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P00518 (PHKG1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.4 Ref.7

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. Ref.3 Ref.5

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 Ref.2
Chain2 – 387386Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
PRO_0000086510

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

Secondary structure

............................................ 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00518 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0EC8710C2A4C1BE8

FASTA38744,803
        10         20         30         40         50         60 
MTRDAALPGS HSTHGFYENY EPKEILGRGV SSVVRRCIHK PTCKEYAVKI IDVTGGGSFS 

        70         80         90        100        110        120 
AEEVQELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF FLVFDLMKKG ELFDYLTEKV 

       130        140        150        160        170        180 
TLSEKETRKI MRALLEVICA LHKLNIVHRD LKPENILLDD DMNIKLTDFG FSCQLDPGEK 

       190        200        210        220        230        240 
LREVCGTPSY LAPEIIECSM NDNHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR 

       250        260        270        280        290        300 
MIMSGNYQFG SPEWDDYSDT VKDLVSRFLV VQPQKRYTAE EALAHPFFQQ YVVEEVRHFS 

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

       370        380 
KGQQQNRAAL FENTPKAVLF SLAEDDY 

« Hide

References

[1]"Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase."
da Cruz e Silva E.F., Cohen P.T.W.
FEBS Lett. 220:36-42(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
[2]"Homology of the gamma subunit of phosphorylase b kinase with cAMP-dependent protein kinase."
Reimann E.M., Titani K., Ericsson L.H., Wade R.D., Fischer E.H., Walsh K.A.
Biochemistry 23:4185-4192(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-387.
[3]"The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin."
Dasgupta M., Honeycutt T., Blumenthal D.K.
J. Biol. Chem. 264:17156-17163(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CALMODULIN-BINDING DOMAINS.
[4]"Phosphorylase kinase phosphorylates the calmodulin-binding regulatory regions of neuronal tissue-specific proteins B-50 (GAP-43) and neurogranin."
Paudel H.K., Zwiers H., Wang J.H.
J. Biol. Chem. 268:6207-6213(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GAP43 AND NRGN/RC3.
[5]"Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory."
Dasgupta M., Blumenthal D.K.
J. Biol. Chem. 270:22283-22289(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CALMODULIN-BINDING DOMAINS.
[6]"Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product."
Owen D.J., Noble M.E.M., Garman E.F., Papageorgiou A.C., Johnson L.N.
Structure 3:467-482(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-292.
[7]"The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase."
Paudel H.K.
J. Biol. Chem. 272:1777-1785(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[8]"The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition."
Lowe E.D., Noble M.E.M., Skamnaki V.T., Oikonomakos N.G., Owen D.J., Johnson L.N.
EMBO J. 16:6646-6658(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-299.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00684 mRNA. Translation: CAA68682.1.
PIRKIRBFG. S00075.
RefSeqNP_001095175.1. NM_001101705.1.
UniGeneOcu.2086.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHKX-ray2.20A2-299[»]
1QL6X-ray2.40A2-299[»]
2PHKX-ray2.60A15-291[»]
ProteinModelPortalP00518.
SMRP00518. Positions 15-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48334N.
STRING9986.ENSOCUP00000011717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000013615; ENSOCUP00000011717; ENSOCUG00000013618.
GeneID100009297.

Organism-specific databases

CTD5260.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117716.
HOGENOMHOG000233016.
HOVERGENHBG106193.

Enzyme and pathway databases

BRENDA2.7.11.19. 1749.

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

EvolutionaryTraceP00518.

Entry information

Entry namePHKG1_RABIT
AccessionPrimary (citable) accession number: P00518
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 122 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references