CAB39_HUMAN
ID CAB39_HUMAN Reviewed; 341 AA.
AC Q9Y376; A8K8L7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Calcium-binding protein 39;
DE AltName: Full=MO25alpha;
DE AltName: Full=Protein Mo25;
GN Name=CAB39; Synonyms=MO25; ORFNames=CGI-66;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RA Jin W., Shi J., Ren S., Gu J., Fu S., Huang Q., Dong H., Yu Y., Fu G.,
RA Wang Y., Chen Z., Han Z.;
RT "A novel gene expressed in the human hypothalamus.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 10-339.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 IN COMPLEX WITH STK11/LKB1
RP AND STRADA, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND STRADA,
RP FUNCTION, AND MUTAGENESIS OF ARG-240 AND PHE-243.
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).
CC -!- FUNCTION: Component of a complex that binds and activates STK11/LKB1.
CC In the complex, required to stabilize the interaction between
CC CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1.
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:19892943}.
CC -!- INTERACTION:
CC Q9Y376; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-306905, EBI-744115;
CC Q9Y376; Q08379: GOLGA2; NbExp=3; IntAct=EBI-306905, EBI-618309;
CC Q9Y376; P59942: MCCD1; NbExp=3; IntAct=EBI-306905, EBI-11987923;
CC Q9Y376; O43513: MED7; NbExp=3; IntAct=EBI-306905, EBI-394632;
CC Q9Y376; O95747: OXSR1; NbExp=3; IntAct=EBI-306905, EBI-620853;
CC Q9Y376; P34897: SHMT2; NbExp=3; IntAct=EBI-306905, EBI-352908;
CC Q9Y376; Q15831: STK11; NbExp=14; IntAct=EBI-306905, EBI-306838;
CC Q9Y376; Q9Y6E0-2: STK24; NbExp=3; IntAct=EBI-306905, EBI-10299018;
CC Q9Y376; O00506: STK25; NbExp=4; IntAct=EBI-306905, EBI-618295;
CC Q9Y376; Q9P289: STK26; NbExp=6; IntAct=EBI-306905, EBI-618239;
CC Q9Y376; Q9P289-1: STK26; NbExp=10; IntAct=EBI-306905, EBI-15996971;
CC Q9Y376; Q9UEW8: STK39; NbExp=4; IntAct=EBI-306905, EBI-2680974;
CC Q9Y376; Q7RTN6: STRADA; NbExp=3; IntAct=EBI-306905, EBI-1109114;
CC Q9Y376; Q7RTN6-1: STRADA; NbExp=7; IntAct=EBI-306905, EBI-15787241;
CC Q9Y376; Q9C0K7: STRADB; NbExp=6; IntAct=EBI-306905, EBI-306893;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mo25 family. {ECO:0000305}.
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DR EMBL; AF151824; AAD34061.1; -; mRNA.
DR EMBL; AF113536; AAF14873.1; -; mRNA.
DR EMBL; AK292382; BAF85071.1; -; mRNA.
DR EMBL; AK315692; BAG38055.1; -; mRNA.
DR EMBL; CH471063; EAW70932.1; -; Genomic_DNA.
DR EMBL; BC020570; AAH20570.1; -; mRNA.
DR CCDS; CCDS2478.1; -.
DR RefSeq; NP_001124321.1; NM_001130849.1.
DR RefSeq; NP_001124322.1; NM_001130850.1.
DR RefSeq; NP_057373.1; NM_016289.3.
DR PDB; 1UPK; X-ray; 1.85 A; A=1-341.
DR PDB; 1UPL; X-ray; 2.60 A; A/B=1-341.
DR PDB; 2WTK; X-ray; 2.65 A; A/D=1-341.
DR PDB; 3GNI; X-ray; 2.35 A; A=1-341.
DR PDB; 4FZA; X-ray; 3.15 A; A=11-334.
DR PDB; 4FZD; X-ray; 3.25 A; A=11-334.
DR PDB; 4FZF; X-ray; 3.64 A; A=11-334.
DR PDB; 4NZW; X-ray; 3.58 A; A=8-334.
DR PDB; 4O27; X-ray; 3.18 A; A=11-333.
DR PDBsum; 1UPK; -.
DR PDBsum; 1UPL; -.
DR PDBsum; 2WTK; -.
DR PDBsum; 3GNI; -.
DR PDBsum; 4FZA; -.
DR PDBsum; 4FZD; -.
DR PDBsum; 4FZF; -.
DR PDBsum; 4NZW; -.
DR PDBsum; 4O27; -.
DR AlphaFoldDB; Q9Y376; -.
DR SMR; Q9Y376; -.
DR BioGRID; 119696; 85.
DR ComplexPortal; CPX-2845; LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39-STRADA variant.
DR ComplexPortal; CPX-2868; LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39-STRADB variant.
DR CORUM; Q9Y376; -.
DR DIP; DIP-31316N; -.
DR IntAct; Q9Y376; 27.
DR MINT; Q9Y376; -.
DR STRING; 9606.ENSP00000258418; -.
DR ChEMBL; CHEMBL3885534; -.
DR iPTMnet; Q9Y376; -.
DR PhosphoSitePlus; Q9Y376; -.
DR BioMuta; CAB39; -.
DR DMDM; 15214082; -.
DR EPD; Q9Y376; -.
DR jPOST; Q9Y376; -.
DR MassIVE; Q9Y376; -.
DR MaxQB; Q9Y376; -.
DR PaxDb; Q9Y376; -.
DR PeptideAtlas; Q9Y376; -.
DR PRIDE; Q9Y376; -.
DR ProteomicsDB; 85981; -.
DR Antibodypedia; 34407; 149 antibodies from 27 providers.
DR DNASU; 51719; -.
DR Ensembl; ENST00000258418.10; ENSP00000258418.5; ENSG00000135932.12.
DR Ensembl; ENST00000409788.7; ENSP00000386238.3; ENSG00000135932.12.
DR Ensembl; ENST00000410084.7; ENSP00000386642.3; ENSG00000135932.12.
DR GeneID; 51719; -.
DR KEGG; hsa:51719; -.
DR MANE-Select; ENST00000258418.10; ENSP00000258418.5; NM_016289.4; NP_057373.1.
DR UCSC; uc002vqx.4; human.
DR CTD; 51719; -.
DR DisGeNET; 51719; -.
DR GeneCards; CAB39; -.
DR HGNC; HGNC:20292; CAB39.
DR HPA; ENSG00000135932; Tissue enhanced (skeletal).
DR MIM; 612174; gene.
DR neXtProt; NX_Q9Y376; -.
DR OpenTargets; ENSG00000135932; -.
DR PharmGKB; PA128394663; -.
DR VEuPathDB; HostDB:ENSG00000135932; -.
DR eggNOG; KOG1566; Eukaryota.
DR GeneTree; ENSGT00390000004360; -.
DR HOGENOM; CLU_035755_0_0_1; -.
DR InParanoid; Q9Y376; -.
DR OMA; HLKLCMN; -.
DR OrthoDB; 865327at2759; -.
DR PhylomeDB; Q9Y376; -.
DR TreeFam; TF314910; -.
DR PathwayCommons; Q9Y376; -.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9Y376; -.
DR BioGRID-ORCS; 51719; 202 hits in 1091 CRISPR screens.
DR ChiTaRS; CAB39; human.
DR EvolutionaryTrace; Q9Y376; -.
DR GeneWiki; CAB39; -.
DR GenomeRNAi; 51719; -.
DR Pharos; Q9Y376; Tbio.
DR PRO; PR:Q9Y376; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y376; protein.
DR Bgee; ENSG00000135932; Expressed in amniotic fluid and 207 other tissues.
DR ExpressionAtlas; Q9Y376; baseline and differential.
DR Genevisible; Q9Y376; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
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:ParkinsonsUK-UCL.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:ComplexPortal.
DR GO; GO:0071476; P:cellular hypotonic response; IC:ParkinsonsUK-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:ParkinsonsUK-UCL.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IC:ParkinsonsUK-UCL.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IC:ParkinsonsUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:ParkinsonsUK-UCL.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013878; Mo25.
DR PANTHER; PTHR10182; PTHR10182; 1.
DR Pfam; PF08569; Mo25; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..341
FT /note="Calcium-binding protein 39"
FT /id="PRO_0000209824"
FT MUTAGEN 240
FT /note="R->A: Abolishes activation of STK11/LKB1; when
FT associated with A-243."
FT /evidence="ECO:0000269|PubMed:19892943"
FT MUTAGEN 243
FT /note="F->A: Abolishes activation of STK11/LKB1; when
FT associated with A-240."
FT /evidence="ECO:0000269|PubMed:19892943"
FT HELIX 12..27
FT /evidence="ECO:0007829|PDB:1UPK"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3GNI"
FT HELIX 34..54
FT /evidence="ECO:0007829|PDB:1UPK"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4FZD"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1UPK"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:1UPK"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:1UPK"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4FZD"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:1UPK"
SQ SEQUENCE 341 AA; 39869 MW; EC710A528B6F9811 CRC64;
MPFPFGKSHK SPADIVKNLK ESMAVLEKQD ISDKKAEKAT EEVSKNLVAM KEILYGTNEK
EPQTEAVAQL AQELYNSGLL STLVADLQLI DFEGKKDVAQ IFNNILRRQI GTRTPTVEYI
CTQQNILFML LKGYESPEIA LNCGIMLREC IRHEPLAKII LWSEQFYDFF RYVEMSTFDI
ASDAFATFKD LLTRHKLLSA EFLEQHYDRF FSEYEKLLHS ENYVTKRQSL KLLGELLLDR
HNFTIMTKYI SKPENLKLMM NLLRDKSRNI QFEAFHVFKV FVANPNKTQP ILDILLKNQA
KLIEFLSKFQ NDRTEDEQFN DEKTYLVKQI RDLKRPAQQE A
