STRAB_MOUSE
ID STRAB_MOUSE Reviewed; 418 AA.
AC Q8K4T3; Q6P922; Q8BU86; Q8BXK0; Q8K4T2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=STE20-related kinase adapter protein beta;
DE Short=STRAD beta;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein homolog;
DE AltName: Full=ILP-interacting protein homolog;
DE AltName: Full=Polyploidy-associated protein kinase;
DE AltName: Full=Pseudokinase ALS2CR2;
GN Name=Stradb; Synonyms=Als2cr2, Papk, Syradb;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12574163; DOI=10.1074/jbc.m208601200;
RA Nishigaki K., Thompson D., Yugawa T., Rulli K., Hanson C., Cmarik J.,
RA Gutkind J.S., Teramoto H., Ruscetti S.;
RT "Identification and characterization of a novel Ste20/germinal center
RT kinase-related kinase, polyploidy-associated protein kinase.";
RL J. Biol. Chem. 278:13520-13530(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Lung, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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).
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 (By
CC similarity). {ECO:0000250}.
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. Interacts with BIRC4/XIAP. These two proteins are
CC likely to coexist in a complex with TAK1, TRAF6, TAB1 and TAB2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PAPK-A;
CC IsoId=Q8K4T3-1; Sequence=Displayed;
CC Name=2; Synonyms=PAPK-B;
CC IsoId=Q8K4T3-2; Sequence=VSP_016626, VSP_016627;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- CAUTION: Ser-184 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; AB057666; BAB68235.1; -; mRNA.
DR EMBL; AB057667; BAB68236.1; -; mRNA.
DR EMBL; AK046790; BAC32870.1; -; mRNA.
DR EMBL; AK080096; BAC37825.1; -; mRNA.
DR EMBL; AK086974; BAC39775.1; -; mRNA.
DR EMBL; AK146079; BAE26883.1; -; mRNA.
DR EMBL; AK140272; BAE24309.1; -; mRNA.
DR EMBL; BC060956; AAH60956.1; -; mRNA.
DR CCDS; CCDS14981.1; -. [Q8K4T3-1]
DR RefSeq; NP_766244.4; NM_172656.5. [Q8K4T3-1]
DR AlphaFoldDB; Q8K4T3; -.
DR SMR; Q8K4T3; -.
DR STRING; 10090.ENSMUSP00000027185; -.
DR iPTMnet; Q8K4T3; -.
DR PhosphoSitePlus; Q8K4T3; -.
DR MaxQB; Q8K4T3; -.
DR PaxDb; Q8K4T3; -.
DR PRIDE; Q8K4T3; -.
DR ProteomicsDB; 257499; -. [Q8K4T3-1]
DR ProteomicsDB; 257500; -. [Q8K4T3-2]
DR Antibodypedia; 19937; 398 antibodies from 39 providers.
DR DNASU; 227154; -.
DR Ensembl; ENSMUST00000027185; ENSMUSP00000027185; ENSMUSG00000026027. [Q8K4T3-1]
DR Ensembl; ENSMUST00000114296; ENSMUSP00000109935; ENSMUSG00000026027. [Q8K4T3-2]
DR GeneID; 227154; -.
DR KEGG; mmu:227154; -.
DR UCSC; uc007bcx.1; mouse. [Q8K4T3-2]
DR UCSC; uc007bcy.1; mouse. [Q8K4T3-1]
DR CTD; 55437; -.
DR MGI; MGI:2144047; Stradb.
DR VEuPathDB; HostDB:ENSMUSG00000026027; -.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000155390; -.
DR HOGENOM; CLU_1434041_0_0_1; -.
DR InParanoid; Q8K4T3; -.
DR OMA; TYCPWDI; -.
DR OrthoDB; 995563at2759; -.
DR PhylomeDB; Q8K4T3; -.
DR TreeFam; TF319817; -.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR BioGRID-ORCS; 227154; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Stradb; mouse.
DR PRO; PR:Q8K4T3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K4T3; protein.
DR Bgee; ENSMUSG00000026027; Expressed in vastus lateralis and 233 other tissues.
DR ExpressionAtlas; Q8K4T3; baseline and differential.
DR Genevisible; Q8K4T3; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IDA:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell cycle; Cytoplasm;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..418
FT /note="STE20-related kinase adapter protein beta"
FT /id="PRO_0000085618"
FT DOMAIN 58..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 184..209
FT /note="SFKASHILISGDGLVTLSGLSHLHSL -> YLLIYSLHKRKNFKEVIQRNFC
FT KDKC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016626"
FT VAR_SEQ 210..418
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016627"
FT CONFLICT 184..189
FT /note="SFKASH -> IYMDIM (in Ref. 1; BAB68236 and 2;
FT BAE24309)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="F -> L (in Ref. 3; AAH60956)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="L -> S (in Ref. 2; BAC32870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 46832 MW; 4EB7FAAEF9F87E0A CRC64;
MSLLDCFCAS RTRVESLRPE KQSETSIHQY LVDESAISRP PPSARASEVI CSTDVSHYEL
QVEIGRGFDN LTSVHLARHT PTGTLVTVKI TNLESCTEER LKALQRAVIL SHFFQHPNIT
TYWTVFTVGS WLWVISPFMA YGSASQLLRT YFPDGMSETL IRNILFGAVQ GLNYLHQNGC
IHRSFKASHI LISGDGLVTL SGLSHLHSLL KHGQRHRAVF DFPQFSTSVQ PWLSPELLRQ
DLHGYNVKSD IYSVGITACE LASGQVPFQD MHRTQMLLQK LKGPPYSPLD VSIFPQSDSR
MRNSQSGVDS GIGESVLVST GTHTVNSDRL HTPSTKTFSP AFFSLVQLCL QQDPEKRPSA
SSLLSHVFFK QMKEESQDSI LPLLPPAYNR PSASLQPVSP WSELEFQFPD DKDPVWEF
