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Q8CFH6 (SIK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase SIK2

EC=2.7.11.1
Alternative name(s):
Salt-inducible kinase 2
Short name=SIK-2
Serine/threonine-protein kinase SNF1-like kinase 2
Gene names
Name:Sik2
Synonyms:Snf1lk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length931 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates 'Ser-789' 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. Ref.1 Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1

Cofactor

Magnesium. Ref.1

Enzyme regulation

Activated by phosphorylation on Thr-175 By similarity. Ref.2

Subunit structure

Interacts with and phosphorylates TORC2/CRTC2 By similarity.

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Present in both white and brown adipose tissues with levels increasing during adipocyte differentiation. Lower levels observed in the testis. Ref.1

Post-translational modification

Phosphorylated at Thr-175 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39 By similarity. Ref.2

Acetylation at Lys-53 inhibits kinase activity. Deacetylated by HDAC6 By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 931931Serine/threonine-protein kinase SIK2
PRO_0000086663

Regions

Domain20 – 271252Protein kinase
Domain295 – 33541UBA
Nucleotide binding26 – 349ATP By similarity UniProtKB Q13131

Sites

Active site1421Proton acceptor By similarity UniProtKB Q13131
Binding site491ATP Ref.1

Amino acid modifications

Modified residue251Phosphothreonine By similarity
Modified residue531N6-acetyllysine; by EP300 By similarity
Modified residue1751Phosphothreonine By similarity UniProtKB Q9H0K1
Modified residue5871Phosphoserine By similarity

Experimental info

Mutagenesis491K → M: Loss of kinase activity. Ref.1 Ref.2
Mutagenesis1751T → E: Low levels of constitutive activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CFH6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5CF2FB8DCDC689F4

FASTA931104,198
        10         20         30         40         50         60 
MVMADGPRHL QRGPVRVGFY DIEGTLGKGN FAVVKLGRHR TTKTEVAIKI IDKSQLDAVN 

        70         80         90        100        110        120 
LEKIYREVQI MKMLDHPHII KLYQVMETKS MLYLVTEYAK NGEIFDYLAN HGRLNESEAR 

       130        140        150        160        170        180 
RKFWQILSAV DYCHGRKVVH RDLKAENLLL DNNMNIKIAD FGFGNFFKTG ELLATWCGSP 

       190        200        210        220        230        240 
PYAAPEVFEG QQYEGPQLDI WSMGVVLYVL VCGALPFDGP TLPILRQRVL EGRFRIPYFM 

       250        260        270        280        290        300 
SEDCEHLIRR MLVLDPSKRL SIAQIKEHKW MLIEVPVQRP ILYPQEQENE PSIGEFNEQV 

       310        320        330        340        350        360 
LRLMHSLGID QQKTVESLQN KSYNHFAAIY FLLVERLKSH RSSFPVEQRL DGRQRRPSTI 

       370        380        390        400        410        420 
AEQTVAKAQT VGLPVTLHPP NVRLMRSTLL PQASNVEAFS FPTSSCQAEA AFMEEECVDT 

       430        440        450        460        470        480 
PKVNGCLLDP VPPVLVRKGC QSLPSSMMET SIDEGLETEG EAEEDPSQAF EAFQATRSGQ 

       490        500        510        520        530        540 
RRHTLSEVTN QLVVMPGAGK MFSMSDNPSL ESVDSEYDMG SAQRDLNFLE DSPSLKDIML 

       550        560        570        580        590        600 
ANQPSPRMTS PFISLRPANP AMQALSSQKR EAHNRSPVSF REGRRASDTS LTQGIVAFRQ 

       610        620        630        640        650        660 
HLQNLARTKG ILELNKVQLL YEQMGSNADP TLTSTAPQLQ DLSSSCPQEE ISQQQESVSS 

       670        680        690        700        710        720 
LSASMHPQLS PQQSLETQYL QHRLQKPNLL PKAQSPCPVY CKEPPRSLEQ QLQEHRLQQK 

       730        740        750        760        770        780 
RLFLQKQSQL QAYFNQMQIA ESSYPGPSQQ LALPHQETPL TSQQPPSFSL TQALSPVLEP 

       790        800        810        820        830        840 
SSEQMQFSSF LSQYPEMQLQ PLPSTPGPRA PPPLPSQLQQ HQQPPPPPPP PPPQQPGAAP 

       850        860        870        880        890        900 
TSLQFSYQTC ELPSTTSSVP NYPASCHYPV DGAQQSNLTG ADCPRSSGLQ DTASSYDPLA 

       910        920        930 
LSELPGLFDC EMVEAVDPQH NGVVSCLARE T 

« Hide

References

[1]"Adipose-specific expression, phosphorylation of Ser794 in insulin receptor substrate-1, and activation in diabetic animals of salt-inducible kinase-2."
Horike N., Takemori H., Katoh Y., Doi J., Min L., Asano T., Sun X.J., Yamamoto H., Kasayama S., Muraoka M., Nonaka Y., Okamoto M.
J. Biol. Chem. 278:18440-18447(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-49.
Tissue: Adipose tissue.
[2]"Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade."
Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T., Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H., Okamoto M.
FEBS J. 273:2730-2748(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-175 AND SER-587, MUTAGENESIS OF LYS-49 AND THR-175.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB067780 mRNA. Translation: BAC53845.1.
CCDSCCDS40627.1.
RefSeqNP_848825.2. NM_178710.3.
UniGeneMm.104932.
Mm.439989.

3D structure databases

ProteinModelPortalQ8CFH6.
SMRQ8CFH6. Positions 17-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231647. 1 interaction.
DIPDIP-60734N.

PTM databases

PhosphoSiteQ8CFH6.

Proteomic databases

MaxQBQ8CFH6.
PaxDbQ8CFH6.
PRIDEQ8CFH6.

Protocols and materials databases

DNASU235344.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID235344.
KEGGmmu:235344.

Organism-specific databases

CTD23235.
MGIMGI:2445031. Sik2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000048716.
InParanoidQ8CFH6.
KOK16311.
PhylomeDBQ8CFH6.

Gene expression databases

CleanExMM_SNF1LK2.
GenevestigatorQ8CFH6.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio382621.
PROQ8CFH6.
SOURCESearch...

Entry information

Entry nameSIK2_MOUSE
AccessionPrimary (citable) accession number: Q8CFH6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot