Sik2
entrez
235344
canonical
uniprot
Q8CFH6
canonical
ensembl
ENSMUSG00000037112
resolver
ensp
ENSMUSP00000038761
resolver
ensp
ENSMUSP00000134954
resolver
ensp
ENSMUSP00000135376
resolver
ensp
ENSMUSP00000191454
resolver
ensp
ENSMUSP00000191455
resolver
enst
ENSMUST00000041375
resolver
enst
ENSMUST00000176491
resolver
enst
ENSMUST00000176663
resolver
genesymbol
Sik2
resolver
genesymbol_syn
Snf1lk2
resolver
uniprot
F8VPT7
resolver
uniprot
H3BKG1
resolver
uniprot_entry
F8VPT7_MOUSE
resolver
uniprot_entry
H3BKG1_MOUSE
resolver
uniprot_entry
SIK2_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation on Thr-175 (By similarity). Inhibited by phosphorylation at Ser-343, Ser-358, Thr-484 and/or Ser-587, probably by PKA, which triggers interaction with 14-3-3 proteins (PubMed:29211348). {ECO:0000250|UniProtKB:Q9H0K1, ECO:0000269|PubMed:29211348}.
uniprot
proteins
amino_acid_sequence
MVMADGPRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRTTKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKVVHRDLKAENLLLDNNMNIKIADFGFGNFFKTGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLSIAQIKEHKWMLIEVPVQRPILYPQEQENEPSIGEFNEQVLRLMHSLGIDQQKTVESLQNKSYNHFAAIYFLLVERLKSHRSSFPVEQRLDGRQRRPSTIAEQTVAKAQTVGLPVTLHPPNVRLMRSTLLPQASNVEAFSFPTSSCQAEAAFMEEECVDTPKVNGCLLDPVPPVLVRKGCQSLPSSMMETSIDEGLETEGEAEEDPSQAFEAFQATRSGQRRHTLSEVTNQLVVMPGAGKMFSMSDNPSLESVDSEYDMGSAQRDLNFLEDSPSLKDIMLANQPSPRMTSPFISLRPANPAMQALSSQKREAHNRSPVSFREGRRASDTSLTQGIVAFRQHLQNLARTKGILELNKVQLLYEQMGSNADPTLTSTAPQLQDLSSSCPQEEISQQQESVSSLSASMHPQLSPQQSLETQYLQHRLQKPNLLPKAQSPCPVYCKEPPRSLEQQLQEHRLQQKRLFLQKQSQLQAYFNQMQIAESSYPGPSQQLALPHQETPLTSQQPPSFSLTQALSPVLEPSSEQMQFSSFLSQYPEMQLQPLPSTPGPRAPPPLPSQLQQHQQPPPPPPPPPPQQPGAAPTSLQFSYQTCELPSTTSSVPNYPASCHYPVDGAQQSNLTGADCPRSSGLQDTASSYDPLALSELPGLFDCEMVEAVDPQHNGVVSCLARET
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase that plays a role in many biological processes such as fatty acid oxidation, autophagy, immune response or glucose metabolism (PubMed:12624099, PubMed:16817901, PubMed:29211348). Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction (PubMed:12624099). Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators (PubMed:16817901). Phosphorylates EP300 and thus inhibits its histone acetyltransferase activity. In turn, regulates the DNA-binding ability of several transcription factors such as PPARA or MLXIPL (By similarity). Also plays a role in thymic T-cell development (PubMed:34732767). {ECO:0000250|UniProtKB:Q9H0K1, ECO:0000269|PubMed:12624099, ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:29211348, ECO:0000269|PubMed:34732767}.
uniprot
proteins
mass_dalton
104198
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="K->M: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:12624099, ECO:0000269|PubMed:16817901"; MUTAGEN 175; /note="T->A: Reduced inhibitory activity towards TORCs in presence and absence of cAMP signaling."; /evidence="ECO:0000269|PubMed:16817901"; MUTAGEN 175; /note="T->E: Low levels of constitutive activity."; /evidence="ECO:0000269|PubMed:16817901"; MUTAGEN 343; /note="S->A: Reduced interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 358; /note="S->A: Reduced interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-484 and A-587."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 484; /note="T->A: Reduced interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-358 and A-587."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 587; /note="S->A: Reduced interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-358 and A-484."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 595..624; /note="Missing: Reduced 14-3-3 interaction. Reduced inactivation following cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (By similarity). Phosphorylated at Thr-484 in response to insulin in adipocytes (By similarity). Phosphorylation at Ser-358, Thr-484 and/or Ser-587 following cAMP signaling is required for 14-3-3 interaction and thus inactivation (PubMed:29211348). {ECO:0000250|UniProtKB:Q9H0K1, ECO:0000269|PubMed:29211348}.; PTM: Acetylation at Lys-53 inhibits kinase activity. Deacetylated by HDAC6 (By similarity). {ECO:0000250|UniProtKB:Q9H0K1}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SNF1 subfamily
uniprot
proteins
pubmed
12624099
uniprot
proteins
pubmed
16817901
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
29211348
uniprot
proteins
pubmed
34732767
uniprot
proteins
sequence_length
931
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12624099}.
uniprot
proteins