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P13286 (PHKG1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

EC=2.7.11.19
Alternative name(s):
Phosphorylase kinase subunit gamma-1
Serine/threonine-protein kinase PHKG1
EC=2.7.11.1
EC=2.7.11.26
Gene names
Name:Phkg1
Synonyms:Phkg
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 By similarity.

Catalytic activity

2 ATP + phosphorylase b = 2 ADP + phosphorylase a.

ATP + [tau protein] = ADP + [tau protein] phosphate.

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin.

Domain

The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 388387Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
PRO_0000086511

Regions

Domain20 – 288269Protein kinase
Nucleotide binding26 – 349ATP By similarity
Region303 – 32725Calmodulin-binding (domain-N)
Region343 – 36725Calmodulin-binding (domain-C)

Sites

Active site1501Proton acceptor By similarity
Binding site491ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P13286 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6ABA8A51D527C149

FASTA38845,015
        10         20         30         40         50         60 
MTRDEALPDS HSAQNFYENY EPKEILGRGV SSVVRRCIHK PTCQEYAVKI IDITGGGSFS 

        70         80         90        100        110        120 
SEEVQELREA TLKEVDILQK VSGHPNIIQL KDTYETNTFF FLVFDLMKRG ELFDYLTEKV 

       130        140        150        160        170        180 
TLTEKETRKI MRALLEVVCT LHKLNIVHRD LKPENILLDD NMNIKLTDFG FSCQLQPGEK 

       190        200        210        220        230        240 
LREVCGTPSY LAPEIIQCSM DEGHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR 

       250        260        270        280        290        300 
MIMDGKYQFG SPEWDDYSDT VKDLVSRFLV VQPQDRCSAE EALAHPFFQE YVVEEVRHFS 

       310        320        330        340        350        360 
PRGKFKVICL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY AFRIYGHWVK 

       370        380 
KGQQQNRAAL FENTPKAVLL SLAEEEDF 

« Hide

References

[1]"Nucleotide sequence of cDNA encoding the catalytic subunit of phosphorylase kinase from rat soleus muscle."
Cawley K.C., Ramachandran C., Gorin F.A., Walsh D.A.
Nucleic Acids Res. 16:2355-2356(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the gene for rat phosphorylase kinase catalytic subunit."
Cawley K.C., Akita C.G., Angelos K.L., Walsh D.A.
J. Biol. Chem. 268:1194-1200(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07320 mRNA. Translation: CAA30280.1.
PIRS00731.
RefSeqNP_113761.1. NM_031573.1.
UniGeneRn.10399.

3D structure databases

ProteinModelPortalP13286.
SMRP13286. Positions 12-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248008. 1 interaction.
STRING10116.ENSRNOP00000001222.

Proteomic databases

PaxDbP13286.
PRIDEP13286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001222; ENSRNOP00000001222; ENSRNOG00000000920.
GeneID29353.
KEGGrno:29353.

Organism-specific databases

CTD5260.
RGD3325. Phkg1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117716.
HOGENOMHOG000233016.
HOVERGENHBG106193.
InParanoidP13286.
KOK00871.
OMAQNRYTAE.
OrthoDBEOG7JMGDM.
PhylomeDBP13286.
TreeFamTF320349.

Enzyme and pathway databases

BRENDA2.7.11.19. 5301.

Gene expression databases

GenevestigatorP13286.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR002291. Phosph_kin_gamma.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01049. PHOSPHBKNASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608858.
PROP13286.

Entry information

Entry namePHKG1_RAT
AccessionPrimary (citable) accession number: P13286
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families