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Serine/threonine-protein kinase SIK1 (EC 2.7.11.1) (HRT-20) (Myocardial SNF1-like kinase) (Salt-inducible kinase 1) (SIK-1) (Serine/threonine-protein kinase SNF1-like kinase 1) (Serine/threonine-protein kinase SNF1LK)

 SIK1_MOUSE              Reviewed;         779 AA.
Q60670; Q3UR46;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 3.
20-JUN-2018, entry version 157.
RecName: Full=Serine/threonine-protein kinase SIK1;
EC=2.7.11.1 {ECO:0000269|PubMed:15177563, ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:19244231};
AltName: Full=HRT-20;
AltName: Full=Myocardial SNF1-like kinase;
AltName: Full=Salt-inducible kinase 1;
Short=SIK-1;
AltName: Full=Serine/threonine-protein kinase SNF1-like kinase 1;
Short=Serine/threonine-protein kinase SNF1LK;
Name=Sik1; Synonyms=Msk, Sik, Snf1lk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=7893599; DOI=10.1016/0925-4773(94)90056-6;
Ruiz J.C., Conlon F.L., Robertson E.J.;
"Identification of novel protein kinases expressed in the myocardium
of the developing mouse heart.";
Mech. Dev. 48:153-164(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-577, AND
MUTAGENESIS OF THR-268; THR-475 AND SER-577.
PubMed=12200423; DOI=10.1074/jbc.M204602200;
Takemori H., Katoh Y., Horike N., Doi J., Okamoto M.;
"ACTH-induced nucleocytoplasmic translocation of salt-inducible
kinase. Implication in the protein kinase A-activated gene
transcription in mouse adrenocortical tumor cells.";
J. Biol. Chem. 277:42334-42343(2002).
[4]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN RK-RICH REGION, AND MUTAGENESIS
OF 593-ARG-LYS-594; 597-ARG--LYS-599; 606-LYS--LYS-608; ILE-607 AND
LEU-610.
PubMed=15511237; DOI=10.1111/j.1432-1033.2004.04372.x;
Katoh Y., Takemori H., Min L., Muraoka M., Doi J., Horike N.,
Okamoto M.;
"Salt-inducible kinase-1 represses cAMP response element-binding
protein activity both in the nucleus and in the cytoplasm.";
Eur. J. Biochem. 271:4307-4319(2004).
[5]
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-56.
PubMed=15177563; DOI=10.1016/j.ygeno.2003.12.007;
Stephenson A., Huang G.Y., Nguyen N.T., Reuter S., McBride J.L.,
Ruiz J.C.;
"snf1lk encodes a protein kinase that may function in cell cycle
regulation.";
Genomics 83:1105-1115(2004).
[6]
FUNCTION IN PHOSPHORYLATION OF CRTC2, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=16148943; DOI=10.1038/nature03967;
Koo S.-H., Flechner L., Qi L., Zhang X., Screaton R.A., Jeffries S.,
Hedrick S., Xu W., Boussouar F., Brindle P., Takemori H., Montminy M.;
"The CREB coactivator TORC2 is a key regulator of fasting glucose
metabolism.";
Nature 437:1109-1111(2005).
[7]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
THR-182 AND SER-577, AND MUTAGENESIS OF LYS-56; THR-182 AND SER-577.
PubMed=16817901; DOI=10.1111/j.1742-4658.2006.05291.x;
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.;
"Silencing the constitutive active transcription factor CREB by the
LKB1-SIK signaling cascade.";
FEBS J. 273:2730-2748(2006).
[8]
FUNCTION IN PHOSPHORYLATION OF HDAC4 AND HDAC5, CATALYTIC ACTIVITY,
INDUCTION, PHOSPHORYLATION AT SER-577, AND MUTAGENESIS OF LYS-56 AND
SER-577.
PubMed=17468767; DOI=10.1038/nm1573;
Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T.,
Shelton G.D., Montminy M.;
"SIK1 is a class II HDAC kinase that promotes survival of skeletal
myocytes.";
Nat. Med. 13:597-603(2007).
[9]
FUNCTION.
PubMed=19622832; DOI=10.1126/scisignal.2000369;
Cheng H., Liu P., Wang Z.C., Zou L., Santiago S., Garbitt V.,
Gjoerup O.V., Iglehart J.D., Miron A., Richardson A.L., Hahn W.C.,
Zhao J.J.;
"SIK1 couples LKB1 to p53-dependent anoikis and suppresses
metastasis.";
Sci. Signal. 2:RA35-RA35(2009).
[10]
FUNCTION IN PHOSPHORYLATION OF SREBF1, AND CATALYTIC ACTIVITY.
PubMed=19244231; DOI=10.1074/jbc.M900096200;
Yoon Y.S., Seo W.Y., Lee M.W., Kim S.T., Koo S.H.;
"Salt-inducible kinase regulates hepatic lipogenesis by controlling
SREBP-1c phosphorylation.";
J. Biol. Chem. 284:10446-10452(2009).
[11]
FUNCTION.
PubMed=20140255; DOI=10.1371/journal.pone.0009029;
Romito A., Lonardo E., Roma G., Minchiotti G., Ballabio A.,
Cobellis G.;
"Lack of sik1 in mouse embryonic stem cells impairs cardiomyogenesis
by down-regulating the cyclin-dependent kinase inhibitor p57kip2.";
PLoS ONE 5:E9029-E9029(2010).
[12]
FUNCTION.
PubMed=23993098; DOI=10.1016/j.cell.2013.08.004;
Jagannath A., Butler R., Godinho S.I., Couch Y., Brown L.A.,
Vasudevan S.R., Flanagan K.C., Anthony D., Churchill G.C., Wood M.J.,
Steiner G., Ebeling M., Hossbach M., Wettstein J.G., Duffield G.E.,
Gatti S., Hankins M.W., Foster R.G., Peirson S.N.;
"The CRTC1-SIK1 pathway regulates entrainment of the circadian
clock.";
Cell 154:1100-1111(2013).
-!- FUNCTION: 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,
CRTC1/TORC1 and CRTC2/TORC2. 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 CRTC1/TORC1 and
CRTC2/TORC2, leading to inhibit CREB activity. Also regulates
hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In
concert with CRTC1/TORC1, regulates the light-induced entrainment
of the circadian clock by attenuating PER1 induction; represses
CREB-mediated transcription of PER1 by phosphorylating and
deactivating CRTC1/TORC1. {ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:15177563, ECO:0000269|PubMed:15511237,
ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:19244231,
ECO:0000269|PubMed:19622832, ECO:0000269|PubMed:20140255,
ECO:0000269|PubMed:23993098}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:15177563, ECO:0000269|PubMed:16148943,
ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:19244231}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: 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. {ECO:0000269|PubMed:16817901}.
-!- SUBUNIT: Interacts (when phosphorylated on Thr-182 and Ser-186)
with YWHAZ. Interacts with ATP1A1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Following ACTH
(adrenocorticotropic hormone) treatment and subsequent
phosphorylation by PKA, translocates to the cytoplasm, where it
binds to YWHAZ.
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:15177563,
ECO:0000269|PubMed:7893599}.
-!- INDUCTION: Expression is stimulated by CREB1 in myocytes; direct
target of CREB1. {ECO:0000269|PubMed:17468767}.
-!- DOMAIN: The RK-rich region determines the subcellular location.
{ECO:0000269|PubMed:15511237}.
-!- PTM: 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.
{ECO:0000269|PubMed:12200423, ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17468767}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. AMPK subfamily. {ECO:0000305}.
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EMBL; U11494; AAA67926.2; -; mRNA.
EMBL; AK141817; BAE24842.1; -; mRNA.
CCDS; CCDS37552.1; -.
PIR; I49072; I49072.
RefSeq; NP_034961.2; NM_010831.3.
UniGene; Mm.290941; -.
ProteinModelPortal; Q60670; -.
SMR; Q60670; -.
STRING; 10090.ENSMUSP00000024839; -.
iPTMnet; Q60670; -.
PhosphoSitePlus; Q60670; -.
MaxQB; Q60670; -.
PaxDb; Q60670; -.
PRIDE; Q60670; -.
DNASU; 17691; -.
Ensembl; ENSMUST00000024839; ENSMUSP00000024839; ENSMUSG00000024042.
GeneID; 17691; -.
KEGG; mmu:17691; -.
UCSC; uc008bvr.1; mouse.
CTD; 150094; -.
MGI; MGI:104754; Sik1.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00900000140806; -.
HOGENOM; HOG000039981; -.
InParanoid; Q60670; -.
KO; K19008; -.
OMA; RQHRWMQ; -.
OrthoDB; EOG091G03A4; -.
TreeFam; TF315213; -.
ChiTaRS; Nop58; mouse.
PRO; PR:Q60670; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024042; -.
CleanEx; MM_SNF1LK; -.
Genevisible; Q60670; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0008140; F:cAMP response element binding protein binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0043276; P:anoikis; IMP:BHF-UCL.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0032792; P:negative regulation of CREB transcription factor activity; IDA:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0010868; P:negative regulation of triglyceride biosynthetic process; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; IEP:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0010830; P:regulation of myotube differentiation; IDA:UniProtKB.
GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
CDD; cd14071; STKc_SIK; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR017090; Ser/Thr_kinase_SIK1/2.
InterPro; IPR034672; SIK.
InterPro; IPR015940; UBA.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF037014; Ser/Thr_PK_SNF1-like; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50030; UBA; 1.
1: Evidence at protein level;
ATP-binding; Biological rhythms; Cell cycle; Complete proteome;
Cytoplasm; Developmental protein; Differentiation; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tumor suppressor.
CHAIN 1 779 Serine/threonine-protein kinase SIK1.
/FTId=PRO_0000086660.
DOMAIN 27 278 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 303 343 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
NP_BIND 33 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 586 612 RK-rich region.
ACT_SITE 149 149 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 56 56 ATP.
MOD_RES 182 182 Phosphothreonine; by LKB1 and GSK3-beta.
{ECO:0000269|PubMed:16817901}.
MOD_RES 186 186 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P57059}.
MOD_RES 322 322 Phosphothreonine; by CaMK1.
{ECO:0000250|UniProtKB:Q9R1U5}.
MOD_RES 577 577 Phosphoserine; by PKA.
{ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17468767}.
MUTAGEN 56 56 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:15177563,
ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17468767}.
MUTAGEN 182 182 T->A: Loss of kinase activity.
{ECO:0000269|PubMed:16817901}.
MUTAGEN 182 182 T->E: Low levels of constitutive
activity. {ECO:0000269|PubMed:16817901}.
MUTAGEN 268 268 T->A: Does not affect phosphorylation by
PKA and nuclear export following ACTH
treatment. {ECO:0000269|PubMed:12200423}.
MUTAGEN 475 475 T->A: Does not affect phosphorylation by
PKA and nuclear export following ACTH
treatment. {ECO:0000269|PubMed:12200423}.
MUTAGEN 577 577 S->A: Abolishes phosphorylation by PKA
and impairs nuclear export following ACTH
treatment. {ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17468767}.
MUTAGEN 577 577 S->A: Constitutively active.
{ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:16817901,
ECO:0000269|PubMed:17468767}.
MUTAGEN 593 594 RK->AA: Localizes mainly in cytoplasm and
not in nucleus.
{ECO:0000269|PubMed:15511237}.
MUTAGEN 597 599 RTK->ATA: Localizes mainly in cytoplasm
and not in nucleus.
{ECO:0000269|PubMed:15511237}.
MUTAGEN 606 608 KIK->AIA: Localizes mainly in cytoplasm
and not in nucleus.
{ECO:0000269|PubMed:15511237}.
MUTAGEN 607 607 I->A: Localizes mainly in cytoplasm and
not in nucleus; when associated with D-
483 and A-610.
{ECO:0000269|PubMed:15511237}.
MUTAGEN 610 610 L->A: Localizes mainly in cytoplasm and
not in nucleus; when associated with D-
483 and A-607.
{ECO:0000269|PubMed:15511237}.
CONFLICT 183 184 WC -> CV (in Ref. 1; AAA67926).
{ECO:0000305}.
SEQUENCE 779 AA; 85115 MW; 9C4D25CCF0C0D06D CRC64;
MVIMSEFSAV PSGTGQGQQK PLRVGFYDVE RTLGKGNFAV VKLARHRVTK TQVAIKIIDK
TRLDSSNLEK IYREVQLMKL LNHPNIIKLY QVMETKDMLY IVTEFAKNGE MFDYLTSNGH
LSENEARQKF WQILSAVEYC HNHHIVHRDL KTENLLLDSN MDIKLADFGF GNFYKPGEPL
STWCGSPPYA APEVFEGKEY EGPQLDVWSL GVVLYVLVCG SLPFDGPNLP TLRQRVLEGR
FRIPFFMSQD CETLIRRMLV VDPAKRITIA QIRQHRWMQA DPTLLQQDDP AFDMQGYTSN
LGDYNEQVLG IMQALGIDRQ RTIESLQNSS YNHFAAIYYL LLERLKEHRS AQPSSRPTPA
PTRQPQLRSS DLSSLEVPQE ILPCDPFRPS LLCPQPQALA QSVLQAEIDC DLHSSLQPLL
FPLDTNCSGV FRHRSISPSS LLDTAISEEA RQGPSLEEEQ EVQEPLPGST GRRHTLAEVS
THFSPLNPPC IIVSSSATAS PSEGTSSDSC LPFSASEGPA GLGSGLATPG LLGTSSPVRL
ASPFLGSQSA TPVLQTQAGL GTAVLPPVSF QEGRRASDTS LTQGLKAFRQ QLRKNARTKG
FLGLNKIKGL ARQVCQSSVR TPRGGMSTFH TPAPSSGLQG CTTSNREGRS LLEEVLHQQR
LLQLQHHSST AAASSGCQQG PQLSPVPYVL APCDSLLVSG IPLLPTPLLQ AGMSPVASAA
HLLDTHLHIS AGPVALPTGP LPQCLTRLSP GCDPAGLPQG DCEMEDLTSG QRGTFVLVQ


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EIAAB38467 HRT-20,Mouse,Msk,Mus musculus,Myocardial SNF1-like kinase,Salt-inducible protein kinase 1,Serine_threonine-protein kinase SIK1,Serine_threonine-protein kinase SNF1-like kinase 1,Serine_threonine-prote
EIAAB38466 Homo sapiens,Human,Salt-inducible protein kinase 1,Serine_threonine-protein kinase SIK1,Serine_threonine-protein kinase SNF1-like kinase 1,Serine_threonine-protein kinase SNF1LK,SIK,SIK1,SIK-1,SNF1LK
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB38465 Kid2,Protein kinase KID2,Rat,Rattus norvegicus,Salt-inducible protein kinase 1,Serine_threonine-protein kinase SIK1,Serine_threonine-protein kinase SNF1-like kinase 1,Serine_threonine-protein kinase S
31-031 Cdk7 is the catalytic subunit of the CDK-activating kinase (CAK) complex, a serine-threonine kinase. CAK activates the cyclin-associated kinases CDC2_CDK1, CDK2, CDK4 and CDK6 by threonine phosphoryla 0.1 mg
EH1603 Serine per threonine-protein kinase SIK1 Elisa Kit 96T
MKNK1_RAT Rat ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 1 96T
MKNK1_MOUSE ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 1; organism: Mouse; gene name: Mknk1 96T
MKNK2_MOUSE ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 2; organism: Mouse; gene name: Mknk2 96T
H0344 Serine threonine-protein kinase SIK1 (SIK1), Human, ELISA Kit 96T
H0345 Serine threonine-protein kinase SIK1 (SIK1), Mouse, ELISA Kit 96T
H0346 Serine threonine-protein kinase SIK1 (SIK1), Rat, ELISA Kit 96T
SIK1_RAT ELISA Kit FOR Serine per threonine-protein kinase SIK1; organism: Rat; gene name: Sik1 96T
SIK1_MOUSE ELISA Kit FOR Serine per threonine-protein kinase SIK1; organism: Mouse; gene name: Sik1 96T
EIAAB38469 Homo sapiens,Human,KIAA0781,QIK,Qin-induced kinase,Salt-inducible protein kinase 2,Serine_threonine-protein kinase SIK2,Serine_threonine-protein kinase SNF1-like kinase 2,SIK2,SIK-2,SNF1LK2
AS10 1601 rabbit polyclonal STN8 kinase | serine per threonine-protein kinase STN8, chloroplastic 100 ug - for reconstitution please add 100 ul of sterile water
31-052 AKT1 is a general protein kinase capable of phosphorylating several known proteins.The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and i 0.05 mg
EIAAB38468 Chicken,Gallus gallus,QIK,Qin-induced kinase,Salt-inducible protein kinase 2,Serine_threonine-protein kinase SIK2,Serine_threonine-protein kinase SNF1-like kinase 2,SIK2,SIK-2,SNF1LK2
GWB-5BE1E2 Serine_threonine-protein kinase SNF1-like kinase 2 (SNF1LK2)_Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
GWB-CEE83D Serine_threonine-protein kinase SNF1-like kinase 2 (SNF1LK2)_Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
EIAAB38470 Mouse,Mus musculus,Salt-inducible protein kinase 2,Serine_threonine-protein kinase SIK2,Serine_threonine-protein kinase SNF1-like kinase 2,Sik2,SIK-2,Snf1lk2
GWB-1BE6A4 Serine threonine Kinase TAO Kinase 3 (TAOK3) Goat anti-Human Polyclonal (Internal) Antibody


 

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