CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021232
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase SIK2 
Protein Synonyms/Alias
 Qin-induced kinase; Salt-inducible kinase 2; SIK-2; Serine/threonine-protein kinase SNF1-like kinase 2 
Gene Name
 SIK2 
Gene Synonyms/Alias
 KIAA0781; QIK; SNF1LK2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
28DIEGTLGKGNFAVVKubiquitination[1, 2]
53VAIKIIDKSQLDAVNacetylation[3]
53VAIKIIDKSQLDAVNubiquitination[2]
100YLVTEYAKNGEIFDYubiquitination[1]
144KIVHRDLKAENLLLDubiquitination[1, 2, 4, 5, 6, 7]
258MLVLDPSKRLTIAQIubiquitination[1]
269IAQIKEHKWMLIEVPubiquitination[1]
313SLGIDQQKTIESLQNubiquitination[1]
367IAEQTVAKAQTVGLPubiquitination[1]
536LEDNPSLKDIMLANQubiquitination[1, 2, 4, 6]
686YLQHRLQKPSLLSKAubiquitination[2]
692QKPSLLSKAQNTCQLubiquitination[8, 9]
702NTCQLYCKEPPRSLEubiquitination[1, 2]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Reversible acetylation regulates salt-inducible kinase (SIK2) and its function in autophagy.
 Yang FC, Tan BC, Chen WH, Lin YH, Huang JY, Chang HY, Sun HY, Hsu PH, Liou GG, Shen J, Chang CJ, Han CC, Tsai MD, Lee SC.
 J Biol Chem. 2013 Mar 1;288(9):6227-37. [PMID: 23322770]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators. 
Sequence Annotation
 DOMAIN 20 271 Protein kinase.
 DOMAIN 295 335 UBA.
 NP_BIND 26 34 ATP (By similarity).
 ACT_SITE 142 142 Proton acceptor (By similarity).
 BINDING 49 49 ATP (By similarity).
 MOD_RES 25 25 Phosphothreonine.
 MOD_RES 175 175 Phosphothreonine; by LKB1.
 MOD_RES 587 587 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 926 AA 
Protein Sequence
MVMADGPRHL QRGPVRVGFY DIEGTLGKGN FAVVKLGRHR ITKTEVAIKI IDKSQLDAVN 60
LEKIYREVQI MKMLDHPHII KLYQVMETKS MLYLVTEYAK NGEIFDYLAN HGRLNESEAR 120
RKFWQILSAV DYCHGRKIVH RDLKAENLLL DNNMNIKIAD FGFGNFFKSG ELLATWCGSP 180
PYAAPEVFEG QQYEGPQLDI WSMGVVLYVL VCGALPFDGP TLPILRQRVL EGRFRIPYFM 240
SEDCEHLIRR MLVLDPSKRL TIAQIKEHKW MLIEVPVQRP VLYPQEQENE PSIGEFNEQV 300
LRLMHSLGID QQKTIESLQN KSYNHFAAIY FLLVERLKSH RSSFPVEQRL DGRQRRPSTI 360
AEQTVAKAQT VGLPVTMHSP NMRLLRSALL PQASNVEAFS FPASGCQAEA AFMEEECVDT 420
PKVNGCLLDP VPPVLVRKGC QSLPSNMMET SIDEGLETEG EAEEDPAHAF EAFQSTRSGQ 480
RRHTLSEVTN QLVVMPGAGK IFSMNDSPSL DSVDSEYDMG SVQRDLNFLE DNPSLKDIML 540
ANQPSPRMTS PFISLRPTNP AMQALSSQKR EVHNRSPVSF REGRRASDTS LTQGIVAFRQ 600
HLQNLARTKG ILELNKVQLL YEQIGPEADP NLAPAAPQLQ DLASSCPQEE VSQQQESVST 660
LPASVHPQLS PRQSLETQYL QHRLQKPSLL SKAQNTCQLY CKEPPRSLEQ QLQEHRLQQK 720
RLFLQKQSQL QAYFNQMQIA ESSYPQPSQQ LPLPRQETPP PSQQAPPFSL TQPLSPVLEP 780
SSEQMQYSPF LSQYQEMQLQ PLPSTSGPRA APPLPTQLQQ QQPPPPPPPP PPRQPGAAPA 840
PLQFSYQTCE LPSAASPAPD YPTPCQYPVD GAQQSDLTGP DCPRSPGLQE APSSYDPLAL 900
SELPGLFDCE MLDAVDPQHN GYVLVN 926 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; IEA:Compara.
 GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:0046626; P:regulation of insulin receptor signaling pathway; ISS:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS.
 IPR017090; Ser/Thr_kinase_SIK1/2.
 IPR015940; UBA/transl_elong_EF1B_N_euk. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS50030; UBA 
PRINTS