5'-AMP-activated protein kinase catalytic subunit alpha-2

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Q95ZQ4 (AAPK2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
5'-AMP-activated protein kinase catalytic subunit alpha-2
Short name=AMPK subunit alpha-2
EC=2.7.11.1

Gene names

Name:	aak-2
ORF Names:	T01C8.1

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a sensor that couples lifespan to information about energy levels and insulin-like signals. Role in motility and response to oxidative stress. Causes germ cell cycle arrest upon dauer entry. Ref.1 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by phosphorylation. Ref.1
Subunit structure	Tetramer, composed of 2 regulatory (R) and 2 catalytic (C) subunits. In the presence of cAMP it dissociates into 2 active monomeric C subunits and an R dimer that binds four cAMP molecules.
Tissue specificity	Expressed in the pharynx, the ventral cord, neurons including the hermaphrodite-specific neuron, body wall muscles, the vulva, the excretory canal, and weakly in the intestine. Ref.6
Post-translational modification	Phosphorylated on Thr-243 in response to oxidative stress. Ref.1
Disruption phenotype	Shortened life-span. Temperature-dependent hypersensitivity to stress, slow body bending, abnormal modulation of head oscillation. Ref.1 Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Stress response
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	determination of adult lifespan Inferred from mutant phenotype Ref.1. Source: WormBase germline cell cycle switching, mitotic to meiotic cell cycle Inferred from mutant phenotype. Source: WormBase response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	axon Inferred from direct assay Ref.6. Source: WormBase cytoplasm Inferred from direct assay Ref.6. Source: WormBase neuronal cell body Inferred from direct assay Ref.6. Source: WormBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aakb-2	Q9NAH7	4	EBI-326514,EBI-2417663

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform b Ref.4 (identifier: Q95ZQ4-1) 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.
Note: No experimental confirmation available.

Isoform a Ref.1 (identifier: Q95ZQ4-2) The sequence of this isoform differs from the canonical sequence as follows: 370-371: Missing.

Isoform c Ref.4 (identifier: Q95ZQ4-3) The sequence of this isoform differs from the canonical sequence as follows: 1-62: Missing. 370-371: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 626

626

5'-AMP-activated protein kinase catalytic subunit alpha-2

PRO_0000085599

Regions

Domain

87 – 339

253

Protein kinase

Nucleotide binding

93 – 101

ATP By similarity

Sites

Active site

210

Proton acceptor By similarity

Binding site

116

ATP By similarity

Amino acid modifications

Modified residue

243

Phosphothreonine; by par-4 Ref.1

Natural variations

Alternative sequence

1 – 62

Missing in isoform c. Ref.4

VSP_051940

Alternative sequence

370 – 371

Missing in isoform a and isoform c. Ref.1 Ref.4

VSP_051941

Sequences

Sequence		Length	Mass (Da)
Isoform b [UniParc]. Last modified October 1, 2002. Version 2. Checksum: D1401DB1286D8624 Show »	FASTA	626	70,443
10 20 30 40 50 60 MFSHQDRDRD RKEDGGGDGT EMKSKSRSQP SGLNRVKNLS RKLSAKSRKE RKDRDSTDNS 70 80 90 100 110 120 SKMSSPGGET STKQQQELKA QIKIGHYILK ETLGVGTFGK VKVGIHETTQ YKVAVKILNR 130 140 150 160 170 180 QKIKSLDVVG KIRREIQNLS LFRHPHIIRL YQVISTPSDI FMIMEHVSGG ELFDYIVKHG 190 200 210 220 230 240 RLKTAEARRF FQQIISGVDY CHRHMVVHRD LKPENLLLDE QNNVKIADFG LSNIMTDGDF 250 260 270 280 290 300 LRTSCGSPNY AAPEVISGKL YAGPEVDVWS CGVILYALLC GTLPFDDEHV PSLFRKIKSG 310 320 330 340 350 360 VFPTPDFLER PIVNLLHHML CVDPMKRATI KDVIAHEWFQ KDLPNYLFPP INESEASIVD 370 380 390 400 410 420 IEAVREVTEF QRYHVAEEEV TSALLGDDPH HHLSIAYNLI VDNKRIADET AKLSIEEFYQ 430 440 450 460 470 480 VTPNKGPGPV HRHPERIAAS VSSKITPTLD NTEASGANRN KRAKWHLGIR SQSRPEDIMF 490 500 510 520 530 540 EVFRAMKQLD MEWKVLNPYH VIVRRKPDAP AADPPKMSLQ LYQVDQRSYL LDFKSLADEE 550 560 570 580 590 600 SGSASASSSR HASMSMPQKP AGIRGTRTSS MPQAMSMEAS IEKMEVHDFS DMSCDVTPPP 610 620 SPGGAKLSQT MQFFEICAAL IGTLAR « Hide
Isoform a [UniParc]. Checksum: 3BF9F9610BA95DB7 Show »	FASTA	624	70,168
10 20 30 40 50 60 MFSHQDRDRD RKEDGGGDGT EMKSKSRSQP SGLNRVKNLS RKLSAKSRKE RKDRDSTDNS 70 80 90 100 110 120 SKMSSPGGET STKQQQELKA QIKIGHYILK ETLGVGTFGK VKVGIHETTQ YKVAVKILNR 130 140 150 160 170 180 QKIKSLDVVG KIRREIQNLS LFRHPHIIRL YQVISTPSDI FMIMEHVSGG ELFDYIVKHG 190 200 210 220 230 240 RLKTAEARRF FQQIISGVDY CHRHMVVHRD LKPENLLLDE QNNVKIADFG LSNIMTDGDF 250 260 270 280 290 300 LRTSCGSPNY AAPEVISGKL YAGPEVDVWS CGVILYALLC GTLPFDDEHV PSLFRKIKSG 310 320 330 340 350 360 VFPTPDFLER PIVNLLHHML CVDPMKRATI KDVIAHEWFQ KDLPNYLFPP INESEASIVD 370 380 390 400 410 420 IEAVREVTER YHVAEEEVTS ALLGDDPHHH LSIAYNLIVD NKRIADETAK LSIEEFYQVT 430 440 450 460 470 480 PNKGPGPVHR HPERIAASVS SKITPTLDNT EASGANRNKR AKWHLGIRSQ SRPEDIMFEV 490 500 510 520 530 540 FRAMKQLDME WKVLNPYHVI VRRKPDAPAA DPPKMSLQLY QVDQRSYLLD FKSLADEESG 550 560 570 580 590 600 SASASSSRHA SMSMPQKPAG IRGTRTSSMP QAMSMEASIE KMEVHDFSDM SCDVTPPPSP 610 620 GGAKLSQTMQ FFEICAALIG TLAR « Hide
Isoform c [UniParc]. Checksum: AA34A96C5BBCAFBD Show »	FASTA	562	63,103
10 20 30 40 50 60 MSSPGGETST KQQQELKAQI KIGHYILKET LGVGTFGKVK VGIHETTQYK VAVKILNRQK 70 80 90 100 110 120 IKSLDVVGKI RREIQNLSLF RHPHIIRLYQ VISTPSDIFM IMEHVSGGEL FDYIVKHGRL 130 140 150 160 170 180 KTAEARRFFQ QIISGVDYCH RHMVVHRDLK PENLLLDEQN NVKIADFGLS NIMTDGDFLR 190 200 210 220 230 240 TSCGSPNYAA PEVISGKLYA GPEVDVWSCG VILYALLCGT LPFDDEHVPS LFRKIKSGVF 250 260 270 280 290 300 PTPDFLERPI VNLLHHMLCV DPMKRATIKD VIAHEWFQKD LPNYLFPPIN ESEASIVDIE 310 320 330 340 350 360 AVREVTERYH VAEEEVTSAL LGDDPHHHLS IAYNLIVDNK RIADETAKLS IEEFYQVTPN 370 380 390 400 410 420 KGPGPVHRHP ERIAASVSSK ITPTLDNTEA SGANRNKRAK WHLGIRSQSR PEDIMFEVFR 430 440 450 460 470 480 AMKQLDMEWK VLNPYHVIVR RKPDAPAADP PKMSLQLYQV DQRSYLLDFK SLADEESGSA 490 500 510 520 530 540 SASSSRHASM SMPQKPAGIR GTRTSSMPQA MSMEASIEKM EVHDFSDMSC DVTPPPSPGG 550 560 AKLSQTMQFF EICAALIGTL AR « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans." Apfeld J., O'Connor G., McDonagh T., DiStefano P.S., Curtis R. Genes Dev. 18:3004-3009(2004) [PubMed: 15574588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-243.
[2]	Erratum Apfeld J., O'Connor G., McDonagh T., DiStefano P.S., Curtis R. Genes Dev. 19:188-188(2005)
[3]	Erratum Apfeld J., O'Connor G., McDonagh T., DiStefano P.S., Curtis R. Genes Dev. 19:411-411(2005)
[4]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[5]	"Cloning, structure, and expression of the gene for a novel regulatory subunit of cAMP-dependent protein kinase in Caenorhabditis elegans." Lu X., Gross R.E., Bagchi S., Rubin C.S. J. Biol. Chem. 265:3293-3303(1990) [PubMed: 2303451] [Abstract] Cited for: IDENTIFICATION IN AMPK COMPLEX.
[6]	"The Caenorhabditis elegans AMP-activated protein kinase AAK-2 is phosphorylated by LKB1 and is required for resistance to oxidative stress and for normal motility and foraging behavior." Lee H., Cho J.S., Lambacher N., Lee J., Lee S.J., Lee T.H., Gartner A., Koo H.S. J. Biol. Chem. 283:14988-14993(2008) [PubMed: 18408008] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY347273 mRNA. Translation: AAR06928.1. FO081053 Genomic DNA. Translation: CCD68833.1. FO081053 Genomic DNA. Translation: CCD68834.1. FO081053 Genomic DNA. Translation: CCD68835.1.
PIR	T29858.
RefSeq	NP_001024868.1. NM_001029697.2. NP_510710.2. NM_078309.3. NP_510711.2. NM_078310.4.
UniGene	Cel.17479.
3D structure databases
ProteinModelPortal	Q95ZQ4.
SMR	Q95ZQ4. Positions 80-626.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-25170N.
IntAct	Q95ZQ4. 7 interactions.
MINT	MINT-1049339.
STRING	Q95ZQ4.
Proteomic databases
PRIDE	Q95ZQ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	T01C8.1b; T01C8.1b; T01C8.1.
GeneID	181727.
KEGG	cel:T01C8.1.
UCSC	T01C8.1c.1. c. elegans.
Organism-specific databases
CTD	181727.
WormBase	T01C8.1a; CE31222; WBGene00020142; aak-2. T01C8.1b; CE31223; WBGene00020142; aak-2. T01C8.1c; CE07458; WBGene00020142; aak-2.
Phylogenomic databases
eggNOG	meNOG05149.
GeneTree	EMGT00050000001128.
HOGENOM	HBG755340.
InParanoid	Q95ZQ4.
OMA	YICKNGK.
PhylomeDB	Q95ZQ4.
Gene expression databases
ArrayExpress	Q95ZQ4.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K07198.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	915106.

Entry information

Entry name

AAPK2_CAEEL

Accession

Primary (citable) accession number: Q95ZQ4
Secondary accession number(s): Q22068, Q86FL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	October 1, 2002
Last modified:	December 14, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents