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Protein

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

Gene

PHKG1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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/RC3.2 Publications

Catalytic activityi

2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
ATP + [tau protein] = ADP + [tau protein] phosphate.
ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei49ATPPROSITE-ProRule annotation1
Active sitei150Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi26 – 34ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Muscle protein, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.19. 1749.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PHKG1
Synonyms:PHKG
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000865102 – 387Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoformAdd BLAST386

Proteomic databases

PRIDEiP00518.

PTM databases

iPTMnetiP00518.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

DIPiDIP-48334N.
STRINGi9986.ENSOCUP00000011717.

Structurei

Secondary structure

1387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni17 – 19Combined sources3
Beta strandi20 – 28Combined sources9
Beta strandi30 – 39Combined sources10
Turni40 – 43Combined sources4
Beta strandi44 – 52Combined sources9
Turni55 – 58Combined sources4
Helixi61 – 81Combined sources21
Beta strandi90 – 95Combined sources6
Beta strandi97 – 105Combined sources9
Helixi112 – 119Combined sources8
Helixi124 – 143Combined sources20
Helixi153 – 155Combined sources3
Beta strandi156 – 158Combined sources3
Beta strandi164 – 166Combined sources3
Helixi188 – 190Combined sources3
Helixi193 – 200Combined sources8
Helixi210 – 225Combined sources16
Helixi235 – 244Combined sources10
Turni251 – 253Combined sources3
Helixi254 – 256Combined sources3
Helixi259 – 268Combined sources10
Helixi273 – 275Combined sources3
Helixi279 – 282Combined sources4
Helixi286 – 288Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PHKX-ray2.20A2-299[»]
1QL6X-ray2.40A2-299[»]
2PHKX-ray2.60A15-291[»]
ProteinModelPortaliP00518.
SMRiP00518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00518.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 288Protein kinasePROSITE-ProRule annotationAdd BLAST269

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni303 – 327Calmodulin-binding (domain-N)Add BLAST25
Regioni343 – 367Calmodulin-binding (domain-C)Add BLAST25

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0599. Eukaryota.
ENOG410Y7VX. LUCA.
GeneTreeiENSGT00840000129744.
HOGENOMiHOG000233016.
HOVERGENiHBG106193.
InParanoidiP00518.
KOiK00871.
OMAiASSYRFG.
OrthoDBiEOG091G07XZ.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR002291. Phosph_kin_gamma.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01049. PHOSPHBKNASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRDAALPGS HSTHGFYENY EPKEILGRGV SSVVRRCIHK PTCKEYAVKI
60 70 80 90 100
IDVTGGGSFS AEEVQELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF
110 120 130 140 150
FLVFDLMKKG ELFDYLTEKV TLSEKETRKI MRALLEVICA LHKLNIVHRD
160 170 180 190 200
LKPENILLDD DMNIKLTDFG FSCQLDPGEK LREVCGTPSY LAPEIIECSM
210 220 230 240 250
NDNHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR MIMSGNYQFG
260 270 280 290 300
SPEWDDYSDT VKDLVSRFLV VQPQKRYTAE EALAHPFFQQ YVVEEVRHFS
310 320 330 340 350
PRGKFKVICL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY
360 370 380
AFRIYGHWVK KGQQQNRAAL FENTPKAVLF SLAEDDY
Length:387
Mass (Da):44,803
Last modified:January 23, 2007 - v2
Checksum:i0EC8710C2A4C1BE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00684 mRNA. Translation: CAA68682.1.
PIRiS00075. KIRBFG.
RefSeqiNP_001095175.1. NM_001101705.1.
XP_008247862.1. XM_008249640.2.
UniGeneiOcu.2086.

Genome annotation databases

EnsembliENSOCUT00000013615; ENSOCUP00000011717; ENSOCUG00000013618.
GeneIDi100009297.
KEGGiocu:100009297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00684 mRNA. Translation: CAA68682.1.
PIRiS00075. KIRBFG.
RefSeqiNP_001095175.1. NM_001101705.1.
XP_008247862.1. XM_008249640.2.
UniGeneiOcu.2086.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PHKX-ray2.20A2-299[»]
1QL6X-ray2.40A2-299[»]
2PHKX-ray2.60A15-291[»]
ProteinModelPortaliP00518.
SMRiP00518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48334N.
STRINGi9986.ENSOCUP00000011717.

PTM databases

iPTMnetiP00518.

Proteomic databases

PRIDEiP00518.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000013615; ENSOCUP00000011717; ENSOCUG00000013618.
GeneIDi100009297.
KEGGiocu:100009297.

Organism-specific databases

CTDi5260.

Phylogenomic databases

eggNOGiKOG0599. Eukaryota.
ENOG410Y7VX. LUCA.
GeneTreeiENSGT00840000129744.
HOGENOMiHOG000233016.
HOVERGENiHBG106193.
InParanoidiP00518.
KOiK00871.
OMAiASSYRFG.
OrthoDBiEOG091G07XZ.

Enzyme and pathway databases

BRENDAi2.7.11.19. 1749.

Miscellaneous databases

EvolutionaryTraceiP00518.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR002291. Phosph_kin_gamma.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01049. PHOSPHBKNASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHKG1_RABIT
AccessioniPrimary (citable) accession number: P00518
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.