Relation Results

Summary

Name CLTB
Full Name Clathrin light chain B
Synonyms Lcb
Primary ID P09497
Links - -
Type protein
Relations 8
Function Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.

Viewer

Type: Score: Layout: SPV 
0.3090.3090.20.7680.7680.768CSNK2A2CLTBCSNK2A1GRK2AP-3/clathrin vescicleAP-1/clathrin vescicleAP-2/clathrin vescicle

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ img/unknown.png phosphorylation CLTB 0.309
Identifier Residue Sequence Organism Cell Line
SIGNOR-250983 Ser11 DFGFFSSsESGAPEA in vitro
pmid sentence
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
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
+ img/unknown.png phosphorylation CLTB 0.309
Identifier Residue Sequence Organism Cell Line
SIGNOR-250842 Ser11 DFGFFSSsESGAPEA in vitro
pmid sentence
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
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
+ img/unknown.png phosphorylation CLTB 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-197873 Ser205 LCDFNPKsSKQCKDV Homo sapiens
pmid sentence
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
+ form complex img/form-complex.png binding AP-3/clathrin vescicle 0.768
Identifier Residue Sequence Organism Cell Line
SIGNOR-260671 Homo sapiens
pmid sentence
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
+ form complex img/form-complex.png binding AP-1/clathrin vescicle 0.768
Identifier Residue Sequence Organism Cell Line
SIGNOR-260677 Homo sapiens
pmid sentence
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
+ form complex img/form-complex.png binding AP-2/clathrin vescicle 0.768
Identifier Residue Sequence Organism Cell Line
SIGNOR-260666 Homo sapiens
pmid sentence
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
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