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P15735

- PHKG2_HUMAN

UniProt

P15735 - PHKG2_HUMAN

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Protein

Phosphorylase b kinase gamma catalytic chain, liver/testis isoform

Gene

PHKG2

Organism
Homo sapiens (Human)
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. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphorylase kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. tau-protein kinase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. generation of precursor metabolites and energy Source: ProtInc
  3. glucose metabolic process Source: Reactome
  4. glycogen biosynthetic process Source: InterPro
  5. glycogen catabolic process Source: Reactome
  6. glycogen metabolic process Source: ProtInc
  7. positive regulation of glycogen catabolic process Source: UniProtKB
  8. protein phosphorylation Source: ProtInc
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08155-MONOMER.
BRENDAi2.7.11.19. 2681.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
SignaLinkiP15735.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphorylase b kinase gamma catalytic chain, liver/testis isoform (EC:2.7.11.19)
Short name:
PHK-gamma-LT
Short name:
PHK-gamma-T
Alternative name(s):
PSK-C3
Phosphorylase kinase subunit gamma-2
Gene namesi
Name:PHKG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:8931. PHKG2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. phosphorylase kinase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061V → E in GSD9C. 1 Publication
VAR_009517
Natural varianti157 – 1571E → K in GSD9C. 1 Publication
VAR_020854
Natural varianti189 – 1891G → E in GSD9C. 1 Publication
VAR_009518
Natural varianti215 – 2151D → N in GSD9C. 1 Publication
VAR_020855

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi613027. phenotype.
Orphaneti264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKBiPA33272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Phosphorylase b kinase gamma catalytic chain, liver/testis isoformPRO_0000086512Add
BLAST

Proteomic databases

MaxQBiP15735.
PaxDbiP15735.
PRIDEiP15735.

PTM databases

PhosphoSiteiP15735.

Expressioni

Gene expression databases

BgeeiP15735.
CleanExiHS_PHKG2.
ExpressionAtlasiP15735. baseline and differential.
GenevestigatoriP15735.

Organism-specific databases

HPAiHPA055455.

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.1 Publication

Protein-protein interaction databases

BioGridi111279. 28 interactions.
IntActiP15735. 19 interactions.
STRINGi9606.ENSP00000329968.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2311
Beta strandi24 – 329
Beta strandi34 – 4310
Turni44 – 463
Beta strandi49 – 568
Helixi64 – 8421
Beta strandi93 – 10715
Helixi115 – 1228
Helixi127 – 14620
Helixi156 – 1583
Beta strandi159 – 1613
Beta strandi167 – 1693
Helixi191 – 1933
Helixi196 – 2016
Helixi214 – 22815
Helixi238 – 24710
Helixi254 – 2574
Beta strandi258 – 2603
Helixi262 – 27110
Turni276 – 2783
Helixi282 – 2876
Helixi289 – 2913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y7JX-ray2.50A/B/C/D6-293[»]
ProteinModelPortaliP15735.
SMRiP15735. Positions 10-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 291268Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni306 – 33025Calmodulin-binding (domain-N)By similarityAdd
BLAST
Regioni346 – 37025Calmodulin-binding (domain-C)By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119185.
HOGENOMiHOG000233016.
HOVERGENiHBG106193.
InParanoidiP15735.
KOiK00871.
OrthoDBiEOG7JMGDM.
PhylomeDBiP15735.
TreeFamiTF320349.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P15735-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTLDVGPEDE LPDWAAAKEF YQKYDPKDVI GRGVSSVVRR CVHRATGHEF
60 70 80 90 100
AVKIMEVTAE RLSPEQLEEV REATRRETHI LRQVAGHPHI ITLIDSYESS
110 120 130 140 150
SFMFLVFDLM RKGELFDYLT EKVALSEKET RSIMRSLLEA VSFLHANNIV
160 170 180 190 200
HRDLKPENIL LDDNMQIRLS DFGFSCHLEP GEKLRELCGT PGYLAPEILK
210 220 230 240 250
CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL MLRMIMEGQY
260 270 280 290 300
QFSSPEWDDR SSTVKDLISR LLQVDPEARL TAEQALQHPF FERCEGSQPW
310 320 330 340 350
NLTPRQRFRV AVWTVLAAGR VALSTHRVRP LTKNALLRDP YALRSVRHLI
360 370 380 390 400
DNCAFRLYGH WVKKGEQQNR AALFQHRPPG PFPIMGPEEE GDSAAITEDE

