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Reviewed, UniProtKB/Swiss-Prot Q9Y478 (AAKB1_HUMAN)

Last modified June 16, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    5'-AMP-activated protein kinase subunit beta-1
      Short name=AMPK beta-1 chain
      Short name=AMPKb
Gene names
Name: PRKAB1
Synonyms: AMPK
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. Also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase and hormone-sensitive lipase. This is a regulatory subunit, may be a positive regulator of AMPK activity. It may also serve as an adaptor molecule for the catalytic alpha-subunit.

Subunit structure

Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic regulatory subunits. Interacts with FNIP1 and FNIP2. Ref.7 Ref.8

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

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

Sequence caution

The sequence AAB71326.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC98897.1 differs from that shown. Reason: Frameshift at position 245.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 2702695'-AMP-activated protein kinase subunit beta-1
PRO_0000204363

Amino acid modifications

Modified residue41Phosphothreonine Ref.9
Modified residue51Phosphoserine Ref.9
Modified residue61Phosphoserine Ref.9
Modified residue191Phosphothreonine Ref.10
Modified residue241Phosphoserine; by autocatalysis By similarity
Modified residue251Phosphoserine; by autocatalysis By similarity
Modified residue401Phosphoserine Ref.10
Modified residue961Phosphoserine By similarity
Modified residue1011Phosphoserine By similarity
Modified residue1081Phosphoserine; by autocatalysis By similarity
Modified residue1821Phosphoserine By similarity
Lipidation21N-myristoyl glycine By similarity

Experimental info

Sequence conflict101A → G Ref.2
Sequence conflict101A → G Ref.4
Sequence conflict151G → A in CAA12024. Ref.1
Sequence conflict201P → A Ref.2
Sequence conflict201P → A Ref.4
Sequence conflict221R → K in AAD09237. Ref.3
Sequence conflict221R → K in AAD00625. Ref.3
Sequence conflict561E → Y in AAD09237. Ref.3
Sequence conflict561E → Y in AAD00625. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9Y478-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F0BCAA94D5BC15FC

FASTA27030,382
        10         20         30         40         50         60 
MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE EIKAPEKEEF 

        70         80         90        100        110        120 
LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSHN NFVAILDLPE 

       130        140        150        160        170        180 
GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS 

       190        200        210        220        230        240 
SSPPGPYHQE PYVCKPEERF RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY 

       250        260        270 
ALSIKDGVMV LSATHRYKKK YVTTLLYKPI 

« Hide

References

« Hide 'large scale' references
[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: 9224708] [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. 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: 16541075] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Muscle.
[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: 17028174] [Abstract]
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: 18403135] [Abstract]
Cited for: INTERACTION WITH FNIP2.
[9]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-5; SER-6 AND SER-108, MASS SPECTROMETRY.
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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND SER-108, MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ224515 mRNA. Translation: CAA12024.1.
Y12556 mRNA. Translation: CAA73146.1.
U83994 mRNA. Translation: AAD09237.1.
U87276 expand/collapse EMBL AC list , 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.
IPIIPI00220409.
PIRT09514.
RefSeqNP_006244.2.
UniGeneHs.6061

3D structure databases

SMRQ9Y478. Positions 77-163.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y478. 166 interactions.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.

PTM databases

PhosphoSiteQ9Y478.

Proteomic databases

PRIDEQ9Y478.

Genome annotation databases

EnsemblENSG00000111725. Homo sapiens. [Contig view]
GeneID5564.
KEGGhsa:5564.

Organism-specific databases

GeneCardsGC12P118568.
H-InvDBHIX0011054.
HGNCHGNC:9378. PRKAB1.
HPACAB005058.
HPA004247.
MIM602740. gene.
PharmGKBPA33746.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9Y478.
HOVERGENQ9Y478.
OMAQ9Y478. YHQEPYI.

Enzyme and pathway databases

Pathway_Interaction_DBmtor_4pathway. mTOR signaling pathway.

Gene expression databases

ArrayExpressQ9Y478.
BgeeQ9Y478.
CleanExHS_PRKAB1.
GermOnlineENSG00000111725. Homo sapiens.

Family and domain databases

InterProIPR006828. AMPKBI.
[Graphical view]
PfamPF04739. AMPKBI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.
DB00331. Metformin.
NextBio21556.
SOURCESearch...

Entry information

Entry nameAAKB1_HUMAN
AccessionPrimary (citable) accession number: Q9Y478
Secondary accession number(s): Q9UBV0 expand/collapse secondary AC list , Q9UE20, Q9UEX2, Q9Y6V8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 82 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 12

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents