CD79A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CD79A_MOUSE
• UniProt AC: P11911
• Protein Name: B-cell antigen receptor complex-associated protein alpha chain
• Gene Name: Cd79a
• Organism: Mus musculus (Mouse).
• Sequence Length: 220
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur
• Protein Description: Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells..
• Protein Sequence: MPGGLEALRALPLLLFLSYACLGPGCQALRVEGGPPSLTVNLGEEARLTCENNGRNPNITWWFSLQSNITWPPVPLGPGQGTTGQLFFPEVNKNHRGLYWCQVIENNILKRSCGTYLRVRNPVPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKFGVDMPDDYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGNLHIGDAQLEKP

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
58	N-linked_Glycosylation	ENNGRNPNITWWFSL CCCCCCCCEEEEEEC	48.12	-
68	N-linked_Glycosylation	WWFSLQSNITWPPVP EEEECCCCCCCCCCC	23.81	-
176	Phosphorylation	GVDMPDDYEDENLYE CCCCCCCCCCCCCCC	32.43	22817900
182	Phosphorylation	DYEDENLYEGLNLDD CCCCCCCCCCCCHHH	21.38	22817900
191	Phosphorylation	GLNLDDCSMYEDISR CCCHHHCCHHHHHHH	31.24	21841126
193	Phosphorylation	NLDDCSMYEDISRGL CHHHCCHHHHHHHHC	8.31	22817900
197	Phosphorylation	CSMYEDISRGLQGTY CCHHHHHHHHCCCCC	32.39	22078222
198	Asymmetric dimethylarginine	SMYEDISRGLQGTYQ CHHHHHHHHCCCCCC	50.61	-
198	Methylation	SMYEDISRGLQGTYQ CHHHHHHHHCCCCCC	50.61	20231378
203	Phosphorylation	ISRGLQGTYQDVGNL HHHHCCCCCCCCCCC	12.68	21841126
204	Phosphorylation	SRGLQGTYQDVGNLH HHHCCCCCCCCCCCE	15.00	11449366
219	Ubiquitination	IGDAQLEKP------ ECCCCCCCC------	65.70	-

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
182	Y	Phosphorylation	Kinase	FYN	P06241	PSP
182	Y	Phosphorylation	Kinase	LYN	P07948	PSP
182	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
182	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot
193	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
193	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot
197	S	Phosphorylation	Kinase	SYK	P43405	PSP
204	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CD79A_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CD79A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD79B_MOUSE	Cd79b	physical	19407814

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Association of SLP-65/BLNK with the B cell antigen receptor through anon-ITAM tyrosine of Ig-alpha.";
Engels N., Wollscheid B., Wienands J.;
Eur. J. Immunol. 31:2126-2134(2001).
Cited for: INTERACTION WITH BLNK, PHOSPHORYLATION AT TYR-204, AND MUTAGENESIS OFTYR-204.
PubMed: 11449366

"Reconstitution of the B cell antigen receptor signaling components inCOS cells.";
Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B.,Mahajan S.;
J. Biol. Chem. 270:27072-27078(1995).
Cited for: INTERACTION WITH BLK, AND PHOSPHORYLATION AT TYR-182 AND TYR-193.
PubMed: 7592958

"Dual role of the tyrosine activation motif of the Ig-alpha proteinduring signal transduction via the B cell antigen receptor.";
Flaswinkel H., Reth M.;
EMBO J. 13:83-89(1994).
Cited for: PHOSPHORYLATION AT TYR-182, AND MUTAGENESIS OF TYR-176; TYR-182 ANDTYR-193.
PubMed: 8306975