AVLVLG
Length:406
Mass (Da):46,442
Last modified:April 1, 1990 - v1
Checksum:iE991CFF2D3D70F60
GO
Isoform 2 (identifier: P15735-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:374
Mass (Da):43,158
Checksum:iD0E2416820A68AA7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461A → P in AAA36518. (PubMed:2948189)Curated
Sequence conflicti176 – 1761C → S in AAA36518. (PubMed:2948189)Curated
Sequence conflicti179 – 1791E → D in AAA36518. (PubMed:2948189)Curated
Sequence conflicti212 – 2143KEV → LVD in AAA36518. (PubMed:2948189)Curated
Sequence conflicti221 – 2211V → E in AAA36518. (PubMed:2948189)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061V → E in GSD9C. 1 Publication
VAR_009517
Natural varianti157 – 1571E → K in GSD9C. 1 Publication
VAR_020854
Natural varianti189 – 1891G → E in GSD9C. 1 Publication
VAR_009518
Natural varianti215 – 2151D → N in GSD9C. 1 Publication
VAR_020855
Natural varianti247 – 2471E → G.
Corresponds to variant rs34006569 [ dbSNP | Ensembl ].
VAR_051658
Natural varianti317 – 3171A → T.1 Publication
VAR_040996

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei362 – 37413VKKGE…RAALF → IRKQWIGKLMACV in isoform 2. 1 PublicationVSP_041858Add
BLAST
Alternative sequencei375 – 40632Missing in isoform 2. 1 PublicationVSP_041859Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10690.1. [P15735-1]
CCDS54002.1. [P15735-2]
PIRiA40069. KIHUCT.
RefSeqiNP_000285.1. NM_000294.2. [P15735-1]
NP_001165903.1. NM_001172432.1. [P15735-2]
UniGeneiHs.65735.

Genome annotation databases

EnsembliENST00000424889; ENSP00000388571; ENSG00000156873. [P15735-2]
ENST00000563588; ENSP00000455607; ENSG00000156873. [P15735-1]
GeneIDi5261.
KEGGihsa:5261.
UCSCiuc002dzk.2. human. [P15735-1]
uc021tgo.1. human. [P15735-2]

Polymorphism databases

DMDMi125536.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10690.1. [P15735-1 ]
CCDS54002.1. [P15735-2 ]
PIRi A40069. KIHUCT.
RefSeqi NP_000285.1. NM_000294.2. [P15735-1 ]
NP_001165903.1. NM_001172432.1. [P15735-2 ]
UniGenei Hs.65735.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y7J X-ray 2.50 A/B/C/D 6-293 [» ]
ProteinModelPortali P15735.
SMRi P15735. Positions 10-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111279. 28 interactions.
IntActi P15735. 19 interactions.
STRINGi 9606.ENSP00000329968.

Chemistry

BindingDBi P15735.
ChEMBLi CHEMBL2111324.
GuidetoPHARMACOLOGYi 2147.

PTM databases

PhosphoSitei P15735.

Polymorphism databases

DMDMi 125536.

Proteomic databases

MaxQBi P15735.
PaxDbi P15735.
PRIDEi P15735.

Protocols and materials databases

DNASUi 5261.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000424889 ; ENSP00000388571 ; ENSG00000156873 . [P15735-2 ]
ENST00000563588 ; ENSP00000455607 ; ENSG00000156873 . [P15735-1 ]
GeneIDi 5261.
KEGGi hsa:5261.
UCSCi uc002dzk.2. human. [P15735-1 ]
uc021tgo.1. human. [P15735-2 ]

Organism-specific databases

CTDi 5261.
GeneCardsi GC16P030759.
GeneReviewsi PHKG2.
HGNCi HGNC:8931. PHKG2.
HPAi HPA055455.
MIMi 172471. gene.
613027. phenotype.
neXtProti NX_P15735.
Orphaneti 264580. Glycogen storage disease due to liver phosphorylase kinase deficiency.
PharmGKBi PA33272.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119185.
HOGENOMi HOG000233016.
HOVERGENi HBG106193.
InParanoidi P15735.
KOi K00871.
OrthoDBi EOG7JMGDM.
PhylomeDBi P15735.
TreeFami TF320349.

Enzyme and pathway databases

BioCyci MetaCyc:HS08155-MONOMER.
BRENDAi 2.7.11.19. 2681.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).
SignaLinki P15735.

Miscellaneous databases

ChiTaRSi PHKG2. human.
GeneWikii PHKG2.
GenomeRNAii 5261.
NextBioi 20322.
PROi P15735.
SOURCEi Search...

Gene expression databases

Bgeei P15735.
CleanExi HS_PHKG2.
ExpressionAtlasi P15735. baseline and differential.
Genevestigatori P15735.

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

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.
    , 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.

Entry informationi

Entry nameiPHKG2_HUMAN
AccessioniPrimary (citable) accession number: P15735
Secondary accession number(s): A8K0C7
, B4DEB7, E9PEU3, P11800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3