
    3OB1 X-ray 2.20 B 25-351 [» ]
    3OB2 X-ray 2.10 B 25-351 [» ]
    3PLF X-ray 1.92 B/D 25-351 [» ]
    4A49 X-ray 2.21 A 354-435 [» ]
    4A4B X-ray 2.79 A 47-435 [» ]
    4A4C X-ray 2.70 A 47-435 [» ]
    4GPL X-ray 3.00 B 47-351 [» ]
    ProteinModelPortali P22681.
    SMRi P22681. Positions 48-435, 851-906.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107315. 218 interactions.
    DIPi DIP-189N.
    IntActi P22681. 67 interactions.
    MINTi MINT-109040.
    STRINGi 9606.ENSP00000264033.

    PTM databases

    PhosphoSitei P22681.

    Polymorphism databases

    DMDMi 251757253.

    Proteomic databases

    MaxQBi P22681.
    PaxDbi P22681.
    PRIDEi P22681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264033 ; ENSP00000264033 ; ENSG00000110395 .
    GeneIDi 867.
    KEGGi hsa:867.
    UCSCi uc001pwe.4. human.

    Organism-specific databases

    CTDi 867.
    GeneCardsi GC11P119110.
    HGNCi HGNC:1541. CBL.
    HPAi CAB004350.
    HPA027956.
    MIMi 165360. gene.
    613563. phenotype.
    neXtProti NX_P22681.
    Orphaneti 86834. Juvenile myelomonocytic leukemia.
    363972. Noonan syndrome-like disorder with juvenile myelomonocytic leukemia.
    PharmGKBi PA26115.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242251.
    HOGENOMi HOG000294176.
    HOVERGENi HBG005255.
    InParanoidi P22681.
    KOi K04707.
    OMAi MEPRADV.
    OrthoDBi EOG7M0NQX.
    PhylomeDBi P22681.
    TreeFami TF314210.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_111080. Spry regulation of FGF signaling.
    REACT_111184. Negative regulation of FGFR signaling.
    REACT_111225. Regulation of KIT signaling.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_120850. TGF-beta receptor signaling activates SMADs.
    REACT_12484. EGFR downregulation.
    REACT_23787. Regulation of signaling by CBL.
    REACT_27307. Interleukin-6 signaling.
    SignaLinki P22681.

    Miscellaneous databases

    EvolutionaryTracei P22681.
    GeneWikii CBL_(gene).
    GenomeRNAii 867.
    NextBioi 3618.
    PMAP-CutDB P22681.
    PROi P22681.
    SOURCEi Search...

    Gene expression databases

    Bgeei P22681.
    CleanExi HS_CBL.
    Genevestigatori P22681.

    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.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR018957. Znf_C3HC4_RING-type.
    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.
    PF00627. UBA. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF47668. SSF47668. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS51506. CBL_PTB. 1 hit.
    PS50030. UBA. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif."
      Blake T.J., Shapiro M., Morse H.C. III, Langdon W.Y.
      Oncogene 6:653-657(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
    4. "The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase."
      Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M.
      Biochem. Biophys. Res. Commun. 257:129-138(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY HCK, INTERACTION WITH HCK.
    5. "The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase."
      Joazeiro C.A., Wing S.S., Huang H.-K., Leverson J.D., Hunter T., Liu Y.-C.
      Science 286:309-312(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor."
      Donovan J.A., Wange R.L., Langdon W.Y., Samelson L.E.
      J. Biol. Chem. 269:22921-22924(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLK.
    7. "Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation."
      Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.
      J. Biol. Chem. 270:20242-20245(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY EGFR, INTERACTION WITH EGFR.
    8. "The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70."
      Lupher M.L. Jr., Songyang Z., Shoelson S.E., Cantley L.C., Band H.
      J. Biol. Chem. 272:33140-33144(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZAP70.
    9. "Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases."
      Deckert M., Elly C., Altman A., Liu Y.C.
      J. Biol. Chem. 273:8867-8874(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY SYK AND FYN.
    10. Cited for: INTERACTION WITH LAT2.
    11. "C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus."
      Wilhelmsen K., Burkhalter S., van der Geer P.
      Oncogene 21:1079-1089(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSF1R, PHOSPHORYLATION.
    12. "Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation."
      Howlett C.J., Robbins S.M.
      Oncogene 21:1707-1716(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-381, INTERACTION WITH HCK.
    13. "Fgr but not Syk tyrosine kinase is a target for beta 2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils."
      Melander F., Andersson T., Dib K.
      Biochem. J. 370:687-694(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGR, PHOSPHORYLATION BY FGR.
    14. "APS, an adaptor protein containing pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl."
      Wakioka T., Sasaki A., Mitsui K., Yokouchi M., Inoue A., Komiya S., Yoshimura A.
      Leukemia 13:760-767(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2B2.
    15. "APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis."
      Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A., Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A.
      Oncogene 18:759-767(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2B2.
    16. "SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling."
      Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.
      Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA AND ZAP70, MUTAGENESIS OF GLY-306.
    17. Cited for: INTERACTION WITH SLA2.
    18. "The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction."
      Kirsch K.H., Georgescu M.M., Shishido T., Langdon W.Y., Birge R.B., Hanafusa H.
      J. Biol. Chem. 276:4957-4963(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD2AP.
    19. "APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes."
      Liu J., Kimura A., Baumann C.A., Saltiel A.R.
      Mol. Cell. Biol. 22:3599-3609(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2B2, MUTAGENESIS OF TYR-371; TYR-700; TYR-731 AND TYR-774, PHOSPHORYLATION AT TYR-371; TYR-700 AND TYR-774.
    20. "The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2."
      Vandenbroere I., Paternotte N., Dumont J.E., Erneux C., Pirson I.
      Biochem. Biophys. Res. Commun. 300:494-500(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INPPL1.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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.
    24. "Signal transduction via the stem cell factor receptor/c-Kit."
      Ronnstrand L.
      Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING AND KIT DEGRADATION.
    25. "Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl."
      Grossmann A.H., Kolibaba K.S., Willis S.G., Corbin A.S., Langdon W.S., Deininger M.W., Druker B.J.
      FEBS Lett. 577:555-562(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-700.
    26. "Src kinase activity is essential for osteoclast function."
      Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.
      J. Biol. Chem. 279:17660-17666(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT TYR-731, MUTAGENESIS OF TYR-731.
    27. "Cbl-mediated degradation of Lyn and Fyn induced by constitutive fibroblast growth factor receptor-2 activation supports osteoblast differentiation."
      Kaabeche K., Lemonnier J., Le Mee S., Caverzasio J., Marie P.J.
      J. Biol. Chem. 279:36259-36267(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH FGFR2; LYN AND FYN.
    28. "ALK receptor tyrosine kinase promotes cell growth and neurite outgrowth."
      Motegi A., Fujimoto J., Kotani M., Sakuraba H., Yamamoto T.
      J. Cell Sci. 117:3319-3329(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALK, PHOSPHORYLATION BY ALK.
    29. "Effects of Gas6 and hydrogen peroxide in Axl ubiquitination and downregulation."
      Valverde P.
      Biochem. Biophys. Res. Commun. 333:180-185(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXL.
    30. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
      Roskoski R. Jr.
      Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING AND KIT DEGRADATION.
    31. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "The localization of FGFR3 mutations causing thanatophoric dysplasia type I differentially affects phosphorylation, processing and ubiquitylation of the receptor."
      Bonaventure J., Horne W.C., Baron R.
      FEBS J. 274:3078-3093(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    34. "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation."
      Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H.
      J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB.
    35. "Lyn regulates BCR-ABL and Gab2 tyrosine phosphorylation and c-Cbl protein stability in imatinib-resistant chronic myelogenous leukemia cells."
      Wu J., Meng F., Lu H., Kong L., Bornmann W., Peng Z., Talpaz M., Donato N.J.
      Blood 111:3821-3829(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYN.
    36. "FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival."
      Dufour C., Guenou H., Kaabeche K., Bouvard D., Sanjay A., Marie P.J.
      Bone 42:1032-1039(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FGFR2, SUBCELLULAR LOCATION.
    37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    38. "Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway."
      Fasen K., Cerretti D.P., Huynh-Do U.
      Traffic 9:251-266(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHB1, PHOSPHORYLATION.
    39. "Angiopoietin-1-induced ubiquitylation of Tie2 by c-Cbl is required for internalization and degradation."
      Wehrle C., Van Slyke P., Dumont D.J.
      Biochem. J. 423:375-380(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TEK/TIE2, FUNCTION.
    40. "An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
      Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
      Curr. Biol. 19:1788-1798(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EGFR.
    41. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    42. "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
      Wardega P., Heldin C.H., Lennartsson J.
      Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION.
    43. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. "The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic differentiation in human mesenchymal stromal cells in part by decreased Cbl-mediated platelet-derived growth factor receptor alpha and fibroblast growth factor receptor 2 ubiquitination."
      Severe N., Miraoui H., Marie P.J.
      J. Biol. Chem. 286:24443-24450(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FGFR2.
    46. "Fibroblast growth factor signalling: from development to cancer."
      Turner N., Grose R.
      Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN FGF SIGNALING, UBIQUITINATION OF FGFR1.
    47. "Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase."
      Meng W., Sawasdikosol S., Burakoff S.J., Eck M.J.
      Nature 398:84-90(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-350 IN COMPLEX WITH ZAP70 PEPTIDE AND CALCIUM IONS, CALCIUM-BINDING SITE, MUTAGENESIS OF SER-80; PRO-82; ASP-229; GLU-240; ARG-294 AND GLY-306.
    48. "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases."
      Zheng N., Wang P., Jeffrey P.D., Pavletich N.P.
      Cell 102:533-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 47-434 IN COMPLEX WITH ZAP70 AND UBE2L3.
    49. Cited for: VARIANTS NSLL PRO-367; GLU-382; TYR-390 AND GLN-420, CHARACTERIZATION OF VARIANTS NSLL PRO-367; GLU-382; TYR-390 AND GLN-420.
    50. "Novel oncogenic mutations of CBL in human acute myeloid leukemia that activate growth and survival pathways depend on increased metabolism."
      Fernandes M.S., Reddy M.M., Croteau N.J., Walz C., Weisbach H., Podar K., Band H., Carroll M., Reiter A., Larson R.A., Salgia R., Griffin J.D., Sattler M.
      J. Biol. Chem. 285:32596-32605(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-287; SER-LYS-365 INS; HIS-371 AND LEU-499, CHARACTERIZATION OF VARIANTS SER-LYS-365 INS AND HIS-371, PHOSPHORYLATION AT TYR-674; TYR-700 AND TYR-774.

    Entry informationi

    Entry nameiCBL_HUMAN
    AccessioniPrimary (citable) accession number: P22681
    Secondary accession number(s): A3KMP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 178 of the entry and version 2 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 11
      Human chromosome 11: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3