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Q16816

- PHKG1_HUMAN

UniProt

Q16816 - PHKG1_HUMAN

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Protein

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

Gene

PHKG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity).By similarity

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. carbohydrate metabolic process Source: Reactome
  2. glucose metabolic process Source: Reactome
  3. glycogen biosynthetic process Source: InterPro
  4. glycogen catabolic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
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

BioCyciMetaCyc:HS09136-MONOMER.
BRENDAi2.7.11.19. 2681.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
SignaLinkiQ16816.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC:2.7.11.19)
Short name:
PHK-gamma-M
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:8930. PHKG1.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

Orphaneti715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKBiPA33271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 387386Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoformPRO_0000086508Add
BLAST

Proteomic databases

PaxDbiQ16816.
PRIDEiQ16816.

PTM databases

PhosphoSiteiQ16816.

Miscellaneous databases

PMAP-CutDBQ16816.

Expressioni

Gene expression databases

BgeeiQ16816.
CleanExiHS_PHKG1.
ExpressionAtlasiQ16816. baseline and differential.
GenevestigatoriQ16816.

Organism-specific databases

HPAiHPA012057.

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

BioGridi111278. 1 interaction.
STRINGi9606.ENSP00000297373.

Structurei

3D structure databases

ProteinModelPortaliQ16816.
SMRiQ16816. Positions 16-366.
ModBaseiSearch...
MobiDBiSearch...

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.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119185.
HOVERGENiHBG106193.
InParanoidiQ16816.
KOiK00871.
OMAiQNRYTAE.
OrthoDBiEOG7JMGDM.
PhylomeDBiQ16816.
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.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16816-1) [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
MTRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV
60 70 80 90 100
IDVTGGGSFS PEEVRELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF
110 120 130 140 150
FLVFDLMKRG ELFDYLTEKV TLSEKETRKI MRALLEVICT LHKLNIVHRD
160 170 180 190 200
LKPENILLDD NMNIKLTDFG FSCQLEPGER LREVCGTPSY LAPEIIECSM
210 220 230 240 250
NEDHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR MIMSGNYQFG
260 270 280 290 300
SPEWDDYSDT VKDLVSRFLV VQPQNRYTAE EALAHPFFQQ YLVEEVRHFS
310 320 330 340 350
PRGKFKVIAL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY
360 370 380
AFRIYGHWVK KGQQQNRAAL FENTPKAVLL SLAEEDY
Length:387
Mass (Da):45,024
Last modified:January 23, 2007 - v3
Checksum:i9CB416CB683920AA
GO
Isoform 2 (identifier: Q16816-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     106-106: L → LWEDTDTMEMEQKWCLGWDSPKSTNFRAQGRAR

Note: No experimental confirmation available.

Show »
Length:419
Mass (Da):48,867
Checksum:i99429FF321971C5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001F → L in BAH11466. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040994
Natural varianti323 – 3231R → C.1 Publication
Corresponds to variant rs149458708 [ dbSNP | Ensembl ].
VAR_040995

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei106 – 1061L → LWEDTDTMEMEQKWCLGWDS PKSTNFRAQGRAR in isoform 2. 1 PublicationVSP_044716

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80590 mRNA. Translation: CAA56681.1.
AF254253
, AF254250, AF254251, AF254252 Genomic DNA. Translation: AAL36972.1.
AK293180 mRNA. Translation: BAH11466.1.
AC092101 Genomic DNA. Translation: AAS07453.1.
CH471140 Genomic DNA. Translation: EAX07987.1.
BC051327 mRNA. Translation: AAH51327.1.
BC069679 mRNA. Translation: AAH69679.1.
BC069738 mRNA. Translation: AAH69738.1.
BC069754 mRNA. Translation: AAH69754.1.
BC074753 mRNA. Translation: AAH74753.1.
CCDSiCCDS5525.1. [Q16816-1]
CCDS59057.1. [Q16816-2]
RefSeqiNP_001245388.1. NM_001258459.1. [Q16816-2]
NP_006204.1. NM_006213.4. [Q16816-1]
UniGeneiHs.730821.

Genome annotation databases

EnsembliENST00000297373; ENSP00000297373; ENSG00000164776. [Q16816-1]
ENST00000452681; ENSP00000445440; ENSG00000164776. [Q16816-2]
GeneIDi5260.
KEGGihsa:5260.
UCSCiuc003try.2. human. [Q16816-1]

Polymorphism databases

DMDMi2833281.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80590 mRNA. Translation: CAA56681.1 .
AF254253
, AF254250 , AF254251 , AF254252 Genomic DNA. Translation: AAL36972.1 .
AK293180 mRNA. Translation: BAH11466.1 .
AC092101 Genomic DNA. Translation: AAS07453.1 .
CH471140 Genomic DNA. Translation: EAX07987.1 .
BC051327 mRNA. Translation: AAH51327.1 .
BC069679 mRNA. Translation: AAH69679.1 .
BC069738 mRNA. Translation: AAH69738.1 .
BC069754 mRNA. Translation: AAH69754.1 .
BC074753 mRNA. Translation: AAH74753.1 .
CCDSi CCDS5525.1. [Q16816-1 ]
CCDS59057.1. [Q16816-2 ]
RefSeqi NP_001245388.1. NM_001258459.1. [Q16816-2 ]
NP_006204.1. NM_006213.4. [Q16816-1 ]
UniGenei Hs.730821.

3D structure databases

ProteinModelPortali Q16816.
SMRi Q16816. Positions 16-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111278. 1 interaction.
STRINGi 9606.ENSP00000297373.

Chemistry

BindingDBi Q16816.
ChEMBLi CHEMBL4004.
GuidetoPHARMACOLOGYi 2145.

PTM databases

PhosphoSitei Q16816.

Polymorphism databases

DMDMi 2833281.

Proteomic databases

PaxDbi Q16816.
PRIDEi Q16816.

Protocols and materials databases

DNASUi 5260.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297373 ; ENSP00000297373 ; ENSG00000164776 . [Q16816-1 ]
ENST00000452681 ; ENSP00000445440 ; ENSG00000164776 . [Q16816-2 ]
GeneIDi 5260.
KEGGi hsa:5260.
UCSCi uc003try.2. human. [Q16816-1 ]

Organism-specific databases

CTDi 5260.
GeneCardsi GC07M056115.
HGNCi HGNC:8930. PHKG1.
HPAi HPA012057.
MIMi 172470. gene.
neXtProti NX_Q16816.
Orphaneti 715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
PharmGKBi PA33271.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119185.
HOVERGENi HBG106193.
InParanoidi Q16816.
KOi K00871.
OMAi QNRYTAE.
OrthoDBi EOG7JMGDM.
PhylomeDBi Q16816.
TreeFami TF320349.

Enzyme and pathway databases

BioCyci MetaCyc:HS09136-MONOMER.
BRENDAi 2.7.11.19. 2681.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).
SignaLinki Q16816.

Miscellaneous databases

GeneWikii PHKG1.
GenomeRNAii 5260.
NextBioi 20318.
PMAP-CutDB Q16816.
PROi Q16816.
SOURCEi Search...

Gene expression databases

Bgeei Q16816.
CleanExi HS_PHKG1.
ExpressionAtlasi Q16816. baseline and differential.
Genevestigatori Q16816.

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. "Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1)."
    Wehner M., Kilimann M.W.
    Hum. Genet. 96:616-618(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  2. Burwinkel B. Jr., Kilimann M.W. Sr.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORM 2).
    Tissue: Adrenal gland.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Salivary gland.
  7. "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: VARIANTS [LARGE SCALE ANALYSIS] MET-48 AND CYS-323.

Entry informationi

Entry nameiPHKG1_HUMAN
AccessioniPrimary (citable) accession number: Q16816
Secondary accession number(s): B7Z1D0, F5H2S1, Q75LP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 146 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3