Tag | Content |
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EKPD ID | EKS-MUM-00254 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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CAMK/CAMKL | 337.9 | 8.0E-101 | 27 | 279 | 253 |
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Status | Reviewed |
Ensembl Protein | ENSMUSP00000063166 |
UniProt Accession | Q5EG47; |
Protein Name | 5'-AMP-activated protein kinase catalytic subunit alpha-1 |
Protein Synonyms/Alias | AMPK subunit alpha-1; Acetyl-CoA carboxylase kinase; ACACA kinase; Hydroxymethylglutaryl-CoA reductase kinase; HMGCR kinase; Tau-protein kinase PRKAA1; |
Gene Name | Prkaa1 |
Gene Synonyms/Alias | Prkaa1; |
Ensembl Information | |
Organism | Mus musculus |
Functional Description | Catalytic subunit of AMP-activated protein kinase(AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. |
Protein Length | 559 |
Protein Sequence (FASTA) | MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR 60 | QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG 120 | RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF 180 | LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG 240 | IFYTPQYLNP SVISLLKHML QVDPMKRAAI KDIREHEWFK QDLPKYLFPE DPSYSSTMID 300 | DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS 360 | FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI 420 | MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE 480 | ITEAKSGTAT PQRSGSISNY RSCQRSDSDA EAQGKPSDVS LTSSVTSLDS SPVDVAPRPG 540 | SHTIEFFEMC ANLIKILAQ 559 |
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Nucleotide Sequence (FASTA) | ATGCGCAGAC TCAGTTCCTG GAGAAAGATG GCGACGGCCG AGAAGCAGAA GCACGACGGG 60 | CGGGTGAAGA TCGGCCACTA CATCCTGGGG GACACGCTTG GTGTCGGCAC CTTCGGGAAA 120 | GTGAAGGTGG GCAAGCACGA GTTGACCGGA CATAAAGTGG CTGTGAAGAT ACTCAACCGG 180 | CAGAAGATTC GGAGCCTTGA CGTGGTGGGA AAAATCCGCC GGGAGATTCA GAACCTGAAG 240 | CTGTTCAGGC ACCCTCACAT CATCAAACTG TACCAGGTCA TCAGTACACC ATCTGATATT 300 | TTCATGGTGA TGGAATATGT CTCTGGAGGA GAGCTATTTG ATTATATCTG TAAAAATGGA 360 | AGGTTGGACG AAAAGGAAAG CCGCCGTCTG TTCCAGCAGA TCCTTTCCGG TGTGGATTAT 420 | TGTCACAGGC ATATGGTGGT CCACAGAGAT TTGAAACCTG AGAACGTCCT GCTTGATGCA 480 | CACATGAATG CAAAGATAGC CGACTTTGGT CTTTCAAACA TGATGTCAGA TGGTGAATTT 540 | TTAAGAACAA GCTGTGGCTC ACCCAATTAT GCCGCACCAG AAGTCATTTC AGGAAGATTG 600 | TACGCAGGCC CCGAGGTGGA CATCTGGAGC AGCGGGGTCA TTCTCTATGC TTTGCTGTGT 660 | GGAACCCTCC CTTTTGATGA TGACCATGTG CCAACTCTTT TTAAGAAGAT ATGTGATGGG 720 | ATCTTTTATA CCCCTCAGTA CTTAAACCCT TCAGTAATCA GCCTTTTGAA ACATATGCTG 780 | CAGGTGGATC CCATGAAGAG GGCCGCAATA AAAGATATCA GGGAACACGA GTGGTTTAAA 840 | CAGGACCTTC CGAAGTATCT CTTTCCTGAG GACCCATCTT ATAGTTCAAC CATGATCGAT 900 | GACGAAGCCT TGAAAGAAGT GTGTGAGAAG TTCGAGTGTT CGGAGGAGGA GGTCCTCAGC 960 | TGCCTGTACA ACAGAAACCA CCAGGACCCA CTAGCCGTCG CCTACCACCT CATCATAGAC 1020 | AACAGGAGAA TAATGAATGA AGCCAAAGAT TTCTACCTAG CAACCAGCCC ACCTGACTCT 1080 | TTCCTGGACG ACCACCATTT AACTCGGCCT CACCCTGAAA GAGTACCGTT CTTGGTTGCC 1140 | GAAACACCAC GGGCCCGGCA CACCCTGGAT GAATTAAACC CACAGAAATC CAAACACCAA 1200 | GGTGTACGGA AGGCAAAATG GCATTTGGGA ATTCGAAGTC AAAGCCGACC CAATGATATC 1260 | ATGGCAGAAG TTTGTAGAGC AATCAAGCAG TTGGATTATG AATGGAAGGT TGTAAACCCC 1320 | TATTATTTGC GTGTACGAAG GAAGAATCCT GTGACAAGCA CATTTTCCAA AATGAGTCTA 1380 | CAGCTATACC AAGTGGATAG TAGGACTTAC TTGTTGGATT TCCGTAGTAT TGATGATGAG 1440 | ATTACAGAAG CCAAATCAGG GACTGCTACT CCACAGAGAT CGGGATCCAT CAGCAACTAT 1500 | CGATCTTGCC AAAGGAGTGA CTCTGATGCC GAAGCTCAAG GAAAGCCCTC AGACGTCTCC 1560 | CTTACCTCAT CTGTCACCTC CCTCGACTCC TCCCCTGTCG ACGTAGCTCC AAGACCAGGA 1620 | AGTCATACAA TAGAATTTTT TGAAATGTGT GCAAATCTAA TTAAAATTCT TGCACAGTAA 1680 |
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Domain Profile | S: 1 ykllktlGegsfgkVklakhketkekvavKiikkkkl.seeslekikrEieilkklkhpn 59 | y l++tlG g+fgkVk+ kh++t++kvavKi++++k+ s + + ki+rEi+ lk ++hp+ | Q: 27 YILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIrSLDVVGKIRREIQNLKLFRHPH 86 | 8899********************************96667788**************** |
| S: 60 iikllevietkkklylvleyasggeLfdyieekgrlkekearklfkqlvsavkYlhskgi 119 | iikl++vi+t +++++v+ey+sggeLfdyi ++grl+eke+r+lf+q++s+v+Y+h++ + | Q: 87 IIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMV 146 | ************************************************************ |
| S: 120 vHrDlKpeNllldkkenikiaDFGlanlfkegklletfcGsppYaaPellkgkkYegpkv 179 | vHrDlKpeN+lld+++n kiaDFGl+n++++g+ l+t+cGsp+YaaPe+++g+ Y gp+v | Q: 147 VHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEV 206 | ************************************************************ |
| S: 180 DvWslGvvLyalvtgklPfdeenlkellekilkgkleipkklskelesLlrklLvvdpek 239 | D+Ws Gv+Lyal++g+lPfd++++ +l++ki +g + +p++l+++++sLl+++L+vdp k | Q: 207 DIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMK 266 | ************************************************************ |
| S: 240 Ratieeilkhewl 252 | Ra i++i++hew+ | Q: 267 RAAIKDIREHEWF 279 | ************7 |
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Domain Sequence (FASTA) | YILGDTLGVG TFGKVKVGKH ELTGHKVAVK ILNRQKIRSL DVVGKIRREI QNLKLFRHPH 60 | IIKLYQVIST PSDIFMVMEY VSGGELFDYI CKNGRLDEKE SRRLFQQILS GVDYCHRHMV 120 | VHRDLKPENV LLDAHMNAKI ADFGLSNMMS DGEFLRTSCG SPNYAAPEVI SGRLYAGPEV 180 | DIWSSGVILY ALLCGTLPFD DDHVPTLFKK ICDGIFYTPQ YLNPSVISLL KHMLQVDPMK 240 | RAAIKDIREH EWF 253 |
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Keyword | ATP-binding; Autophagy; Biological rhythms; Cholesterol biosynthesis; Cholesterol metabolism; Chromatin regulator; Complete proteome; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transcription; Transcription regulation; Transferase; Ubl conjugation; Wnt signaling pathway. |
Sequence Source | Ensembl |
Orthology | |
Gene Ontology | |
KEGG | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |