BLK_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BLK_MOUSE
• UniProt AC: P16277
• Protein Name: Tyrosine-protein kinase Blk
• Gene Name: Blk
• Organism: Mus musculus (Mouse).
• Sequence Length: 499
• Subcellular Localization: Cell membrane; Lipid-anchor. Present and active in lipid rafts (By similarity). Membrane location is required for the phosphorylation of CD79A and CD79B.
• Protein Description: Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207'. Phosphorylates also the immunoglobulin G receptor FCGR2. With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation. Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation. In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose..
• Protein Sequence: MGLLSSKRQVSEKGKGWSPVKIRTQDKAPPPLPPLVVFNHLAPPSPNQDPDEEERFVVALFDYAAVNDRDLQVLKGEKLQVLRSTGDWWLARSLVTGREGYVPSNFVAPVETLEVEKWFFRTISRKDAERQLLAPMNKAGSFLIRESESNKGAFSLSVKDITTQGEVVKHYKIRSLDNGGYYISPRITFPTLQALVQHYSKKGDGLCQKLTLPCVNLAPKNLWAQDEWEIPRQSLKLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKTLQHERLVRLYAVVTREPIYIVTEYMARGCLLDFLKTDEGSRLSLPRLIDMSAQVAEGMAYIERMNSIHRDLRAANILVSETLCCKIADFGLARIIDSEYTAQEGAKFPIKWTAPEAIHFGVFTIKADVWSFGVLLMEIVTYGRVPYPGMSNPEVIRSLEHGYRMPCPETCPPELYNDIITECWRGRPEERPTFEFLQSVLEDFYTATEGQYELQP

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
2	Myristoylation	------MGLLSSKRQ ------CCCCCCCCC	35.01	-
45	Phosphorylation	FNHLAPPSPNQDPDE EECCCCCCCCCCCCH	35.11	24704852
163	Phosphorylation	LSVKDITTQGEVVKH EEEEECCCCCEEEEE	34.60	23375375
175	Phosphorylation	VKHYKIRSLDNGGYY EEEEEEEECCCCCEE	43.48	22499769
181	Phosphorylation	RSLDNGGYYISPRIT EECCCCCEEECCCCC	10.06	25168779
182	Phosphorylation	SLDNGGYYISPRITF ECCCCCEEECCCCCH	9.74	25168779
184	Phosphorylation	DNGGYYISPRITFPT CCCCEEECCCCCHHH	7.63	22499769
294	Phosphorylation	HERLVRLYAVVTREP HHHHHHHEEEEECCC	6.18	-
303	Phosphorylation	VVTREPIYIVTEYMA EEECCCCHHHHHHHH	10.47	-
327	Phosphorylation	TDEGSRLSLPRLIDM CCCCCCCCHHHHHHH	34.91	24719451
381	Phosphorylation	GLARIIDSEYTAQEG CHHEEECCCCCCCCC	23.30	30635358
383	Phosphorylation	ARIIDSEYTAQEGAK HEEECCCCCCCCCCC	16.01	24704852
384	Phosphorylation	RIIDSEYTAQEGAKF EEECCCCCCCCCCCC	20.15	24704852
414	Phosphorylation	TIKADVWSFGVLLME EEEHHHHHHHHHHHH	16.39	28059163
434	Phosphorylation	RVPYPGMSNPEVIRS CCCCCCCCCHHHHHH	55.97	28059163
495	Phosphorylation	YTATEGQYELQP--- HHHCCCCCCCCC---	29.48	9636152

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
383	Y	Phosphorylation	Kinase	BLK	P51451	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BLK_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 BLK_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BLK_MOUSE !!

Drug and Disease Associations

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