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Reviewed, UniProtKB/Swiss-Prot Q13131 (AAPK1_HUMAN)

Last modified February 9, 2010. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    5'-AMP-activated protein kinase catalytic subunit alpha-1
      Short name=AMPK subunit alpha-1
    EC=2.7.11.1
Gene names
Name: PRKAA1
Synonyms: AMPK1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit. Ref.8 Ref.9

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-183 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. Ref.8 Ref.9

Subunit structure

Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2. Ref.14 Ref.15

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAH48980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCholesterol biosynthesis
Fatty acid biosynthesis
Lipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processactivation of MAPK activity

Non-traceable author statement. Source: UniProtKB

cholesterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of glucosylceramide biosynthetic process

Non-traceable author statement. Source: UniProtKB

positive regulation of anti-apoptosis

Non-traceable author statement. Source: UniProtKB

positive regulation of cholesterol biosynthetic process Ref.7

Non-traceable author statement. Source: UniProtKB

regulation of fatty acid oxidation

Inferred from Experiment. Source: Reactome

response to hypoxia Ref.7

Non-traceable author statement. Source: UniProtKB

   Cellular componentintracellular Ref.7

Inferred by curator. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase activity Ref.7

Non-traceable author statement. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.15

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABI1Q8IZP01EBI-1181405,EBI-375446
CPEP168701EBI-1181405,EBI-711320
PpardP353961EBI-1181405,EBI-1809541From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13131-1)

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: Q13131-2)

The sequence of this isoform differs from the canonical sequence as follows:
     121-121: R → RKSDVPGVVKTGSTKE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5595595'-AMP-activated protein kinase catalytic subunit alpha-1
PRO_0000085589

Regions

Domain27 – 279253Protein kinase
Nucleotide binding33 – 419ATP By similarity

Sites

Active site1501Proton acceptor By similarity
Binding site561ATP By similarity

Amino acid modifications

Modified residue321Phosphothreonine
Modified residue1831Phosphothreonine; by STK11 By similarity
Modified residue1841Phosphoserine
Modified residue1871Phosphoserine
Modified residue2691Phosphothreonine By similarity
Modified residue3551Phosphothreonine
Modified residue3561Phosphoserine Ref.16 Ref.17
Modified residue3821Phosphothreonine Ref.17 Ref.13 Ref.20
Modified residue3971Phosphoserine
Modified residue4411Phosphotyrosine
Modified residue4421Phosphotyrosine Ref.11
Modified residue4671Phosphoserine
Modified residue4761Phosphoserine
Modified residue4861Phosphoserine Ref.16 Ref.17
Modified residue4881Phosphothreonine
Modified residue4901Phosphothreonine Ref.16 Ref.17 Ref.20
Modified residue4961Phosphoserine Ref.16 Ref.17 Ref.10 Ref.12
Modified residue5021Phosphoserine
Modified residue5061Phosphoserine
Modified residue5081Phosphoserine Ref.16
Modified residue5161Phosphoserine
Modified residue5201Phosphoserine
Modified residue5221Phosphothreonine
Modified residue5231Phosphoserine Ref.16
Modified residue5241Phosphoserine
Modified residue5271Phosphoserine Ref.16

Natural variations

Alternative sequence1211R → RKSDVPGVVKTGSTKE in isoform 2.
VSP_035431
Natural variant101M → L: dbSNP rs17855679. Ref.2
VAR_058401
Natural variant161Q → R in a breast cancer sample; somatic mutation. Ref.21
VAR_035622

Experimental info

Sequence conflict51S → C in BAG35788. Ref.4
Sequence conflict91K → S in AAD43027. Ref.5
Sequence conflict371T → A in AAA64850. Ref.6
Sequence conflict2021A → V in AAA64850. Ref.6
Sequence conflict2081I → L in AAA64850. Ref.6
Sequence conflict2691T → S in BAA36547. Ref.3

Sequences

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

Last modified July 28, 2009. Version 4.
Checksum: ABAE71FBF912947A

FASTA55964,009
        10         20         30         40         50         60 
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR 

        70         80         90        100        110        120 
QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG 

       130        140        150        160        170        180 
RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF 

       190        200        210        220        230        240 
LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG 

       250        260        270        280        290        300 
IFYTPQYLNP SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID 

       310        320        330        340        350        360 
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS 

       370        380        390        400        410        420 
FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI 

       430        440        450        460        470        480 
MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTYSKMSL QLYQVDSRTY LLDFRSIDDE 

       490        500        510        520        530        540 
ITEAKSGTAT PQRSGSVSNY RSCQRSDSDA EAQGKSSEVS LTSSVTSLDS SPVDLTPRPG 

       550 
SHTIEFFEMC ANLIKILAQ 

« Hide

Isoform 2.

Checksum: 8EA8B85393F48DAA
Show »

FASTA57465,523

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed: 15372022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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] (ISOFORMS 1 AND 2), VARIANT LEU-10.
Tissue: Brain and Testis.
[3]"Nucleotide sequence of cDNA for human AMP-activated protein kinase alpha-1."
Yano K.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-559 (ISOFORM 1).
Tissue: Mammary gland.
[4]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-559 (ISOFORM 1).
Tissue: Trachea.
[5]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-559 (ISOFORM 1).
Tissue: Umbilical cord blood.
[6]Taboada E.N., Hickey D.A.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-209 (ISOFORM 1).
Tissue: Intestine.
[7]"Mammalian AMP-activated protein kinase subfamily."
Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J., Teh T., House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E.
J. Biol. Chem. 271:611-614(1996) [PubMed: 8557660] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 303-559 (ISOFORMS 1/2).
Tissue: Liver.
[8]"LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
EMBO J. 23:833-843(2004) [PubMed: 14976552] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[9]"Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase."
Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M., Frenguelli B.G., Hardie D.G.
Cell Metab. 2:9-19(2005) [PubMed: 16054095] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[10]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, MASS SPECTROMETRY.
[11]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-442, MASS SPECTROMETRY.
[12]"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 SER-496, MASS SPECTROMETRY.
Tissue: Platelet.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, MASS SPECTROMETRY.
[14]"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.
[15]"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.
[16]"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 SER-356; SER-486; THR-490; SER-496; SER-508; SER-523 AND SER-527, MASS SPECTROMETRY.
[17]"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-356; THR-382; SER-486; THR-490 AND SER-496, MASS SPECTROMETRY.
[18]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; THR-183; SER-184; SER-187; THR-355; SER-356; SER-397; TYR-441; SER-467; SER-476; SER-486; THR-488; THR-490; SER-496; SER-502; SER-506; SER-508; SER-516; SER-520; THR-522; SER-523; SER-524 AND SER-527, MASS SPECTROMETRY.
[20]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382 AND THR-490, MASS SPECTROMETRY.
Tissue: T-cell.
[21]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC008810 Genomic DNA. No translation available.
BC048980 mRNA. Translation: AAH48980.1.
AB022017 mRNA. Translation: BAA36547.1. Different initiation.
AK312947 mRNA. Translation: BAG35788.1. Different initiation.
BC037303 mRNA. Translation: AAH37303.1. Different initiation.
AF100763 mRNA. Translation: AAD43027.1. Different initiation.
U22456 mRNA. Translation: AAA64850.1. Different initiation.
Y12856 mRNA. Translation: CAA73361.1. Different initiation.
IPIIPI00410287.
IPI00792482.
PIRG01743.
RefSeqNP_006242.5.
NP_996790.3.
UniGeneHs.43322

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-39973N.
IntActQ13131. 46 interactions.
STRINGQ13131.

PTM databases

PhosphoSiteQ13131.

Proteomic databases

PRIDEQ13131.

Genome annotation databases

EnsemblENST00000397128; ENSP00000380317; ENSG00000132356; Homo sapiens. [Genome view]
GeneID5562.
KEGGhsa:5562.

Organism-specific databases

CTD5562.
GeneCardsGC05M040795.
H-InvDBHIX0004832.
HGNCHGNC:9376. PRKAA1.
HPACAB005050.
MIM602739. gene.
PharmGKBPA33744.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16386.
HOVERGENQ13131.
OMAQGVRRAK.
OrthoDBEOG90ZTGR.
PhylomeDBQ13131.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.
ReactomeREACT_1505. Integration of energy metabolism.

Gene expression databases

ArrayExpressQ13131.
BgeeQ13131.
CleanExHS_PRKAA1.
GenevestigatorQ13131.
GermOnlineENSG00000132356. Homo sapiens.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_prot_kinase-like.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR015741. Prot_kinase_Snf1-like_AMPK.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PANTHERPTHR22982:SF61. AMPK. 1 hit.
PTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.
DB00914. Phenformin.
SOURCESearch...

Entry information

Entry nameAAPK1_HUMAN
AccessionPrimary (citable) accession number: Q13131
Secondary accession number(s): A8MTQ6 expand/collapse secondary AC list , B2R7E1, O00286, Q5D0E1, Q86VS1, Q9UNQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 28, 2009
Last modified: February 9, 2010
This is version 108 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

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