SNRK_HUMAN
ID SNRK_HUMAN Reviewed; 765 AA.
AC Q9NRH2; B2RAV6; Q14706; Q68D15; Q6IQ46; Q9NXI7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 175.
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|EMBL:AAH71567.1};
GN Synonyms=KIAA0096 {ECO:0000312|EMBL:BAA07744.2},
GN SNFRK {ECO:0000312|EMBL:AAF86944.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP AUTOPHOSPHORYLATION.
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION
RP AT THR-173, AND MUTAGENESIS OF THR-173.
RX PubMed=15733851; DOI=10.1016/j.febslet.2005.01.042;
RA Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,
RA Alessi D.R.;
RT "Identification of the sucrose non-fermenting related kinase SNRK, as a
RT novel LKB1 substrate.";
RL FEBS Lett. 579:1417-1423(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA07744.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow {ECO:0000305};
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [4] {ECO:0000305}
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAF86944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland {ECO:0000312|EMBL:AAF86944.1};
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAA91023.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon mucosa {ECO:0000312|EMBL:BAA91023.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAF86944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000305, ECO:0000312|EMBL:AAH71567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH71567.1};
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 [10] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=8654423; DOI=10.1111/j.1432-1033.1996.00736.x;
RA Becker W., Heukelbach J., Kentrup H., Joost H.G.;
RT "Molecular cloning and characterization of a novel mammalian protein kinase
RT harboring a homology domain that defines a subfamily of serine/threonine
RT kinases.";
RL Eur. J. Biochem. 235:736-743(1996).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-607, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-260; SER-391; SER-611; LEU-748 AND
RP MET-765.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: May play a role in hematopoietic cell proliferation or
CC differentiation. Potential mediator of neuronal apoptosis.
CC {ECO:0000250|UniProtKB:Q63553, ECO:0000269|PubMed:12234663,
CC ECO:0000269|PubMed:15733851}.
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:0000269|PubMed:12234663, ECO:0000269|PubMed:15733851};
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:0000269|PubMed:12234663,
CC ECO:0000269|PubMed:15733851};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12234663, ECO:0000269|PubMed:15733851};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-173.
CC {ECO:0000269|PubMed:15733851}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12234663, ECO:0000269|PubMed:15489334,
CC ECO:0000269|PubMed:7788527};
CC IsoId=Q9NRH2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14702039};
CC IsoId=Q9NRH2-2; Sequence=VSP_051959, VSP_051960;
CC -!- TISSUE SPECIFICITY: Expressed in hematopoietic progenitor cells and
CC leukemic cell lines. Weakly expressed in the testis.
CC {ECO:0000269|PubMed:12234663, ECO:0000269|PubMed:8654423}.
CC -!- PTM: Autophosphorylated. Phosphorylation on Thr-173 by STK11/LKB1 in
CC complex with STE20-related adapter-alpha (STRADA) pseudo kinase and
CC CAB39. {ECO:0000269|PubMed:15733851}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07744.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAH18415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D43636; BAA07744.2; ALT_INIT; mRNA.
DR EMBL; AF226044; AAF86944.1; -; mRNA.
DR EMBL; AK000231; BAA91023.1; -; mRNA.
DR EMBL; AK314376; BAG37003.1; -; mRNA.
DR EMBL; CR749621; CAH18415.1; ALT_INIT; mRNA.
DR EMBL; CH471055; EAW64693.1; -; Genomic_DNA.
DR EMBL; BC071567; AAH71567.1; -; mRNA.
DR CCDS; CCDS43075.1; -. [Q9NRH2-1]
DR RefSeq; NP_001094064.1; NM_001100594.1. [Q9NRH2-1]
DR RefSeq; NP_001317679.1; NM_001330750.1.
DR RefSeq; NP_060189.3; NM_017719.4. [Q9NRH2-1]
DR RefSeq; XP_005265302.1; XM_005265245.3. [Q9NRH2-1]
DR PDB; 5YKS; X-ray; 2.90 A; A/B=1-356.
DR PDBsum; 5YKS; -.
DR AlphaFoldDB; Q9NRH2; -.
DR SMR; Q9NRH2; -.
DR BioGRID; 120211; 14.
DR IntAct; Q9NRH2; 20.
DR MINT; Q9NRH2; -.
DR STRING; 9606.ENSP00000296088; -.
DR BindingDB; Q9NRH2; -.
DR ChEMBL; CHEMBL1908384; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9NRH2; -.
DR iPTMnet; Q9NRH2; -.
DR PhosphoSitePlus; Q9NRH2; -.
DR BioMuta; SNRK; -.
DR DMDM; 90185235; -.
DR EPD; Q9NRH2; -.
DR jPOST; Q9NRH2; -.
DR MassIVE; Q9NRH2; -.
DR MaxQB; Q9NRH2; -.
DR PaxDb; Q9NRH2; -.
DR PeptideAtlas; Q9NRH2; -.
DR PRIDE; Q9NRH2; -.
DR ProteomicsDB; 82362; -. [Q9NRH2-1]
DR ProteomicsDB; 82363; -. [Q9NRH2-2]
DR Antibodypedia; 29346; 157 antibodies from 29 providers.
DR DNASU; 54861; -.
