SAMTR_HUMAN
ID SAMTR_HUMAN Reviewed; 405 AA.
AC Q1RMZ1; Q8N3D0; Q96MV7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=S-adenosylmethionine sensor upstream of mTORC1 {ECO:0000255|HAMAP-Rule:MF_03044, ECO:0000303|PubMed:29123071};
DE AltName: Full=Probable methyltransferase BMT2 homolog {ECO:0000255|HAMAP-Rule:MF_03044};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03044};
GN Name=BMT2 {ECO:0000255|HAMAP-Rule:MF_03044, ECO:0000312|HGNC:HGNC:26475};
GN Synonyms=C7orf60 {ECO:0000312|HGNC:HGNC:26475},
GN SAMTOR {ECO:0000303|PubMed:29123071};
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-405.
RC TISSUE=Melanoma;
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 FUNCTION, AND INTERACTION WITH THE GATOR1 AND KICSTOR COMPLEXES.
RX PubMed=29123071; DOI=10.1126/science.aao3265;
RA Gu X., Orozco J.M., Saxton R.A., Condon K.J., Liu G.Y., Krawczyk P.A.,
RA Scaria S.M., Harper J.W., Gygi S.P., Sabatini D.M.;
RT "SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway.";
RL Science 358:813-818(2017).
CC -!- FUNCTION: S-adenosyl-L-methionine-binding protein that acts as an
CC inhibitor of mTORC1 signaling via interaction with the GATOR1 and
CC KICSTOR complexes (PubMed:29123071). Acts as a sensor of S-adenosyl-L-
CC methionine to signal methionine sufficiency to mTORC1: in presence of
CC methionine, binds S-adenosyl-L-methionine, leading to disrupt
CC interaction with the GATOR1 and KICSTOR complexes and promote mTORC1
CC signaling (PubMed:29123071). Upon methionine starvation, S-adenosyl-L-
CC methionine levels are reduced, thereby promoting the association with
CC GATOR1 and KICSTOR, leading to inhibit mTORC1 signaling
CC (PubMed:29123071). Probably also acts as a S-adenosyl-L-methionine-
CC dependent methyltransferase (Potential). {ECO:0000255|HAMAP-
CC Rule:MF_03044, ECO:0000269|PubMed:29123071}.
CC -!- SUBUNIT: Interacts with the GATOR1 complex; interaction is disrupted
CC when BMT2/SAMTOR binds S-adenosyl-L-methionine (PubMed:29123071).
CC Interacts with the KICSTOR complex; interaction is disrupted when
CC BMT2/SAMTOR binds S-adenosyl-L-methionine (PubMed:29123071).
CC {ECO:0000255|HAMAP-Rule:MF_03044, ECO:0000269|PubMed:29123071}.
CC -!- SIMILARITY: Belongs to the BMT2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03044}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71169.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK056380; BAB71169.1; ALT_FRAME; mRNA.
DR EMBL; CH471070; EAW83474.1; -; Genomic_DNA.
DR EMBL; BC114615; AAI14616.1; -; mRNA.
DR EMBL; AL834437; CAD39097.1; -; mRNA.
DR CCDS; CCDS43634.1; -.
DR RefSeq; NP_689769.2; NM_152556.2.
DR AlphaFoldDB; Q1RMZ1; -.
DR BioGRID; 127552; 22.
DR IntAct; Q1RMZ1; 21.
DR MINT; Q1RMZ1; -.
DR STRING; 9606.ENSP00000297145; -.
DR iPTMnet; Q1RMZ1; -.
DR PhosphoSitePlus; Q1RMZ1; -.
DR BioMuta; BMT2; -.
DR DMDM; 121947576; -.
DR EPD; Q1RMZ1; -.
DR jPOST; Q1RMZ1; -.
DR MassIVE; Q1RMZ1; -.
DR PaxDb; Q1RMZ1; -.
DR PeptideAtlas; Q1RMZ1; -.
DR PRIDE; Q1RMZ1; -.
DR ProteomicsDB; 61242; -.
DR TopDownProteomics; Q1RMZ1; -.
DR Antibodypedia; 50763; 11 antibodies from 7 providers.
DR DNASU; 154743; -.
DR Ensembl; ENST00000297145.9; ENSP00000297145.4; ENSG00000164603.12.
DR GeneID; 154743; -.
DR KEGG; hsa:154743; -.
DR MANE-Select; ENST00000297145.9; ENSP00000297145.4; NM_152556.3; NP_689769.2.
DR UCSC; uc003vgo.2; human.
DR CTD; 154743; -.
DR GeneCards; BMT2; -.
DR HGNC; HGNC:26475; BMT2.
DR HPA; ENSG00000164603; Low tissue specificity.
DR MIM; 617855; gene.
DR neXtProt; NX_Q1RMZ1; -.
DR OpenTargets; ENSG00000164603; -.
DR PharmGKB; PA162380700; -.
DR VEuPathDB; HostDB:ENSG00000164603; -.
DR eggNOG; ENOG502QRK4; Eukaryota.
DR GeneTree; ENSGT00390000010382; -.
DR HOGENOM; CLU_036404_1_1_1; -.
DR InParanoid; Q1RMZ1; -.
DR OMA; DNHWTKK; -.
DR OrthoDB; 836637at2759; -.
DR PhylomeDB; Q1RMZ1; -.
DR TreeFam; TF324724; -.
DR PathwayCommons; Q1RMZ1; -.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q1RMZ1; -.
DR BioGRID-ORCS; 154743; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; BMT2; human.
DR GenomeRNAi; 154743; -.
DR Pharos; Q1RMZ1; Tbio.
DR PRO; PR:Q1RMZ1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q1RMZ1; protein.
DR Bgee; ENSG00000164603; Expressed in secondary oocyte and 172 other tissues.
DR ExpressionAtlas; Q1RMZ1; baseline and differential.
DR Genevisible; Q1RMZ1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03044; BMT2; 1.
DR InterPro; IPR021867; Bmt2/SAMTOR.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21008; PTHR21008; 1.
DR Pfam; PF11968; Bmt2; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..405
FT /note="S-adenosylmethionine sensor upstream of mTORC1"
FT /id="PRO_0000321539"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03044,
FT ECO:0000269|PubMed:29123071"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03044,
FT ECO:0000269|PubMed:29123071"
FT CONFLICT 219
FT /note="I -> T (in Ref. 1; BAB71169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 46324 MW; 5C19614953ABD670 CRC64;
MEPGAGGRNT ARAQRAGSPN TPPPREQERK LEQEKLSGVV KSVHRRLRKK YREVGDFDKI
WREHCEDEET LCEYAVAMKN LADNHWAKTC EGEGRIEWCC SVCREYFQNG GKRKALEKDE
KRAVLATKTT PALNMHESSQ LEGHLTNLSF TNPEFITELL QASGKIRLLD VGSCFNPFLK
FEEFLTVGID IVPAVESVYK CDFLNLQLQQ PLQLAQDAID AFLKQLKNPI DSLPGELFHV
VVFSLLLSYF PSPYQRWICC KKAHELLVLN GLLLIITPDS SHQNRHAMMM KSWKIAIESL
GFKRFKYSKF SHMHLMAFRK ISLKTTSDLV SRNYPGMLYI PQDFNSIEDE EYSNPSCYVR
SDIEDEQLAY GFTELPDAPY DSDSGESQAS SIPFYELEDP ILLLS
