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 24-JAN-2024, entry version 183. 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}, SNFRK GN {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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 30. DR IntAct; Q9NRH2; 22. DR MINT; Q9NRH2; -. DR STRING; 9606.ENSP00000296088; -. DR BindingDB; Q9NRH2; -. DR ChEMBL; CHEMBL1908384; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q9NRH2; -. DR GlyGen; Q9NRH2; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000296088; -. DR PeptideAtlas; Q9NRH2; -. DR ProteomicsDB; 82362; -. [Q9NRH2-1] DR ProteomicsDB; 82363; -. [Q9NRH2-2] DR Pumba; Q9NRH2; -. DR Antibodypedia; 29346; 181 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 AGR; HGNC:30598; -. 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; QTTCCHV; -. DR OrthoDB; 5475340at2759; -. DR PhylomeDB; Q9NRH2; -. DR TreeFam; TF351991; -. DR PathwayCommons; Q9NRH2; -. DR SignaLink; Q9NRH2; -. DR SIGNOR; Q9NRH2; -. DR BioGRID-ORCS; 54861; 10 hits in 1203 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 217 other cell types or tissues. DR ExpressionAtlas; Q9NRH2; baseline and differential. 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 CDD; cd14074; STKc_SNRK; 1. DR CDD; cd14339; UBA_SNRK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF45; SNF RELATED KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR Genevisible; Q9NRH2; HS. 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 //