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Reviewed, UniProtKB/Swiss-Prot Q5RDH5 (AAPK1_PONAB)

Last modified February 9, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length554 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-178 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 By similarity.

Subunit structure

Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2 By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 554›5545'-AMP-activated protein kinase catalytic subunit alpha-1
PRO_0000085592

Regions

Domain22 – 274253Protein kinase
Nucleotide binding28 – 369ATP By similarity

Sites

Active site1451Proton acceptor By similarity
Binding site511ATP By similarity

Amino acid modifications

Modified residue271Phosphothreonine By similarity
Modified residue1781Phosphothreonine; by STK11 By similarity
Modified residue1791Phosphoserine By similarity
Modified residue1821Phosphoserine By similarity
Modified residue2641Phosphothreonine By similarity
Modified residue3501Phosphothreonine By similarity
Modified residue3511Phosphoserine By similarity
Modified residue3771Phosphothreonine By similarity
Modified residue3921Phosphoserine By similarity
Modified residue4361Phosphotyrosine By similarity
Modified residue4371Phosphotyrosine By similarity
Modified residue4621Phosphoserine By similarity
Modified residue4711Phosphoserine By similarity
Modified residue4811Phosphoserine By similarity
Modified residue4831Phosphothreonine By similarity
Modified residue4851Phosphothreonine By similarity
Modified residue4911Phosphoserine By similarity
Modified residue4971Phosphoserine By similarity
Modified residue5011Phosphoserine By similarity
Modified residue5031Phosphoserine By similarity
Modified residue5111Phosphoserine By similarity
Modified residue5151Phosphoserine By similarity
Modified residue5171Phosphothreonine By similarity
Modified residue5181Phosphoserine By similarity
Modified residue5191Phosphoserine By similarity
Modified residue5221Phosphoserine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q5RDH5-1 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: D33AA742EA2FAEE7

FASTA55463,393
        10         20         30         40         50         60 
SWRKMATAEK QKHDGRVRIG HYILGDTLGV GTFGKVKVGK HELTGHKVAV KILNRQKIRS 

        70         80         90        100        110        120 
LDVVGKIRRE IQNLKLFRHP HIIKLYQVIS TPSDIFMVME YVSGGELFDY ICKNGRLDEK 

       130        140        150        160        170        180 
ESRRLFQQIL SGVDYCHRHM VVHRDLKPEN VLLDAHMNAK IADFGLSNMM SDGEFLRTSC 

       190        200        210        220        230        240 
GSPNYAAPEV ISGRLYAGPE VDIWSSGVIL YALLCGTLPF DDDHVPTLFK KICDGIFYTP 

       250        260        270        280        290        300 
QYLNPSVISL LKHMLQVDPM KRATIKDIRE HEWFKQDLPK YLFPEDPSYS STMIDDEALK 

       310        320        330        340        350        360 
EVCEKFECSE EEVLSCLYNR NHQDPLAVAY HLIIDNRRIM NEAKDFYLAT SPPDSFLDDH 

       370        380        390        400        410        420 
HLTRPHPERV PFLVAETPRA RHTLDELNPQ KSKHQGVRKA KWHLGIRSQS RPNDIMAEVC 

       430        440        450        460        470        480 
RAIKQLDYEW KVVNPYYLRV RRKNPVTSTY SKMSLQLYQV DSRTYLLDFR SIDDEITEAK 

       490        500        510        520        530        540 
SGTATPQRSG SVSNYRSCQR SDSDAEAQGK SSEVSLTSSV TSLDSSPVDL TPRPGSHTIE 

       550 
FFEMCANLIK ILAQ 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857935 mRNA. Translation: CAH90182.1. Different initiation.
RefSeqNP_001127249.1.
UniGenePab.8607

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID100174304.

Organism-specific databases

CTD100174304.

Phylogenomic databases

HOVERGENQ5RDH5.

Enzyme and pathway databases

BRENDA2.7.11.1. 269192.

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...

Entry information

Entry nameAAPK1_PONAB
AccessionPrimary (citable) accession number: Q5RDH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 28, 2009
Last modified: February 9, 2010
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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