STRAA_HUMAN
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 03-AUG-2022, entry version 165.
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
RC Teratocarcinoma {ECO:0000305, 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=14; 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}.
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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. [Q7RTN6-5]
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; 15.
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; 15.
DR MINT; Q7RTN6; -.
DR STRING; 9606.ENSP00000336655; -.
DR ChEMBL; CHEMBL1795198; -.
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; Q7RTN6; -.
DR PeptideAtlas; Q7RTN6; -.
DR PRIDE; 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 TopDownProteomics; Q7RTN6-4; -. [Q7RTN6-4]
DR Antibodypedia; 64277; 340 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 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; QRDPENR; -.
DR OrthoDB; 995563at2759; -.
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; 16 hits in 1111 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 92 other tissues.
DR ExpressionAtlas; Q7RTN6; baseline and differential.
DR Genevisible; Q7RTN6; HS.
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 IDEAL; IID00217; -.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
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
