SIK3
entrez
23387
canonical
uniprot
Q9Y2K2
canonical
ensembl
ENSG00000160584
resolver
ensp
ENSP00000364449
resolver
ensp
ENSP00000390442
resolver
ensp
ENSP00000391295
resolver
ensp
ENSP00000548091
resolver
ensp
ENSP00000548092
resolver
ensp
ENSP00000593969
resolver
ensp
ENSP00000593970
resolver
ensp
ENSP00000593972
resolver
ensp
ENSP00000624121
resolver
ensp
ENSP00000777434
resolver
ensp
ENSP00000777436
resolver
ensp
ENSP00000777437
resolver
ensp
ENSP00000777438
resolver
enst
ENST00000445177
resolver
enst
ENST00000954062
resolver
genesymbol
SIK3
resolver
genesymbol_syn
KIAA0999
resolver
genesymbol_syn
QSK
resolver
hgnc
HGNC:29165
resolver
uniprot
A1A5A8
resolver
uniprot
H0Y494
resolver
uniprot
H0Y4E8
resolver
uniprot
J3KPC8
resolver
uniprot
Q59FY2
resolver
uniprot
Q5M9N1
resolver
uniprot
Q6P3R6
resolver
uniprot
Q8IYM8
resolver
uniprot
Q9HA50
resolver
uniprot_entry
H0Y4E8_HUMAN
resolver
uniprot_entry
SIK3_HUMAN
resolver
uniprot_sec
A1A5A8
resolver
uniprot_sec
H0Y494
resolver
uniprot_sec
J3KPC8
resolver
uniprot_sec
Q59FY2
resolver
uniprot_sec
Q5M9N1
resolver
uniprot_sec
Q6P3R6
resolver
uniprot_sec
Q8IYM8
resolver
uniprot_sec
Q9HA50
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation on Thr-221. {ECO:0000250|UniProtKB:Q9H0K1}.
uniprot
proteins
amino_acid_sequence
MAAAAASGAGGAAGAGTGGAGPAGRLLPPPAPGSPAAPAAVSPAAGQPRPPAPASRGPMPARIGYYEIDRTIGKGNFAVVKRATHLVTKAKVAIKIIDKTQLDEENLKKIFREVQIMKMLCHPHIIRLYQVMETERMIYLVTEYASGGEIFDHLVAHGRMAEKEARRKFKQIVTAVYFCHCRNIVHRDLKAENLLLDANLNIKIADFGFSNLFTPGQLLKTWCGSPPYAAPELFEGKEYDGPKVDIWSLGVVLYVLVCGALPFDGSTLQNLRARVLSGKFRIPFFMSTECEHLIRHMLVLDPNKRLSMEQICKHKWMKLGDADPNFDRLIAECQQLKEERQVDPLNEDVLLAMEDMGLDKEQTLQSLRSDAYDHYSAIYSLLCDRHKRHKTLRLGALPSMPRALAFQAPVNIQAEQAGTAMNISVPQVQLINPENQIVEPDGTLNLDSDEGEEPSPEALVRYLSMRRHTVGVADPRTEVMEDLQKLLPGFPGVNPQAPFLQVAPNVNFMHNLLPMQNLQPTGQLEYKEQSLLQPPTLQLLNGMGPLGRRASDGGANIQLHAQQLLKRPRGPSPLVTMTPAVPAVTPVDEESSDGEPDQEAVQSSTYKDSNTLHLPTERFSPVRRFSDGAASIQAFKAHLEKMGNNSSIKQLQQECEQLQKMYGGQIDERTLEKTQQQHMLYQQEQHHQILQQQIQDSICPPQPSPPLQAACENQPALLTHQLQRLRIQPSSPPPNHPNNHLFRQPSNSPPPMSSAMIQPHGAASSSQFQGLPSRSAIFQQQPENCSSPPNVALTCLGMQQPAQSQQVTIQVQEPVDMLSNMPGTAAGSSGRGISISPSAGQMQMQHRTNLMATLSYGHRPLSKQLSADSAEAHSLNVNRFSPANYDQAHLHPHLFSDQSRGSPSSYSPSTGVGFSPTQALKVPPLDQFPTFPPSAHQQPPHYTTSALQQALLSPTPPDYTRHQQVPHILQGLLSPRHSLTGHSDIRLPPTEFAQLIKRQQQQRQQQQQQQQQQEYQELFRHMNQGDAGSLAPSLGGQSMTERQALSYQNADSYHHHTSPQHLLQIRAQECVSQASSPTPPHGYAHQPALMHSESMEEDCSCEGAKDGFQDSKSSSTLTKGCHDSPLLLSTGGPGDPESLLGTVSHAQELGIHPYGHQPTAAFSKNKVPSREPVIGNCMDRSSPGQAVELPDHNGLGYPARPSVHEHHRPRALQRHHTIQNSDDAYVQLDNLPGMSLVAGKALSSARMSDAVLSQSSLMGSQQFQDGENEECGASLGGHEHPDLSDGSQHLNSSCYPSTCITDILLSYKHPEVSFSMEQAGV
uniprot
proteins
disease_involvement
DISEASE: Spondyloepimetaphyseal dysplasia, Krakow type (SEMDK) [MIM:618162]: An autosomal recessive skeletal disorder characterized by severe spondyloepimetaphyseal dysplasia, rhizomelia, mesomelia with significant anterior bowing of all limbs, severe immunodeficiency, and developmental delay. {ECO:0000269|PubMed:30232230}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Positive regulator of mTOR signaling that functions by triggering the degradation of DEPTOR, an mTOR inhibitor. Involved in the dynamic regulation of mTOR signaling in chondrocyte differentiation during skeletogenesis (PubMed:30232230). Negatively regulates cAMP signaling pathway possibly by acting on CRTC2/TORC2 and CRTC3/TORC3 (Probable). Prevents HDAC4 translocation to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q6P4S6, ECO:0000269|PubMed:30232230, ECO:0000305|PubMed:29211348}.
uniprot
proteins
mass_dalton
144851
uniprot
proteins
mutagenesis
MUTAGEN 221; /note="T->A: Prevents phosphorylation and activation by STK11/LKB1 complex."; /evidence="ECO:0000269|PubMed:14976552"; MUTAGEN 469; /note="T->A: Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 469; /note="T->E: Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 551; /note="S->A: Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 551; /note="S->E: Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 626; /note="S->A: No effect on interaction with 14-3-3 proteins, nor on cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348"; MUTAGEN 626; /note="S->E: No effect on cAMP signaling."; /evidence="ECO:0000269|PubMed:29211348
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-221 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 (PubMed:14976552). Phosphorylation at Thr-221 is inhibited in response to PTHLH/PTHrP (PubMed:30232230). Phosphorylated at Thr-469 and Ser-551 in response to cAMP signaling (Probable). {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:30232230, ECO:0000305|PubMed:29211348}.
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
10231032
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14976552
uniprot
proteins
pubmed
15334068
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16306228
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29211348
uniprot
proteins
pubmed
30232230
uniprot
proteins
sequence_length
1321
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16306228}. Note=Locates to punctate structures within the cytoplasm on binding to YWHAZ. {ECO:0000269|PubMed:16306228}.
uniprot
proteins