CBLC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CBLC_HUMAN
• UniProt AC: Q9ULV8
• Protein Name: E3 ubiquitin-protein ligase CBL-C
• Gene Name: CBLC
• Organism: Homo sapiens (Human).
• Sequence Length: 474
• Protein Description: 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. Functionally coupled with the E2 ubiquitin-protein ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1, but not isoform 2, inhibits EGF stimulated MAPK1 activation. Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In collaboration with CD2AP may act as regulatory checkpoint for Ret signaling by modulating the rate of RET degradation after ligand activation; CD2AP converts it from an inhibitor to a promoter of RET degradation; the function limits the potency of GDNF on neuronal survival..
• Protein Sequence: MALAVAPWGRQWEEARALGRAVRMLQRLEEQCVDPRLSVSPPSLRDLLPRTAQLLREVAHSRRAAGGGGPGGPGGSGDFLLIYLANLEAKSRQVAALLPPRGRRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNPDLTELGQAEPQQRIHVSEEQLQLYWAMDSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWEAVSIYQFHGQATAEDSGNSSDQEGRELELGQVPLSAPPLPPRPDLPPRKPRNAQPKVRLLKGNSPPAALGPQDPAPA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
40	Phosphorylation	VDPRLSVSPPSLRDL CCCCCCCCCCCHHHH	27.93	28355574
43	Phosphorylation	RLSVSPPSLRDLLPR CCCCCCCCHHHHHHH	39.15	22167270
61	Phosphorylation	LLREVAHSRRAAGGG HHHHHHHHHHHCCCC	17.45	19413330
90	Ubiquitination	YLANLEAKSRQVAAL EEECCHHHHHHHHHH	36.47	-
105	Phosphorylation	LPPRGRRSANDELFR CCCCCCCCCCHHHHH	30.02	29496963
144	Phosphorylation	ALFPGGKYCGHMYQL HHCCCCCCCCCCEEE	13.62	22817900
223	Phosphorylation	RLFQPWPTLLKNWQL HHCCCHHHHHHHCEE	40.63	-
257	Ubiquitination	RLQACRDKPGSYIFR HHHHHCCCCCCEEEC	31.74	27667366
267	Ubiquitination	SYIFRPSCTRLGQWA CEEECCCCCCCCCEE	2.58	22817900
309	Phosphorylation	QKDGFYLYPDGKTHN CCCCEEECCCCCCCC	6.47	-
313	Ubiquitination	FYLYPDGKTHNPDLT EEECCCCCCCCCCHH	54.73	22817900
341	Phosphorylation	SEEQLQLYWAMDSTF CHHHHHHHHHHHCHH	4.34	10571044
402	Phosphorylation	GWEAVSIYQFHGQAT CEEEEEEEEEECEEE	9.53	27642862
416	Phosphorylation	TAEDSGNSSDQEGRE ECCCCCCCCCCCCCE	38.53	27642862
417	Phosphorylation	AEDSGNSSDQEGREL CCCCCCCCCCCCCEE	47.52	27642862
461	Phosphorylation	VRLLKGNSPPAALGP EEEECCCCCCHHHCC	40.71	25394399

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
341	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CBLC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CBLC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGFR_HUMAN	EGFR	physical	10571044
FYN_HUMAN	FYN	physical	10571044
LYN_HUMAN	LYN	physical	10362357
CRK_HUMAN	CRK	physical	10362357
EGFR_HUMAN	EGFR	physical	10362357
ITCH_HUMAN	ITCH	physical	12226085
NACAD_HUMAN	NACAD	physical	21900206
SHC1_HUMAN	SHC1	physical	21900206
SH3G3_HUMAN	SH3GL3	physical	21900206
RET_HUMAN	RET	physical	18753381
CD2AP_HUMAN	CD2AP	physical	18753381
KCRM_HUMAN	CKM	physical	20525694
SRC_HUMAN	SRC	physical	20525694
EGFR_HUMAN	EGFR	physical	22888118
SRC_HUMAN	SRC	physical	22888118
ZAP70_HUMAN	ZAP70	physical	22888118
UB2D2_HUMAN	UBE2D2	physical	20525694
TGFI1_HUMAN	TGFB1I1	physical	23145173
TRIP6_HUMAN	TRIP6	physical	23145173
CHFR_HUMAN	CHFR	physical	22493164
OXA1L_HUMAN	OXA1L	physical	21988832
PDLI7_HUMAN	PDLIM7	physical	24466333
RET_HUMAN	RET	physical	24466333
UB2D2_HUMAN	UBE2D2	physical	14661060
UB2D3_HUMAN	UBE2D3	physical	14661060
UB2D1_HUMAN	UBE2D1	physical	14661060
SRC_HUMAN	SRC	physical	14661060
UBC_HUMAN	UBC	physical	14661060
ABI2_HUMAN	ABI2	physical	28514442
WASF1_HUMAN	WASF1	physical	28514442
BRK1_HUMAN	BRK1	physical	28514442
NCKP1_HUMAN	NCKAP1	physical	28514442
WASF2_HUMAN	WASF2	physical	28514442
LPP_HUMAN	LPP	physical	28514442
ZNHI2_HUMAN	ZNHIT2	physical	28514442
CYFP2_HUMAN	CYFIP2	physical	28514442
GAK_HUMAN	GAK	physical	28514442
CYFP1_HUMAN	CYFIP1	physical	28514442
MGME1_HUMAN	MGME1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY.
PubMed: 15302935