SNRK_MOUSE
ID SNRK_MOUSE Reviewed; 748 AA.
AC Q8VDU5; Q91WX6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=SNF-related serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE AltName: Full=SNF1-related kinase;
GN Name=Snrk {ECO:0000312|MGI:MGI:108104};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK97440.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAK97440.1};
RC TISSUE=Yolk sac {ECO:0000312|EMBL:AAK97440.1};
RX PubMed=12234663; DOI=10.1016/s0378-1119(02)00829-6;
RA Kertesz N., Samson J., Debacker C., Wu H., Labastie M.-C.;
RT "Cloning and characterization of human and mouse SNRK sucrose non-
RT fermenting protein (SNF-1)-related kinases.";
RL Gene 294:13-24(2002).
RN [2] {ECO:0000312|EMBL:AAH94658.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH94658.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH20189.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH94658.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH20189.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-362 AND SER-482, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-534, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May play a role in hematopoietic cell proliferation or
CC differentiation. Potential mediator of neuronal apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:Q63553,
CC ECO:0000250|UniProtKB:Q9NRH2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q63553,
CC ECO:0000250|UniProtKB:Q9NRH2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q63553,
CC ECO:0000250|UniProtKB:Q9NRH2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q63553,
CC ECO:0000250|UniProtKB:Q9NRH2};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-173.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined.
CC {ECO:0000269|PubMed:12234663}.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 8 dpc along the epithelium of
CC the differentiating neural tube. Expression persists along the dorsal
CC axis until 12.5 dpc, but becomes progressively restricted to the more
CC caudal part of the neural tube with much stronger intensity in the
CC caudal neuropore. Also observed in the endoderm of the primitive gut
CC between 8.5 and 11.5 dpc, at 10.5 dpc, in the endocardium and
CC pericardium of the developing heart, and in both the endothelium and
CC blood cells clustered at the ventral part of the dorsal aorta. Later in
CC development (12.5 dpc), expressed in the endocardium and the
CC interventricular septum of the heart. {ECO:0000269|PubMed:12234663}.
CC -!- PTM: Autophosphorylated. Phosphorylation on Thr-173 by STK11/LKB1 in
CC complex with STE20-related adapter-alpha (STRADA) pseudo kinase and
CC CAB39 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF387809; AAK97440.1; -; mRNA.
DR EMBL; BC020189; AAH20189.1; -; mRNA.
DR EMBL; BC094658; AAH94658.1; -; mRNA.
DR CCDS; CCDS23644.1; -.
DR RefSeq; NP_001158044.1; NM_001164572.1.
DR RefSeq; NP_598502.2; NM_133741.2.
DR RefSeq; XP_006512061.1; XM_006511998.3.
DR RefSeq; XP_006512062.1; XM_006511999.3.
DR RefSeq; XP_006512063.1; XM_006512000.3.
DR RefSeq; XP_006512065.1; XM_006512002.3.
DR RefSeq; XP_006512066.1; XM_006512003.3.
DR AlphaFoldDB; Q8VDU5; -.
DR SMR; Q8VDU5; -.
DR BioGRID; 203371; 2.
DR IntAct; Q8VDU5; 1.
DR MINT; Q8VDU5; -.
DR STRING; 10090.ENSMUSP00000112919; -.
DR iPTMnet; Q8VDU5; -.
DR PhosphoSitePlus; Q8VDU5; -.
DR SwissPalm; Q8VDU5; -.
DR jPOST; Q8VDU5; -.
DR MaxQB; Q8VDU5; -.
DR PaxDb; Q8VDU5; -.
DR PeptideAtlas; Q8VDU5; -.
DR PRIDE; Q8VDU5; -.
DR ProteomicsDB; 261092; -.
DR Antibodypedia; 29346; 157 antibodies from 29 providers.
DR DNASU; 20623; -.
DR Ensembl; ENSMUST00000118886; ENSMUSP00000114132; ENSMUSG00000038145.
DR Ensembl; ENSMUST00000120173; ENSMUSP00000112919; ENSMUSG00000038145.
DR GeneID; 20623; -.
DR KEGG; mmu:20623; -.
DR UCSC; uc009sen.2; mouse.
DR CTD; 54861; -.
DR MGI; MGI:108104; Snrk.
DR VEuPathDB; HostDB:ENSMUSG00000038145; -.
DR eggNOG; KOG4717; Eukaryota.
DR GeneTree; ENSGT00940000155365; -.
DR HOGENOM; CLU_007233_3_0_1; -.
DR InParanoid; Q8VDU5; -.
DR OMA; VGSIKFF; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q8VDU5; -.
DR TreeFam; TF351991; -.
DR BioGRID-ORCS; 20623; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Snrk; mouse.
DR PRO; PR:Q8VDU5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VDU5; protein.
DR Bgee; ENSMUSG00000038145; Expressed in cerebellar vermis and 260 other tissues.
DR ExpressionAtlas; Q8VDU5; baseline and differential.
DR Genevisible; Q8VDU5; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..748
FT /note="SNF-related serine/threonine-protein kinase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000225606"
FT DOMAIN 16..269
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 291..334
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 383..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P57059,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P57059,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P57059,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000250|UniProtKB:Q9NRH2"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRH2"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63553"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRH2"
FT MOD_RES 534
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRH2"
FT CONFLICT 5
FT /note="K -> R (in Ref. 1; AAK97440)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> D (in Ref. 1; AAK97440)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> K (in Ref. 1; AAK97440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 81913 MW; 9E3F7EA90136FCDA CRC64;
MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL
FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF
AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY
SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPPRVSA
GCRDLITRML QRDPKRRASL EEIESHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ
RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA SPSNIKAQFR
QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAGDNVLN GHRSKGLCDP AKKDELPELA
GPALSTVPPA SMKPAASGRK CLFRVEEDEE EDEEDKKPVS LSTQVVLRRK PSVTNRLTSR
KSAPVLNQIF EEGESDDEFD MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS
SETSDDDSES RRRLDKDSGF AYSWHRRDSS EGPPGSEGDG GGQSKPSSGG GVDKASPGEQ
GTGGGSQGGS GGTPSGTAGS SRRCAGPDSS SPSPASASAA PRGAELVQSL KLVSLCLGSQ
LHGAKYILDP QKALFSSVKV QEKSTWKMCI SAPGPSPSAD LDPVRTKKLR NNALQLPLCE
KTISVNIQRS RKEGLLCASS PASCCHVI
