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Q60670

- SIK1_MOUSE

UniProt

Q60670 - SIK1_MOUSE

Protein

Serine/threonine-protein kinase SIK1

Gene

Sik1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (19 Oct 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, TORC1/CRTC1 and TORC2/CRTC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators TORC1/CRTC1 and TORC2/CRTC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1.9 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by phosphorylation on Thr-182. Also activated by phosphorylation on Thr-322 in response to increases in intracellular sodium in parallel with elevations in intracellular calcium through the reversible sodium/calcium exchanger.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561ATP
    Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi33 – 419ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: UniProtKB
    2. ATP binding Source: UniProtKB
    3. cAMP response element binding protein binding Source: UniProtKB
    4. histone deacetylase binding Source: UniProtKB
    5. magnesium ion binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein kinase binding Source: UniProtKB
    8. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. anoikis Source: BHF-UCL
    2. cardiac muscle cell differentiation Source: UniProtKB
    3. cell cycle Source: UniProtKB-KW
    4. intracellular signal transduction Source: UniProtKB
    5. negative regulation of CREB transcription factor activity Source: UniProtKB
    6. negative regulation of gluconeogenesis Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. negative regulation of triglyceride biosynthetic process Source: UniProtKB
    9. positive regulation of anoikis Source: Ensembl
    10. protein autophosphorylation Source: UniProtKB
    11. protein phosphorylation Source: UniProtKB
    12. regulation of cell differentiation Source: UniProtKB
    13. regulation of mitotic cell cycle Source: UniProtKB
    14. regulation of myotube differentiation Source: UniProtKB
    15. regulation of sodium ion transport Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Differentiation

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase SIK1 (EC:2.7.11.1)
    Alternative name(s):
    HRT-20
    Myocardial SNF1-like kinase
    Salt-inducible kinase 1
    Short name:
    SIK-1
    Serine/threonine-protein kinase SNF1-like kinase 1
    Short name:
    Serine/threonine-protein kinase SNF1LK
    Gene namesi
    Name:Sik1
    Synonyms:Msk, Sik, Snf1lk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:104754. Sik1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Ensembl
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561K → M: Loss of kinase activity. 3 Publications
    Mutagenesisi182 – 1821T → A: Loss of kinase activity. 1 Publication
    Mutagenesisi182 – 1821T → E: Low levels of constitutive activity. 1 Publication
    Mutagenesisi268 – 2681T → A: Does not affect phosphorylation by PKA and nuclear export following ACTH treatment. 1 Publication
    Mutagenesisi475 – 4751T → A: Does not affect phosphorylation by PKA and nuclear export following ACTH treatment. 1 Publication
    Mutagenesisi577 – 5771S → A: Abolishes phosphorylation by PKA and impairs nuclear export following ACTH treatment. 3 Publications
    Mutagenesisi577 – 5771S → A: Constitutively active. 3 Publications
    Mutagenesisi593 – 5942RK → AA: Localizes mainly in cytoplasm and not in nucleus.
    Mutagenesisi597 – 5993RTK → ATA: Localizes mainly in cytoplasm and not in nucleus.
    Mutagenesisi606 – 6083KIK → AIA: Localizes mainly in cytoplasm and not in nucleus.
    Mutagenesisi607 – 6071I → A: Localizes mainly in cytoplasm and not in nucleus; when associated with D-483 and A-610. 1 Publication
    Mutagenesisi610 – 6101L → A: Localizes mainly in cytoplasm and not in nucleus; when associated with D-483 and A-607. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 779779Serine/threonine-protein kinase SIK1PRO_0000086660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei182 – 1821Phosphothreonine; by LKB1 and GSK3-beta1 Publication
    Modified residuei186 – 1861Phosphoserine; by autocatalysisBy similarity
    Modified residuei322 – 3221Phosphothreonine; by CaMK1By similarity
    Modified residuei577 – 5771Phosphoserine; by PKA3 Publications

    Post-translational modificationi

    Phosphorylated at Thr-182 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39, leading to its activation. Phosphorylation at Thr-182 promotes autophosphorylation at Ser-186, which is required for sustained activity. Autophosphorylation at Ser-186 is maintained by sequential phosphorylation at Thr-182 by GSK3-beta. GSK3-beta cannot initiate phosphorylation at Thr-182, it can only maintain it. Phosphorylation at Ser-577 by PKA promotes translocation to the cytoplasm. Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ60670.

    PTM databases

    PhosphoSiteiQ60670.

    Expressioni

    Tissue specificityi

    Expressed in lung, skin, ovary, heart and stomach. No expression in brain, liver or adult skeletal muscle but is present in skeletal muscle progenitor cells of the somite beginning at 9.5 dpc. Present at 8.0 dpc in the monolayer of presumptive myocardial cells but rapidly down-regulated at 8.5 dpc upon primitive ventricle formation, although still present in myocardial cells that will populate the primitive atrium and bulbus cordis. At 9.5 dpc expression is down-regulated in the primitive atrium but observed in the sinus venosus and truncus arteriosus.2 Publications

    Inductioni

    Expression is stimulated by CREB1 in myocytes; direct target of CREB1.1 Publication

    Gene expression databases

    ArrayExpressiQ60670.
    BgeeiQ60670.
    CleanExiMM_SNF1LK.
    GenevestigatoriQ60670.

    Interactioni

    Subunit structurei

    Interacts (when phosphorylated on Thr-182 and Ser-186) with YWHAZ. Interacts with ATP1A1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ60670.
    SMRiQ60670. Positions 24-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 278252Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini303 – 34341UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni586 – 61227RK-rich regionAdd
    BLAST

    Domaini

    The RK-rich region determines the subcellular location.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117510.
    HOGENOMiHOG000039981.
    InParanoidiQ60670.
    KOiK16311.
    OMAiQIRQHRW.
    OrthoDBiEOG70ZZMM.
    TreeFamiTF315213.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60670-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVIMSEFSAV PSGTGQGQQK PLRVGFYDVE RTLGKGNFAV VKLARHRVTK    50
    TQVAIKIIDK TRLDSSNLEK IYREVQLMKL LNHPNIIKLY QVMETKDMLY 100
    IVTEFAKNGE MFDYLTSNGH LSENEARQKF WQILSAVEYC HNHHIVHRDL 150
    KTENLLLDSN MDIKLADFGF GNFYKPGEPL STWCGSPPYA APEVFEGKEY 200
    EGPQLDVWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR FRIPFFMSQD 250
    CETLIRRMLV VDPAKRITIA QIRQHRWMQA DPTLLQQDDP AFDMQGYTSN 300
    LGDYNEQVLG IMQALGIDRQ RTIESLQNSS YNHFAAIYYL LLERLKEHRS 350
    AQPSSRPTPA PTRQPQLRSS DLSSLEVPQE ILPCDPFRPS LLCPQPQALA 400
    QSVLQAEIDC DLHSSLQPLL FPLDTNCSGV FRHRSISPSS LLDTAISEEA 450
    RQGPSLEEEQ EVQEPLPGST GRRHTLAEVS THFSPLNPPC IIVSSSATAS 500
    PSEGTSSDSC LPFSASEGPA GLGSGLATPG LLGTSSPVRL ASPFLGSQSA 550
    TPVLQTQAGL GTAVLPPVSF QEGRRASDTS LTQGLKAFRQ QLRKNARTKG 600
    FLGLNKIKGL ARQVCQSSVR TPRGGMSTFH TPAPSSGLQG CTTSNREGRS 650
    LLEEVLHQQR LLQLQHHSST AAASSGCQQG PQLSPVPYVL APCDSLLVSG 700
    IPLLPTPLLQ AGMSPVASAA HLLDTHLHIS AGPVALPTGP LPQCLTRLSP 750
    GCDPAGLPQG DCEMEDLTSG QRGTFVLVQ 779
    Length:779
    Mass (Da):85,115
    Last modified:October 19, 2011 - v3
    Checksum:i9C4D25CCF0C0D06D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti183 – 1842WC → CV in AAA67926. (PubMed:7893599)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11494 mRNA. Translation: AAA67926.2.
    AK141817 mRNA. Translation: BAE24842.1.
    CCDSiCCDS37552.1.
    PIRiI49072.
    RefSeqiNP_034961.2. NM_010831.2.
    UniGeneiMm.290941.