DR Ensembl; ENST00000296088.12; ENSP00000296088.7; ENSG00000163788.14. [Q9NRH2-1]
DR Ensembl; ENST00000429705.6; ENSP00000411375.2; ENSG00000163788.14. [Q9NRH2-1]
DR Ensembl; ENST00000454177.5; ENSP00000401246.1; ENSG00000163788.14. [Q9NRH2-1]
DR GeneID; 54861; -.
DR KEGG; hsa:54861; -.
DR MANE-Select; ENST00000296088.12; ENSP00000296088.7; NM_017719.5; NP_060189.3.
DR UCSC; uc003cms.5; human. [Q9NRH2-1]
DR CTD; 54861; -.
DR DisGeNET; 54861; -.
DR GeneCards; SNRK; -.
DR HGNC; HGNC:30598; SNRK.
DR HPA; ENSG00000163788; Low tissue specificity.
DR MIM; 612760; gene.
DR neXtProt; NX_Q9NRH2; -.
DR OpenTargets; ENSG00000163788; -.
DR PharmGKB; PA142670894; -.
DR VEuPathDB; HostDB:ENSG00000163788; -.
DR eggNOG; KOG4717; Eukaryota.
DR GeneTree; ENSGT00940000155365; -.
DR HOGENOM; CLU_007233_3_0_1; -.
DR InParanoid; Q9NRH2; -.
DR OMA; VGSIKFF; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9NRH2; -.
DR TreeFam; TF351991; -.
DR PathwayCommons; Q9NRH2; -.
DR SignaLink; Q9NRH2; -.
DR SIGNOR; Q9NRH2; -.
DR BioGRID-ORCS; 54861; 10 hits in 1124 CRISPR screens.
DR ChiTaRS; SNRK; human.
DR GeneWiki; SNRK; -.
DR GenomeRNAi; 54861; -.
DR Pharos; Q9NRH2; Tchem.
DR PRO; PR:Q9NRH2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NRH2; protein.
DR Bgee; ENSG00000163788; Expressed in pericardium and 215 other tissues.
DR ExpressionAtlas; Q9NRH2; baseline and differential.
DR Genevisible; Q9NRH2; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030099; P:myeloid cell differentiation; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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 3D-structure; Alternative splicing; ATP-binding; Kinase; Magnesium;
KW Metal-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..765
FT /note="SNF-related serine/threonine-protein kinase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000225605"
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 512..634
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 581..634
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:0000250|UniProtKB:Q8VDU5"
FT MOD_RES 173
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000269|PubMed:15733851"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDU5"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDU5"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63553"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 534
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDU5"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 244
FT /note="D -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051959"
FT VAR_SEQ 245..765
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051960"
FT VARIANT 260
FT /note="L -> S (in dbSNP:rs35624204)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041096"
FT VARIANT 391
FT /note="P -> S (in dbSNP:rs56104180)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041097"
FT VARIANT 611
FT /note="G -> S (in an ovarian mucinous carcinoma sample;
FT somatic mutation; dbSNP:rs368877591)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041098"
FT VARIANT 748
FT /note="P -> L (in an ovarian serous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041099"
FT VARIANT 765
FT /note="I -> M (in a breast pleomorphic lobular carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041100"
FT MUTAGEN 173
FT /note="T->A,E: Prevents phosphorylation and activation by
FT STK11/LKB1 complex."
FT /evidence="ECO:0000269|PubMed:15733851"
FT CONFLICT 97
FT /note="G -> E (in Ref. 5; AAF86944)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> P (in Ref. 5; AAF86944)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="V -> A (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> P (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="V -> A (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="G -> E (in Ref. 6; BAA91023)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="N -> D (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="S -> Y (in Ref. 9; AAH71567)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> A (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="S -> G (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="L -> V (in Ref. 9; AAH71567)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="A -> V (in Ref. 7; CAH18415)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="K -> R (in Ref. 9; AAH71567)"
FT /evidence="ECO:0000305"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:5YKS"
FT STRAND 36..52
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:5YKS"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5YKS"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5YKS"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5YKS"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:5YKS"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5YKS"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:5YKS"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:5YKS"
FT HELIX 324..343
FT /evidence="ECO:0007829|PDB:5YKS"
SQ SEQUENCE 765 AA; 84276 MW; 06EF88CF7F8A393D CRC64;
MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL
FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF
AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY
SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPSHVSK
ECKDLITRML QRDPKRRASL EEIENHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ
RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA SPSNIKAQFR
QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAADSVLN GHRSKGLCDS AKKDDLPELA
GPALSTVPPA SLKPTASGRK CLFRVEEDEE EDEEDKKPMS LSTQVVLRRK PSVTNRLTSR
KSAPVLNQIF EEGESDDEFD MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS
SETSDDDSES RRRLDKDSGF TYSWHRRDSS EGPPGSEGDG GGQSKPSNAS GGVDKASPSE
NNAGGGSPSS GSGGNPTNTS GTTRRCAGPS NSMQLASRSA GELVESLKLM SLCLGSQLHG
STKYIIDPQN GLSFSSVKVQ EKSTWKMCIS STGNAGQVPA VGGIKFFSDH MADTTTELER
IKSKNLKNNV LQLPLCEKTI SVNIQRNPKE GLLCASSPAS CCHVI
