logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0018 : Phosphorylase b kinase [gamma] catalytic chain

[ CaMP Format ]

* Basic Information

OrganismOryctolagus cuniculus (rabbit)
Protein Namesunnamed protein product [Oryctolagus cuniculus]; Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform; 2.7.11.19; Phosphorylase kinase subunit gamma-1; Serine/threonine-protein kinase PHKG1; 2.7.11.1; 2.7.11.26
Gene NamesPHKG
Gene LocusNot available
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
CAA68682 N/A N/A P00518 N/A N/A N/A ocu:100009297

* Information From OMIM

Not Available.

* Structure Information

1. Primary Information

Length: 387 aa

Average Mass: 44.802 kDa

Monoisotopic Mass: 44.774 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Phosphotransferase enzyme family 1. 146173168.00.3

3. Sequence Information

Fasta Sequence: SB0018.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1PHK (X-ray; 220 A; A=2-299), 1QL6 (X-ray; 240 A; A=2-299), 2PHK (X-ray; 260 A; A=15-291)

* Cleavage Information

1 [sites] cleaved by Calpain 2

Source Reference: [PubMed ID: 10375405] Pete MJ, Liao CX, Bartleson C, Graves DJ, A recombinant form of the catalytic subunit of phosphorylase kinase that is soluble, monomeric, and includes key C-terminal residues. Arch Biochem Biophys. 1999 Jul 1;367(1):104-14.

Cleavage sites (±10aa)

[Site 1] EEVRHFSPRG303-KFKVICLTVL

Gly303 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Glu294Glu295Val296Arg297His298Phe299Ser300Pro301Arg302Gly303
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Lys304Phe305Lys306Val307Ile308Cys309Leu310Thr311Val312Leu313

Sequence conservation (by blast)

* References

[PubMed ID: 3609320] da Cruz e Silva EF, Cohen PT, Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase. FEBS Lett. 1987 Aug 10;220(1):36-42.