    Genome annotation databases

    EnsembliENSMUST00000024839; ENSMUSP00000024839; ENSMUSG00000024042.
    GeneIDi17691.
    KEGGimmu:17691.
    UCSCiuc008bvr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11494 mRNA. Translation: AAA67926.2 .
    AK141817 mRNA. Translation: BAE24842.1 .
    CCDSi CCDS37552.1.
    PIRi I49072.
    RefSeqi NP_034961.2. NM_010831.2.
    UniGenei Mm.290941.

    3D structure databases

    ProteinModelPortali Q60670.
    SMRi Q60670. Positions 24-341.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q60670.

    Proteomic databases

    PRIDEi Q60670.

    Protocols and materials databases

    DNASUi 17691.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024839 ; ENSMUSP00000024839 ; ENSMUSG00000024042 .
    GeneIDi 17691.
    KEGGi mmu:17691.
    UCSCi uc008bvr.1. mouse.

    Organism-specific databases

    CTDi 150094.
    MGIi MGI:104754. Sik1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117510.
    HOGENOMi HOG000039981.
    InParanoidi Q60670.
    KOi K16311.
    OMAi QIRQHRW.
    OrthoDBi EOG70ZZMM.
    TreeFami TF315213.

    Miscellaneous databases

    NextBioi 292274.
    PROi Q60670.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60670.
    Bgeei Q60670.
    CleanExi MM_SNF1LK.
    Genevestigatori Q60670.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037014. Ser/Thr_PK_SNF1-like. 1 hit.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel protein kinases expressed in the myocardium of the developing mouse heart."
      Ruiz J.C., Conlon F.L., Robertson E.J.
      Mech. Dev. 48:153-164(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Embryo.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Spinal ganglion.
    3. "ACTH-induced nucleocytoplasmic translocation of salt-inducible kinase. Implication in the protein kinase A-activated gene transcription in mouse adrenocortical tumor cells."
      Takemori H., Katoh Y., Horike N., Doi J., Okamoto M.
      J. Biol. Chem. 277:42334-42343(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-577, MUTAGENESIS OF THR-268; THR-475 AND SER-577.
    4. "Salt-inducible kinase-1 represses cAMP response element-binding protein activity both in the nucleus and in the cytoplasm."
      Katoh Y., Takemori H., Min L., Muraoka M., Doi J., Horike N., Okamoto M.
      Eur. J. Biochem. 271:4307-4319(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN RK-RICH REGION, MUTAGENESIS OF 593-ARG-LYS-594; 597-ARG--LYS-599; 606-LYS--LYS-608; ILE-607 AND LEU-610.
    5. "snf1lk encodes a protein kinase that may function in cell cycle regulation."
      Stephenson A., Huang G.Y., Nguyen N.T., Reuter S., McBride J.L., Ruiz J.C.
      Genomics 83:1105-1115(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-56.
    6. Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2, SUBCELLULAR LOCATION.
    7. "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, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-182 AND SER-577, MUTAGENESIS OF LYS-56; THR-182 AND SER-577.
    8. "SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes."
      Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T., Shelton G.D., Montminy M.
      Nat. Med. 13:597-603(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC4 AND HDAC5, INDUCTION, PHOSPHORYLATION AT SER-577, MUTAGENESIS OF LYS-56 AND SER-577.
    9. Cited for: FUNCTION.
    10. "Salt-inducible kinase regulates hepatic lipogenesis by controlling SREBP-1c phosphorylation."
      Yoon Y.S., Seo W.Y., Lee M.W., Kim S.T., Koo S.H.
      J. Biol. Chem. 284:10446-10452(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SREBF1.
    11. "Lack of sik1 in mouse embryonic stem cells impairs cardiomyogenesis by down-regulating the cyclin-dependent kinase inhibitor p57kip2."
      Romito A., Lonardo E., Roma G., Minchiotti G., Ballabio A., Cobellis G.
      PLoS ONE 5:E9029-E9029(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiSIK1_MOUSE
    AccessioniPrimary (citable) accession number: Q60670
    Secondary accession number(s): Q3UR46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3