Full text data of STRADB
STRADB
(ALS2CR2, ILPIP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
STE20-related kinase adapter protein beta; STRAD beta (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein; CALS-21; ILP-interacting protein; Pseudokinase ALS2CR2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
STE20-related kinase adapter protein beta; STRAD beta (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein; CALS-21; ILP-interacting protein; Pseudokinase ALS2CR2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Comments
Isoform Q9C0K7-2 was detected.
Isoform Q9C0K7-2 was detected.
UniProt
Q9C0K7
ID STRAB_HUMAN Reviewed; 418 AA.
AC Q9C0K7; Q5BKY7; Q9P1L0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
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;
DE AltName: Full=CALS-21;
DE AltName: Full=ILP-interacting protein;
DE AltName: Full=Pseudokinase ALS2CR2;
GN Name=STRADB; Synonyms=ALS2CR2, ILPIP; ORFNames=PRO1038;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11161814; DOI=10.1006/geno.2000.6392;
RA Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J.,
RA Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A.,
RA Ikeda J.-E., Hayden M.R.;
RT "Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2,
RT and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2)
RT critical region at chromosome 2q33-q34: candidate genes for ALS2.";
RL Genomics 71:200-213(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP INTERACTION WITH BIRC4.
RX PubMed=12048196; DOI=10.1074/jbc.M203312200;
RA Sanna M.G., Da Silva Correia J., Luo Y., Chuang B., Paulson L.M.,
RA Nguyen B., Deveraux Q.L., Ulevitch R.J.;
RT "ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated
RT activation of JNK1 and protection against apoptosis.";
RL J. Biol. Chem. 277:30454-30462(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STK11/LKB1 AND
RP CAB39.
RX PubMed=14517248; DOI=10.1093/emboj/cdg490;
RA Boudeau J., Baas A.F., Deak M., Morrice N.A., Kieloch A.,
RA Schutkowski M., Prescott A.R., Clevers H.C., Alessi D.R.;
RT "MO25alpha/beta interact with STRADalpha/beta enhancing their ability
RT to bind, activate and localize LKB1 in the cytoplasm.";
RL EMBO J. 22:5102-5114(2003).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-155 AND LEU-386.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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 (By
CC similarity).
CC -!- SUBUNIT: Component of a trimeric complex composed of STK11/LKB1,
CC STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CC CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm
CC and stimulates its catalytic activity. Interacts with BIRC4/XIAP.
CC These two proteins are likely to coexist in a complex with TAK1,
CC TRAF6, TAB1 and TAB2.
CC -!- INTERACTION:
CC Q9Y376:CAB39; NbExp=5; IntAct=EBI-306893, EBI-306905;
CC Q15831:STK11; NbExp=6; IntAct=EBI-306893, EBI-306838;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ILPIP-alpha;
CC IsoId=Q9C0K7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0K7-2; Sequence=VSP_016623, VSP_016624;
CC Note=No experimental confirmation available;
CC Name=3; Synonyms=ILPIP-beta;
CC IsoId=Q9C0K7-3; Sequence=VSP_016625;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC testis, liver and colon.
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.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- CAUTION: Ser-184 is present instead of the conserved Asp which is
CC expected to be an active site residue.
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DR EMBL; AB038950; BAB32500.1; -; mRNA.
DR EMBL; AY093697; AAM19143.1; -; mRNA.
DR EMBL; AF116618; AAF71042.1; -; mRNA.
DR EMBL; AK027637; BAB55254.1; -; mRNA.
DR EMBL; AC007282; AAY14692.1; -; Genomic_DNA.
DR EMBL; BC008302; AAH08302.1; -; mRNA.
DR EMBL; BC090871; AAH90871.1; -; mRNA.
DR RefSeq; NP_001193793.1; NM_001206864.1.
DR RefSeq; NP_061041.2; NM_018571.5.
DR RefSeq; XP_005246724.1; XM_005246667.1.
