Tag | Content |
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EKPD ID | EKS-HOS-00265 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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CAMK/CAMKL | 251.0 | 5.6E-74 | 49 | 309 | 261 |
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Status | Reviewed |
Ensembl Protein | ENSP00000324856 |
UniProt Accession | Q15831; B2RBX7; E7EW76; |
Protein Name | Serine/threonine-protein kinase STK11 |
Protein Synonyms/Alias | Liver kinase B1; LKB1; hLKB1; Renal carcinoma antigen NY-REN-19; |
Gene Name | STK11 |
Gene Synonyms/Alias | STK11; LKB1, PJS; |
Ensembl Information | |
Organism | Homo sapiens |
Functional Description | Tumor suppressor serine/threonine-protein kinase thatcontrols the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, leading to promote their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2: it thereby regulates inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neurons polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1 Also acts as a mediator p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. |
Protein Length | 433 |
Protein Sequence (FASTA) | MEVVDPQQLG MFTEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY 60 | GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHKNV IQLVDVLYNE 120 | EKQKMYMVME YCVCGMQEML DSVPEKRFPV CQAHGYFCQL IDGLEYLHSQ GIVHKDIKPG 180 | NLLLTTGGTL KISDLGVAEA LHPFAADDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS 240 | AGVTLYNITT GLYPFEGDNI YKLFENIGKG SYAIPGDCGP PLSDLLKGML EYEPAKRFSI 300 | RQIRQHSWFR KKHPPAEAPV PIPPSPDTKD RWRSMTVVPY LEDLHGADED EDLFDIEDDI 360 | IYTQDFTVPG QVPEEEASHN GQRRGLPKAV CMNGTEAAQL STKSRAEGRA PNPARKACSA 420 | SSKIRRLSAC KQQ 433 |
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Nucleotide Sequence (FASTA) | ATGGAGGTGG TGGACCCGCA GCAGCTGGGC ATGTTCACGG AGGGCGAGCT GATGTCGGTG 60 | GGTATGGACA CGTTCATCCA CCGCATCGAC TCCACCGAGG TCATCTACCA GCCGCGCCGC 120 | AAGCGGGCCA AGCTCATCGG CAAGTACCTG ATGGGGGACC TGCTGGGGGA AGGCTCTTAC 180 | GGCAAGGTGA AGGAGGTGCT GGACTCGGAG ACGCTGTGCA GGAGGGCCGT CAAGATCCTC 240 | AAGAAGAAGA AGTTGCGAAG GATCCCCAAC GGGGAGGCCA ACGTGAAGAA GGAAATTCAA 300 | CTACTGAGGA GGTTACGGCA CAAAAATGTC ATCCAGCTGG TGGATGTGTT ATACAACGAA 360 | GAGAAGCAGA AAATGTATAT GGTGATGGAG TACTGCGTGT GTGGCATGCA GGAAATGCTG 420 | GACAGCGTGC CGGAGAAGCG TTTCCCAGTG TGCCAGGCCC ACGGGTACTT CTGTCAGCTG 480 | ATTGACGGCC TGGAGTACCT GCATAGCCAG GGCATTGTGC ACAAGGACAT CAAGCCGGGG 540 | AACCTGCTGC TCACCACCGG TGGCACCCTC AAAATCTCCG ACCTGGGCGT GGCCGAGGCA 600 | CTGCACCCGT TCGCGGCGGA CGACACCTGC CGGACCAGCC AGGGCTCCCC GGCTTTCCAG 660 | CCGCCCGAGA TTGCCAACGG CCTGGACACC TTCTCCGGCT TCAAGGTGGA CATCTGGTCG 720 | GCTGGGGTCA CCCTCTACAA CATCACCACG GGTCTGTACC CCTTCGAAGG GGACAACATC 780 | TACAAGTTGT TTGAGAACAT CGGGAAGGGG AGCTACGCCA TCCCGGGCGA CTGTGGCCCC 840 | CCGCTCTCTG ACCTGCTGAA AGGGATGCTT GAGTACGAAC CGGCCAAGAG GTTCTCCATC 900 | CGGCAGATCC GGCAGCACAG CTGGTTCCGG AAGAAACATC CTCCGGCTGA AGCACCAGTG 960 | CCCATCCCAC CGAGCCCAGA CACCAAGGAC CGGTGGCGCA GCATGACTGT GGTGCCGTAC 1020 | TTGGAGGACC TGCACGGCGC GGACGAGGAC GAGGACCTCT TCGACATCGA GGATGACATC 1080 | ATCTACACTC AGGACTTCAC GGTGCCCGGA CAGGTCCCAG AAGAGGAGGC CAGTCACAAT 1140 | GGACAGCGCC GGGGCCTCCC CAAGGCCGTG TGTATGAACG GCACAGAGGC GGCGCAGCTG 1200 | AGCACCAAAT CCAGGGCGGA GGGCCGGGCC CCCAACCCTG CCCGCAAGGC CTGCTCCGCC 1260 | AGCAGCAAGA TCCGCCGGCT GTCGGCCTGC AAGCAGCAGT GA 1302 |
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Domain Profile | S: 1 ykllktlGegsfgkVklakhketkekvavKiikkkkl..seeslekikrEieilkklkhp 58 | y +++ lGegs+gkVk++ ++et + avKi+kkkkl + ++k+Ei++l++l+h+ | Q: 49 YLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLrrIPNGEANVKKEIQLLRRLRHK 108 | 778999******************************965334567*************** |
| S: 59 niikllevi..etkkklylvleyasgg..eLfdyieekgrlkekearklfkqlvsavkYl 114 | n+i+l++v+ e+k+k+y+v+ey+ g e++d + ++r++ +a+ +f ql+++++Yl | Q: 109 NVIQLVDVLynEEKQKMYMVMEYCVCGmqEMLDSV-PEKRFPVCQAHGYFCQLIDGLEYL 167 | ********9888999********998888*****6.8899******************** |
| S: 115 hskgivHrDlKpeNllldkkenikiaDFGlan...lfkegklletfcGsppYaaPellkg 171 | hs+givH+D+Kp Nlll++ +++ki+D+G+a+ f +++++t++Gsp++++Pe+ +g | Q: 168 HSQGIVHKDIKPGNLLLTTGGTLKISDLGVAEalhPFAADDTCRTSQGSPAFQPPEIANG 227 | *******************************955556778******************99 |
| S: 172 .kkYegpkvDvWslGvvLyalvtgklPfdeenlkellekilkgkleipkklskelesLlr 230 | ++++g kvD+Ws+Gv+Ly++ tg +Pf+++n+ +l+e+i kg++ ip + + l++Ll+ | Q: 228 lDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLK 287 | 899********************************************************* |
| S: 231 klLvvdpekRatieeilkhewl 252 | +L+ +p+kR++i++i++h+w+ | Q: 288 GMLEYEPAKRFSIRQIRQHSWF 309 | *********************7 |
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Domain Sequence (FASTA) | YLMGDLLGEG SYGKVKEVLD SETLCRRAVK ILKKKKLRRI PNGEANVKKE IQLLRRLRHK 60 | NVIQLVDVLY NEEKQKMYMV MEYCVCGMQE MLDSVPEKRF PVCQAHGYFC QLIDGLEYLH 120 | SQGIVHKDIK PGNLLLTTGG TLKISDLGVA EALHPFAADD TCRTSQGSPA FQPPEIANGL 180 | DTFSGFKVDI WSAGVTLYNI TTGLYPFEGD NIYKLFENIG KGSYAIPGDC GPPLSDLLKG 240 | MLEYEPAKRF SIRQIRQHSW F 261 |
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Keyword | 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Autophagy; Cell cycle; Complete proteome; Cytoplasm; Disease mutation; DNA damage; Kinase; Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Prenylation; Reference proteome; Serine/threonine-protein kinase; Transferase; Tumor suppressor. |
Sequence Source | Ensembl |
Orthology | |
Gene Ontology | |
KEGG | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |