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Q9Y478

- AAKB1_HUMAN

UniProt

Q9Y478 - AAKB1_HUMAN

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Protein
5'-AMP-activated protein kinase subunit beta-1
Gene
PRKAB1, AMPK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-catalytic 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. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein kinase activity Source: UniProtKB

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. protein heterooligomerization Source: Ensembl
  7. protein phosphorylation Source: UniProtKB
  8. regulation of catalytic activity Source: Ensembl
  9. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

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

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.
SignaLinkiQ9Y478.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit beta-1
Short name:
AMPK subunit beta-1
Short name:
AMPKb
Gene namesi
Name:PRKAB1
Synonyms:AMPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9378. PRKAB1.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: Ensembl
  2. cytosol Source: Reactome
  3. nucleus Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Abolishes myristoylation and AMP-enhanced phosphorylation of PRKAA1 or PRKAA2. 1 Publication

Organism-specific databases

PharmGKBiPA33746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 2702695'-AMP-activated protein kinase subunit beta-1
PRO_0000204363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei4 – 41Phosphothreonine1 Publication
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei19 – 191Phosphothreonine2 Publications
Modified residuei24 – 241Phosphoserine; by autocatalysis By similarity
Modified residuei25 – 251Phosphoserine; by autocatalysis By similarity
Modified residuei40 – 401Phosphoserine3 Publications
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei101 – 1011Phosphoserine By similarity
Modified residuei108 – 1081Phosphoserine7 Publications
Modified residuei148 – 1481Phosphothreonine1 Publication
Modified residuei182 – 1821Phosphoserine By similarity

Post-translational modificationi

Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ9Y478.
PaxDbiQ9Y478.
PRIDEiQ9Y478.

PTM databases

PhosphoSiteiQ9Y478.

Expressioni

Gene expression databases

ArrayExpressiQ9Y478.
BgeeiQ9Y478.
CleanExiHS_PRKAB1.
GenevestigatoriQ9Y478.

Organism-specific databases

HPAiCAB005058.
HPA004247.

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
CideaO703024EBI-719769,EBI-7927848From a different organism.
GRB2P629932EBI-719769,EBI-401755
PRKAA1Q131315EBI-719769,EBI-1181405
PRKAG1P546194EBI-719769,EBI-1181439

Protein-protein interaction databases

BioGridi111551. 28 interactions.
IntActiQ9Y478. 16 interactions.
MINTiMINT-1400840.
STRINGi9606.ENSP00000229328.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 846
Beta strandi91 – 955
Turni96 – 1005
Beta strandi112 – 1176
Beta strandi120 – 12910
Beta strandi132 – 1343
Beta strandi141 – 1433
Beta strandi145 – 1473
Beta strandi149 – 1557
Helixi157 – 1604
Helixi162 – 17110
Helixi208 – 2114
Helixi214 – 2163
Beta strandi238 – 2414
Beta strandi248 – 25710
Beta strandi260 – 26910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CFEX-ray3.02B/D1-270[»]
4CFFX-ray3.92B/D1-270[»]
ProteinModelPortaliQ9Y478.
SMRiQ9Y478. Positions 77-270.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 16396Glycogen-binding domain By similarity
Add
BLAST

Domaini

The glycogen-binding domain may target AMPK to glycogen so that other factors like glycogen-bound debranching enzyme or protein phosphatases can directly affect AMPK activity By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238368.
HOGENOMiHOG000230597.
HOVERGENiHBG050430.
InParanoidiQ9Y478.
KOiK07199.
OMAiCKAEERF.
OrthoDBiEOG7SXW3Z.
PhylomeDBiQ9Y478.
TreeFamiTF313827.

Family and domain databases

InterProiIPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9Y478-1 [UniParc]FASTAAdd to Basket

« Hide

MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE    50
EIKAPEKEEF LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW 100
SKLPLTRSHN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN 150
NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYVCKPEERF 200
RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV 250
LSATHRYKKK YVTTLLYKPI 270
Length:270
Mass (Da):30,382
Last modified:January 23, 2007 - v4
Checksum:iF0BCAA94D5BC15FC
GO

Sequence cautioni

The sequence AAC98897.1 differs from that shown. Reason: Frameshift at position 245.
The sequence AAB71326.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → G in CAA73146. 1 Publication
Sequence conflicti10 – 101A → G in AAC98897. 1 Publication
Sequence conflicti15 – 151G → A in CAA12024. 1 Publication
Sequence conflicti20 – 201P → A in CAA73146. 1 Publication
Sequence conflicti20 – 201P → A in AAC98897. 1 Publication
Sequence conflicti22 – 221R → K in AAD09237. 1 Publication
Sequence conflicti22 – 221R → K in AAD00625. 1 Publication
Sequence conflicti56 – 561E → Y in AAD09237. 1 Publication
Sequence conflicti56 – 561E → Y in AAD00625. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ224515 mRNA. Translation: CAA12024.1.
Y12556 mRNA. Translation: CAA73146.1.
U83994 mRNA. Translation: AAD09237.1.
U87276
, U87271, U87272, U87273, U87274, U87275 Genomic DNA. Translation: AAD00625.1.
AF022116 mRNA. Translation: AAC98897.1. Frameshift.
AC002563 Genomic DNA. Translation: AAB71326.1. Sequence problems.
BC001007 mRNA. Translation: AAH01007.1.
BC001056 mRNA. Translation: AAH01056.1.
BC001823 mRNA. Translation: AAH01823.1.
BC017671 mRNA. Translation: AAH17671.1.
CCDSiCCDS9191.1.
PIRiT09514.
RefSeqiNP_006244.2. NM_006253.4.
XP_005253966.1. XM_005253909.1.
UniGeneiHs.741184.

Genome annotation databases

EnsembliENST00000229328; ENSP00000229328; ENSG00000111725.
ENST00000541640; ENSP00000441369; ENSG00000111725.
GeneIDi5564.
KEGGihsa:5564.
UCSCiuc001txg.3. human.

Polymorphism databases

DMDMi14194425.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ224515 mRNA. Translation: CAA12024.1 .
Y12556 mRNA. Translation: CAA73146.1 .
U83994 mRNA. Translation: AAD09237.1 .
U87276
, U87271 , U87272 , U87273 , U87274 , U87275 Genomic DNA. Translation: AAD00625.1 .
AF022116 mRNA. Translation: AAC98897.1 . Frameshift.
AC002563 Genomic DNA. Translation: AAB71326.1 . Sequence problems.
BC001007 mRNA. Translation: AAH01007.1 .
BC001056 mRNA. Translation: AAH01056.1 .
BC001823 mRNA. Translation: AAH01823.1 .
BC017671 mRNA. Translation: AAH17671.1 .
CCDSi CCDS9191.1.
PIRi T09514.
RefSeqi NP_006244.2. NM_006253.4.
XP_005253966.1. XM_005253909.1.
UniGenei Hs.741184.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CFE X-ray 3.02 B/D 1-270 [» ]
4CFF X-ray 3.92 B/D 1-270 [» ]
ProteinModelPortali Q9Y478.
SMRi Q9Y478. Positions 77-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111551. 28 interactions.
IntActi Q9Y478. 16 interactions.
MINTi MINT-1400840.
STRINGi 9606.ENSP00000229328.

Chemistry

BindingDBi Q9Y478.
ChEMBLi CHEMBL2111345.
DrugBanki DB00131. Adenosine monophosphate.
DB00331. Metformin.

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.

PTM databases

PhosphoSitei Q9Y478.

Polymorphism databases

DMDMi 14194425.

Proteomic databases

MaxQBi Q9Y478.
PaxDbi Q9Y478.
PRIDEi Q9Y478.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229328 ; ENSP00000229328 ; ENSG00000111725 .
ENST00000541640 ; ENSP00000441369 ; ENSG00000111725 .
GeneIDi 5564.
KEGGi hsa:5564.
UCSCi uc001txg.3. human.

Organism-specific databases

CTDi 5564.
GeneCardsi GC12P120105.
HGNCi HGNC:9378. PRKAB1.
HPAi CAB005058.
HPA004247.
MIMi 602740. gene.
neXtProti NX_Q9Y478.
PharmGKBi PA33746.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238368.
HOGENOMi HOG000230597.
HOVERGENi HBG050430.
InParanoidi Q9Y478.
KOi K07199.
OMAi CKAEERF.
OrthoDBi EOG7SXW3Z.
PhylomeDBi Q9Y478.
TreeFami TF313827.

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 Q9Y478.

Miscellaneous databases

GeneWikii PRKAB1.
GenomeRNAii 5564.
NextBioi 21556.
PROi Q9Y478.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y478.
Bgeei Q9Y478.
CleanExi HS_PRKAB1.
Genevestigatori Q9Y478.

Family and domain databases

InterProi IPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF04739. AMPKBI. 1 hit.
[Graphical view ]
SMARTi SM01010. AMPKBI. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Non-catalytic beta and gamma subunits isoforms of the AMP-activated protein kinase."
    Carling D.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location."
    Stapleton D., Woollatt E., Mitchelhill K., Nicholl J.K., Fernandez C.S., Michell B.J., Witters L.A., Power D.A., Sutherland G.R., Kemp B.E.
    FEBS Lett. 409:452-456(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
    Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. "Cloning and expression of the complete mRNA coding human AMP-activated protein kinase."
    Wang X., Yu L., Tu Q.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "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].
  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].
    Tissue: Lung and Muscle.
  7. Cited for: INTERACTION WITH FNIP1.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-5; SER-6 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40; SER-108 AND THR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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 PRKAG1, MUTAGENESIS OF GLY-2, MYRISTOYLATION AT GLY-2.
  19. "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.
  20. "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 nameiAAKB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y478
Secondary accession number(s): Q9UBV0
, Q9UE20, Q9UEX2, Q9Y6V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 141 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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