ID STRAA_HUMAN Reviewed; 431 AA. AC Q7RTN6; B4DDE3; B4DW17; J3KTC9; Q5JPI2; Q7Z4K9; Q8NC31; Q8NCF1; Q9H272; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=STE20-related kinase adapter protein alpha; DE Short=STRAD alpha; DE AltName: Full=STE20-related adapter protein; DE AltName: Full=Serologically defined breast cancer antigen NY-BR-96; GN Name=STRADA; Synonyms=LYK5 {ECO:0000312|EMBL:AAP42280.1}, STRAD; 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, ECO:0000312|EMBL:AAG48269.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAG48269.1}; RX PubMed=12747765; RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.; RT "Humoral immunity to human breast cancer: antigen definition and RT quantitative analysis of mRNA expression."; RL Cancer Immun. 1:4-4(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP42280.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Shan Y.X., Huang C.Q., Yu L.; RT "Cloning, characterization and localization of lyk5 gene."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC11349.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6). RC TISSUE=Synovium, and Teratocarcinoma {ECO:0000305, RC ECO:0000312|EMBL:BAC11349.1}; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Lymph node; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] {ECO:0000305, ECO:0000312|EMBL:AAP42280.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000305, ECO:0000312|EMBL:DAA01797.1} RP IDENTIFICATION (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION RP WITH STK11/LKB1, MUTAGENESIS OF THR-329 AND THR-419, AND PHOSPHORYLATION AT RP THR-329 AND THR-419. RX PubMed=12805220; DOI=10.1093/emboj/cdg292; RA Baas A.F., Boudeau J., Sapkota G.P., Smit L., Medema R., Morrice N.A., RA Alessi D.R., Clevers H.C.; RT "Activation of the tumour suppressor kinase LKB1 by the STE20-like RT pseudokinase STRAD."; RL EMBO J. 22:3062-3072(2003). RN [8] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STK11/LKB1 AND CAB39. RX PubMed=14517248; DOI=10.1093/emboj/cdg490; RA Boudeau J., Baas A.F., Deak M., Morrice N.A., Kieloch A., Schutkowski M., RA Prescott A.R., Clevers H.C., Alessi D.R.; RT "MO25alpha/beta interact with STRADalpha/beta enhancing their ability to RT bind, activate and localize LKB1 in the cytoplasm."; RL EMBO J. 22:5102-5114(2003). RN [9] RP INVOLVEMENT IN PMSE. RX PubMed=17522105; DOI=10.1093/brain/awm100; RA Puffenberger E.G., Strauss K.A., Ramsey K.E., Craig D.W., Stephan D.A., RA Robinson D.L., Hendrickson C.L., Gottlieb S., Ramsay D.A., Siu V.M., RA Heuer G.G., Crino P.B., Morton D.H.; RT "Polyhydramnios, megalencephaly and symptomatic epilepsy caused by a RT homozygous 7-kilobase deletion in LYK5."; RL Brain 130:1929-1941(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-46, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [12] {ECO:0000305} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CAB39. RX PubMed=14730349; DOI=10.1038/nsmb716; RA Milburn C.C., Boudeau J., Deak M., Alessi D.R., van Aalten D.M.; RT "Crystal structure of MO25 alpha in complex with the C-terminus of the RT pseudo kinase STE20-related adaptor."; RL Nat. Struct. Mol. Biol. 11:193-200(2004). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 59-431 IN COMPLEX WITH STK11/LKB1 RP AND CAB39, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND CAB39, FUNCTION, RP AND MUTAGENESIS OF TYR-185; HIS-231; PHE-233; LEU-241 AND GLN-251. RX PubMed=19892943; DOI=10.1126/science.1178377; RA Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.; RT "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism RT of kinase activation."; RL Science 326:1707-1711(2009). RN [14] RP VARIANTS [LARGE SCALE ANALYSIS] TRP-13; ILE-60 AND SER-64. 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: Pseudokinase which, in complex with CAB39/MO25 CC (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates CC STK11/LKB1. Adopts a closed conformation typical of active protein CC kinases and binds STK11/LKB1 as a pseudosubstrate, promoting CC conformational change of STK11/LKB1 in an active conformation. CC {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248, CC ECO:0000269|PubMed:19892943}. CC -!- SUBUNIT: Component of a trimeric complex composed of STK11/LKB1, STRAD CC (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta): CC the complex tethers STK11/LKB1 in the cytoplasm and stimulates its CC catalytic activity. {ECO:0000269|PubMed:14730349, CC ECO:0000269|PubMed:19892943}. CC -!- INTERACTION: CC Q7RTN6; Q9Y376: CAB39; NbExp=3; IntAct=EBI-1109114, EBI-306905; CC Q7RTN6; Q15831: STK11; NbExp=16; IntAct=EBI-1109114, EBI-306838; CC Q7RTN6-1; Q9Y376: CAB39; NbExp=7; IntAct=EBI-15787241, EBI-306905; CC Q7RTN6-1; Q15831: STK11; NbExp=3; IntAct=EBI-15787241, EBI-306838; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12805220, CC ECO:0000269|PubMed:14517248}. Cytoplasm {ECO:0000269|PubMed:12805220, CC ECO:0000269|PubMed:14517248}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1 {ECO:0000269|PubMed:12805220}; CC IsoId=Q7RTN6-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2}; CC IsoId=Q7RTN6-2; Sequence=VSP_052219, VSP_052220, VSP_052221; CC Name=3 {ECO:0000269|PubMed:14702039}; CC IsoId=Q7RTN6-3; Sequence=VSP_052219; CC Name=4; CC IsoId=Q7RTN6-4; Sequence=VSP_043707, VSP_043708; CC Name=5; CC IsoId=Q7RTN6-5; Sequence=VSP_044278; CC Name=6; CC IsoId=Q7RTN6-6; Sequence=VSP_044717, VSP_043708; CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically CC inactive. {ECO:0000255}. CC -!- DISEASE: Note=A homozygous 7-kb deletion involving STRADA is a cause of CC a syndrome characterized by polyhydramnios, megalencephaly and CC symptomatic epilepsy. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {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; AF308302; AAG48269.1; -; mRNA. DR EMBL; AY290821; AAP42280.1; -; mRNA. DR EMBL; AK074771; BAC11197.1; -; mRNA. DR EMBL; AK075005; BAC11349.1; -; mRNA. DR EMBL; AK293160; BAG56704.1; -; mRNA. DR EMBL; AK301331; BAG62879.1; -; mRNA. DR EMBL; AL832407; CAI46194.1; -; mRNA. DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC046185; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94283.1; -; Genomic_DNA. DR EMBL; BK001542; DAA01797.1; -; mRNA. DR CCDS; CCDS11642.1; -. [Q7RTN6-2] DR CCDS; CCDS32703.1; -. [Q7RTN6-1] DR CCDS; CCDS42367.1; -. [Q7RTN6-5] DR CCDS; CCDS54156.1; -. [Q7RTN6-4] DR CCDS; CCDS58585.1; -. [Q7RTN6-6] DR CCDS; CCDS86632.1; -. [Q7RTN6-3] DR RefSeq; NP_001003786.1; NM_001003786.2. [Q7RTN6-3] DR RefSeq; NP_001003787.1; NM_001003787.2. [Q7RTN6-1] DR RefSeq; NP_001003788.1; NM_001003788.2. [Q7RTN6-5] DR RefSeq; NP_001159441.1; NM_001165969.1. [Q7RTN6-6] DR RefSeq; NP_001159442.1; NM_001165970.1. [Q7RTN6-4] DR RefSeq; NP_699166.2; NM_153335.5. [Q7RTN6-2] DR RefSeq; XP_005257856.1; XM_005257799.2. DR PDB; 1UPK; X-ray; 1.85 A; B=420-431. DR PDB; 2WTK; X-ray; 2.65 A; B/E=59-431. DR PDB; 3GNI; X-ray; 2.35 A; B=59-431. DR PDBsum; 1UPK; -. DR PDBsum; 2WTK; -. DR PDBsum; 3GNI; -. DR AlphaFoldDB; Q7RTN6; -. DR SMR; Q7RTN6; -. DR BioGRID; 124934; 26. DR ComplexPortal; CPX-2431; LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39L-STRADA variant. DR ComplexPortal; CPX-2845; LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39-STRADA variant. DR CORUM; Q7RTN6; -. DR DIP; DIP-35775N; -. DR IntAct; Q7RTN6; 16. DR MINT; Q7RTN6; -. DR STRING; 9606.ENSP00000336655; -. DR ChEMBL; CHEMBL1795198; -. DR GlyGen; Q7RTN6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7RTN6; -. DR PhosphoSitePlus; Q7RTN6; -. DR BioMuta; STRADA; -. DR DMDM; 74759034; -. DR EPD; Q7RTN6; -. DR jPOST; Q7RTN6; -. DR MassIVE; Q7RTN6; -. DR MaxQB; Q7RTN6; -. DR PaxDb; 9606-ENSP00000336655; -. DR PeptideAtlas; Q7RTN6; -. DR ProteomicsDB; 63016; -. DR ProteomicsDB; 68873; -. [Q7RTN6-1] DR ProteomicsDB; 68874; -. [Q7RTN6-2] DR ProteomicsDB; 68875; -. [Q7RTN6-3] DR ProteomicsDB; 68876; -. [Q7RTN6-4] DR Pumba; Q7RTN6; -. DR TopDownProteomics; Q7RTN6-4; -. [Q7RTN6-4] DR Antibodypedia; 64277; 381 antibodies from 31 providers. DR DNASU; 92335; -. DR Ensembl; ENST00000336174.12; ENSP00000336655.6; ENSG00000266173.7. [Q7RTN6-1] DR Ensembl; ENST00000375840.9; ENSP00000365000.4; ENSG00000266173.7. [Q7RTN6-5] DR Ensembl; ENST00000392950.9; ENSP00000376677.4; ENSG00000266173.7. [Q7RTN6-2] DR Ensembl; ENST00000447001.8; ENSP00000398841.3; ENSG00000266173.7. [Q7RTN6-4] DR Ensembl; ENST00000582137.6; ENSP00000462922.1; ENSG00000266173.7. [Q7RTN6-6] DR Ensembl; ENST00000638702.1; ENSP00000491017.1; ENSG00000266173.7. [Q7RTN6-5] DR Ensembl; ENST00000639835.1; ENSP00000492578.1; ENSG00000266173.7. [Q7RTN6-3] DR Ensembl; ENST00000640999.1; ENSP00000491643.1; ENSG00000266173.7. [Q7RTN6-3] DR GeneID; 92335; -. DR KEGG; hsa:92335; -. DR MANE-Select; ENST00000336174.12; ENSP00000336655.6; NM_001003787.4; NP_001003787.1. DR UCSC; uc002jbm.4; human. [Q7RTN6-1] DR AGR; HGNC:30172; -. DR CTD; 92335; -. DR DisGeNET; 92335; -. DR GeneCards; STRADA; -. DR HGNC; HGNC:30172; STRADA. DR HPA; ENSG00000266173; Low tissue specificity. DR MalaCards; STRADA; -. DR MIM; 608626; gene. DR MIM; 611087; phenotype. DR neXtProt; NX_Q7RTN6; -. DR OpenTargets; ENSG00000266173; -. DR Orphanet; 500533; Polyhydramnios-megalencephaly-symptomatic epilepsy syndrome. DR PharmGKB; PA164726342; -. DR VEuPathDB; HostDB:ENSG00000266173; -. DR eggNOG; KOG0582; Eukaryota. DR GeneTree; ENSGT00940000158827; -. DR InParanoid; Q7RTN6; -. DR OMA; PLMCFGS; -. DR OrthoDB; 5389025at2759; -. DR PhylomeDB; Q7RTN6; -. DR TreeFam; TF319817; -. DR PathwayCommons; Q7RTN6; -. DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR SignaLink; Q7RTN6; -. DR SIGNOR; Q7RTN6; -. DR BioGRID-ORCS; 92335; 19 hits in 1189 CRISPR screens. DR ChiTaRS; STRADA; human. DR EvolutionaryTrace; Q7RTN6; -. DR GeneWiki; LYK5; -. DR GenomeRNAi; 92335; -. DR Pharos; Q7RTN6; Tbio. DR PRO; PR:Q7RTN6; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q7RTN6; Protein. DR Bgee; ENSG00000266173; Expressed in right uterine tube and 94 other cell types or tissues. DR ExpressionAtlas; Q7RTN6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0140535; C:intracellular protein-containing complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1902554; C:serine/threonine protein kinase complex; IPI:ComplexPortal. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL. DR GO; GO:0030295; F:protein kinase activator activity; IDA:UniProtKB. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB. DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB. DR GO; GO:0070314; P:G1 to G0 transition; IPI:UniProtKB. DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB. DR CDD; cd08227; PK_STRAD_alpha; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00217; -. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR047173; STRAD_A/B-like. DR PANTHER; PTHR48014; SERINE/THREONINE-PROTEIN KINASE FRAY2; 1. DR PANTHER; PTHR48014:SF20; STE20-RELATED KINASE ADAPTER PROTEIN ALPHA; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q7RTN6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; KW Chromosomal rearrangement; Cytoplasm; Nucleotide-binding; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..431 FT /note="STE20-related kinase adapter protein alpha" FT /id="PRO_0000260035" FT DOMAIN 69..379 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 310..347 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..343 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 329 FT /note="Phosphothreonine; by LKB1" FT /evidence="ECO:0000269|PubMed:12805220" FT MOD_RES 419 FT /note="Phosphothreonine; by LKB1" FT /evidence="ECO:0000269|PubMed:12805220" FT VAR_SEQ 1..58 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_044278" FT VAR_SEQ 5..41 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_052219" FT VAR_SEQ 13..41 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044717" FT