Q16816 (PHKG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
Short name=PHK-gamma-M
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 names

Name:	PHKG1
Synonyms:	PHKG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 By similarity.
Catalytic activity	2 ATP + phosphorylase b = 2 ADP + phosphorylase a. ATP + [tau protein] = ADP + [tau protein] phosphate. ATP + a protein = ADP + a phosphoprotein.
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.
Domain	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 similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Muscle protein Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome phosphorylase kinase complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorylase kinase activity Inferred from electronic annotation. Source: EC tau-protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16816-1)

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: Q16816-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 387	386	Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform		PRO_0000086508
Regions
	Domain	20 – 288	269	Protein kinase
	Nucleotide binding	26 – 34	9	ATP By similarity
	Region	303 – 327	25	Calmodulin-binding (domain-N)
	Region	343 – 367	25	Calmodulin-binding (domain-C)
Sites
	Active site	150	1	Proton acceptor By similarity
	Binding site	49	1	ATP By similarity
Natural variations
	Alternative sequence	106	1	L → LWEDTDTMEMEQKWCLGWDS PKSTNFRAQGRAR in isoform 2.		VSP_044716
	Natural variant	48	1	V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.7		VAR_040994
	Natural variant	323	1	R → C. Ref.7		VAR_040995
Experimental info
	Sequence conflict	100	1	F → L in BAH11466. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9CB416CB683920AA	FASTA	387	45,024
	10 20 30 40 50 60 MTRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV IDVTGGGSFS 70 80 90 100 110 120 PEEVRELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF FLVFDLMKRG ELFDYLTEKV 130 140 150 160 170 180 TLSEKETRKI MRALLEVICT LHKLNIVHRD LKPENILLDD NMNIKLTDFG FSCQLEPGER 190 200 210 220 230 240 LREVCGTPSY LAPEIIECSM NEDHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR 250 260 270 280 290 300 MIMSGNYQFG SPEWDDYSDT VKDLVSRFLV VQPQNRYTAE EALAHPFFQQ YLVEEVRHFS 310 320 330 340 350 360 PRGKFKVIAL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY AFRIYGHWVK 370 380 KGQQQNRAAL FENTPKAVLL SLAEEDY
	Isoform 2 [UniParc]. Checksum: 99429FF321971C5E	FASTA	419	48,867
	10 20 30 40 50 60 MTRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV IDVTGGGSFS 70 80 90 100 110 120 PEEVRELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF FLVFDLWEDT DTMEMEQKWC 130 140 150 160 170 180 LGWDSPKSTN FRAQGRARMK RGELFDYLTE KVTLSEKETR KIMRALLEVI CTLHKLNIVH 190 200 210 220 230 240 RDLKPENILL DDNMNIKLTD FGFSCQLEPG ERLREVCGTP SYLAPEIIEC SMNEDHPGYG 250 260 270 280 290 300 KEVDMWSTGV IMYTLLAGSP PFWHRKQMLM LRMIMSGNYQ FGSPEWDDYS DTVKDLVSRF 310 320 330 340 350 360 LVVQPQNRYT AEEALAHPFF QQYLVEEVRH FSPRGKFKVI ALTVLASVRI YYQYRRVKPV 370 380 390 400 410 TREIVIRDPY ALRPLRRLID AYAFRIYGHW VKKGQQQNRA ALFENTPKAV LLSLAEEDY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00220396. IPI00922459.
RefSeq	NP_001245388.1. NM_001258459.1. NP_006204.1. NM_006213.4.
UniGene	Hs.730821.
3D structure databases
ProteinModelPortal	Q16816.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000297373.
PTM databases
PhosphoSite	Q16816.
Polymorphism databases
DMDM	2833281.
Proteomic databases
PaxDb	Q16816.
PRIDE	Q16816.
Protocols and materials databases
DNASU	5260.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297373; ENSP00000297373; ENSG00000164776. ENST00000452681; ENSP00000445440; ENSG00000164776.
GeneID	5260.
KEGG	hsa:5260.
UCSC	uc003try.1. human. uc011kdb.1. human.
Organism-specific databases
CTD	5260.
GeneCards	GC07M056115.
HGNC	HGNC:8930. PHKG1.
HPA	HPA012057.
MIM	172470. gene.
neXtProt	NX_Q16816.
PharmGKB	PA33271.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG106193.
KO	K00871.
OMA	DFYENYE.
OrthoDB	EOG4CNQR5.
PhylomeDB	Q16816.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09136-MONOMER.
BRENDA	2.7.11.19. 2681.
Reactome	REACT_111217. Metabolism.
SignaLink	Q16816.
Gene expression databases
ArrayExpress	Q16816.
Bgee	Q16816.
CleanEx	HS_PHKG1.
Genevestigator	Q16816.
GermOnline	ENSG00000164776. Homo sapiens.
Family and domain databases
InterPro	IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase. IPR011009. Kinase-like_dom. IPR002291. Phosph_kin_gamma. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
PANTHER	PTHR24347. PTHR24347. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR01049. PHOSPHBKNASE.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q16816.
ChEMBL	CHEMBL4004.
GenomeRNAi	5260.
NextBio	20318.
PMAP-CutDB	Q16816.
SOURCE	Search...

Entry information

Entry name

PHKG1_HUMAN

Accession

Primary (citable) accession number: Q16816
Secondary accession number(s): B7Z1D0, F5H2S1, Q75LP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.