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Q9DB30

- PHKG2_MOUSE

UniProt

Q9DB30 - PHKG2_MOUSE

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Protein

Phosphorylase b kinase gamma catalytic chain, liver/testis isoform

Gene
Phkg2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATP By similarity
Active sitei153 – 1531Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. glycogen biosynthetic process Source: InterPro
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

BRENDAi2.7.11.19. 3474.

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):
Phosphorylase kinase subunit gamma-2
Gene namesi
Name:Phkg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1916211. Phkg2.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Phosphorylase b kinase gamma catalytic chain, liver/testis isoformPRO_0000086513Add
BLAST

Proteomic databases

PaxDbiQ9DB30.
PRIDEiQ9DB30.

PTM databases

PhosphoSiteiQ9DB30.

Expressioni

Gene expression databases

BgeeiQ9DB30.
CleanExiMM_PHKG2.
GenevestigatoriQ9DB30.

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 By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033086.

Structurei

3D structure databases

ProteinModelPortaliQ9DB30.
SMRiQ9DB30. Positions 10-355.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 291268Protein kinaseAdd
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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117716.
HOGENOMiHOG000233016.
HOVERGENiHBG106193.
InParanoidiA6H632.
KOiK00871.
OMAiHRPPGPF.
OrthoDBiEOG7JMGDM.
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_dom.
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.

Q9DB30-1 [UniParc]FASTAAdd to Basket

« Hide

MTLDVGPEDE LPDWAAAKEF YQKYDPKDII GRGVSSVVRR CVHRATGDEF    50
AVKIMEVSAE RLSLEQLEEV RDATRREMHI LRQVAGHPHI ITLIDSYESS 100
SFMFLVFDLM RKGELFDYLT EKVALSEKET RSIMRSLLEA VSFLHANNIV 150
HRDLKPENIL LDDNMQIRLS DFGFSCHLEA GEKLRELCGT PGYLAPEILK 200
CSMDETHPGY GKEVDLWACG VILFTLLAGS PPFWHRRQIL MLRMIMEGQY 250
QFTSPEWDDR SNTVKDLISK LLQVDPEARL TAEQALQHPF FERCEGSQPW 300
NLTPRQRFRV AVWTILAAGR VALSSHRLRP LTKNALLRDP YALRPVRRLI 350
DNCAFRLYGH WVKKGEQQNR AALFQHQPPR LFPIAATELE GDSGAITEDE 400
ATLVRS 406
Length:406
Mass (Da):46,572
Last modified:July 27, 2011 - v2
Checksum:i2B12C7F0F8FE054C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601R → C in BAB23926. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK005277 mRNA. Translation: BAB23926.1.
CH466531 Genomic DNA. Translation: EDL17548.1.
CH466531 Genomic DNA. Translation: EDL17549.1.
BC138913 mRNA. Translation: AAI38914.1.
BC145734 mRNA. Translation: AAI45735.1.
CCDSiCCDS21869.1.
RefSeqiNP_081164.2. NM_026888.3.
XP_006508230.1. XM_006508167.1.
UniGeneiMm.274473.

Genome annotation databases

EnsembliENSMUST00000033086; ENSMUSP00000033086; ENSMUSG00000030815.
ENSMUST00000121004; ENSMUSP00000113533; ENSMUSG00000030815.
GeneIDi68961.
KEGGimmu:68961.
UCSCiuc009jwc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK005277 mRNA. Translation: BAB23926.1 .
CH466531 Genomic DNA. Translation: EDL17548.1 .
CH466531 Genomic DNA. Translation: EDL17549.1 .
BC138913 mRNA. Translation: AAI38914.1 .
BC145734 mRNA. Translation: AAI45735.1 .
CCDSi CCDS21869.1.
RefSeqi NP_081164.2. NM_026888.3.
XP_006508230.1. XM_006508167.1.
UniGenei Mm.274473.

3D structure databases

ProteinModelPortali Q9DB30.
SMRi Q9DB30. Positions 10-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000033086.

PTM databases

PhosphoSitei Q9DB30.

Proteomic databases

PaxDbi Q9DB30.
PRIDEi Q9DB30.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033086 ; ENSMUSP00000033086 ; ENSMUSG00000030815 .
ENSMUST00000121004 ; ENSMUSP00000113533 ; ENSMUSG00000030815 .
GeneIDi 68961.
KEGGi mmu:68961.
UCSCi uc009jwc.2. mouse.

Organism-specific databases

CTDi 5261.
MGIi MGI:1916211. Phkg2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117716.
HOGENOMi HOG000233016.
HOVERGENi HBG106193.
InParanoidi A6H632.
KOi K00871.
OMAi HRPPGPF.
OrthoDBi EOG7JMGDM.
TreeFami TF320349.

Enzyme and pathway databases

BRENDAi 2.7.11.19. 3474.

Miscellaneous databases

NextBioi 328293.
PROi Q9DB30.
SOURCEi Search...

Gene expression databases

Bgeei Q9DB30.
CleanExi MM_PHKG2.
Genevestigatori Q9DB30.

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_dom.
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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Brain.

Entry informationi

Entry nameiPHKG2_MOUSE
AccessioniPrimary (citable) accession number: Q9DB30
Secondary accession number(s): A6H632
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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