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P15735 (PHKG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphorylase b kinase gamma catalytic chain, liver/testis isoform

Short name=PHK-gamma-LT
Short name=PHK-gamma-T
EC=2.7.11.19
Alternative name(s):
PSK-C3
Phosphorylase kinase subunit gamma-2
Gene names
Name:PHKG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
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. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM By similarity. Ref.8

Catalytic activity

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

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.

Involvement in disease

Glycogen storage disease 9C (GSD9C) [MIM:613027]: A metabolic disorder manifesting in infancy with hepatomegaly, growth retardation, hypotonia, liver dysfunction, and elevated plasma aminotransferases and lipids. These symptoms improve with age in most cases; however, some patients may develop hepatic fibrosis or cirrhosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.11 Ref.12

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glycogen metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Glycogen storage disease
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

generation of precursor metabolites and energy

Traceable author statement Ref.11. Source: ProtInc

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen biosynthetic process

Inferred from electronic annotation. Source: InterPro

glycogen catabolic process

Traceable author statement. Source: Reactome

glycogen metabolic process

Traceable author statement Ref.11. Source: ProtInc

positive regulation of glycogen catabolic process

Traceable author statement Ref.8. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.6. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

phosphorylase kinase complex

Traceable author statement Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorylase kinase activity

Traceable author statement Ref.8. Source: UniProtKB

protein serine/threonine kinase activity

Traceable author statement Ref.8. Source: UniProtKB

tau-protein kinase activity

Traceable author statement PubMed 8999860. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P15735-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P15735-2)

The sequence of this isoform differs from the canonical sequence as follows:
     362-374: VKKGEQQNRAALF → IRKQWIGKLMACV
     375-406: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
PRO_0000086512

Regions

Domain24 – 291268Protein kinase
Nucleotide binding30 – 389ATP By similarity
Region306 – 33025Calmodulin-binding (domain-N) By similarity
Region346 – 37025Calmodulin-binding (domain-C) By similarity

Sites

Active site1531Proton acceptor By similarity
Binding site531ATP By similarity

Natural variations

Alternative sequence362 – 37413VKKGE…RAALF → IRKQWIGKLMACV in isoform 2.
VSP_041858
Alternative sequence375 – 40632Missing in isoform 2.
VSP_041859
Natural variant1061V → E in GSD9C. Ref.11
VAR_009517
Natural variant1571E → K in GSD9C. Ref.12
VAR_020854
Natural variant1891G → E in GSD9C. Ref.11
VAR_009518
Natural variant2151D → N in GSD9C. Ref.12
VAR_020855
Natural variant2471E → G.
Corresponds to variant rs34006569 [ dbSNP | Ensembl ].
VAR_051658
Natural variant3171A → T. Ref.13
VAR_040996

Experimental info

Sequence conflict1461A → P in AAA36518. Ref.6
Sequence conflict1761C → S in AAA36518. Ref.6
Sequence conflict1791E → D in AAA36518. Ref.6
Sequence conflict212 – 2143KEV → LVD in AAA36518. Ref.6
Sequence conflict2211V → E in AAA36518. Ref.6

Secondary structure

......................................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E991CFF2D3D70F60

FASTA40646,442
        10         20         30         40         50         60 
MTLDVGPEDE LPDWAAAKEF YQKYDPKDVI GRGVSSVVRR CVHRATGHEF AVKIMEVTAE 

        70         80         90        100        110        120 
RLSPEQLEEV REATRRETHI LRQVAGHPHI ITLIDSYESS SFMFLVFDLM RKGELFDYLT 

       130        140        150        160        170        180 
EKVALSEKET RSIMRSLLEA VSFLHANNIV HRDLKPENIL LDDNMQIRLS DFGFSCHLEP 

       190        200        210        220        230        240 
GEKLRELCGT PGYLAPEILK CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL 

       250        260        270        280        290        300 
MLRMIMEGQY QFSSPEWDDR SSTVKDLISR LLQVDPEARL TAEQALQHPF FERCEGSQPW 

       310        320        330        340        350        360 
NLTPRQRFRV AVWTVLAAGR VALSTHRVRP LTKNALLRDP YALRSVRHLI DNCAFRLYGH 

       370        380        390        400 
WVKKGEQQNR AALFQHRPPG PFPIMGPEEE GDSAAITEDE AVLVLG 

« Hide

Isoform 2 [UniParc].

Checksum: D0E2416820A68AA7
Show »

FASTA37443,158

References

« Hide 'large scale' references
[1]"Messenger ribonucleic acid encoding an apparent isoform of phosphorylase kinase catalytic subunit is abundant in the adult testis."
Hanks S.K.
Mol. Endocrinol. 3:110-116(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene structure and mutations associated with cirrhosis."
Burwinkel B., Shiomi S., Al Zaben A., Kilimann M.W.
Hum. Mol. Genet. 7:149-154(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Cerebellum.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[6]"Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family."
Hanks S.K.
Proc. Natl. Acad. Sci. U.S.A. 84:388-392(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 129-273.
[7]"Autosomal recessive liver phosphorylase kinase deficiency caused by a novel splice-site mutation in the gene encoding the liver gamma subunit (PHKG2)."
van Beurden E.A., de Graaf M., Wendel U., Gitzelmann R., Berger R., van den Berg I.E.
Biochem. Biophys. Res. Commun. 236:544-548(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GSD9C.
[8]"Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure."
Brushia R.J., Walsh D.A.
Front. Biosci. 4:D618-D641(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, STRUCTURE.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Structure of human phosphorylase kinase, gamma 2."
Structural genomics consortium (SGC)
Submitted (FEB-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-293 IN COMPLEX WITH INHIBITOR.
[11]"Mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit (PHKG2) cause autosomal liver glycogenosis in the gsd rat and in humans."
Maichele A.J., Burwinkel B., Maire I., Sovik O., Kilimann M.W.
Nat. Genet. 14:337-340(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD9C GLU-106 AND GLU-189.
[12]"Severe phenotype of phosphorylase kinase-deficient liver glycogenosis with mutations in the PHKG2 gene."
Burwinkel B., Rootwelt T., Kvittingen E.A., Chakraborty P.K., Kilimann M.W.
Pediatr. Res. 54:834-839(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD9C LYS-157 AND ASN-215.
[13]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-317.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31606 mRNA. Translation: AAA36442.1.
Y11950, Y11951 Genomic DNA. Translation: CAA72694.1.
AK289492 mRNA. Translation: BAF82181.1.
AK293551 mRNA. Translation: BAG57028.1.
AC106886 Genomic DNA. No translation available.
BC002541 mRNA. Translation: AAH02541.1.
M14503 mRNA. Translation: AAA36518.1.
CCDSCCDS10690.1. [P15735-1]
CCDS54002.1. [P15735-2]
PIRKIHUCT. A40069.
RefSeqNP_000285.1. NM_000294.2. [P15735-1]
NP_001165903.1. NM_001172432.1. [P15735-2]
UniGeneHs.65735.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y7JX-ray2.50A/B/C/D6-293[»]
ProteinModelPortalP15735.
SMRP15735. Positions 10-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111279. 251 interactions.
IntActP15735. 19 interactions.
STRING9606.ENSP00000329968.

Chemistry

BindingDBP15735.
ChEMBLCHEMBL2349.
GuidetoPHARMACOLOGY2147.

PTM databases

PhosphoSiteP15735.

Polymorphism databases

DMDM125536.

Proteomic databases

MaxQBP15735.
PaxDbP15735.
PRIDEP15735.

Protocols and materials databases

DNASU5261.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000424889; ENSP00000388571; ENSG00000156873. [P15735-2]
ENST00000563588; ENSP00000455607; ENSG00000156873. [P15735-1]
GeneID5261.
KEGGhsa:5261.
UCSCuc002dzk.2. human. [P15735-1]
uc021tgo.1. human. [P15735-2]

Organism-specific databases

CTD5261.
GeneCardsGC16P030759.
GeneReviewsPHKG2.
HGNCHGNC:8931. PHKG2.
HPAHPA055455.
MIM172471. gene.
613027. phenotype.
neXtProtNX_P15735.
Orphanet264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKBPA33272.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG106193.
InParanoidP15735.
KOK00871.
OrthoDBEOG7JMGDM.
PhylomeDBP15735.
TreeFamTF320349.

Enzyme and pathway databases

BioCycMetaCyc:HS08155-MONOMER.
BRENDA2.7.11.19. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SignaLinkP15735.

Gene expression databases

ArrayExpressP15735.
BgeeP15735.
CleanExHS_PHKG2.
GenevestigatorP15735.

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

ChiTaRSPHKG2. human.
GeneWikiPHKG2.
GenomeRNAi5261.
NextBio20322.
PROP15735.
SOURCESearch...

Entry information

Entry namePHKG2_HUMAN
AccessionPrimary (citable) accession number: P15735
Secondary accession number(s): A8K0C7 expand/collapse secondary AC list , B4DEB7, E9PEU3, P11800
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM