Reviewed, UniProtKB/Swiss-Prot Q9Y478 (AAKB1_HUMAN)

Names and origin

Protein names

Recommended name:
    5'-AMP-activated protein kinase subunit beta-1
      Short name=AMPK beta-1 chain
      Short name=AMPKb

Gene names

Name:	PRKAB1
Synonyms:	AMPK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
PTM	Lipoprotein Myristate Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	protein binding Ref.8 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACLY	P53396	1	EBI-719769,EBI-1042794
DHX36	Q9H2U1	1	EBI-719769,EBI-1047643
EZR	P15311	1	EBI-719769,EBI-1056902
GRB2	P62993	1	EBI-719769,EBI-401755
GYS1	P13807	1	EBI-719769,EBI-963094
MARS	P56192	1	EBI-719769,EBI-355848
MYH10	P35580	1	EBI-719769,EBI-351758
PRKAB2	O43741	1	EBI-719769,EBI-1053424
SNRNP200	O75643	1	EBI-719769,EBI-1045395

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 270	269	5'-AMP-activated protein kinase subunit beta-1		PRO_0000204363
Amino acid modifications
	Modified residue	4	1	Phosphothreonine Ref.9
	Modified residue	5	1	Phosphoserine Ref.9
	Modified residue	6	1	Phosphoserine Ref.9
	Modified residue	19	1	Phosphothreonine Ref.10
	Modified residue	24	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	25	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	40	1	Phosphoserine Ref.10
	Modified residue	96	1	Phosphoserine By similarity
	Modified residue	101	1	Phosphoserine By similarity
	Modified residue	108	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	182	1	Phosphoserine By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
Experimental info
	Sequence conflict	10	1	A → G Ref.2
	Sequence conflict	10	1	A → G Ref.4
	Sequence conflict	15	1	G → A in CAA12024. Ref.1
	Sequence conflict	20	1	P → A Ref.2
	Sequence conflict	20	1	P → A Ref.4
	Sequence conflict	22	1	R → K in AAD09237. Ref.3
	Sequence conflict	22	1	R → K in AAD00625. Ref.3
	Sequence conflict	56	1	E → Y in AAD09237. Ref.3
	Sequence conflict	56	1	E → Y in AAD00625. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y478-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: F0BCAA94D5BC15FC	FASTA	270	30,382
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00220409.
PIR	T09514.
RefSeq	NP_006244.2.
UniGene	Hs.6061
3D structure databases
SMR	Q9Y478. Positions 77-163.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y478. 166 interactions.
Protein family/group databases
CAZy	CBM48. Carbohydrate-Binding Module Family 48.
PTM databases
PhosphoSite	Q9Y478.
Proteomic databases
PRIDE	Q9Y478.
Genome annotation databases
Ensembl	ENSG00000111725. Homo sapiens. [Contig view]
GeneID	5564.
KEGG	hsa:5564.
Organism-specific databases
GeneCards	GC12P118568.
H-InvDB	HIX0011054.
HGNC	HGNC:9378. PRKAB1.
HPA	CAB005058. HPA004247.
MIM	602740. gene.
PharmGKB	PA33746.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9Y478.
HOVERGEN	Q9Y478.
OMA	Q9Y478. YHQEPYI.
Enzyme and pathway databases
Pathway_Interaction_DB	mtor_4pathway. mTOR signaling pathway.
Gene expression databases
ArrayExpress	Q9Y478.
Bgee	Q9Y478.
CleanEx	HS_PRKAB1.
GermOnline	ENSG00000111725. Homo sapiens.
Family and domain databases
InterPro	IPR006828. AMPKBI. [Graphical view]
Pfam	PF04739. AMPKBI. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00131. Adenosine monophosphate. DB00331. Metformin.
NextBio	21556.
SOURCE	Search...

Entry information

Entry name

AAKB1_HUMAN

Accession

Primary (citable) accession number: Q9Y478
Secondary accession number(s): Q9UBV0 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)