RAMAC_HUMAN
ID RAMAC_HUMAN Reviewed; 118 AA.
AC Q9BTL3; Q2M1J8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RNA guanine-N7 methyltransferase activating subunit {ECO:0000305};
DE AltName: Full=Protein FAM103A1;
DE AltName: Full=RNA guanine-7 methyltransferase activating subunit {ECO:0000312|HGNC:HGNC:31022};
DE AltName: Full=RNMT-activating mRNA cap methyltransferase subunit {ECO:0000312|HGNC:HGNC:31022};
DE AltName: Full=RNMT-activating mini protein {ECO:0000303|PubMed:22099306};
DE Short=RAM {ECO:0000303|PubMed:22099306};
GN Name=RAMAC {ECO:0000312|HGNC:HGNC:31022};
GN Synonyms=C15orf18, FAM103A1, RAMMET;
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].
RC TISSUE=Melanoma, Ovarian adenocarcinoma, and Skin;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH RNMT.
RX PubMed=22099306; DOI=10.1016/j.molcel.2011.08.041;
RA Gonatopoulos-Pournatzis T., Dunn S., Bounds R., Cowling V.H.;
RT "RAM/Fam103a1 is required for mRNA cap methylation.";
RL Mol. Cell 44:585-596(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-45 IN COMPLEX WITH RNMT AND
RP S-ADENOSYL-L-METHIONINE, FUNCTION, SUBUNIT, AND RNMT-ACTIVATION DOMAIN.
RX PubMed=27422871; DOI=10.1093/nar/gkw637;
RA Varshney D., Petit A.P., Bueren-Calabuig J.A., Jansen C., Fletcher D.A.,
RA Peggie M., Weidlich S., Scullion P., Pisliakov A.V., Cowling V.H.;
RT "Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by
RT RAM.";
RL Nucleic Acids Res. 44:10423-10436(2016).
CC -!- FUNCTION: Regulatory subunit of the mRNA-capping methyltransferase
CC RNMT:RAMAC complex that methylates the N7 position of the added
CC guanosine to the 5'-cap structure of mRNAs (PubMed:22099306,
CC PubMed:27422871). Promotes the recruitment of the methyl donor, S-
CC adenosyl-L-methionine, to RNMT (PubMed:27422871). Regulates RNMT
CC expression by a post-transcriptional stabilizing mechanism
CC (PubMed:22099306). Binds RNA (PubMed:22099306).
CC {ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:27422871}.
CC -!- SUBUNIT: Interacts with RNMT; this interaction enhances mRNA binding
CC and cap methyltransferase activity. {ECO:0000269|PubMed:22099306,
CC ECO:0000269|PubMed:27422871}.
CC -!- INTERACTION:
CC Q9BTL3; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-744023, EBI-357530;
CC Q9BTL3; O95429: BAG4; NbExp=6; IntAct=EBI-744023, EBI-2949658;
CC Q9BTL3; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-744023, EBI-953896;
CC Q9BTL3; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-744023, EBI-12809220;
CC Q9BTL3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-744023, EBI-3867333;
CC Q9BTL3; O75553: DAB1; NbExp=3; IntAct=EBI-744023, EBI-7875264;
CC Q9BTL3; Q15038: DAZAP2; NbExp=3; IntAct=EBI-744023, EBI-724310;
CC Q9BTL3; Q96MA1: DMRTB1; NbExp=3; IntAct=EBI-744023, EBI-954466;
CC Q9BTL3; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-744023, EBI-12193763;
CC Q9BTL3; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-744023, EBI-12018822;
CC Q9BTL3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-744023, EBI-618309;
CC Q9BTL3; P31943: HNRNPH1; NbExp=3; IntAct=EBI-744023, EBI-351590;
CC Q9BTL3; P61978-2: HNRNPK; NbExp=5; IntAct=EBI-744023, EBI-7060731;
CC Q9BTL3; Q0VD86: INCA1; NbExp=6; IntAct=EBI-744023, EBI-6509505;
CC Q9BTL3; P19012: KRT15; NbExp=3; IntAct=EBI-744023, EBI-739566;
CC Q9BTL3; Q15323: KRT31; NbExp=6; IntAct=EBI-744023, EBI-948001;
CC Q9BTL3; Q14525: KRT33B; NbExp=3; IntAct=EBI-744023, EBI-1049638;
CC Q9BTL3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-744023, EBI-11749135;
CC Q9BTL3; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-744023, EBI-10261141;
CC Q9BTL3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-744023, EBI-741037;
CC Q9BTL3; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-744023, EBI-716006;
CC Q9BTL3; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-744023, EBI-741424;
CC Q9BTL3; Q96HR8: NAF1; NbExp=3; IntAct=EBI-744023, EBI-2515597;
CC Q9BTL3; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-744023, EBI-12813389;
CC Q9BTL3; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-744023, EBI-769257;
CC Q9BTL3; Q16633: POU2AF1; NbExp=3; IntAct=EBI-744023, EBI-943588;
CC Q9BTL3; P79522: PRR3; NbExp=3; IntAct=EBI-744023, EBI-2803328;
CC Q9BTL3; P25788: PSMA3; NbExp=3; IntAct=EBI-744023, EBI-348380;
CC Q9BTL3; Q15415: RBMY1J; NbExp=3; IntAct=EBI-744023, EBI-8642021;
CC Q9BTL3; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-744023, EBI-726876;
CC Q9BTL3; O43148: RNMT; NbExp=7; IntAct=EBI-744023, EBI-877832;
CC Q9BTL3; Q15427: SF3B4; NbExp=3; IntAct=EBI-744023, EBI-348469;
CC Q9BTL3; P09234: SNRPC; NbExp=3; IntAct=EBI-744023, EBI-766589;
CC Q9BTL3; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-744023, EBI-8644516;
CC Q9BTL3; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-744023, EBI-750487;
CC Q9BTL3; Q63HR2: TNS2; NbExp=3; IntAct=EBI-744023, EBI-949753;
CC Q9BTL3; P36406: TRIM23; NbExp=6; IntAct=EBI-744023, EBI-740098;
CC Q9BTL3; P14373: TRIM27; NbExp=3; IntAct=EBI-744023, EBI-719493;
CC Q9BTL3; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-744023, EBI-5235829;
CC Q9BTL3; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-744023, EBI-11975223;
CC Q9BTL3; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-744023, EBI-2559305;
CC Q9BTL3; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-744023, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22099306}.
CC -!- SIMILARITY: Belongs to the RAM family. {ECO:0000305}.
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DR EMBL; BC003627; AAH03627.1; -; mRNA.
DR EMBL; BC027181; AAH27181.1; -; mRNA.
DR EMBL; BC112329; AAI12330.1; -; mRNA.
DR CCDS; CCDS10321.1; -.
DR RefSeq; NP_113640.1; NM_031452.3.
DR PDB; 5E8J; X-ray; 2.35 A; C/D=2-45.
DR PDBsum; 5E8J; -.
DR AlphaFoldDB; Q9BTL3; -.
DR SMR; Q9BTL3; -.
DR BioGRID; 123704; 78.
DR IntAct; Q9BTL3; 56.
DR STRING; 9606.ENSP00000307181; -.
DR iPTMnet; Q9BTL3; -.
DR MetOSite; Q9BTL3; -.
DR PhosphoSitePlus; Q9BTL3; -.
DR BioMuta; FAM103A1; -.
DR EPD; Q9BTL3; -.
DR jPOST; Q9BTL3; -.
DR MassIVE; Q9BTL3; -.
DR MaxQB; Q9BTL3; -.
DR PaxDb; Q9BTL3; -.
DR PeptideAtlas; Q9BTL3; -.
DR PRIDE; Q9BTL3; -.
DR ProteomicsDB; 78995; -.
DR Antibodypedia; 49864; 22 antibodies from 8 providers.
DR DNASU; 83640; -.
DR Ensembl; ENST00000304191.4; ENSP00000307181.3; ENSG00000169612.4.
DR GeneID; 83640; -.
DR KEGG; hsa:83640; -.
DR MANE-Select; ENST00000304191.4; ENSP00000307181.3; NM_031452.4; NP_113640.1.
DR UCSC; uc002bjl.3; human.
DR CTD; 83640; -.
DR DisGeNET; 83640; -.
DR GeneCards; RAMAC; -.
DR HGNC; HGNC:31022; RAMAC.
DR HPA; ENSG00000169612; Low tissue specificity.
DR MIM; 614547; gene.
DR neXtProt; NX_Q9BTL3; -.
DR PharmGKB; PA142671786; -.
DR VEuPathDB; HostDB:ENSG00000169612; -.
DR eggNOG; ENOG502S60Q; Eukaryota.
DR GeneTree; ENSGT00390000011190; -.
DR HOGENOM; CLU_144253_0_0_1; -.
DR InParanoid; Q9BTL3; -.
DR OMA; QRFPAND; -.
DR PhylomeDB; Q9BTL3; -.
DR TreeFam; TF335880; -.
DR PathwayCommons; Q9BTL3; -.
DR SignaLink; Q9BTL3; -.
DR SIGNOR; Q9BTL3; -.
DR BioGRID-ORCS; 83640; 319 hits in 1050 CRISPR screens.
DR GenomeRNAi; 83640; -.
DR Pharos; Q9BTL3; Tbio.
DR PRO; PR:Q9BTL3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BTL3; protein.
DR Bgee; ENSG00000169612; Expressed in adrenal tissue and 103 other tissues.
DR Genevisible; Q9BTL3; HS.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IMP:UniProtKB.
DR GO; GO:0036031; P:recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0106005; P:RNA 5'-cap (guanine-N7)-methylation; IEA:InterPro.
DR DisProt; DP02346; -.
DR InterPro; IPR028271; RAMAC.
DR Pfam; PF15320; RAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Methylation; mRNA capping; mRNA processing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..118
FT /note="RNA guanine-N7 methyltransferase activating subunit"
FT /id="PRO_0000089983"
FT REGION 2..55
FT /note="Interaction with RNMT"
FT /evidence="ECO:0000269|PubMed:22099306"
FT REGION 29..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..118
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:22099306"
FT MOTIF 36..42
FT /note="RNMT-activating domain"
FT /evidence="ECO:0000269|PubMed:27422871"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:5E8J"
FT TURN 15..19
FT /evidence="ECO:0007829|PDB:5E8J"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:5E8J"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5E8J"
SQ SEQUENCE 118 AA; 14381 MW; 266B56E66A73A1AE CRC64;
MTDTAEAVPK FEEMFASRFT ENDKEYQEYL KRPPESPPIV EEWNSRAGGN QRNRGNRLQD
NRQFRGRDNR WGWPSDNRSN QWHGRSWGNN YPQHRQEPYY PQQYGHYGYN QRPPYGYY
