P22682

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession CBL_MOUSE; P22682;
Entrez ID 12402
GenBank Protein ID
GenBank Nucleotide ID
Protein Name E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)
Gene Name Cbl
Organism Mus musculus
NCBI Taxa ID 10090
Functional DescriptionAdapter 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.
Sequence
(Fasta)
MAGNVKKSSG AGGGGSGGSG AGGLIGLMKD AFQPHHHHHH LSPHPPCTVD KKMVEKCWKL 60
MDKVVRLCQN PKLALKNSPP YILDLLPDTY QHLRTVLSRY EGKMETLGEN EYFRVFMENL 120
MKKTKQTISL FKEGKERMYE ENSQPRRNLT KLSLIFSHML AELKGIFPSG LFQGDTFRIT 180
KADAAEFWRK AFGEKTIVPW KSFRQALHEV HPISSGLEAM ALKSTIDLTC NDYISVFEFD 240
IFTRLFQPWS SLLRNWNSLA VTHPGYMAFL TYDEVKARLQ KFIHKPGSYI FRLSCTRLGQ 300
WAIGYVTADG NILQTIPHNK PLFQALIDGF REGFYLFPDG RNQNPDLTGL CEPTPQDHIK 360
VTQEQYELYC EMGSTFQLCK ICAENDKDVK IEPCGHLMCT SCLTSWQESE GQGCPFCRCE 420
IKGTEPIVVD PFDPRGSGSL LRQGAEGAPS PNYDDDDDER ADDSLFMMKE LAGAKVERPS 480
SPFSMAPQAS LPPVPPRLDL LQQRAPVPAS TSVLGTASKA ASGSLHKDKP LPIPPTLRDL 540
PPPPPPDRPY SVGAETRPQR RPLPCTPGDC PSRDKLPPVP SSRPGDSWLS RPIPKVPVAT 600
PNPGDPWNGR ELTNRHSLPF SLPSQMEPRA DVPRLGSTFS LDTSMTMNSS PVAGPESEHP 660
KIKPSSSANA IYSLAARPLP MPKLPPGEQG ESEEDTEYMT PTSRPVGVQK PEPKRPLEAT 720
QSSRACDCDQ QIDSCTYEAM YNIQSQALSV AENSASGEGN LATAHTSTGP EESENEDDGY 780
DVPKPPVPAV LARRTLSDIS NASSSFGWLS LDGDPTNFNE GSQVPERPPK PFPRRINSER 840
KASSYQQGGG ATANPVATAP SPQLSSEIER LMSQGYSYQD IQKALVIAHN NIEMAKNILR 900
EFVSISSPAH VAT 914

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1PhosphorylationLymphomaU8770364
[Reference]: A mutation to cbl in the 70Z/3 pre-B cell lymphoma produces an oncogenic protein which exhibits a marked enhancement of tyrosine phosphorylation.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 7)
(view all)
MESH:D003456 ; Cryptorchidism
MESH:D002658 ; Developmental Disabilities
MESH:D006130 ; Growth Disorders
MESH:D007248 ; Infertility, Male
MESH:D054429 ; Leukemia, Myelomonocytic, Juvenile
OMIM:613563 ; NOONAN SYNDROME-LIKE DISORDER WITH OR WITHOUT JUVENILE MYELOMONOCYTIC LEUKEMIA

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 40)
(view all)
362       PQDHIKVTQEQYELY     dbPAF
437       DPFDPRGSGSLLRQG     dbPAF
439       FDPRGSGSLLRQGAE     dbPAF
450       QGAEGAPSPNYDDDD     dbPAF
453       EGAPSPNYDDDDDER     dbPAF
480       GAKVERPSSPFSMAP     dbPAF
Acetylation
(count: 1)
285       RLQKFIHKPGSYIFR     PLMD
Ubiquitination
(count: 1)
201       EKTIVPWKSFRQALH     PLMD
Succinylation
(count: 1)
285       RLQKFIHKPGSYIFR     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource