P22682 (CBL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Cbl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	913 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. Ref.9 Ref.11 Ref.13 Ref.22 Ref.23
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.16 Ref.17 Ref.18 Ref.20 Ref.21
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.16 Ref.17 Ref.21 Ref.22 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 process	Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Domain	Repeat Zinc-finger
Ligand	Calcium Metal-binding Zinc
Molecular function	Ligase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone 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: Compara positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro 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
EGFR	P00533	2	EBI-640919,EBI-297353	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 913

913

E3 ubiquitin-protein ligase CBL

PRO_0000055859

Regions

Domain

45 – 349

305

Cbl-PTB

Domain

863 – 902

40

UBA

Calcium binding

225 – 238

14

By similarity

Zinc finger

379 – 418

40

RING-type

Region

1 – 355

355

Sufficient for interaction with EPHB1

Region

45 – 173

129

4H

Region

174 – 246

73

EF-hand-like

Region

247 – 349

103

SH2-like

Region

350 – 378

29

Linker

Region

646 – 913

268

Interaction with CD2AP By similarity

Compositional bias

372 – 474

103

Asp/Glu-rich (acidic)

Compositional bias

475 – 686

212

Pro-rich

Compositional bias

687 – 839

153

Asp/Glu-rich (acidic)

Sites

Binding site

292

1

Phosphotyrosine By similarity

Amino acid modifications

Modified residue

139

1

Phosphotyrosine By similarity

Modified residue

195

1

N6-acetyllysine By similarity

Modified residue

369

1

Phosphotyrosine By similarity

Modified residue

450

1

Phosphoserine By similarity

Modified residue

453

1

Phosphotyrosine By similarity

Modified residue

550

1

Phosphotyrosine By similarity

Modified residue

665

1

Phosphoserine By similarity

Modified residue

666

1

Phosphoserine Ref.19

Modified residue

667

1

Phosphoserine Ref.19

Modified residue

672

1

Phosphotyrosine Ref.15 Ref.19

Modified residue

673

1

Phosphoserine By similarity

Modified residue

692

1

Phosphoserine Ref.15

Modified residue

698

1

Phosphotyrosine; by ABL1 Ref.15

Modified residue

737

1

Phosphotyrosine; by SRC By similarity

Modified residue

780

1

Phosphotyrosine By similarity

Modified residue

907

1

Phosphoserine By similarity

Natural variations

Natural variant

364 – 380

17

Missing in oncogenic variant 70Z/3.

Experimental info

Mutagenesis

304

1

G → E: Abolishes interaction with ZAP70, but does not affect interaction with SLA. Ref.12

Sequence conflict

72 – 73

2

KL → NV in CAA40394. Ref.1

Sequence conflict

218

1

E → D in BAC26087. Ref.2

Sequence conflict

592

1

P → T in CAA40394. Ref.1

Sequence conflict

742

1

N → T in CAA40394. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

913

Helix Strand Turn

Details...

Helix

865 – 874

10

Helix

878 – 887

10

Turn

888 – 890

3

Helix

892 – 902

11

Sequences

	Sequence		Length	Mass (Da)
	P22682 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 22F8A5C29F0262B8	FASTA	913	100,564
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672; SER-692 AND TYR-698, MASS SPECTROMETRY.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Mast cell.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.

IPI

IPI00323590.

PIR

B43817.

RefSeq

NP_031645.2. NM_007619.2.

UniGene

Mm.266871.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9S	NMR	-	A/B	863-902	[»]

ProteinModelPortal

P22682.

SMR

P22682. Positions 46-435, 857-913.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22682. 5 interactions.

MINT

MINT-255892.

PTM databases

PhosphoSite

P22682.

Proteomic databases

PaxDb

P22682.

PRIDE

P22682.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000037644; ENSMUSP00000041902; ENSMUSG00000034342.

GeneID

12402.

KEGG

mmu:12402.

Organism-specific databases

CTD

867.

MGI

MGI:88279. Cbl.

Phylogenomic databases

eggNOG

NOG242251.

GeneTree

ENSGT00390000011617.

HOGENOM

HOG000294176.

HOVERGEN

HBG005255.

InParanoid

Q3U527.

KO

K04707.

OMA

TTNFTEG.

OrthoDB

EOG444KJR.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

Bgee

P22682.

CleanEx

MM_CBL.

Genevestigator

P22682.

GermOnline

ENSMUSG00000034342. Mus musculus.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.
1.20.930.20. 1 hit.
3.30.40.10. 1 hit.
3.30.505.10. 1 hit.

InterPro

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-like_dom.
IPR000980. SH2.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

PANTHER

PTHR23007. PTHR23007. 1 hit.

Pfam

PF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]

SUPFAM

SSF47668. Adaptor_Cbl_N. 1 hit.
SSF46934. UBA_like. 1 hit.

PROSITE

PS51506. CBL_PTB. 1 hit.
PS50030. UBA. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22682.

NextBio

281170.

SOURCE

Search...

Entry information

Entry name

CBL_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program