Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P54619 (AAKG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-AMP-activated protein kinase subunit gamma-1

Short name=AMPK gamma1
Short name=AMPK subunit gamma-1
Short name=AMPKg
Gene names
Name:PRKAG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.13

Subunit structure

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. Ref.7 Ref.9 Ref.13

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. Ref.6 Ref.8 Ref.13

The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP. Ref.6 Ref.8 Ref.13

Post-translational modification

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. Ref.11

Sequence similarities

Belongs to the 5'-AMP-activated protein kinase gamma subunit family.

Contains 4 CBS domains.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCBS domain
Repeat
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Traceable author statement. Source: Reactome

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

positive regulation of gene expression

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of protein kinase activity

Traceable author statement PubMed 8663446. Source: BHF-UCL

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of glycolysis

Traceable author statement PubMed 8663446. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 2342480. Source: ProtInc

spermatogenesis

Traceable author statement PubMed 9598317. Source: ProtInc

   Cellular_componentAMP-activated protein kinase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionADP binding

Inferred from sequence or structural similarity. Source: UniProtKB

AMP binding

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

cAMP-dependent protein kinase activity

Traceable author statement PubMed 9598317. Source: ProtInc

cAMP-dependent protein kinase regulator activity

Traceable author statement PubMed 8663446. Source: BHF-UCL

protein kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

protein kinase binding

Inferred from direct assay PubMed 10698692. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRKAB1Q9Y4784EBI-1181439,EBI-719769
PRKAB2O437413EBI-1181439,EBI-1053424

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54619-1)

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: P54619-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P54619-3)

The sequence of this isoform differs from the canonical sequence as follows:
     83-83: V → VVLRALSCPL
Note: No experimental confirmation available. May be due to competing acceptor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3313315'-AMP-activated protein kinase subunit gamma-1
PRO_0000204377

Regions

Domain43 – 10361CBS 1
Domain125 – 18763CBS 2
Domain198 – 26063CBS 3
Domain272 – 32958CBS 4
Motif138 – 15922AMPK pseudosubstrate

Sites

Binding site701AMP 1 By similarity
Binding site701ATP 1 By similarity
Binding site1511AMP 2 By similarity
Binding site1511AMP 3 By similarity
Binding site1511ATP 2 By similarity
Binding site1521ATP 1 By similarity
Binding site1521ATP 2 By similarity
Binding site1701AMP 1 By similarity
Binding site1701ATP 1 By similarity
Binding site2981AMP 3 By similarity
Binding site2991AMP 1 By similarity
Binding site2991ATP 1 By similarity

Amino acid modifications

Modified residue2611Phosphoserine; by ULK1 By similarity
Modified residue2631Phosphothreonine; by ULK1 By similarity
Modified residue2701Phosphoserine; by ULK1 By similarity

Natural variations

Alternative sequence1 – 3232Missing in isoform 2.
VSP_046711
Alternative sequence831V → VVLRALSCPL in isoform 3.
VSP_046712
Natural variant891T → S.
Corresponds to variant rs1126930 [ dbSNP | Ensembl ].
VAR_033453
Natural variant3291K → N.
Corresponds to variant rs34210356 [ dbSNP | Ensembl ].
VAR_033454

Experimental info

Mutagenesis901D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2. Ref.13
Mutagenesis2451D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2. Ref.13
Mutagenesis3171D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Does not affect ADP activation of phosphorylation of PRKAA1 or PRKAA2. Ref.13

Secondary structure

....................................................... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0F22B9CA1DBD87AE

FASTA33137,579
        10         20         30         40         50         60 
METVISSDSS PAVENEHPQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV FDTSLQVKKA 

        70         80         90        100        110        120 
FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK SALVQIYELE EHKIETWREV 

       130        140        150        160        170        180 
YLQDSFKPLV CISPNASLFD AVSSLIRNKI HRLPVIDPES GNTLYILTHK RILKFLKLFI 

       190        200        210        220        230        240 
TEFPKPEFMS KSLEELQIGT YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI 

       250        260        270        280        290        300 
YSKFDVINLA AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL 

       310        320        330 
VVVDENDVVK GIVSLSDILQ ALVLTGGEKK P 

« Hide

Isoform 2 [UniParc].

Checksum: A9BA11BA1205419E
Show »

FASTA29934,084
Isoform 3 [UniParc].

Checksum: BCDF1B75723C4321
Show »

FASTA34038,533

References

« Hide 'large scale' references
[1]"Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase."
Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., Dyck J.R.B., Kemp B.E., Witters L.A.
J. Biol. Chem. 271:8675-8681(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Fetal liver.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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 2 AND 3).
Tissue: Glial tumor and Testis.
[4]"The finished DNA sequence of human chromosome 12."
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. expand/collapse author list , 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.
Nature 440:346-351(2006) [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: Muscle.
[6]"CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations."
Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G.
J. Clin. Invest. 113:274-284(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN CBS, AMP-BINDING, ATP-BINDING.
[7]"Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."
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.
Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FNIP1, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit."
Scott J.W., Ross F.A., Liu J.K., Hardie D.G.
EMBO J. 26:806-815(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN AMPK PSEUDOSUBSTRATE.
[9]"Identification and characterization of a novel folliculin-interacting protein FNIP2."
Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A., Linehan W.M., Schmidt L.S.
Gene 415:60-67(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FNIP2.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
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.
Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ULK1 AND ULK2.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"AMPK is a direct adenylate charge-regulated protein kinase."
Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., Kemp B.E.
Science 332:1433-1435(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKAA1 AND PRKAB1, DOMAIN CBS, ADP-BINDING, MUTAGENESIS OF ASP-90; ASP-245 AND ASP-317, FUNCTION.
[14]"AMP-activated protein kinase in metabolic control and insulin signaling."
Towler M.C., Hardie D.G.
Circ. Res. 100:328-341(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[15]"AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy."
Hardie D.G.
Nat. Rev. Mol. Cell Biol. 8:774-785(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U42412 mRNA. Translation: AAC50495.1.
BT007345 mRNA. Translation: AAP36009.1.
AK097606 mRNA. Translation: BAC05117.1.
AK293332 mRNA. Translation: BAG56848.1.
AC011603 Genomic DNA. No translation available.
BC000358 mRNA. Translation: AAH00358.1.
RefSeqNP_001193638.1. NM_001206709.1.
NP_001193639.1. NM_001206710.1.
NP_002724.1. NM_002733.4.
UniGeneHs.530862.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UV4X-ray1.33A182-325[»]
2UV5X-ray1.69A182-325[»]
2UV6X-ray2.00A182-325[»]
2UV7X-ray2.00A182-325[»]
4CFEX-ray3.02E/F1-331[»]
4CFFX-ray3.92E/F1-331[»]
ProteinModelPortalP54619.
SMRP54619. Positions 24-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111558. 19 interactions.
IntActP54619. 19 interactions.
MINTMINT-4649712.
STRING9606.ENSP00000323867.

Chemistry

BindingDBP54619.
ChEMBLCHEMBL2096907.

PTM databases

PhosphoSiteP54619.

Polymorphism databases

DMDM1703037.

Proteomic databases

PaxDbP54619.
PRIDEP54619.

Protocols and materials databases

DNASU5571.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316299; ENSP00000323867; ENSG00000181929. [P54619-3]
ENST00000548065; ENSP00000447433; ENSG00000181929. [P54619-1]
ENST00000552212; ENSP00000448972; ENSG00000181929. [P54619-2]
GeneID5571.
KEGGhsa:5571.
UCSCuc001rsy.3. human. [P54619-1]
uc001rsz.3. human.

Organism-specific databases

CTD5571.
GeneCardsGC12M049396.
HGNCHGNC:9385. PRKAG1.
MIM602742. gene.
neXtProtNX_P54619.
PharmGKBPA33751.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0517.
HOVERGENHBG050431.
InParanoidP54619.
KOK07200.
OMAKGGAYDE.
PhylomeDBP54619.
TreeFamTF313247.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
SignaLinkP54619.

Gene expression databases

ArrayExpressP54619.
BgeeP54619.
CleanExHS_PRKAG1.
GenevestigatorP54619.

Family and domain databases

InterProIPR000644. CBS_dom.
[Graphical view]
PfamPF00571. CBS. 4 hits.
[Graphical view]
SMARTSM00116. CBS. 4 hits.
[Graphical view]
PROSITEPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKAG1. human.
EvolutionaryTraceP54619.
GeneWikiPRKAG1.
GenomeRNAi5571.
NextBio21596.
PROP54619.
SOURCESearch...

Entry information

Entry nameAAKG1_HUMAN
AccessionPrimary (citable) accession number: P54619
Secondary accession number(s): B4DDT7, Q8N7V9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM