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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.
02-JUN-2021, entry version 173.
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, ACTIVITY 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:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
Evidence={ECO:0000269|PubMed:15177563, ECO:0000269|PubMed:16148943,
ECO:0000269|PubMed:17468767, ECO:0000269|PubMed:19244231};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={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};
-!- ACTIVITY 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.
SMR; Q60670; -.
BioGRID; 201531; 3.
IntAct; Q60670; 1.
STRING; 10090.ENSMUSP00000024839; -.
iPTMnet; Q60670; -.
PhosphoSitePlus; Q60670; -.
MaxQB; Q60670; -.
PaxDb; Q60670; -.
PRIDE; Q60670; -.
ProteomicsDB; 261041; -.
DNASU; 17691; -.
Ensembl; ENSMUST00000024839; ENSMUSP00000024839; ENSMUSG00000024042.
GeneID; 17691; -.
KEGG; mmu:17691; -.
UCSC; uc008bvr.1; mouse.
CTD; 150094; -.
MGI; MGI:104754; Sik1.
eggNOG; KOG0586; Eukaryota.
GeneTree; ENSGT00940000154989; -.
HOGENOM; CLU_000288_87_2_1; -.
InParanoid; Q60670; -.
OMA; LHISAGP; -.
OrthoDB; 1127668at2759; -.
TreeFam; TF315213; -.
BioGRID-ORCS; 17691; 1 hit in 46 CRISPR screens.
ChiTaRS; Nop58; mouse.
PRO; PR:Q60670; -.
Proteomes; UP000000589; Chromosome 17.
RNAct; Q60670; protein.
Bgee; ENSMUSG00000024042; Expressed in granulocyte and 279 other tissues.
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:0106310; F:protein serine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC.
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:0042149; P:cellular response to glucose starvation; 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; Cytoplasm;
Developmental protein; Differentiation; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tumor suppressor.
CHAIN 1..779
/note="Serine/threonine-protein kinase SIK1"
/id="PRO_0000086660"
DOMAIN 27..278
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
DOMAIN 303..343
/note="UBA"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
NP_BIND 33..41
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 350..375
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 449..472
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 586..612
/note="RK-rich region"
REGION 621..641
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 352..375
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 149
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 56
/note="ATP"
MOD_RES 182
/note="Phosphothreonine; by LKB1 and GSK3-beta"
/evidence="ECO:0000269|PubMed:16817901"
MOD_RES 186
/note="Phosphoserine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P57059"
MOD_RES 322
/note="Phosphothreonine; by CaMK1"
/evidence="ECO:0000250|UniProtKB:Q9R1U5"
MOD_RES 577
/note="Phosphoserine; by PKA"
/evidence="ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17468767"
MUTAGEN 56
/note="K->M: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:15177563,
ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17468767"
MUTAGEN 182
/note="T->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:16817901"
MUTAGEN 182
/note="T->E: Low levels of constitutive activity."
/evidence="ECO:0000269|PubMed:16817901"
MUTAGEN 268
/note="T->A: Does not affect phosphorylation by PKA and
nuclear export following ACTH treatment."
/evidence="ECO:0000269|PubMed:12200423"
MUTAGEN 475
/note="T->A: Does not affect phosphorylation by PKA and
nuclear export following ACTH treatment."
/evidence="ECO:0000269|PubMed:12200423"
MUTAGEN 577
/note="S->A: Abolishes phosphorylation by PKA and impairs
nuclear export following ACTH treatment."
/evidence="ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17468767"
MUTAGEN 577
/note="S->A: Constitutively active."
/evidence="ECO:0000269|PubMed:12200423,
ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17468767"
MUTAGEN 593..594
/note="RK->AA: Localizes mainly in cytoplasm and not in
nucleus."
/evidence="ECO:0000269|PubMed:15511237"
MUTAGEN 597..599
/note="RTK->ATA: Localizes mainly in cytoplasm and not in
nucleus."
