| + |
CSNK2A1 |
phosphorylation
|
CLTB |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250842 |
Ser11 |
DFGFFSSsESGAPEA |
in vitro |
|
| pmid |
sentence |
| 3128543 |
To date, the only evidence for a functional distinction of LCa and LCb is the preferential phosphorylation of LCb, which takes place at serine residues and is mediated by coated vesicle-associated casein kinase II. As a first step toward determining the function of light chain diversity, we have mapped the in vitro phosphorylation sites on LCb. We use [32P]ATP to phosphorylate LCb within coated vesicles, followed by sequencing of 32P-labeled chymotryptic peptides thereof, to identify serine residues at positions 11 and 13 as the phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250843 |
Ser13 |
GFFSSSEsGAPEAAE |
in vitro |
|
| pmid |
sentence |
| 3128543 |
To date, the only evidence for a functional distinction of LCa and LCb is the preferential phosphorylation of LCb, which takes place at serine residues and is mediated by coated vesicle-associated casein kinase II. As a first step toward determining the function of light chain diversity, we have mapped the in vitro phosphorylation sites on LCb. We use [32P]ATP to phosphorylate LCb within coated vesicles, followed by sequencing of 32P-labeled chymotryptic peptides thereof, to identify serine residues at positions 11 and 13 as the phosphorylation sites. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK2A2 |
phosphorylation
|
CLTB |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250983 |
Ser11 |
DFGFFSSsESGAPEA |
in vitro |
|
| pmid |
sentence |
| 3128543 |
To date, the only evidence for a functional distinction of LCa and LCb is the preferential phosphorylation of LCb, which takes place at serine residues and is mediated by coated vesicle-associated casein kinase II. As a first step toward determining the function of light chain diversity, we have mapped the in vitro phosphorylation sites on LCb. We use [32P]ATP to phosphorylate LCb within coated vesicles, followed by sequencing of 32P-labeled chymotryptic peptides thereof, to identify serine residues at positions 11 and 13 as the phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250984 |
Ser13 |
GFFSSSEsGAPEAAE |
in vitro |
|
| pmid |
sentence |
| 3128543 |
To date, the only evidence for a functional distinction of LCa and LCb is the preferential phosphorylation of LCb, which takes place at serine residues and is mediated by coated vesicle-associated casein kinase II. As a first step toward determining the function of light chain diversity, we have mapped the in vitro phosphorylation sites on LCb. We use [32P]ATP to phosphorylate LCb within coated vesicles, followed by sequencing of 32P-labeled chymotryptic peptides thereof, to identify serine residues at positions 11 and 13 as the phosphorylation sites. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
GRK2 |
phosphorylation
|
CLTB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197873 |
Ser205 |
LCDFNPKsSKQCKDV |
Homo sapiens |
|
| pmid |
sentence |
| 22704991 |
Moreover, we demonstrate that phosphorylation of ser204 in clcb is required for efficient endocytosis of a subset of gpcrs and identify g protein-coupled receptor kinase 2 (grk2) as a kinase that can phosphorylate clcb on ser204. Overexpression of clcb(s204a) specifically inhibits the endocytosis of those gpcrs whose endocytosis is grk2-dependent. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLTB | form complex 
binding
|
AP-3/clathrin vescicle |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260671 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23103167 |
Clathrin-coated pits and vesicles are diffraction-limited objects with typical diameters ranging between 75 and 130 nm. The smaller ∼75 nm coats contain at least 36 copies of clathrin, a heterohexameric protein of three heavy chains and three light chains, and about half that number of copies of the heterotetrameric AP adaptor complex | Intracellular clathrin-coated vesicles contain AP1 or AP3 adaptors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLTB | form complex
binding
|
AP-2/clathrin vescicle |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260666 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24789820 |
AP2 adaptor complexes, associated at the membrane with PtdIns(4,5)P2 (PIP2), recruit clathin triskelions to initiate lattice assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLTB | form complex
binding
|
AP-1/clathrin vescicle |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260677 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23103167 |
Clathrin-coated pits and vesicles are diffraction-limited objects with typical diameters ranging between 75 and 130 nm. The smaller ∼75 nm coats contain at least 36 copies of clathrin, a heterohexameric protein of three heavy chains and three light chains, and about half that number of copies of the heterotetrameric AP adaptor complex | Intracellular clathrin-coated vesicles contain AP1 or AP3 adaptors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CLTB
- 
- 