Reviewed,
UniProtKB/Swiss-Prot Q5RDH5 (AAPK1_PONAB)
Last modified
February 9, 2010.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 5'-AMP-activated protein kinase catalytic subunit alpha-1 Short name=AMPK subunit alpha-1 EC=2.7.11.1 | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 554 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cholesterol biosynthesis Fatty acid biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylationInferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 554 | ›554 | 5'-AMP-activated protein kinase catalytic subunit alpha-1 | PRO_0000085592 | |||||
Regions | |||||||||
| Domain | 22 – 274 | 253 | Protein kinase | ||||||
| Nucleotide binding | 28 – 36 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 145 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 51 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 27 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 178 | 1 | Phosphothreonine; by STK11 By similarity | ||||||
| Modified residue | 179 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 182 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 264 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 350 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 351 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 377 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 392 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 436 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 437 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 462 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 471 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 481 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 483 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 485 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 491 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 497 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 501 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 503 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 511 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 515 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 517 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 518 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 519 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 522 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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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. |
| RefSeq | NP_001127249.1. |
| UniGene | Pab.8607 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100174304. |
Organism-specific databases | |
| CTD | 100174304. |
Phylogenomic databases | |
| HOVERGEN | Q5RDH5. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.1. 269192. |
Family and domain databases | |
| InterPro | IPR020636. 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] |
| PANTHER | PTHR22982:SF61. AMPK. 1 hit. PTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit. |
| Pfam | PF00069. Pkinase. 1 hit. [Graphical view] |
| SMART | SM00220. S_TKc. 1 hit. [Graphical view] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AAPK1_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RDH5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


