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5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg)

 AAKG1_HUMAN             Reviewed;         331 AA.
P54619; B4DDT7; Q8N7V9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 164.
RecName: Full=5'-AMP-activated protein kinase subunit gamma-1;
Short=AMPK gamma1;
Short=AMPK subunit gamma-1;
Short=AMPKg;
Name=PRKAG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fetal liver;
PubMed=8621499; DOI=10.1074/jbc.271.15.8675;
Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J.,
Dyck J.R.B., Kemp B.E., Witters L.A.;
"Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-
activated protein kinase.";
J. Biol. Chem. 271:8675-8681(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Glial tumor, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DOMAIN CBS, AMP-BINDING, AND ATP-BINDING.
PubMed=14722619; DOI=10.1172/JCI19874;
Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G.,
Scullion G.A., Norman D.G., Hardie D.G.;
"CBS domains form energy-sensing modules whose binding of adenosine
ligands is disrupted by disease mutations.";
J. Clin. Invest. 113:274-284(2004).
[7]
INTERACTION WITH FNIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17028174; DOI=10.1073/pnas.0603781103;
Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L.,
Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III,
Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr.,
Linehan W.M., Schmidt L.S., Zbar B.;
"Folliculin encoded by the BHD gene interacts with a binding protein,
FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).
[8]
DOMAIN AMPK PSEUDOSUBSTRATE.
PubMed=17255938; DOI=10.1038/sj.emboj.7601542;
Scott J.W., Ross F.A., Liu J.K., Hardie D.G.;
"Regulation of AMP-activated protein kinase by a pseudosubstrate
sequence on the gamma subunit.";
EMBO J. 26:806-815(2007).
[9]
INTERACTION WITH FNIP2.
PubMed=18403135; DOI=10.1016/j.gene.2008.02.022;
Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M.,
Valera V.A., Linehan W.M., Schmidt L.S.;
"Identification and characterization of a novel folliculin-interacting
protein FNIP2.";
Gene 415:60-67(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION BY ULK1 AND ULK2.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH PRKAA1 AND PRKAB1, DOMAIN CBS, ADP-BINDING,
MUTAGENESIS OF ASP-90; ASP-245 AND ASP-317, AND FUNCTION.
PubMed=21680840; DOI=10.1126/science.1200094;
Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S.,
Kemp B.E.;
"AMPK is a direct adenylate charge-regulated protein kinase.";
Science 332:1433-1435(2011).
[14]
REVIEW ON FUNCTION.
PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05;
Towler M.C., Hardie D.G.;
"AMP-activated protein kinase in metabolic control and insulin
signaling.";
Circ. Res. 100:328-341(2007).
[15]
REVIEW ON FUNCTION.
PubMed=17712357; DOI=10.1038/nrm2249;
Hardie D.G.;
"AMP-activated/SNF1 protein kinases: conserved guardians of cellular
energy.";
Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 182-325 IN COMPLEX WITH AMP.
PubMed=17452784; DOI=10.1107/S0907444907009110;
Day P., Sharff A., Parra L., Cleasby A., Williams M., Hoerer S.,
Nar H., Redemann N., Tickle I., Yon J.;
"Structure of a CBS-domain pair from the regulatory gamma1 subunit of
human AMPK in complex with AMP and ZMP.";
Acta Crystallogr. D 63:587-596(2007).
[18]
X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH AMP.
PubMed=24352254; DOI=10.1038/ncomms4017;
Xiao B., Sanders M.J., Carmena D., Bright N.J., Haire L.F.,
Underwood E., Patel B.R., Heath R.B., Walker P.A., Hallen S.,
Giordanetto F., Martin S.R., Carling D., Gamblin S.J.;
"Structural basis of AMPK regulation by small molecule activators.";
Nat. Commun. 4:3017-3017(2013).
[19]
X-RAY CRYSTALLOGRAPHY (4.05 ANGSTROMS) OF 24-327 IN COMPLEX WITH AMP.
PubMed=25412657; DOI=10.1038/cr.2014.150;
Li X., Wang L., Zhou X.E., Ke J., de Waal P.W., Gu X., Tan M.H.,
Wang D., Wu D., Xu H.E., Melcher K.;
"Structural basis of AMPK regulation by adenine nucleotides and
glycogen.";
Cell Res. 25:50-66(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 2-331.
PubMed=26952388; DOI=10.1038/ncomms10912;
Langendorf C.G., Ngoei K.R., Scott J.W., Ling N.X., Issa S.M.,
Gorman M.A., Parker M.W., Sakamoto K., Oakhill J.S., Kemp B.E.;
"Structural basis of allosteric and synergistic activation of AMPK by
furan-2-phosphonic derivative C2 binding.";
Nat. Commun. 7:10912-10912(2016).
-!- FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase
(AMPK), an energy sensor protein kinase that plays a key role in
regulating cellular energy metabolism. In response to reduction of
intracellular ATP levels, AMPK activates energy-producing pathways
and inhibits energy-consuming processes: inhibits protein,
carbohydrate and lipid biosynthesis, as well as cell growth and
proliferation. AMPK acts via direct phosphorylation of metabolic
enzymes, and by longer-term effects via phosphorylation of
transcription regulators. Also acts as a regulator of cellular
polarity by remodeling the actin cytoskeleton; probably by
indirectly activating myosin. Gamma non-catalytic subunit mediates
binding to AMP, ADP and ATP, leading to activate or inhibit AMPK:
AMP-binding results in allosteric activation of alpha catalytic
subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and
preventing dephosphorylation of catalytic subunits. ADP also
stimulates phosphorylation, without stimulating already
phosphorylated catalytic subunit. ATP promotes dephosphorylation
of catalytic subunit, rendering the AMPK enzyme inactive.
{ECO:0000269|PubMed:21680840}.
-!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit
(PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-
catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with
FNIP1 and FNIP2. {ECO:0000269|PubMed:17028174,
ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:21680840}.
-!- INTERACTION:
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-1181439, EBI-946029;
P35520:CBS; NbExp=3; IntAct=EBI-1181439, EBI-740135;
Q14145:KEAP1; NbExp=5; IntAct=EBI-1181439, EBI-751001;
P60370:KRTAP10-5; NbExp=4; IntAct=EBI-1181439, EBI-10172150;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-1181439, EBI-10172511;
Q13131:PRKAA1; NbExp=10; IntAct=EBI-1181439, EBI-1181405;
P54646:PRKAA2; NbExp=9; IntAct=EBI-1181439, EBI-1383852;
Q9Y478:PRKAB1; NbExp=8; IntAct=EBI-1181439, EBI-719769;
O43741:PRKAB2; NbExp=12; IntAct=EBI-1181439, EBI-1053424;
P06782:SNF1 (xeno); NbExp=3; IntAct=EBI-1181439, EBI-17516;
Q969V4:TEKT1; NbExp=5; IntAct=EBI-1181439, EBI-10180409;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P54619-1; Sequence=Displayed;
Name=2;
IsoId=P54619-2; Sequence=VSP_046711;
Note=No experimental confirmation available.;
Name=3;
IsoId=P54619-3; Sequence=VSP_046712;
Note=No experimental confirmation available. May be due to
competing acceptor splice site.;
-!- DOMAIN: The AMPK pseudosubstrate motif resembles the sequence
around sites phosphorylated on target proteins of AMPK, except the
presence of a non-phosphorylatable residue in place of Ser. In the
absence of AMP this pseudosubstrate sequence may bind to the
active site groove on the alpha subunit (PRKAA1 or PRKAA2),
preventing phosphorylation by the upstream activating kinase
STK11/LKB1.
-!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4
potential nucleotide-binding sites, 3 are occupied, designated as
sites 1, 3, and 4 based on the CBS modules that provide the acidic
residue for coordination with the 2'- and 3'-hydroxyl groups of
the ribose of AMP. Of these, site 4 appears to be a structural
site that retains a tightly held AMP molecule (AMP 3). The 2
remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1
(AMP, ADP or ATP 1) is the high-affinity binding site and likely
accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest
nucleotide-binding site on the gamma subunit, yet it is
exquisitely sensitive to changes in nucleotide levels and this
allows AMPK to respond rapidly to changes in cellular energy
status. Site 3 is likely to be responsible for protection of a
conserved threonine in the activation loop of the alpha catalytic
subunit through conformational changes induced by binding of AMP
or ADP. {ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
-!- PTM: Phosphorylated by ULK1 and ULK2; leading to negatively
regulate AMPK activity and suggesting the existence of a
regulatory feedback loop between ULK1, ULK2 and AMPK.
{ECO:0000269|PubMed:21460634}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
subunit family. {ECO:0000305}.
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EMBL; U42412; AAC50495.1; -; mRNA.
EMBL; BT007345; AAP36009.1; -; mRNA.
EMBL; AK097606; BAC05117.1; -; mRNA.
EMBL; AK293332; BAG56848.1; -; mRNA.
EMBL; AC011603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000358; AAH00358.1; -; mRNA.
CCDS; CCDS55824.1; -. [P54619-2]
CCDS; CCDS55825.1; -. [P54619-3]
CCDS; CCDS8777.1; -. [P54619-1]
RefSeq; NP_001193638.1; NM_001206709.1. [P54619-3]
RefSeq; NP_001193639.1; NM_001206710.1. [P54619-2]
RefSeq; NP_002724.1; NM_002733.4. [P54619-1]
RefSeq; XP_006719562.1; XM_006719499.2. [P54619-2]
RefSeq; XP_011536864.1; XM_011538562.2. [P54619-2]
UniGene; Hs.530862; -.
PDB; 2UV4; X-ray; 1.33 A; A=182-325.
PDB; 2UV5; X-ray; 1.69 A; A=182-325.
PDB; 2UV6; X-ray; 2.00 A; A=182-325.
PDB; 2UV7; X-ray; 2.00 A; A=182-325.
PDB; 4CFE; X-ray; 3.02 A; E/F=1-331.
PDB; 4CFF; X-ray; 3.92 A; E/F=1-331.
PDB; 4RER; X-ray; 4.05 A; G=24-327.
PDB; 4REW; X-ray; 4.58 A; G=24-327.
PDB; 4ZHX; X-ray; 2.99 A; E/F=2-331.
PDB; 5EZV; X-ray; 2.99 A; E/F=2-331.
PDB; 5ISO; X-ray; 2.63 A; E/F=1-331.
PDBsum; 2UV4; -.
PDBsum; 2UV5; -.
PDBsum; 2UV6; -.
PDBsum; 2UV7; -.
PDBsum; 4CFE; -.
PDBsum; 4CFF; -.
PDBsum; 4RER; -.
PDBsum; 4REW; -.
PDBsum; 4ZHX; -.
PDBsum; 5EZV; -.
PDBsum; 5ISO; -.
ProteinModelPortal; P54619; -.
SMR; P54619; -.
BioGrid; 111558; 51.
CORUM; P54619; -.
DIP; DIP-39974N; -.
IntAct; P54619; 40.
MINT; MINT-4649712; -.
STRING; 9606.ENSP00000323867; -.
BindingDB; P54619; -.
ChEMBL; CHEMBL2393; -.
DrugBank; DB00945; Acetylsalicylic acid.
iPTMnet; P54619; -.
PhosphoSitePlus; P54619; -.
BioMuta; PRKAG1; -.
DMDM; 1703037; -.
EPD; P54619; -.
MaxQB; P54619; -.
PaxDb; P54619; -.
PeptideAtlas; P54619; -.
PRIDE; P54619; -.
DNASU; 5571; -.
Ensembl; ENST00000316299; ENSP00000323867; ENSG00000181929. [P54619-3]
Ensembl; ENST00000548065; ENSP00000447433; ENSG00000181929. [P54619-1]
Ensembl; ENST00000552212; ENSP00000448972; ENSG00000181929. [P54619-2]
GeneID; 5571; -.
KEGG; hsa:5571; -.
UCSC; uc001rsy.4; human. [P54619-1]
CTD; 5571; -.
DisGeNET; 5571; -.
EuPathDB; HostDB:ENSG00000181929.11; -.
GeneCards; PRKAG1; -.
HGNC; HGNC:9385; PRKAG1.
HPA; HPA077805; -.
MIM; 602742; gene.
neXtProt; NX_P54619; -.
OpenTargets; ENSG00000181929; -.
PharmGKB; PA33751; -.
eggNOG; KOG1764; Eukaryota.
eggNOG; COG0517; LUCA.
GeneTree; ENSGT00390000009849; -.
HOGENOM; HOG000176880; -.
HOVERGEN; HBG050431; -.
KO; K07200; -.
OMA; FPGVVIC; -.
OrthoDB; EOG091G0CZV; -.
PhylomeDB; P54619; -.
TreeFam; TF313247; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; P54619; -.
SIGNOR; P54619; -.
ChiTaRS; PRKAG1; human.
EvolutionaryTrace; P54619; -.
GeneWiki; PRKAG1; -.
GenomeRNAi; 5571; -.
PRO; PR:P54619; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000181929; -.
CleanEx; HS_PRKAG1; -.
ExpressionAtlas; P54619; baseline and differential.
Genevisible; P54619; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISS:UniProtKB.
GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; TAS:ProtInc.
GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; TAS:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; TAS:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0006110; P:regulation of glycolytic process; TAS:BHF-UCL.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:1902593; P:single-organism nuclear import; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
InterPro; IPR000644; CBS_dom.
Pfam; PF00571; CBS; 3.
SMART; SM00116; CBS; 4.
PROSITE; PS51371; CBS; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; CBS domain;
Complete proteome; Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat.
CHAIN 1 331 5'-AMP-activated protein kinase subunit
gamma-1.
/FTId=PRO_0000204377.
DOMAIN 43 103 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 125 187 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 198 260 CBS 3. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 272 329 CBS 4. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
NP_BIND 87 90 AMP, ADP or ATP 1.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
NP_BIND 151 152 AMP, ADP or ATP 1.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
NP_BIND 226 227 AMP 3. {ECO:0000269|PubMed:17452784,
ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
NP_BIND 242 245 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
NP_BIND 298 299 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
NP_BIND 314 317 AMP 3. {ECO:0000269|PubMed:17452784,
ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
MOTIF 138 159 AMPK pseudosubstrate.
BINDING 70 70 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 130 130 AMP, ADP or ATP 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 151 151 AMP 3. {ECO:0000269|PubMed:17452784,
ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 170 170 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 200 200 AMP 3. {ECO:0000269|PubMed:17452784,
ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 205 205 AMP 3; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:17452784,
ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 269 269 AMP, ADP or ATP 2.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 277 277 AMP, ADP or ATP 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
BINDING 298 298 AMP 3. {ECO:0000269|PubMed:17452784,
ECO:0000269|PubMed:24352254,
ECO:0000269|PubMed:25412657}.
MOD_RES 261 261 Phosphoserine; by ULK1. {ECO:0000250}.
MOD_RES 263 263 Phosphothreonine; by ULK1. {ECO:0000250}.
MOD_RES 270 270 Phosphoserine; by ULK1.
{ECO:0000250|UniProtKB:P80385}.
VAR_SEQ 1 32 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046711.
VAR_SEQ 83 83 V -> VVLRALSCPL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046712.
VARIANT 89 89 T -> S (in dbSNP:rs1126930).
/FTId=VAR_033453.
VARIANT 329 329 K -> N (in dbSNP:rs34210356).
/FTId=VAR_033454.
MUTAGEN 90 90 D->A: Reduced AMP-activation of
phosphorylation of PRKAA1 or PRKAA2.
Reduced ADP activation of phosphorylation
of PRKAA1 or PRKAA2.
{ECO:0000269|PubMed:21680840}.
MUTAGEN 245 245 D->A: Reduced AMP-activation of
phosphorylation of PRKAA1 or PRKAA2.
Reduced ADP activation of phosphorylation
of PRKAA1 or PRKAA2.
{ECO:0000269|PubMed:21680840}.
MUTAGEN 317 317 D->A: Reduced AMP-activation of
phosphorylation of PRKAA1 or PRKAA2. Does
not affect ADP activation of
phosphorylation of PRKAA1 or PRKAA2.
{ECO:0000269|PubMed:21680840}.
HELIX 29 35 {ECO:0000244|PDB:4ZHX}.
HELIX 38 40 {ECO:0000244|PDB:4ZHX}.
STRAND 44 52 {ECO:0000244|PDB:4ZHX}.
HELIX 57 67 {ECO:0000244|PDB:4ZHX}.
STRAND 72 76 {ECO:0000244|PDB:4ZHX}.
TURN 77 80 {ECO:0000244|PDB:4ZHX}.
STRAND 81 86 {ECO:0000244|PDB:4ZHX}.
HELIX 88 98 {ECO:0000244|PDB:4ZHX}.
STRAND 102 104 {ECO:0000244|PDB:4ZHX}.
HELIX 107 111 {ECO:0000244|PDB:4ZHX}.
HELIX 114 122 {ECO:0000244|PDB:4ZHX}.
HELIX 138 147 {ECO:0000244|PDB:4ZHX}.
STRAND 151 156 {ECO:0000244|PDB:4ZHX}.
TURN 158 160 {ECO:0000244|PDB:4ZHX}.
STRAND 163 168 {ECO:0000244|PDB:4ZHX}.
HELIX 169 177 {ECO:0000244|PDB:4ZHX}.
TURN 178 182 {ECO:0000244|PDB:4ZHX}.
HELIX 186 189 {ECO:0000244|PDB:2UV4}.
HELIX 193 196 {ECO:0000244|PDB:2UV4}.
HELIX 213 223 {ECO:0000244|PDB:2UV4}.
STRAND 226 231 {ECO:0000244|PDB:2UV4}.
STRAND 235 242 {ECO:0000244|PDB:2UV4}.
HELIX 243 251 {ECO:0000244|PDB:2UV4}.
STRAND 259 261 {ECO:0000244|PDB:5EZV}.
HELIX 262 267 {ECO:0000244|PDB:2UV4}.
HELIX 271 274 {ECO:0000244|PDB:2UV4}.
STRAND 277 279 {ECO:0000244|PDB:2UV4}.
HELIX 285 295 {ECO:0000244|PDB:2UV4}.
STRAND 298 303 {ECO:0000244|PDB:2UV4}.
STRAND 307 314 {ECO:0000244|PDB:2UV4}.
HELIX 315 322 {ECO:0000244|PDB:2UV4}.
TURN 323 325 {ECO:0000244|PDB:5EZV}.
SEQUENCE 331 AA; 37579 MW; 0F22B9CA1DBD87AE CRC64;
METVISSDSS PAVENEHPQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV FDTSLQVKKA
FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK SALVQIYELE EHKIETWREV
YLQDSFKPLV CISPNASLFD AVSSLIRNKI HRLPVIDPES GNTLYILTHK RILKFLKLFI
TEFPKPEFMS KSLEELQIGT YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI
YSKFDVINLA AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL
VVVDENDVVK GIVSLSDILQ ALVLTGGEKK P


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