VAR_SEQ 32..75 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043707" FT VAR_SEQ 338..431 FT /note="DSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEA FT LPELLRPVTPITNFEGSQSQDHSGIFGLVTNLEELEVDDWEF -> PVPAPS (in FT isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043708" FT VAR_SEQ 368..417 FT /note="PSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGL FT -> YPCWPGPGLRESRGCSGG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_052220" FT VAR_SEQ 418..431 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_052221" FT VARIANT 13 FT /note="R -> W (in dbSNP:rs35808156)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041377" FT VARIANT 60 FT /note="S -> I (in dbSNP:rs56271007)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041378" FT VARIANT 64 FT /note="P -> S (in dbSNP:rs55695051)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041379" FT MUTAGEN 185 FT /note="Y->F: Suppresses STK11/LKB1 activation without FT affecting complex assembly." FT /evidence="ECO:0000269|PubMed:19892943" FT MUTAGEN 231 FT /note="H->A: Inhibits interaction with STK11/LKB1; when FT associated with A-." FT /evidence="ECO:0000269|PubMed:19892943" FT MUTAGEN 233 FT /note="F->A: Inhibits interaction with STK11/LKB1; when FT associated with A-." FT /evidence="ECO:0000269|PubMed:19892943" FT MUTAGEN 241 FT /note="L->A: Inhibits interaction with STK11/LKB1." FT /evidence="ECO:0000269|PubMed:19892943" FT MUTAGEN 251 FT /note="Q->A: Inhibits interaction with STK11/LKB1." FT /evidence="ECO:0000269|PubMed:19892943" FT MUTAGEN 329 FT /note="T->A: Loss of STK11/LKB1-mediated phosphorylation." FT /evidence="ECO:0000269|PubMed:12805220" FT MUTAGEN 419 FT /note="T->A: Loss of STK11/LKB1-mediated phosphorylation." FT /evidence="ECO:0000269|PubMed:12805220" FT CONFLICT 163 FT /note="F -> S (in Ref. 3; BAG62879)" FT /evidence="ECO:0000305" FT CONFLICT 339 FT /note="S -> W (in Ref. 1; AAG48269)" FT /evidence="ECO:0000305" FT CONFLICT 363 FT /note="N -> H (in Ref. 3; BAC11349)" FT /evidence="ECO:0000305" FT CONFLICT 388 FT /note="E -> K (in Ref. 1; AAG48269)" FT /evidence="ECO:0000305" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 69..78 FT /evidence="ECO:0007829|PDB:3GNI" FT TURN 79..82 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:3GNI" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 96..103 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 109..124 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 133..139 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 142..148 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 155..161 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 169..188 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:3GNI" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 241..243 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 259..274 FT /evidence="ECO:0007829|PDB:3GNI" FT TURN 278..281 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 350..359 FT /evidence="ECO:0007829|PDB:3GNI" FT TURN 364..366 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 377..381 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 386..388 FT /evidence="ECO:0007829|PDB:2WTK" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:3GNI" FT TURN 394..396 FT /evidence="ECO:0007829|PDB:3GNI" FT HELIX 406..409 FT /evidence="ECO:0007829|PDB:2WTK" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:2WTK" SQ SEQUENCE 431 AA; 48369 MW; 9CC0A78D9CC6FC2C CRC64; MSFLVSKPER IRRWVSEKFI VEGLRDLELF GEQPPGDTRR KTNDASSESI ASFSKQEVMS SFLPEGGCYE LLTVIGKGFE DLMTVNLARY KPTGEYVTVR RINLEACSNE MVTFLQGELH VSKLFNHPNI VPYRATFIAD NELWVVTSFM AYGSAKDLIC THFMDGMNEL AIAYILQGVL KALDYIHHMG YVHRSVKASH ILISVDGKVY LSGLRSNLSM ISHGQRQRVV HDFPKYSVKV LPWLSPEVLQ QNLQGYDAKS DIYSVGITAC ELANGHVPFK DMPATQMLLE KLNGTVPCLL DTSTIPAEEL TMSPSRSVAN SGLSDSLTTS TPRPSNGDSP SHPYHRTFSP HFHHFVEQCL QRNPDARPSA STLLNHSFFK QIKRRASEAL PELLRPVTPI TNFEGSQSQD HSGIFGLVTN LEELEVDDWE F //