DR RefSeq; XP_005246727.1; XM_005246670.1.
DR UniGene; Hs.652338; -.
DR ProteinModelPortal; Q9C0K7; -.
DR SMR; Q9C0K7; 3-386.
DR IntAct; Q9C0K7; 5.
DR MINT; MINT-7969373; -.
DR STRING; 9606.ENSP00000194530; -.
DR PhosphoSite; Q9C0K7; -.
DR DMDM; 74762722; -.
DR PaxDb; Q9C0K7; -.
DR PRIDE; Q9C0K7; -.
DR DNASU; 55437; -.
DR Ensembl; ENST00000194530; ENSP00000194530; ENSG00000082146.
DR Ensembl; ENST00000392249; ENSP00000376080; ENSG00000082146.
DR GeneID; 55437; -.
DR KEGG; hsa:55437; -.
DR UCSC; uc002uyd.4; human.
DR CTD; 55437; -.
DR GeneCards; GC02P202252; -.
DR HGNC; HGNC:13205; STRADB.
DR HPA; HPA026549; -.
DR HPA; HPA028520; -.
DR MIM; 607333; gene.
DR neXtProt; NX_Q9C0K7; -.
DR PharmGKB; PA24743; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000005157; -.
DR HOVERGEN; HBG055069; -.
DR InParanoid; Q9C0K7; -.
DR KO; K17532; -.
DR OMA; CSTNVSH; -.
DR PhylomeDB; Q9C0K7; -.
DR Reactome; REACT_111102; Signal Transduction.
DR SignaLink; Q9C0K7; -.
DR GeneWiki; ALS2CR2; -.
DR GenomeRNAi; 55437; -.
DR NextBio; 59838; -.
DR PRO; PR:Q9C0K7; -.
DR ArrayExpress; Q9C0K7; -.
DR Bgee; Q9C0K7; -.
DR CleanEx; HS_STRADB; -.
DR Genevestigator; Q9C0K7; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Complete proteome;
KW Cytoplasm; Nucleotide-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 418 STE20-related kinase adapter protein
FT beta.
FT /FTId=PRO_0000085617.
FT DOMAIN 58 369 Protein kinase.
FT NP_BIND 64 72 ATP (By similarity).
FT BINDING 89 89 ATP (By similarity).
FT VAR_SEQ 1 138 Missing (in isoform 3).
FT /FTId=VSP_016625.
FT VAR_SEQ 372 377 MKEESQ -> PYFEFL (in isoform 2).
FT /FTId=VSP_016623.
FT VAR_SEQ 378 418 Missing (in isoform 2).
FT /FTId=VSP_016624.
FT VARIANT 155 155 G -> E (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041335.
FT VARIANT 386 386 P -> L (in dbSNP:rs35636836).
FT /FTId=VAR_041336.
SQ SEQUENCE 418 AA; 47026 MW; A63ED6CCE1E18C96 CRC64;
MSLLDCFCTS RTQVESLRPE KQSETSIHQY LVDEPTLSWS RPSTRASEVL CSTNVSHYEL
QVEIGRGFDN LTSVHLARHT PTGTLVTIKI TNLENCNEER LKALQKAVIL SHFFRHPNIT
TYWTVFTVGS WLWVISPFMA YGSASQLLRT YFPEGMSETL IRNILFGAVR GLNYLHQNGC
IHRSIKASHI LISGDGLVTL SGLSHLHSLV KHGQRHRAVY DFPQFSTSVQ PWLSPELLRQ
DLHGYNVKSD IYSVGITACE LASGQVPFQD MHRTQMLLQK LKGPPYSPLD ISIFPQSESR
MKNSQSGVDS GIGESVLVSS GTHTVNSDRL HTPSSKTFSP AFFSLVQLCL QQDPEKRPSA
SSLLSHVFFK QMKEESQDSI LSLLPPAYNK PSISLPPVLP WTEPECDFPD EKDSYWEF
//
ID STRAB_HUMAN Reviewed; 418 AA.
AC Q9C0K7; Q5BKY7; Q9P1L0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 112.
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;
DE AltName: Full=CALS-21;
DE AltName: Full=ILP-interacting protein;
DE AltName: Full=Pseudokinase ALS2CR2;
GN Name=STRADB; Synonyms=ALS2CR2, ILPIP; ORFNames=PRO1038;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11161814; DOI=10.1006/geno.2000.6392;
RA Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J.,
RA Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A.,
RA Ikeda J.-E., Hayden M.R.;
RT "Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2,
RT and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2)
RT critical region at chromosome 2q33-q34: candidate genes for ALS2.";
RL Genomics 71:200-213(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP INTERACTION WITH BIRC4.
RX PubMed=12048196; DOI=10.1074/jbc.M203312200;
RA Sanna M.G., Da Silva Correia J., Luo Y., Chuang B., Paulson L.M.,
RA Nguyen B., Deveraux Q.L., Ulevitch R.J.;
RT "ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated
RT activation of JNK1 and protection against apoptosis.";
RL J. Biol. Chem. 277:30454-30462(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STK11/LKB1 AND
RP CAB39.
RX PubMed=14517248; DOI=10.1093/emboj/cdg490;
RA Boudeau J., Baas A.F., Deak M., Morrice N.A., Kieloch A.,
RA Schutkowski M., Prescott A.R., Clevers H.C., Alessi D.R.;
RT "MO25alpha/beta interact with STRADalpha/beta enhancing their ability
RT to bind, activate and localize LKB1 in the cytoplasm.";
RL EMBO J. 22:5102-5114(2003).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-155 AND LEU-386.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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 (By
CC similarity).
CC -!- SUBUNIT: Component of a trimeric complex composed of STK11/LKB1,
CC STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CC CAB39L/MO25beta): the complex tethers STK11/LKB1 in the cytoplasm
CC and stimulates its catalytic activity. Interacts with BIRC4/XIAP.
CC These two proteins are likely to coexist in a complex with TAK1,
CC TRAF6, TAB1 and TAB2.
CC -!- INTERACTION:
CC Q9Y376:CAB39; NbExp=5; IntAct=EBI-306893, EBI-306905;
CC Q15831:STK11; NbExp=6; IntAct=EBI-306893, EBI-306838;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ILPIP-alpha;
CC IsoId=Q9C0K7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0K7-2; Sequence=VSP_016623, VSP_016624;
CC Note=No experimental confirmation available;
CC Name=3; Synonyms=ILPIP-beta;
CC IsoId=Q9C0K7-3; Sequence=VSP_016625;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC testis, liver and colon.
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.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- CAUTION: Ser-184 is present instead of the conserved Asp which is
CC expected to be an active site residue.
CC -----------------------------------------------------------------------
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DR EMBL; AB038950; BAB32500.1; -; mRNA.
DR EMBL; AY093697; AAM19143.1; -; mRNA.
DR EMBL; AF116618; AAF71042.1; -; mRNA.
DR EMBL; AK027637; BAB55254.1; -; mRNA.
DR EMBL; AC007282; AAY14692.1; -; Genomic_DNA.
DR EMBL; BC008302; AAH08302.1; -; mRNA.
DR EMBL; BC090871; AAH90871.1; -; mRNA.
DR RefSeq; NP_001193793.1; NM_001206864.1.
DR RefSeq; NP_061041.2; NM_018571.5.
DR RefSeq; XP_005246724.1; XM_005246667.1.
DR RefSeq; XP_005246727.1; XM_005246670.1.
DR UniGene; Hs.652338; -.
DR ProteinModelPortal; Q9C0K7; -.
DR SMR; Q9C0K7; 3-386.
DR IntAct; Q9C0K7; 5.
DR MINT; MINT-7969373; -.
DR STRING; 9606.ENSP00000194530; -.
DR PhosphoSite; Q9C0K7; -.
DR DMDM; 74762722; -.
DR PaxDb; Q9C0K7; -.
DR PRIDE; Q9C0K7; -.
DR DNASU; 55437; -.
DR Ensembl; ENST00000194530; ENSP00000194530; ENSG00000082146.
DR Ensembl; ENST00000392249; ENSP00000376080; ENSG00000082146.
DR GeneID; 55437; -.
DR KEGG; hsa:55437; -.
DR UCSC; uc002uyd.4; human.
DR CTD; 55437; -.
DR GeneCards; GC02P202252; -.
DR HGNC; HGNC:13205; STRADB.
DR HPA; HPA026549; -.
DR HPA; HPA028520; -.
DR MIM; 607333; gene.
DR neXtProt; NX_Q9C0K7; -.
DR PharmGKB; PA24743; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000005157; -.
DR HOVERGEN; HBG055069; -.
DR InParanoid; Q9C0K7; -.
DR KO; K17532; -.
DR OMA; CSTNVSH; -.
DR PhylomeDB; Q9C0K7; -.
DR Reactome; REACT_111102; Signal Transduction.
DR SignaLink; Q9C0K7; -.
DR GeneWiki; ALS2CR2; -.
DR GenomeRNAi; 55437; -.
DR NextBio; 59838; -.
DR PRO; PR:Q9C0K7; -.
DR ArrayExpress; Q9C0K7; -.
DR Bgee; Q9C0K7; -.
DR CleanEx; HS_STRADB; -.
DR Genevestigator; Q9C0K7; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Complete proteome;
KW Cytoplasm; Nucleotide-binding; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 418 STE20-related kinase adapter protein
FT beta.
FT /FTId=PRO_0000085617.
FT DOMAIN 58 369 Protein kinase.
FT NP_BIND 64 72 ATP (By similarity).
FT BINDING 89 89 ATP (By similarity).
FT VAR_SEQ 1 138 Missing (in isoform 3).
FT /FTId=VSP_016625.
FT VAR_SEQ 372 377 MKEESQ -> PYFEFL (in isoform 2).
FT /FTId=VSP_016623.
FT VAR_SEQ 378 418 Missing (in isoform 2).
FT /FTId=VSP_016624.
FT VARIANT 155 155 G -> E (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041335.
FT VARIANT 386 386 P -> L (in dbSNP:rs35636836).
FT /FTId=VAR_041336.
SQ SEQUENCE 418 AA; 47026 MW; A63ED6CCE1E18C96 CRC64;
MSLLDCFCTS RTQVESLRPE KQSETSIHQY LVDEPTLSWS RPSTRASEVL CSTNVSHYEL
QVEIGRGFDN LTSVHLARHT PTGTLVTIKI TNLENCNEER LKALQKAVIL SHFFRHPNIT
TYWTVFTVGS WLWVISPFMA YGSASQLLRT YFPEGMSETL IRNILFGAVR GLNYLHQNGC
IHRSIKASHI LISGDGLVTL SGLSHLHSLV KHGQRHRAVY DFPQFSTSVQ PWLSPELLRQ
DLHGYNVKSD IYSVGITACE LASGQVPFQD MHRTQMLLQK LKGPPYSPLD ISIFPQSESR
MKNSQSGVDS GIGESVLVSS GTHTVNSDRL HTPSSKTFSP AFFSLVQLCL QQDPEKRPSA
SSLLSHVFFK QMKEESQDSI LSLLPPAYNK PSISLPPVLP WTEPECDFPD EKDSYWEF
//
MIM
607333
*RECORD*
*FIELD* NO
607333
*FIELD* TI
*607333 STE20-RELATED KINASE ADAPTOR BETA; STRADB
;;ILP-INTERACTING PROTEIN; ILPIP;;
read moreALS2 CHROMOSOME REGION GENE 2; ALS2CR2
*FIELD* TX
CLONING
By sequencing candidate genes in the ALS2 (205100) critical region,
Hadano et al. (2001) identified ALS2CR2. The deduced 418-amino acid
protein has a calculated molecular mass of about 47 kD. ALS2CR2 contains
a typical protein kinase domain and shares significant homology with
more than 30 serine/threonine protein kinases. Northern blot analysis
revealed highest expression of a 2.4-kb transcript in heart, skeletal
muscle, and colon. A 2.6-kb transcript, which may represent use of an
alternate polyadenylation signal, was detected in testis.
Sanna et al. (2002) cloned ALS2CR2, which they called ILPIP, in a yeast
2-hybrid screen of a fetal brain cDNA library using XIAP (300079) as
bait. They isolated the full-length cDNA by screening a liver cDNA
library. The 418-amino acid ILPIP protein, which the authors termed
ILPIP-alpha, contains a putative N-terminal ATP-binding site, a protein
kinase domain, and several C-terminal phosphorylation sites. Sanna et
al. (2002) also identified a 280-amino acid isoform, which they termed
ILPIP-beta, that lacks the first 138 amino acids of the N terminus of
ILPIP-alpha. Northern blot analysis detected expression of a 2.4-kb
transcript in muscle, liver, and heart, as well as in embryonic kidney
cells.
GENE FUNCTION
Sanna et al. (2002) determined that ILPIP potentiates the antiapoptotic
activity of XIAP by enhancing XIAP-mediated activation of JNK1 (MAPK8;
601158) and other JNK family members, but not by modulating
XIAP-mediated caspase inhibition. They also found that expression of a
catalytically inactive TAK1 (MAP3K7; 602614) mutant blocked the
XIAP/ILPIP activation of JNK1. In vivo coprecipitation experiments
showed that both ILPIP and XIAP interact with TAK1 and TRAF6 (602355).
Sanna et al. (2002) concluded that XIAP-mediated protection from
apoptosis utilizes both a JNK1 activation pathway that involves ILPIP
and a caspase inhibition pathway that is independent of ILPIP.
GENE STRUCTURE
Hadano et al. (2001) determined that the ALS2CR2 gene contains 12 exons
and spans 30 kb. It is transcribed in the centromere-to-telomere
direction. The promoter for ALS2CR2 is close to, or overlaps, the
promoter for ALS2CR3 (607334), which is transcribed in the opposite
orientation.
MAPPING
Hadano et al. (2001) mapped the STRADB gene within the ALS2 critical
region on chromosome 2q33-q34. They identified 2 intronless pseudogenes
that map to chromosomes 1 and 9.
*FIELD* RF
1. Hadano, S.; Yanagisawa, Y.; Skaug, J.; Fichter, K.; Nasir, J.;
Martindale, D.; Koop, B. F.; Scherer, S. W.; Nicholson, D. W.; Rouleau,
G. A.; Ikeda, J.-E.; Hayden, M. R.: Cloning and characterization
of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile
amyotrophic lateral sclerosis (ALS2) critical region at chromosome
2q33-q34: candidate genes for ALS2. Genomics 71: 200-213, 2001.
2. Sanna, M. G.; Correia, J. S.; Luo, Y.; Chuang, B.; Paulson, L.
M.; Nguyen, B.; Deveraux, Q. L.; Ulevitch, R. J.: ILPIP, a novel
anti-apoptotic protein that enhances XIAP-mediated activation of JNK1
and protection against apoptosis. J. Biol. Chem. 277: 30454-30462,
2002.
*FIELD* CD
Patricia A. Hartz: 11/8/2002
*FIELD* ED
carol: 07/19/2012
wwang: 1/5/2011
alopez: 5/13/2009
mgross: 11/8/2002
*RECORD*
*FIELD* NO
607333
*FIELD* TI
*607333 STE20-RELATED KINASE ADAPTOR BETA; STRADB
;;ILP-INTERACTING PROTEIN; ILPIP;;
read moreALS2 CHROMOSOME REGION GENE 2; ALS2CR2
*FIELD* TX
CLONING
By sequencing candidate genes in the ALS2 (205100) critical region,
Hadano et al. (2001) identified ALS2CR2. The deduced 418-amino acid
protein has a calculated molecular mass of about 47 kD. ALS2CR2 contains
a typical protein kinase domain and shares significant homology with
more than 30 serine/threonine protein kinases. Northern blot analysis
revealed highest expression of a 2.4-kb transcript in heart, skeletal
muscle, and colon. A 2.6-kb transcript, which may represent use of an
alternate polyadenylation signal, was detected in testis.
Sanna et al. (2002) cloned ALS2CR2, which they called ILPIP, in a yeast
2-hybrid screen of a fetal brain cDNA library using XIAP (300079) as
bait. They isolated the full-length cDNA by screening a liver cDNA
library. The 418-amino acid ILPIP protein, which the authors termed
ILPIP-alpha, contains a putative N-terminal ATP-binding site, a protein
kinase domain, and several C-terminal phosphorylation sites. Sanna et
al. (2002) also identified a 280-amino acid isoform, which they termed
ILPIP-beta, that lacks the first 138 amino acids of the N terminus of
ILPIP-alpha. Northern blot analysis detected expression of a 2.4-kb
transcript in muscle, liver, and heart, as well as in embryonic kidney
cells.
GENE FUNCTION
Sanna et al. (2002) determined that ILPIP potentiates the antiapoptotic
activity of XIAP by enhancing XIAP-mediated activation of JNK1 (MAPK8;
601158) and other JNK family members, but not by modulating
XIAP-mediated caspase inhibition. They also found that expression of a
catalytically inactive TAK1 (MAP3K7; 602614) mutant blocked the
XIAP/ILPIP activation of JNK1. In vivo coprecipitation experiments
showed that both ILPIP and XIAP interact with TAK1 and TRAF6 (602355).
Sanna et al. (2002) concluded that XIAP-mediated protection from
apoptosis utilizes both a JNK1 activation pathway that involves ILPIP
and a caspase inhibition pathway that is independent of ILPIP.
GENE STRUCTURE
Hadano et al. (2001) determined that the ALS2CR2 gene contains 12 exons
and spans 30 kb. It is transcribed in the centromere-to-telomere
direction. The promoter for ALS2CR2 is close to, or overlaps, the
promoter for ALS2CR3 (607334), which is transcribed in the opposite
orientation.
MAPPING
Hadano et al. (2001) mapped the STRADB gene within the ALS2 critical
region on chromosome 2q33-q34. They identified 2 intronless pseudogenes
that map to chromosomes 1 and 9.
*FIELD* RF
1. Hadano, S.; Yanagisawa, Y.; Skaug, J.; Fichter, K.; Nasir, J.;
Martindale, D.; Koop, B. F.; Scherer, S. W.; Nicholson, D. W.; Rouleau,
G. A.; Ikeda, J.-E.; Hayden, M. R.: Cloning and characterization
of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile
amyotrophic lateral sclerosis (ALS2) critical region at chromosome
2q33-q34: candidate genes for ALS2. Genomics 71: 200-213, 2001.
2. Sanna, M. G.; Correia, J. S.; Luo, Y.; Chuang, B.; Paulson, L.
M.; Nguyen, B.; Deveraux, Q. L.; Ulevitch, R. J.: ILPIP, a novel
anti-apoptotic protein that enhances XIAP-mediated activation of JNK1
and protection against apoptosis. J. Biol. Chem. 277: 30454-30462,
2002.
*FIELD* CD
Patricia A. Hartz: 11/8/2002
*FIELD* ED
carol: 07/19/2012
wwang: 1/5/2011
alopez: 5/13/2009
mgross: 11/8/2002