Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00518

- PHKG1_RABIT

UniProt

P00518 - PHKG1_RABIT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

PHKG1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphorylase kinase activity Source: UniProtKB-EC
  3. tau-protein kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycogen biosynthetic process Source: InterPro
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
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. phosphorylase kinase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 387386Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoformPRO_0000086510Add
BLAST

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

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni17 – 193
Beta strandi20 – 289
Beta strandi30 – 3910
Turni40 – 434
Beta strandi44 – 529
Turni55 – 584
Helixi61 – 8121
Beta strandi90 – 956
Beta strandi97 – 1059
Helixi112 – 1198
Helixi124 – 14320
Helixi153 – 1553
Beta strandi156 – 1583
Beta strandi164 – 1663
Helixi188 – 1903
Helixi193 – 2008
Helixi210 – 22516
Helixi235 – 24410
Turni251 – 2533
Helixi254 – 2563
Helixi259 – 26810
Helixi273 – 2753
Helixi279 – 2824
Helixi286 – 2883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHKX-ray2.20A2-299[»]
1QL6X-ray2.40A2-299[»]
2PHKX-ray2.60A15-291[»]
ProteinModelPortaliP00518.
SMRiP00518. Positions 15-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00518.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 288269Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni303 – 32725Calmodulin-binding (domain-N)Add
BLAST
Regioni343 – 36725Calmodulin-binding (domain-C)Add
BLAST

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000119185.
HOGENOMiHOG000233016.
HOVERGENiHBG106193.
InParanoidiP00518.

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.
IPR002290. Ser/Thr_dual-sp_kinase.
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:
EMBL
GenBank
DDBJ
Links Updated
Y00684 mRNA. Translation: CAA68682.1.
PIRiS00075. KIRBFG.
RefSeqiNP_001095175.1. NM_001101705.1.
XP_008247862.1. XM_008249640.1.
UniGeneiOcu.2086.

Genome annotation databases

EnsembliENSOCUT00000013615; ENSOCUP00000011717; ENSOCUG00000013618.
GeneIDi100009297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00684 mRNA. Translation: CAA68682.1 .
PIRi S00075. KIRBFG.
RefSeqi NP_001095175.1. NM_001101705.1.
XP_008247862.1. XM_008249640.1.
UniGenei Ocu.2086.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P00518.
SMRi P00518. Positions 15-291.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48334N.
STRINGi 9986.ENSOCUP00000011717.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSOCUT00000013615 ; ENSOCUP00000011717 ; ENSOCUG00000013618 .
GeneIDi 100009297.

Organism-specific databases

CTDi 5260.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119185.
HOGENOMi HOG000233016.
HOVERGENi HBG106193.
InParanoidi P00518.

Enzyme and pathway databases

BRENDAi 2.7.11.19. 1749.

Miscellaneous databases

EvolutionaryTracei P00518.

Family and domain databases

InterProi IPR020636. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01049. PHOSPHBKNASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 124 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

External Data

Dasty 3