/evidence="ECO:0000269|PubMed:15511237"
MUTAGEN 606..608
/note="KIK->AIA: Localizes mainly in cytoplasm and not in
nucleus."
/evidence="ECO:0000269|PubMed:15511237"
MUTAGEN 607
/note="I->A: Localizes mainly in cytoplasm and not in
nucleus; when associated with D-483 and A-610."
/evidence="ECO:0000269|PubMed:15511237"
MUTAGEN 610
/note="L->A: Localizes mainly in cytoplasm and not in
nucleus; when associated with D-483 and A-607."
/evidence="ECO:0000269|PubMed:15511237"
CONFLICT 183..184
/note="WC -> CV (in Ref. 1; AAA67926)"
/evidence="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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Pathways :
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WP253: Glycolysis
WP1703: Streptomycin biosynthesis
WP2199: Seed Development
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1946: Cori Cycle
WP1701: Starch and sucrose metabolism
WP2185: Purine metabolism
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2032: TSH signaling pathway
WP1049: G Protein Signaling Pathways
WP1692: Protein export
WP1438: Influenza A virus infection
WP1700: Selenoamino acid metabolism
WP35: G Protein Signaling Pathways
WP218: Serine and Glycine biosynthesis
WP1665: Limonene and pinene degradation
WP2203: TSLP Signaling Pathway

Related Genes :
[Sik1 Msk Sik Snf1lk] 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 SIK SNF1LK] Serine/threonine-protein kinase SIK1 (EC 2.7.11.1) (Salt-inducible kinase 1) (SIK-1) (Serine/threonine-protein kinase SNF1-like kinase 1) (Serine/threonine-protein kinase SNF1LK)
[Sik2 Snf1lk2] Serine/threonine-protein kinase SIK2 (EC 2.7.11.1) (Salt-inducible kinase 2) (SIK-2) (Serine/threonine-protein kinase SNF1-like kinase 2)
[CIPK14 PKS24 SnRK3.15 SR1 At5g01820 T20L15.90] CBL-interacting serine/threonine-protein kinase 14 (EC 2.7.11.1) (SNF1-related kinase 3.15) (SOS2-like protein kinase PKS24) (Serine/threonine-protein kinase SR1) (AtSR1)
[CIPK24 SnRK3.11 SOS2 At5g35410 F6I13.1 K21B8.3] CBL-interacting serine/threonine-protein kinase 24 (EC 2.7.11.1) (Protein SALT OVERLY SENSITIVE 2) (SNF1-related kinase 3.11)
[CIPK7 PKS7 SnRK3.10 SR2 SRPK1 At3g23000 MXC7.3] CBL-interacting serine/threonine-protein kinase 7 (EC 2.7.11.1) (SNF1-related kinase 3.10) (SOS2-like protein kinase PKS7) (Serine/threonine-protein kinase SR2) (AtSR2) (AtSRPK1)
[CIPK9 PKS6 SnRK3.12 At1g01140 F6F3.28 T25K16.13] CBL-interacting serine/threonine-protein kinase 9 (EC 2.7.11.1) (SNF1-related kinase 3.12) (SOS2-like protein kinase PKS6)
[CIPK6 PKS4 SIP3 SnRK3.14 At4g30960 F6I18.130] CBL-interacting serine/threonine-protein kinase 6 (EC 2.7.11.1) (SNF1-related kinase 3.14) (SOS2-like protein kinase PKS4) (SOS3-interacting protein 3)
[CIPK23 LKS1 PKS17 SnRK3.23 At1g30270 F12P21.6] CBL-interacting serine/threonine-protein kinase 23 (EC 2.7.11.1) (Protein LOW-K(+)-SENSITIVE 1) (SNF1-related kinase 3.23) (SOS2-like protein kinase PKS17)
[SRK2E OST1 SNRK2.6 At4g33950 F17I5.140] Serine/threonine-protein kinase SRK2E (EC 2.7.11.1) (Protein OPEN STOMATA 1) (SNF1-related kinase 2.6) (SnRK2.6) (Serine/threonine-protein kinase OST1)
[CIPK16 PKS15 SnRK3.18 At2g25090 F13D4.161] CBL-interacting serine/threonine-protein kinase 16 (EC 2.7.11.1) (SNF1-related kinase 3.18) (SOS2-like protein kinase PKS15)
[Snrk] SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase)
[SNRK KIAA0096 SNFRK] SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase)
[KIN10 AK21 AKIN10 SKIN10 SNR2 SNRK1.1 At3g01090 T4P13.22] SNF1-related protein kinase catalytic subunit alpha KIN10 (AKIN10) (EC 2.7.11.1) (AKIN alpha-2) (AKINalpha2) (SNF1-related kinase 1.1) (SnRK1.1)
[NUAK2 OMPHK2 SNARK] NUAK family SNF1-like kinase 2 (EC 2.7.11.1) (Omphalocele kinase 2) (SNF1/AMP kinase-related kinase) (SNARK)
[KIN11 AKIN11 SNR1 SNRK1.2 At3g29160 MXE2.16] SNF1-related protein kinase catalytic subunit alpha KIN11 (AKIN11) (EC 2.7.11.1) (AKIN alpha-1) (AKINalpha1) (SNF1-related kinase 1.2) (SnRK1.2)
[Nuak2] NUAK family SNF1-like kinase 2 (EC 2.7.11.1) (SNF1/AMP kinase-related kinase) (SNARK)
[Nuak1 Kiaa0537 Omphk1] NUAK family SNF1-like kinase 1 (EC 2.7.11.1) (AMPK-related protein kinase 5) (Omphalocele kinase 1)
[AMPKalpha AK AMPK ampk AMPK alpha AMPK-alpha AmpKalpha ampkalpha dAMPK dAMPKa dAMPKalpha DmAMPK alpha Dmel\CG3051 EG:132E8.2 FBgn0023169 Gprk-4 Gprk4 SNF1A snf1A snf1a SNF1A-RA SNF4A-a CG3051 Dmel_CG3051] AMP-activated protein kinase alpha subunit, isoform A (EC 2.7.11.-) (EC 2.7.11.16) (AMP-activated protein kinase alpha subunit, isoform B) (AMP-activated protein kinase alpha subunit, isoform C) (EG:132E8.2 protein) (FI03728p) (SNF1A/AMP-activated protein kinase)
[BRSK1 KIAA1811 SAD1 SADB] Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (Brain-selective kinase 1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B) (Synapses of Amphids Defective homolog 1) (SAD1 homolog) (hSAD1)
[GSK3B] Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)
[Brsk1 Gm1100 Sadb] Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B)
[Brsk1 Sadb] Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B)
[SAK1 PAK1 YER129W SYGP-ORF45] SNF1-activating kinase 1 (EC 2.7.11.1)
[kin-29 sma-11 F58H12.1] Serine/threonine-protein kinase kin-29 (EC 2.7.11.1)
[Mark1 Emk3 Kiaa1477] Serine/threonine-protein kinase MARK1 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif serine/threonine-protein kinase 3) (MAP/microtubule affinity-regulating kinase 1) (PAR1 homolog c) (Par-1c) (mPar-1c)
[Snrk] SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase)
[MARK2 EMK1] Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2) (PAR1 homolog) (PAR1 homolog b) (Par-1b) (Par1b)
[Mark2] Serine/threonine-protein kinase MARK2 (EC 2.7.11.1) (EC 2.7.11.26) (ELKL motif kinase 1) (EMK-1) (MAP/microtubule affinity-regulating kinase 2)
[SNF4 CBSCBS3 At1g09020 F7G19.11] Sucrose nonfermenting 4-like protein (SNF4) (CBS domain-containing protein CBSCBS3) (SNF1-related protein kinase regulatory subunit betagamma) (AKIN subunit betagamma) (AKINbetagamma)

Bibliography :