Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

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P00518 (PHKG1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Muscle protein Serine/threonine-protein kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycogen biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	phosphorylase kinase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorylase kinase activity Inferred from electronic annotation. Source: EC tau-protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 387

386

Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

PRO_0000086510

Regions

Domain

20 – 288

269

Protein kinase

Nucleotide binding

26 – 34

ATP By similarity

Region

303 – 327

Calmodulin-binding (domain-N)

Region

343 – 367

Calmodulin-binding (domain-C)

Sites

Active site

150

Proton acceptor By similarity

Binding site

ATP By similarity

Secondary structure

387

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00518 [UniParc].

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

387

44,803

        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.

PIR

KIRBFG. S00075.

RefSeq

NP_001095175.1. NM_001101705.1.

UniGene

Ocu.2086.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PHK	X-ray	2.20	A	2-299	[»]
1QL6	X-ray	2.40	A	2-299	[»]
2PHK	X-ray	2.60	A	15-291	[»]

ProteinModelPortal

P00518.

SMR

P00518. Positions 15-291.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48334N.

STRING

9986.ENSOCUP00000011717.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100009297.

Organism-specific databases

CTD

5260.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233016.

HOVERGEN

HBG106193.

OrthoDB

EOG4CNQR5.

Enzyme and pathway databases

BRENDA

2.7.11.19. 1749.

Family and domain databases

InterPro

IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR002291. Phosph_kin_gamma.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR24347. PTHR24347. 1 hit.

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR01049. PHOSPHBKNASE.

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00518.

Entry information

Entry name

PHKG1_RABIT

Accession

Primary (citable) accession number: P00518

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents