Q9CXB8
uniprot
Q9CXB8
canonical
activity_regulation
ACTIVITY REGULATION: Serine/threonine-protein kinase activity is stimulated upon ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose)-binding. {ECO:0000250|UniProtKB:Q96QP1}.
uniprot
proteins
amino_acid_sequence
MNNQDAVASILHECKQVLDRLLLETPDVSTEDKSEDQRCRASLPSELRTLIQEAEEMKWPFVPEKWQYKQAMSPEDKTNLQDVIGAGLQQLLAALRASILVQDCAAASAIVFLMDRFLYGLDVSGKLLQVAKGLHKLKPATPIAPQVVIRQARVSVNSGKLLKAEYILSSLISNNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEAAELIWASVIGYLTLPQPDKKGISTSLGILADIFVSMSKTDYEKFKKSPKVNLALLKEFDHHLLSAAEACKLAAAFSAYTPLFVLRAVNIRGTCLLSYSCSADCPPGMKSVHLCEAKEAFEIGLLTKKDGELVSGKQELHSFIKAAFGLTTVHSRLHGETDAVRAARQLCSEAVGKLYTFSTSPTSQDREGLSQEIMSLISQVKGHLRVQSFPNLDVCSYVPESFKCGLDRLILHGHVDFQQILETYSQHHTSVCEVFESTCGNSKSNQRDTKSEVCITTLKTETNTADTMVATLERVSSQDSRSTASSKMSKKDQGKLQRERGRSWTRSKAFRVSLDLDMETETEPPNHSNGGTDVFNKSLRDNSSSCSWGRLSGLSSSTSWEEVNCAVQDVVRKGSGQEKHPVEAQSSEAVSEEPKRNRSSRAVFLSSKLRGVSLQTTGDDNLESSPSQLHNHTSILPFNAKDTCLASGAGLVETAEGSNNTSLQSSHSCGSDSWSLSSSDRFTDVTTNPSVQEEEPSGIMGDVPESKYDFKDWHGEKNGGTLTEICTGPELTFAPSSVDPEGETAESTDDGLSPSQVALGCLEGSHSMSTRRTFFPDGSVQNADSAKTGCSVRDQTVDPDASTVDEEGQMLDSTEVCSIGQDGAHRPRALRSGQSAEGPKSFVNGSRPSPIFDEDFSTTEEGEELGSMLKSSQNSSSYSPWWLKSPAFSRSSSDGESSWSLLNSSRSSFASLAGQTSQEILEARTLQPDDLEKLLAGVRHDWLLQRLENTGVLKSNQLQQAHSALLLKYSKKSELWTAQETVVYLGDYLKVKKKGKQRNAFWVHYLHQEETLGRYVGKEYKERKGLRHHFTDVERQMTAQHYVTEFNKRLYEQKIPTQIFYVPSTILLILEDRTIKGCISVEPYILGEFVKLSNNTKVVKNEYKATEYGLAYGHFSYEFSNHRDVVVDLQGWVTGNGKGLIYLTDPQIHSVDQKDVTTNFGKRGIFYFFNNQHASCNEICHRLSLTRPSLEQTSKV
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase that detects bacterial pathogen-associated molecular pattern metabolites (PAMPs) and initiates an innate immune response, a critical step for pathogen elimination and engagement of adaptive immunity (By similarity). Specifically recognizes and binds ADP-D-glycero-beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria (PubMed:30111836). ADP-Heptose-binding stimulates its kinase activity to phosphorylate and activate TIFA, triggering pro-inflammatory NF-kappa-B signaling (By similarity). May be involved in monosodium urate monohydrate (MSU)-induced inflammation by mediating phosphorylation of unconventional myosin MYO9A (By similarity). May also play a role in apical protein transport by mediating phosphorylation of unconventional myosin MYO1A (By similarity). May play a role in ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q96QP1, ECO:0000269|PubMed:30111836}.
uniprot
proteins
mass_dalton
136134
uniprot
proteins
mutagenesis
MUTAGEN 237; /note="T->M: Knockin mice have elevated serum levels of cytokines CXCL1, CXCL10 and CCL2."; /evidence="ECO:0000269|PubMed:35868845
uniprot
proteins
protein_family
ALPK subfamily
uniprot
proteins
protein_family
Alpha-type protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21208416
uniprot
proteins
pubmed
30111836
uniprot
proteins
pubmed
30967659
uniprot
proteins
pubmed
35868845
uniprot
proteins
sequence_length
1231
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96QP1}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96QP1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96QP1}. Cell projection, cilium {ECO:0000269|PubMed:30967659}. Note=Localized to the basal body region of the photoreceptor cilium and the region of the adjacent centriole. {ECO:0000269|PubMed:30967659}.
uniprot
proteins