SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54619

- AAKG1_HUMAN

UniProt

P54619 - AAKG1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

5'-AMP-activated protein kinase subunit gamma-1

Gene
PRKAG1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701AMP 1 By similarity
Binding sitei70 – 701ATP 1 By similarity
Binding sitei151 – 1511AMP 2 By similarity
Binding sitei151 – 1511AMP 3 By similarity
Binding sitei151 – 1511ATP 2 By similarity
Binding sitei152 – 1521ATP 1 By similarity
Binding sitei152 – 1521ATP 2 By similarity
Binding sitei170 – 1701AMP 1 By similarity
Binding sitei170 – 1701ATP 1 By similarity
Binding sitei298 – 2981AMP 3 By similarity
Binding sitei299 – 2991AMP 1 By similarity
Binding sitei299 – 2991ATP 1 By similarity

GO - Molecular functioni

  1. ADP binding Source: UniProtKB
  2. AMP binding Source: UniProtKB
  3. ATP binding Source: UniProtKB
  4. cAMP-dependent protein kinase activity Source: ProtInc
  5. cAMP-dependent protein kinase regulator activity Source: BHF-UCL
  6. protein binding Source: UniProtKB
  7. protein kinase activity Source: UniProtKB
  8. protein kinase binding Source: BHF-UCL

GO - Biological processi

  1. cell cycle arrest Source: Reactome
  2. fatty acid biosynthetic process Source: UniProtKB-KW
  3. insulin receptor signaling pathway Source: Reactome
  4. membrane organization Source: Reactome
  5. positive regulation of gene expression Source: UniProtKB
  6. positive regulation of protein kinase activity Source: BHF-UCL
  7. protein heterooligomerization Source: Ensembl
  8. protein phosphorylation Source: UniProtKB
  9. regulation of glycolytic process Source: BHF-UCL
  10. signal transduction Source: ProtInc
  11. spermatogenesis Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21285. Regulation of AMPK activity via LKB1.
REACT_21393. Regulation of Rheb GTPase activity by AMPK.
SignaLinkiP54619.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma-1
Short name:
AMPK gamma1
Short name:
AMPK subunit gamma-1
Short name:
AMPKg
Gene namesi
Name:PRKAG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9385. PRKAG1.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2. 1 Publication
Mutagenesisi245 – 2451D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2. 1 Publication
Mutagenesisi317 – 3171D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Does not affect ADP activation of phosphorylation of PRKAA1 or PRKAA2. 1 Publication

Organism-specific databases

PharmGKBiPA33751.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3313315'-AMP-activated protein kinase subunit gamma-1PRO_0000204377Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei261 – 2611Phosphoserine; by ULK1 By similarity
Modified residuei263 – 2631Phosphothreonine; by ULK1 By similarity
Modified residuei270 – 2701Phosphoserine; by ULK1 By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP54619.
PaxDbiP54619.
PRIDEiP54619.

PTM databases

PhosphoSiteiP54619.

Expressioni

Gene expression databases

ArrayExpressiP54619.
BgeeiP54619.
CleanExiHS_PRKAG1.
GenevestigatoriP54619.

Interactioni

Subunit structurei

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 FNIP2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKAB1Q9Y4784EBI-1181439,EBI-719769
PRKAB2O437413EBI-1181439,EBI-1053424

Protein-protein interaction databases

BioGridi111558. 19 interactions.
IntActiP54619. 19 interactions.
MINTiMINT-4649712.
STRINGi9606.ENSP00000323867.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 336
Helixi38 – 414
Beta strandi44 – 529
Helixi57 – 6610
Beta strandi72 – 765
Turni77 – 804
Beta strandi81 – 866
Helixi88 – 9710
Beta strandi102 – 1043
Helixi107 – 1115
Helixi114 – 1207
Helixi138 – 14710
Beta strandi151 – 1566
Turni158 – 1603
Beta strandi163 – 1686
Helixi169 – 1779
Turni178 – 1825
Helixi186 – 1894
Helixi193 – 1964
Helixi213 – 22311
Beta strandi226 – 2316
Beta strandi235 – 2428
Helixi243 – 2519
Helixi262 – 2676
Helixi271 – 2744
Beta strandi277 – 2793
Helixi285 – 29511
Beta strandi298 – 3036
Beta strandi307 – 3148
Helixi315 – 3228

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP54619.
SMRiP54619. Positions 27-325.

Miscellaneous databases

EvolutionaryTraceiP54619.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 10361CBS 1Add
BLAST
Domaini125 – 18763CBS 2Add
BLAST
Domaini198 – 26063CBS 3Add
BLAST
Domaini272 – 32958CBS 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi138 – 15922AMPK pseudosubstrateAdd
BLAST

Domaini

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/LKB1.3 Publications
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.3 Publications

Sequence similaritiesi

Contains 4 CBS domains.

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOVERGENiHBG050431.
InParanoidiP54619.
KOiK07200.
OMAiKGGAYDE.
PhylomeDBiP54619.
TreeFamiTF313247.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 4 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54619-1) [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

METVISSDSS PAVENEHPQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV    50
FDTSLQVKKA FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK 100
SALVQIYELE EHKIETWREV YLQDSFKPLV CISPNASLFD AVSSLIRNKI 150
HRLPVIDPES GNTLYILTHK RILKFLKLFI TEFPKPEFMS KSLEELQIGT 200
YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI YSKFDVINLA 250
AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL 300
VVVDENDVVK GIVSLSDILQ ALVLTGGEKK P 331
Length:331
Mass (Da):37,579
Last modified:October 1, 1996 - v1
Checksum:i0F22B9CA1DBD87AE
GO
Isoform 2 (identifier: P54619-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: No experimental confirmation available.

Show »
Length:299
Mass (Da):34,084
Checksum:iA9BA11BA1205419E
GO
Isoform 3 (identifier: P54619-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:340
Mass (Da):38,533
Checksum:iBCDF1B75723C4321
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891T → S.
Corresponds to variant rs1126930 [ dbSNP | Ensembl ].
VAR_033453
Natural varianti329 – 3291K → N.
Corresponds to variant rs34210356 [ dbSNP | Ensembl ].
VAR_033454

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232Missing in isoform 2. VSP_046711Add
BLAST
Alternative sequencei83 – 831V → VVLRALSCPL in isoform 3. VSP_046712

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS55824.1. [P54619-2]
CCDS55825.1. [P54619-3]
CCDS8777.1. [P54619-1]
RefSeqiNP_001193638.1. NM_001206709.1. [P54619-3]
NP_001193639.1. NM_001206710.1. [P54619-2]
NP_002724.1. NM_002733.4. [P54619-1]
XP_006719562.1. XM_006719499.1. [P54619-2]
UniGeneiHs.530862.

Genome annotation databases

EnsembliENST00000316299; ENSP00000323867; ENSG00000181929. [P54619-3]
ENST00000548065; ENSP00000447433; ENSG00000181929. [P54619-1]
ENST00000552212; ENSP00000448972; ENSG00000181929. [P54619-2]
GeneIDi5571.
KEGGihsa:5571.
UCSCiuc001rsy.3. human. [P54619-1]
uc001rsz.3. human.

Polymorphism databases

DMDMi1703037.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS55824.1. [P54619-2 ]
CCDS55825.1. [P54619-3 ]
CCDS8777.1. [P54619-1 ]
RefSeqi NP_001193638.1. NM_001206709.1. [P54619-3 ]
NP_001193639.1. NM_001206710.1. [P54619-2 ]
NP_002724.1. NM_002733.4. [P54619-1 ]
XP_006719562.1. XM_006719499.1. [P54619-2 ]
UniGenei Hs.530862.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UV4 X-ray 1.33 A 182-325 [» ]
2UV5 X-ray 1.69 A 182-325 [» ]
2UV6 X-ray 2.00 A 182-325 [» ]
2UV7 X-ray 2.00 A 182-325 [» ]
4CFE X-ray 3.02 E/F 1-331 [» ]
4CFF X-ray 3.92 E/F 1-331 [» ]
ProteinModelPortali P54619.
SMRi P54619. Positions 27-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111558. 19 interactions.
IntActi P54619. 19 interactions.
MINTi MINT-4649712.
STRINGi 9606.ENSP00000323867.

Chemistry

BindingDBi P54619.
ChEMBLi CHEMBL2096907.

PTM databases

PhosphoSitei P54619.

Polymorphism databases

DMDMi 1703037.

Proteomic databases

MaxQBi P54619.
PaxDbi P54619.
PRIDEi P54619.

Protocols and materials databases

DNASUi 5571.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316299 ; ENSP00000323867 ; ENSG00000181929 . [P54619-3 ]
ENST00000548065 ; ENSP00000447433 ; ENSG00000181929 . [P54619-1 ]
ENST00000552212 ; ENSP00000448972 ; ENSG00000181929 . [P54619-2 ]
GeneIDi 5571.
KEGGi hsa:5571.
UCSCi uc001rsy.3. human. [P54619-1 ]
uc001rsz.3. human.

Organism-specific databases

CTDi 5571.
GeneCardsi GC12M049396.
HGNCi HGNC:9385. PRKAG1.
MIMi 602742. gene.
neXtProti NX_P54619.
PharmGKBi PA33751.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0517.
HOVERGENi HBG050431.
InParanoidi P54619.
KOi K07200.
OMAi KGGAYDE.
PhylomeDBi P54619.
TreeFami TF313247.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21285. Regulation of AMPK activity via LKB1.
REACT_21393. Regulation of Rheb GTPase activity by AMPK.
SignaLinki P54619.

Miscellaneous databases

ChiTaRSi PRKAG1. human.
EvolutionaryTracei P54619.
GeneWikii PRKAG1.
GenomeRNAii 5571.
NextBioi 21596.
PROi P54619.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54619.
Bgeei P54619.
CleanExi HS_PRKAG1.
Genevestigatori P54619.

Family and domain databases

InterProi IPR000644. CBS_dom.
[Graphical view ]
Pfami PF00571. CBS. 4 hits.
[Graphical view ]
SMARTi SM00116. CBS. 4 hits.
[Graphical view ]
PROSITEi PS51371. CBS. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiAAKG1_HUMAN
AccessioniPrimary (citable) accession number: P54619
Secondary accession number(s): B4DDT7, Q8N7V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 131 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi