Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P22682 (CBL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cbl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length913 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.13 Ref.21 Ref.22

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.4 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20

Subcellular location

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

Domain

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.

Post-translational modification

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. Ref.4 Ref.5 Ref.6 Ref.10 Ref.15 Ref.16 Ref.20 Ref.21

Ubiquitinated, leading to its degradation via the proteasome By similarity.

Involvement in disease

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

Miscellaneous

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

Sequence similarities

Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain.

Contains 1 RING-type zinc finger.

Contains 1 UBA domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DiseaseProto-oncogene
   DomainRepeat
Zinc-finger
   LigandCalcium
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: InterPro

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSH3 domain binding

Inferred from physical interaction Ref.8. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

ephrin receptor binding

Inferred from physical interaction Ref.20. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ddx58Q6Q8993EBI-640919,EBI-6841237
EGFRP005332EBI-640919,EBI-297353From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 913913E3 ubiquitin-protein ligase CBL
PRO_0000055859

Regions

Domain45 – 349305Cbl-PTB
Domain863 – 90240UBA
Calcium binding225 – 23814 By similarity
Zinc finger379 – 41840RING-type
Region1 – 355355Sufficient for interaction with EPHB1
Region45 – 1731294H
Region174 – 24673EF-hand-like
Region247 – 349103SH2-like
Region350 – 37829Linker
Region646 – 913268Interaction with CD2AP By similarity
Compositional bias372 – 474103Asp/Glu-rich (acidic)
Compositional bias475 – 686212Pro-rich
Compositional bias687 – 839153Asp/Glu-rich (acidic)

Sites

Binding site2921Phosphotyrosine By similarity

Amino acid modifications

Modified residue1391Phosphotyrosine By similarity
Modified residue1951N6-acetyllysine By similarity
Modified residue3691Phosphotyrosine By similarity
Modified residue4501Phosphoserine By similarity
Modified residue4531Phosphotyrosine By similarity
Modified residue5501Phosphotyrosine By similarity
Modified residue6651Phosphoserine By similarity
Modified residue6661Phosphoserine Ref.18
Modified residue6671Phosphoserine Ref.18
Modified residue6721Phosphotyrosine Ref.18
Modified residue6731Phosphoserine By similarity
Modified residue6981Phosphotyrosine; by ABL1
Modified residue7371Phosphotyrosine; by SRC By similarity
Modified residue7801Phosphotyrosine By similarity
Modified residue9071Phosphoserine By similarity

Natural variations

Natural variant364 – 38017Missing in oncogenic variant 70Z/3.

Experimental info

Mutagenesis3041G → E: Abolishes interaction with ZAP70, but does not affect interaction with SLA. Ref.12
Sequence conflict72 – 732KL → NV in CAA40394. Ref.1
Sequence conflict2181E → D in BAC26087. Ref.2
Sequence conflict5921P → T in CAA40394. Ref.1
Sequence conflict7421N → T in CAA40394. Ref.1

Secondary structure

........ 913
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22682 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 22F8A5C29F0262B8

FASTA913100,564
        10         20         30         40         50         60 
MAGNVKKSSG AGGGGSGGSG AGGLIGLMKD AFQPHHHHHH LSPHPPCTVD KKMVEKCWKL 

        70         80         90        100        110        120 
MDKVVRLCQN PKLALKNSPP YILDLLPDTY QHLRTVLSRY EGKMETLGEN EYFRVFMENL 

       130        140        150        160        170        180 
MKKTKQTISL FKEGKERMYE ENSQPRRNLT KLSLIFSHML AELKGIFPSG LFQGDTFRIT 

       190        200        210        220        230        240 
KADAAEFWRK AFGEKTIVPW KSFRQALHEV HPISSGLEAM ALKSTIDLTC NDYISVFEFD 

       250        260        270        280        290        300 
IFTRLFQPWS SLLRNWNSLA VTHPGYMAFL TYDEVKARLQ KFIHKPGSYI FRLSCTRLGQ 

       310        320        330        340        350        360 
WAIGYVTADG NILQTIPHNK PLFQALIDGF REGFYLFPDG RNQNPDLTGL CEPTPQDHIK 

       370        380        390        400        410        420 
VTQEQYELYC EMGSTFQLCK ICAENDKDVK IEPCGHLMCT SCLTSWQESE GQGCPFCRCE 

       430        440        450        460        470        480 
IKGTEPIVVD PFDPRGSGSL LRQGAEGAPS PNYDDDDDER ADDSLFMMKE LAGAKVERPS 

       490        500        510        520        530        540 
SPFSMAPQAS LPPVPPRLDL LQQRAPVPAS TSVLGTASKA ASGSLHKDKP LPIPPTLRDL 

       550        560        570        580        590        600 
PPPPPPDRPY SVGAETRPQR RPLPCTPGDC PSRDKLPPVP SSRPGDSWLS RPIPKVPVAT 

       610        620        630        640        650        660 
PNPGDPWNGR ELTNRHSLPF SLPSQMEPRA DVPRLGSTFS LDTSMTMNSS PVAGPESEHP 

       670        680        690        700        710        720 
KIKPSSSANA IYSLAARPLP MPKLPPGEQG ESEEDTEYMT PTSRPVGVQK PEPKRPLEAT 

       730        740        750        760        770        780 
QSSRACDCDQ QIDSCTYEAM YNIQSQALSV AENSASGEGN LATAHTSTGP EESENEDDGY 

       790        800        810        820        830        840 
DVPKPPVPAV LARRTLSDIS NASSSFGWLS LDGDPTNFNE GSQVPERPPK PFPRRINSER 

       850        860        870        880        890        900 
KASSYQQGGG ATANPVATAP SPQLSSEIER LMSQGYSYQD IQKALVIAHN NIEMAKNILR 

       910 
EFVSISSPAH VAT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57111 mRNA. Translation: CAA40394.1.
AK028730 mRNA. Translation: BAC26087.1.
AK153915 mRNA. Translation: BAE32253.1.
BC125285 mRNA. Translation: AAI25286.1.
PIRB43817.
RefSeqNP_031645.2. NM_007619.2.
UniGeneMm.266871.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9SNMR-A/B863-902[»]
ProteinModelPortalP22682.
SMRP22682. Positions 46-435, 857-913.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198527. 54 interactions.
IntActP22682. 15 interactions.
MINTMINT-255892.

PTM databases

PhosphoSiteP22682.

Proteomic databases

PaxDbP22682.
PRIDEP22682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037644; ENSMUSP00000041902; ENSMUSG00000034342.
GeneID12402.
KEGGmmu:12402.
UCSCuc009pce.1. mouse.

Organism-specific databases

CTD867.
MGIMGI:88279. Cbl.

Phylogenomic databases

eggNOGNOG242251.
GeneTreeENSGT00390000011617.
HOGENOMHOG000294176.
HOVERGENHBG005255.
InParanoidQ3U527.
KOK04707.
OMATTNFTEG.
OrthoDBEOG7M0NQX.
TreeFamTF314210.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeP22682.
CleanExMM_CBL.
GenevestigatorP22682.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.20.930.20. 1 hit.
3.30.40.10. 1 hit.
3.30.505.10. 1 hit.
InterProIPR024162. 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]
PANTHERPTHR23007. PTHR23007. 1 hit.
PfamPF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF47668. SSF47668. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS51506. CBL_PTB. 1 hit.
PS50030. UBA. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22682.
NextBio281170.
PROP22682.
SOURCESearch...

Entry information

Entry nameCBL_MOUSE
AccessionPrimary (citable) accession number: P22682
Secondary accession number(s): Q3U527, Q8CEA1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot