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P22682

- CBL_MOUSE

UniProt

P22682 - CBL_MOUSE

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Protein
E3 ubiquitin-protein ligase CBL
Gene
Cbl
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-737' 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 UB2D3.5 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei292 – 2921Phosphotyrosine By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi225 – 23814 By similarity
Add
BLAST
Zinc fingeri379 – 41840RING-type
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. bone resorption Source: UniProtKB
  2. cell surface receptor signaling pathway Source: InterPro
  3. negative regulation of apoptotic process Source: Ensembl
  4. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  5. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_198525. Negative regulation of FGFR signaling.
REACT_198526. Spry regulation of FGF signaling.
REACT_198634. Regulation of signaling by CBL.
REACT_199118. Interleukin-6 signaling.
REACT_199123. Signaling by constitutively active EGFR.
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_203917. EGFR downregulation.
REACT_227425. Regulation of KIT signaling.
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
Signal transduction protein CBL
Gene namesi
Name:Cbl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:88279. Cbl.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: InterPro
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Can be converted to an oncogenic protein by deletions or mutations that disturb its ability to down-regulate RTKs.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi304 – 3041G → E: Abolishes interaction with ZAP70, but does not affect interaction with SLA. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 913913E3 ubiquitin-protein ligase CBL
PRO_0000055859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei139 – 1391Phosphotyrosine By similarity
Modified residuei369 – 3691Phosphotyrosine By similarity
Modified residuei450 – 4501Phosphoserine By similarity
Modified residuei453 – 4531Phosphotyrosine By similarity
Modified residuei550 – 5501Phosphotyrosine By similarity
Modified residuei665 – 6651Phosphoserine By similarity
Modified residuei666 – 6661Phosphoserine1 Publication
Modified residuei667 – 6671Phosphoserine1 Publication
Modified residuei672 – 6721Phosphotyrosine1 Publication
Modified residuei673 – 6731Phosphoserine By similarity
Modified residuei698 – 6981Phosphotyrosine; by ABL1
Modified residuei737 – 7371Phosphotyrosine; by SRC By similarity
Modified residuei780 – 7801Phosphotyrosine By similarity
Modified residuei907 – 9071Phosphoserine By similarity

Post-translational modificationi

Phosphorylated on tyrosine residues by ALK, EGFR, FGR, INSR, SYK, FYN and ZAP70. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Phosphorylated on tyrosine residues by activated PDGFRA and PDGFRB By similarity. Phosphorylated on tyrosine residues in response to CSF1R, FLT1 and KIT signaling. Phosphorylated on tyrosine residues by HCK.8 Publications
Ubiquitinated, leading to its degradation via the proteasome By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP22682.
PaxDbiP22682.
PRIDEiP22682.

PTM databases

PhosphoSiteiP22682.

Expressioni

Gene expression databases

BgeeiP22682.
CleanExiMM_CBL.
GenevestigatoriP22682.

Interactioni

Subunit structurei

Interacts (phosphorylated) with PIK3R1. Interacts with phosphorylated LAT2 By similarity. 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. Interacts with FGR. Also interacts with BLK, SORBS1 and INPPL1/SHIP2. May interact with CBLB. Interacts with TEK/TIE2 (tyrosine phosphorylated) By similarity. Interacts with ALK, AXL and FGFR2. Interacts with CSF1R, EPHB1, FLT1, KDR, PDGFRA and PDGFRB; regulates receptor degradation through ubiquitination. Interacts with HCK and LYN. Interacts with ATX2.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ddx58Q6Q8993EBI-640919,EBI-6841237
EGFRP005332EBI-640919,EBI-297353From a different organism.
EgfrQ012792EBI-640919,EBI-6296235
MetP160562EBI-640919,EBI-1798780

Protein-protein interaction databases

BioGridi198527. 54 interactions.
IntActiP22682. 15 interactions.
MINTiMINT-255892.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi865 – 87410
Helixi878 – 88710
Turni888 – 8903
Helixi892 – 90211

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9SNMR-A/B863-902[»]
ProteinModelPortaliP22682.
SMRiP22682. Positions 46-435, 857-913.

Miscellaneous databases

EvolutionaryTraceiP22682.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 349305Cbl-PTB
Add
BLAST
Domaini863 – 90240UBA
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 355355Sufficient for interaction with EPHB1
Add
BLAST
Regioni45 – 1731294H
Add
BLAST
Regioni174 – 24673EF-hand-like
Add
BLAST
Regioni247 – 349103SH2-like
Add
BLAST
Regioni350 – 37829Linker
Add
BLAST
Regioni646 – 913268Interaction with CD2AP By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi372 – 474103Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi475 – 686212Pro-rich
Add
BLAST
Compositional biasi687 – 839153Asp/Glu-rich (acidic)
Add
BLAST

Domaini

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG242251.
GeneTreeiENSGT00390000011617.
HOGENOMiHOG000294176.
HOVERGENiHBG005255.
InParanoidiQ3U527.
KOiK04707.
OMAiMEPRADV.
OrthoDBiEOG7M0NQX.
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.
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.
[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.

P22682-1 [UniParc]FASTAAdd to Basket

« Hide

MAGNVKKSSG AGGGGSGGSG AGGLIGLMKD AFQPHHHHHH LSPHPPCTVD    50
KKMVEKCWKL MDKVVRLCQN PKLALKNSPP YILDLLPDTY QHLRTVLSRY 100
EGKMETLGEN EYFRVFMENL MKKTKQTISL FKEGKERMYE ENSQPRRNLT 150
KLSLIFSHML AELKGIFPSG LFQGDTFRIT KADAAEFWRK AFGEKTIVPW 200
KSFRQALHEV HPISSGLEAM ALKSTIDLTC NDYISVFEFD IFTRLFQPWS 250
SLLRNWNSLA VTHPGYMAFL TYDEVKARLQ KFIHKPGSYI FRLSCTRLGQ 300
WAIGYVTADG NILQTIPHNK PLFQALIDGF REGFYLFPDG RNQNPDLTGL 350
CEPTPQDHIK VTQEQYELYC EMGSTFQLCK ICAENDKDVK IEPCGHLMCT 400
SCLTSWQESE GQGCPFCRCE IKGTEPIVVD PFDPRGSGSL LRQGAEGAPS 450
PNYDDDDDER ADDSLFMMKE LAGAKVERPS SPFSMAPQAS LPPVPPRLDL 500
LQQRAPVPAS TSVLGTASKA ASGSLHKDKP LPIPPTLRDL PPPPPPDRPY 550
SVGAETRPQR RPLPCTPGDC PSRDKLPPVP SSRPGDSWLS RPIPKVPVAT 600
PNPGDPWNGR ELTNRHSLPF SLPSQMEPRA DVPRLGSTFS LDTSMTMNSS 650
PVAGPESEHP KIKPSSSANA IYSLAARPLP MPKLPPGEQG ESEEDTEYMT 700
PTSRPVGVQK PEPKRPLEAT QSSRACDCDQ QIDSCTYEAM YNIQSQALSV 750
AENSASGEGN LATAHTSTGP EESENEDDGY DVPKPPVPAV LARRTLSDIS 800
NASSSFGWLS LDGDPTNFNE GSQVPERPPK PFPRRINSER KASSYQQGGG 850
ATANPVATAP SPQLSSEIER LMSQGYSYQD IQKALVIAHN NIEMAKNILR 900
EFVSISSPAH VAT 913
Length:913
Mass (Da):100,564
Last modified:July 27, 2011 - v3
Checksum:i22F8A5C29F0262B8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti364 – 38017Missing in oncogenic variant 70Z/3.
Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 732KL → NV in CAA40394. 1 Publication
Sequence conflicti218 – 2181E → D in BAC26087. 1 Publication
Sequence conflicti592 – 5921P → T in CAA40394. 1 Publication
Sequence conflicti742 – 7421N → T in CAA40394. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57111 mRNA. Translation: CAA40394.1.
AK028730 mRNA. Translation: BAC26087.1.
AK153915 mRNA. Translation: BAE32253.1.
BC125285 mRNA. Translation: AAI25286.1.
CCDSiCCDS40598.1.
PIRiB43817.
RefSeqiNP_031645.2. NM_007619.2.
UniGeneiMm.266871.

Genome annotation databases

EnsembliENSMUST00000037644; ENSMUSP00000041902; ENSMUSG00000034342.
GeneIDi12402.
KEGGimmu:12402.
UCSCiuc009pce.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57111 mRNA. Translation: CAA40394.1 .
AK028730 mRNA. Translation: BAC26087.1 .
AK153915 mRNA. Translation: BAE32253.1 .
BC125285 mRNA. Translation: AAI25286.1 .
CCDSi CCDS40598.1.
PIRi B43817.
RefSeqi NP_031645.2. NM_007619.2.
UniGenei Mm.266871.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D9S NMR - A/B 863-902 [» ]
ProteinModelPortali P22682.
SMRi P22682. Positions 46-435, 857-913.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198527. 54 interactions.
IntActi P22682. 15 interactions.
MINTi MINT-255892.

PTM databases

PhosphoSitei P22682.

Proteomic databases

MaxQBi P22682.
PaxDbi P22682.
PRIDEi P22682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037644 ; ENSMUSP00000041902 ; ENSMUSG00000034342 .
GeneIDi 12402.
KEGGi mmu:12402.
UCSCi uc009pce.1. mouse.

Organism-specific databases

CTDi 867.
MGIi MGI:88279. Cbl.

Phylogenomic databases

eggNOGi NOG242251.
GeneTreei ENSGT00390000011617.
HOGENOMi HOG000294176.
HOVERGENi HBG005255.
InParanoidi Q3U527.
KOi K04707.
OMAi MEPRADV.
OrthoDBi EOG7M0NQX.
TreeFami TF314210.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_198525. Negative regulation of FGFR signaling.
REACT_198526. Spry regulation of FGF signaling.
REACT_198634. Regulation of signaling by CBL.
REACT_199118. Interleukin-6 signaling.
REACT_199123. Signaling by constitutively active EGFR.
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_203917. EGFR downregulation.
REACT_227425. Regulation of KIT signaling.

Miscellaneous databases

EvolutionaryTracei P22682.
NextBioi 281170.
PROi P22682.
SOURCEi Search...

Gene expression databases

Bgeei P22682.
CleanExi MM_CBL.
Genevestigatori P22682.

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.
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.
[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

« Hide 'large scale' publications
  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], MUTANT 70Z/3.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Skin and Thymus.
  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].
    Tissue: Brain.
  4. "Tyrosine phosphorylation and translocation of the c-cbl protein after activation of tyrosine kinase signaling pathways."
    Tanaka S., Neff L., Baron R., Levy J.B.
    J. Biol. Chem. 270:14347-14351(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN, PHOSPHORYLATION.
  5. "Differential intrinsic enzymatic activity of Syk and Zap-70 protein-tyrosine kinases."
    Latour S., Chow L.M., Veillette A.
    J. Biol. Chem. 271:22782-22790(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SYK.
  6. "Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes."
    Fournel M., Davidson D., Weil R., Veillette A.
    J. Exp. Med. 183:301-306(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY ZAP70.
  7. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
    Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
    J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1.
  8. "A novel, multifunctional c-Cbl binding protein in insulin receptor signaling in 3T3-L1 adipocytes."
    Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.
    Mol. Cell. Biol. 18:872-879(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SORBS1.
  9. "The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha."
    Miyake S., Lupher M.L. Jr., Druker B., Band H.
    Proc. Natl. Acad. Sci. U.S.A. 95:7927-7932(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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.
  11. "The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation."
    Lee P.S., Wang Y., Dominguez M.G., Yeung Y.G., Murphy M.A., Bowtell D.D., Stanley E.R.
    EMBO J. 18:3616-3628(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Functional cooperation between c-Cbl and Src-like adaptor protein 2 in the negative regulation of T-cell receptor signaling."
    Loreto M.P., Berry D.M., McGlade C.J.
    Mol. Cell. Biol. 22:4241-4255(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLA2 AND ZAP70, MUTAGENESIS OF GLY-304.
  13. "Vascular endothelial growth factor-dependent down-regulation of Flk-1/KDR involves Cbl-mediated ubiquitination. Consequences on nitric oxide production from endothelial cells."
    Duval M., Bedard-Goulet S., Delisle C., Gratton J.P.
    J. Biol. Chem. 278:20091-20097(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDR, FUNCTION.
  14. "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport."
    Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.
    J. Biol. Chem. 278:36754-36762(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLB.
  15. "The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and degradation of Flt-1 (VEGFR-1)."
    Kobayashi S., Sawano A., Nojima Y., Shibuya M., Maru Y.
    FASEB J. 18:929-931(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1 AND CD2AP, PHOSPHORYLATION IN RESPONSE TO VEGFA.
  16. "The Src-like adaptor protein 2 regulates colony-stimulating factor-1 receptor signaling and down-regulation."
    Pakuts B., Debonneville C., Liontos L.M., Loreto M.P., McGlade C.J.
    J. Biol. Chem. 282:17953-17963(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH SLA2 AND CSF1R.
  17. "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.
  18. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-667 AND TYR-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  19. "Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking."
    Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.
    Cell. Signal. 20:1725-1739(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATX2.
  20. "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.
  21. "The D816V mutation of c-Kit circumvents a requirement for Src family kinases in c-Kit signal transduction."
    Sun J., Pedersen M., Ronnstrand L.
    J. Biol. Chem. 284:11039-11047(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF KIT, PHOSPHORYLATION.
  22. "The SAM domains of Anks family proteins are critically involved in modulating the degradation of EphA receptors."
    Kim J., Lee H., Kim Y., Yoo S., Park E., Park S.
    Mol. Cell. Biol. 30:1582-1592(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF EPHA8.

Entry informationi

Entry nameiCBL_MOUSE
AccessioniPrimary (citable) accession number: P22682
Secondary accession number(s): Q3U527, Q8CEA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein has one functional calcium-binding site By similarity.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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