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P57059

- SIK1_HUMAN

UniProt

P57059 - SIK1_HUMAN

Protein

Serine/threonine-protein kinase SIK1

Gene

SIK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      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 SREBF1.4 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 – 561ATPCurated
    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. magnesium ion binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein kinase binding Source: UniProtKB
    7. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. anoikis Source: Ensembl
    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: BHF-UCL
    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

    Enzyme and pathway databases

    SignaLinkiP57059.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase SIK1 (EC:2.7.11.1)
    Alternative name(s):
    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:SIK, SNF1LK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:11142. SIK1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    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

    Involvement in diseasei

    Defects in SIK1 may be associated with some cancers, such as breast cancers. Loss of SIK1 correlates with poor patient outcome in breast cancers (PubMed:19622832).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561K → M: Loss of kinase activity. 2 Publications
    Mutagenesisi135 – 1351S → A: Decreased kinase activity without affecting much autophosphorylation status. 1 Publication
    Mutagenesisi182 – 1821T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication
    Mutagenesisi186 – 1861S → A, D, C or G: Impaired autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi186 – 1861S → T: Does not autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi209 – 2091S → A: Decreased kinase activity without affecting much autophosphorylation status. 1 Publication
    Mutagenesisi248 – 2481S → A: Decreased kinase activity without affecting much autophosphorylation status. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA164725717.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 783783Serine/threonine-protein kinase SIK1PRO_0000086659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei182 – 1821Phosphothreonine; by LKB1 and GSK3-beta2 Publications
    Modified residuei186 – 1861Phosphoserine; by autocatalysis1 Publication
    Modified residuei322 – 3221Phosphothreonine; by CaMK1By similarity
    Modified residuei575 – 5751Phosphoserine; by PKACurated

    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-575 by PKA promotes translocation to the cytoplasm. Phosphorylation at Thr-322 by CaMK1 following intracellular sodium concentration leads to activation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP57059.
    PaxDbiP57059.
    PRIDEiP57059.

    PTM databases

    PhosphoSiteiP57059.

    Expressioni

    Gene expression databases

    BgeeiP57059.
    GenevestigatoriP57059.

    Organism-specific databases

    HPAiCAB023801.

    Interactioni

    Subunit structurei

    Interacts with ATP1A1 By similarity. Interacts (when phosphorylated on Thr-182 and Ser-186) with YWHAZ.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YWHAZP631044EBI-1181640,EBI-347088

    Protein-protein interaction databases

    BioGridi127260. 12 interactions.
    IntActiP57059. 6 interactions.
    STRINGi9606.ENSP00000270162.

    Structurei

    3D structure databases

    ProteinModelPortaliP57059.
    SMRiP57059. Positions 22-362.
    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
    Regioni584 – 61027RK-rich regionBy similarityAdd
    BLAST

    Domaini

    The RK-rich region determines the subcellular location.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000039981.
    InParanoidiP57059.
    KOiK16311.
    OMAiQIRQHRW.
    OrthoDBiEOG70ZZMM.
    PhylomeDBiP57059.
    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.
    SM00165. UBA. 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.

    P57059-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVIMSEFSAD PAGQGQGQQK PLRVGFYDIE RTLGKGNFAV VKLARHRVTK    50
    TQVAIKIIDK TRLDSSNLEK IYREVQLMKL LNHPHIIKLY QVMETKDMLY 100
    IVTEFAKNGE MFDYLTSNGH LSENEARKKF WQILSAVEYC HDHHIVHRDL 150
    KTENLLLDGN MDIKLADFGF GNFYKSGEPL STWCGSPPYA APEVFEGKEY 200
    EGPQLDIWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR FRIPFFMSQD 250
    CESLIRRMLV VDPARRITIA QIRQHRWMRA EPCLPGPACP AFSAHSYTSN 300
    LGDYDEQALG IMQTLGVDRQ RTVESLQNSS YNHFAAIYYL LLERLKEYRN 350
    AQCARPGPAR QPRPRSSDLS GLEVPQEGLS TDPFRPALLC PQPQTLVQSV 400
    LQAEMDCELQ SSLQWPLFFP VDASCSGVFR PRPVSPSSLL DTAISEEARQ 450
    GPGLEEEQDT QESLPSSTGR RHTLAEVSTR LSPLTAPCIV VSPSTTASPA 500
    EGTSSDSCLT FSASKSPAGL SGTPATQGLL GACSPVRLAS PFLGSQSATP 550
    VLQAQGGLGG AVLLPVSFQE GRRASDTSLT QGLKAFRQQL RKTTRTKGFL 600
    GLNKIKGLAR QVCQAPASRA SRGGLSPFHA PAQSPGLHGG AAGSREGWSL 650
    LEEVLEQQRL LQLQHHPAAA PGCSQAPQPA PAPFVIAPCD GPGAAPLPST 700
    LLTSGLPLLP PPLLQTGASP VASAAQLLDT HLHIGTGPTA LPAVPPPRLA 750
    RLAPGCEPLG LLQGDCEMED LMPCSLGTFV LVQ 783
    Length:783
    Mass (Da):84,902
    Last modified:February 15, 2005 - v2
    Checksum:iD646123C0715DAAC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1661A → AGTE in BAA95536. (PubMed:10830953)Curated
    Sequence conflicti489 – 4902IV → KF in BAA95536. (PubMed:10830953)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151G → S.1 Publication
    Corresponds to variant rs3746951 [ dbSNP | Ensembl ].
    VAR_041087
    Natural varianti142 – 1421D → N.1 Publication
    Corresponds to variant rs45491503 [ dbSNP | Ensembl ].
    VAR_041088
    Natural varianti211 – 2111G → S in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_041089
    Natural varianti430 – 4301R → W.
    Corresponds to variant rs34164089 [ dbSNP | Ensembl ].
    VAR_033910
    Natural varianti469 – 4691G → D in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041090
    Natural varianti615 – 6151A → V.3 Publications
    Corresponds to variant rs430554 [ dbSNP | Ensembl ].
    VAR_021255
    Natural varianti696 – 6961P → L.1 Publication
    Corresponds to variant rs56386767 [ dbSNP | Ensembl ].
    VAR_041091
    Natural varianti725 – 7251A → V.1 Publication
    Corresponds to variant rs35596465 [ dbSNP | Ensembl ].
    VAR_041092

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047786 mRNA. Translation: BAD74070.1.
    AP001751 Genomic DNA. Translation: BAA95536.1.
    BC038504 mRNA. Translation: AAH38504.1.
    AK131076 mRNA. Translation: BAC85126.1.
    CCDSiCCDS33575.1.
    RefSeqiNP_775490.2. NM_173354.3.
    XP_006723983.1. XM_006723920.1.
    XP_006726866.1. XM_006726803.1.
    UniGeneiHs.282113.
    Hs.700423.

    Genome annotation databases

    EnsembliENST00000270162; ENSP00000270162; ENSG00000142178.
    GeneIDi102724428.
    150094.
    KEGGihsa:102724428.
    hsa:150094.
    UCSCiuc002zdf.2. human.

    Polymorphism databases

    DMDMi59803093.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB047786 mRNA. Translation: BAD74070.1 .
    AP001751 Genomic DNA. Translation: BAA95536.1 .
    BC038504 mRNA. Translation: AAH38504.1 .
    AK131076 mRNA. Translation: BAC85126.1 .
    CCDSi CCDS33575.1.
    RefSeqi NP_775490.2. NM_173354.3.
    XP_006723983.1. XM_006723920.1.
    XP_006726866.1. XM_006726803.1.
    UniGenei Hs.282113.
    Hs.700423.

    3D structure databases

    ProteinModelPortali P57059.
    SMRi P57059. Positions 22-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127260. 12 interactions.
    IntActi P57059. 6 interactions.
    STRINGi 9606.ENSP00000270162.

    Chemistry

    BindingDBi P57059.
    ChEMBLi CHEMBL6082.
    GuidetoPHARMACOLOGYi 2197.

    PTM databases

    PhosphoSitei P57059.

    Polymorphism databases

    DMDMi 59803093.

    Proteomic databases

    MaxQBi P57059.
    PaxDbi P57059.
    PRIDEi P57059.

    Protocols and materials databases

    DNASUi 150094.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270162 ; ENSP00000270162 ; ENSG00000142178 .
    GeneIDi 102724428.
    150094.
    KEGGi hsa:102724428.
    hsa:150094.
    UCSCi uc002zdf.2. human.

    Organism-specific databases

    CTDi 150094.
    GeneCardsi GC21M044836.
    HGNCi HGNC:11142. SIK1.
    HPAi CAB023801.
    MIMi 605705. gene.
    neXtProti NX_P57059.
    PharmGKBi PA164725717.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000039981.
    InParanoidi P57059.
    KOi K16311.
    OMAi QIRQHRW.
    OrthoDBi EOG70ZZMM.
    PhylomeDBi P57059.
    TreeFami TF315213.

    Enzyme and pathway databases

    SignaLinki P57059.

    Miscellaneous databases

    ChiTaRSi SIK1. human.
    GeneWikii SNF1LK.
    GenomeRNAii 150094.
    NextBioi 86328.
    PROi P57059.
    SOURCEi Search...

    Gene expression databases

    Bgeei P57059.
    Genevestigatori P57059.

    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.
    SM00165. UBA. 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. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
      Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
      EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-182, MUTAGENESIS OF THR-182.
    2. Shimizu N., Kudoh J., Shibuya K.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal lung.
    3. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-615.
      Tissue: Testis.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-783, VARIANT VAL-615.
      Tissue: Spleen.
    6. "14-3-3 cooperates with LKB1 to regulate the activity and localization of QSK and SIK."
      Al-Hakim A.K., Goransson O., Deak M., Toth R., Campbell D.G., Morrice N.A., Prescott A.R., Alessi D.R.
      J. Cell Sci. 118:5661-5673(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAZ.
    7. "Importance of autophosphorylation at Ser186 in the A-loop of salt inducible kinase 1 for its sustained kinase activity."
      Hashimoto Y.K., Satoh T., Okamoto M., Takemori H.
      J. Cell. Biochem. 104:1724-1739(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-182 AND SER-186, INTERACTION WITH YWHAZ, MUTAGENESIS OF LYS-56; SER-135; SER-186; SER-209 AND SER-248.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: FUNCTION, MUTAGENESIS OF LYS-56.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-15; ASN-142; SER-211; ASP-469; VAL-615; LEU-696 AND VAL-725.

    Entry informationi

    Entry nameiSIK1_HUMAN
    AccessioniPrimary (citable) accession number: P57059
    Secondary accession number(s): A6NC84
    , Q5R2V5, Q6ZNL8, Q86YJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3