PHKG2

Protein identityUniProt · HPA

UniProt accession

P15735

Gene

PHKG2

Ensembl

ENSG00000156873

Chromosome

16

Canonical length

406 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins

Subcellular location

Cytosol

OverviewNCBI Gene

Phosphorylase kinase is a polymer of 16 subunits, four each of alpha, beta, gamma and delta. The alpha subunit includes the skeletal muscle and hepatic isoforms, encoded by two different genes. The beta subunit is the same in both the muscle and hepatic isoforms, and encoded by one gene. The gamma subunit also includes the skeletal muscle and hepatic isoforms, and the hepatic isoform is encoded by this gene. The delta subunit is a calmodulin and can be encoded by three different genes. The gamma subunits contain the active site of the enzyme, whereas the alpha and beta subunits have regulatory functions controlled by phosphorylation. The delta subunit mediates the dependence of the enzyme on calcium concentration. Mutations in this gene cause glycogen storage disease type 9C, also known as autosomal liver glycogenosis. Alternatively spliced transcript variants encoding different isoforms have been identified in this gene.[provided by RefSeq, Feb 2010]

Canonical amino-acid sequenceUniProt

406 residues, UniProt reviewed canonical sequence.

>P15735|PHKG2
     1  MTLDVGPEDE LPDWAAAKEF YQKYDPKDVI GRGVSSVVRR CVHRATGHEF AVKIMEVTAE
    61  RLSPEQLEEV REATRRETHI LRQVAGHPHI ITLIDSYESS SFMFLVFDLM RKGELFDYLT
   121  EKVALSEKET RSIMRSLLEA VSFLHANNIV HRDLKPENIL LDDNMQIRLS DFGFSCHLEP
   181  GEKLRELCGT PGYLAPEILK CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL
   241  MLRMIMEGQY QFSSPEWDDR SSTVKDLISR LLQVDPEARL TAEQALQHPF FERCEGSQPW
   301  NLTPRQRFRV AVWTVLAAGR VALSTHRVRP LTKNALLRDP YALRSVRHLI DNCAFRLYGH
   361  WVKKGEQQNR AALFQHRPPG PFPIMGPEEE GDSAAITEDE AVLVLG

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PHKG2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.35

Highest tissue expression

124 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PHKG2.

Disease | AllUniProt

Conditions PHKG2 is implicated in, by any mechanism.

• Glycogen storage disease 9C (GSD9C) MIM:613027

Disease | GeneticClinVar

54 pathogenic / likely-pathogenic of 441 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Glycogen storage disease IXc
• Glycogen phosphorylase kinase deficiency
• Inborn genetic diseases
• Glycogen storage disease type IXc
• PHKG2-related disorder

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.66

gnomAD pLI

0

gnomAD missense Z

0.45

DepMap mean gene effect

-0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• generation of precursor metabolites and energy
• glycogen catabolic process
• glycogen metabolic process
• positive regulation of glycogen catabolic process
• protein phosphorylation
• signal transduction

Molecular functions

• ATP binding
• calmodulin binding
• enzyme binding
• phosphorylase kinase activity
• protein serine/threonine kinase activity
• tau-protein kinase activity

Cellular components

• cytoplasm
• cytosol
• phosphorylase kinase complex

Protein domainsUniProt · Pfam · InterPro

• Protein kinase domain
• Phosphorylase kinase, gamma catalytic subunit
• Serine/threonine-protein kinase, active site
• Protein kinase-like domain superfamily
• Protein kinase, ATP binding site
• Protein kinase domain

KeywordsUniProt

• ATP-binding
• Calmodulin-binding
• Carbohydrate metabolism
• Glycogen metabolism
• Glycogen storage disease
• Kinase
• Nucleotide-binding
• Phosphoprotein
• Serine/threonine-protein kinase
• Transferase

InteractionsUniProt · HPA

Protein binding partners of PHKG2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CALM1
• PHKA1
• PHKA2
• PHKB