ID SN1L2_MOUSE Reviewed; 931 AA. AC Q8CFH6; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-OCT-2007, entry version 41. DE Serine/threonine-protein kinase SNF1-like kinase 2 (EC 2.7.11.1) DE (Salt-inducible kinase 2). GN Name=Snf1lk2; Synonyms=Sik2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF LYS-49. RC TISSUE=Adipose tissue; RX MEDLINE=22625648; PubMed=12624099; DOI=10.1074/jbc.M211770200; RA Horike N., Takemori H., Katoh Y., Doi J., Min L., Asano T., Sun X.J., RA Yamamoto H., Kasayama S., Muraoka M., Nonaka Y., Okamoto M.; RT "Adipose-specific expression, phosphorylation of Ser794 in insulin RT receptor substrate-1, and activation in diabetic animals of salt- RT inducible kinase-2."; RL J. Biol. Chem. 278:18440-18447(2003). RN [2] RP FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-175 AND SER-587, RP AND MUTAGENESIS OF LYS-49 AND THR-175. RX PubMed=16817901; DOI=10.1111/j.1742-4658.2006.05291.x; RA Katoh Y., Takemori H., Lin X.Z., Tamura M., Muraoka M., Satoh T., RA Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H., RA Okamoto M.; RT "Silencing the constitutive active transcription factor CREB by the RT LKB1-SIK signaling cascade."; RL FEBS J. 273:2730-2748(2006). CC -!- FUNCTION: Phosphorylates Ser-789 of IRS1 in insulin-stimulated CC adipocytes, potentially modulating the efficiency of insulin CC signal transduction. Inhibits CREB activity by phosphorylating and CC repressing the CREB-specific coactivators, CRTC1-3. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: Magnesium. CC -!- ENZYME REGULATION: Activated by phosphorylation on Thr-175 by CC STK11 in complex with STE20-related adapter-alpha (STRAD alpha) CC pseudo kinase and CAB39 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Present in both white and brown adipose CC tissues with levels increasing during adipocyte differentiation. CC Lower levels observed in the testis. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 UBA domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB067780; BAC53845.1; -; mRNA. DR RefSeq; NP_848825.2; -. DR UniGene; Mm.104932; -. DR UniGene; Mm.7726; -. DR HSSP; P49137; 1NY3. DR Ensembl; ENSMUSG00000037112; Mus musculus. DR GeneID; 235344; -. DR KEGG; mmu:235344; -. DR MGI; MGI:2445031; Snf1lk2. DR ArrayExpress; Q8CFH6; -. DR GermOnline; ENSMUSG00000037112; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0006468; P:protein amino acid phosphorylation; IDA:UniProtKB. DR GO; GO:0007243; P:protein kinase cascade; IDA:UniProtKB. DR GO; GO:0046626; P:regulation of insulin receptor signaling pa...; IDA:UniProtKB. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR015738; Snf1_like_pk. DR InterPro; IPR000449; UBA/Transl_elong_EF1B_N. DR PANTHER; PTHR22982:SF56; Snf1_like_pk; 2. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50030; UBA; 1. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Phosphorylation; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 931 Serine/threonine-protein kinase SNF1-like FT kinase 2. FT /FTId=PRO_0000086663. FT DOMAIN 20 271 Protein kinase. FT DOMAIN 295 335 UBA. FT NP_BIND 26 34 ATP (By similarity). FT ACT_SITE 142 142 Proton acceptor (By similarity). FT BINDING 49 49 ATP. FT MOD_RES 175 175 Phosphothreonine (By similarity). FT MOD_RES 179 179 Phosphoserine (By similarity). FT MOD_RES 587 587 Phosphoserine (By similarity). FT MUTAGEN 49 49 K->M: Loss of kinase activity. FT MUTAGEN 175 175 T->E: Low levels of constitutive FT activity. SQ SEQUENCE 931 AA; 104198 MW; 5CF2FB8DCDC689F4 CRC64; MVMADGPRHL QRGPVRVGFY DIEGTLGKGN FAVVKLGRHR TTKTEVAIKI IDKSQLDAVN LEKIYREVQI MKMLDHPHII KLYQVMETKS MLYLVTEYAK NGEIFDYLAN HGRLNESEAR RKFWQILSAV DYCHGRKVVH RDLKAENLLL DNNMNIKIAD FGFGNFFKTG ELLATWCGSP PYAAPEVFEG QQYEGPQLDI WSMGVVLYVL VCGALPFDGP TLPILRQRVL EGRFRIPYFM SEDCEHLIRR MLVLDPSKRL SIAQIKEHKW MLIEVPVQRP ILYPQEQENE PSIGEFNEQV LRLMHSLGID QQKTVESLQN KSYNHFAAIY FLLVERLKSH RSSFPVEQRL DGRQRRPSTI AEQTVAKAQT VGLPVTLHPP NVRLMRSTLL PQASNVEAFS FPTSSCQAEA AFMEEECVDT PKVNGCLLDP VPPVLVRKGC QSLPSSMMET SIDEGLETEG EAEEDPSQAF EAFQATRSGQ RRHTLSEVTN QLVVMPGAGK MFSMSDNPSL ESVDSEYDMG SAQRDLNFLE DSPSLKDIML ANQPSPRMTS PFISLRPANP AMQALSSQKR EAHNRSPVSF REGRRASDTS LTQGIVAFRQ HLQNLARTKG ILELNKVQLL YEQMGSNADP TLTSTAPQLQ DLSSSCPQEE ISQQQESVSS LSASMHPQLS PQQSLETQYL QHRLQKPNLL PKAQSPCPVY CKEPPRSLEQ QLQEHRLQQK RLFLQKQSQL QAYFNQMQIA ESSYPGPSQQ LALPHQETPL TSQQPPSFSL TQALSPVLEP SSEQMQFSSF LSQYPEMQLQ PLPSTPGPRA PPPLPSQLQQ HQQPPPPPPP PPPQQPGAAP TSLQFSYQTC ELPSTTSSVP NYPASCHYPV DGAQQSNLTG ADCPRSSGLQ DTASSYDPLA LSELPGLFDC EMVEAVDPQH NGVVSCLARE T //