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RNMT-activating mini protein (RAM) (Protein FAM103A1)

 RAM_HUMAN               Reviewed;         118 AA.
Q9BTL3; Q2M1J8;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=RNMT-activating mini protein;
Short=RAM;
AltName: Full=Protein FAM103A1;
Name=FAM103A1; Synonyms=C15orf18;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma, Ovarian adenocarcinoma, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH
RNMT.
PubMed=22099306; DOI=10.1016/j.molcel.2011.08.041;
Gonatopoulos-Pournatzis T., Dunn S., Bounds R., Cowling V.H.;
"RAM/Fam103a1 is required for mRNA cap methylation.";
Mol. Cell 44:585-596(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-86, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-85, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-45 IN COMPLEX WITH RNMT
AND S-ADENOSYL-L-METHIONINE, FUNCTION, SUBUNIT, AND RNMT-ACTIVATION
DOMAIN.
PubMed=27422871; DOI=10.1093/nar/gkw637;
Varshney D., Petit A.P., Bueren-Calabuig J.A., Jansen C.,
Fletcher D.A., Peggie M., Weidlich S., Scullion P., Pisliakov A.V.,
Cowling V.H.;
"Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation
by RAM.";
Nucleic Acids Res. 44:10423-10436(2016).
-!- FUNCTION: Regulatory subunit of the mRNA-capping methyltransferase
RNMT:RAM/FAM103A1 complex that methylates the N7 position of the
added guanosine to the 5'-cap structure of mRNAs (PubMed:22099306,
PubMed:27422871). Promotes the recruitment of the methyl donor, S-
adenosyl-L-methionine, to RNMT (PubMed:27422871). Regulates RNMT
expression by a post-transcriptional stabilizing mechanism
(PubMed:22099306). Binds RNA (PubMed:22099306).
{ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:27422871}.
-!- SUBUNIT: Interacts with RNMT; this interaction enhances mRNA
binding and cap methyltransferase activity.
{ECO:0000269|PubMed:22099306, ECO:0000269|PubMed:27422871}.
-!- INTERACTION:
O75553:DAB1; NbExp=3; IntAct=EBI-744023, EBI-7875264;
Q0VD86:INCA1; NbExp=5; IntAct=EBI-744023, EBI-6509505;
Q15323:KRT31; NbExp=5; IntAct=EBI-744023, EBI-948001;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-744023, EBI-741037;
P25788:PSMA3; NbExp=3; IntAct=EBI-744023, EBI-348380;
Q15415:RBMY1J; NbExp=3; IntAct=EBI-744023, EBI-8642021;
P36406:TRIM23; NbExp=5; IntAct=EBI-744023, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-744023, EBI-719493;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-744023, EBI-5235829;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22099306}.
-!- SIMILARITY: Belongs to the RAM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC003627; AAH03627.1; -; mRNA.
EMBL; BC027181; AAH27181.1; -; mRNA.
EMBL; BC112329; AAI12330.1; -; mRNA.
CCDS; CCDS10321.1; -.
RefSeq; NP_113640.1; NM_031452.3.
UniGene; Hs.80624; -.
PDB; 5E8J; X-ray; 2.35 A; C/D=2-45.
PDBsum; 5E8J; -.
ProteinModelPortal; Q9BTL3; -.
SMR; Q9BTL3; -.
BioGrid; 123704; 26.
IntAct; Q9BTL3; 49.
MINT; MINT-1452092; -.
STRING; 9606.ENSP00000307181; -.
iPTMnet; Q9BTL3; -.
PhosphoSitePlus; Q9BTL3; -.
BioMuta; FAM103A1; -.
EPD; Q9BTL3; -.
MaxQB; Q9BTL3; -.
PaxDb; Q9BTL3; -.
PeptideAtlas; Q9BTL3; -.
PRIDE; Q9BTL3; -.
DNASU; 83640; -.
Ensembl; ENST00000304191; ENSP00000307181; ENSG00000169612.
GeneID; 83640; -.
KEGG; hsa:83640; -.
UCSC; uc002bjl.3; human.
CTD; 83640; -.
DisGeNET; 83640; -.
EuPathDB; HostDB:ENSG00000169612.3; -.
GeneCards; FAM103A1; -.
H-InvDB; HIX0012517; -.
H-InvDB; HIX0200864; -.
HGNC; HGNC:31022; FAM103A1.
HPA; HPA041923; -.
HPA; HPA041948; -.
MIM; 614547; gene.
neXtProt; NX_Q9BTL3; -.
PharmGKB; PA142671786; -.
eggNOG; ENOG410IY7E; Eukaryota.
eggNOG; ENOG41122CR; LUCA.
GeneTree; ENSGT00390000011190; -.
HOGENOM; HOG000112423; -.
HOVERGEN; HBG081491; -.
InParanoid; Q9BTL3; -.
KO; K18708; -.
OMA; PYYPHQY; -.
OrthoDB; EOG091G172R; -.
PhylomeDB; Q9BTL3; -.
TreeFam; TF335880; -.
GenomeRNAi; 83640; -.
PRO; PR:Q9BTL3; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000169612; -.
CleanEx; HS_FAM103A1; -.
Genevisible; Q9BTL3; HS.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0031533; C:mRNA cap methyltransferase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
GO; GO:0032259; P:methylation; IMP:UniProtKB.
GO; GO:0036031; P:recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex; IDA:UniProtKB.
GO; GO:0106005; P:RNA 5'-cap (guanine-N7)-methylation; IEA:GOC.
InterPro; IPR028271; RAM.
Pfam; PF15320; RAM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Methylation;
mRNA capping; mRNA processing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 118 RNMT-activating mini protein.
/FTId=PRO_0000089983.
REGION 2 55 Interaction with RNMT.
{ECO:0000269|PubMed:22099306}.
REGION 56 118 RNA-binding.
{ECO:0000269|PubMed:22099306}.
MOTIF 36 42 RNMT-activating domain.
{ECO:0000269|PubMed:27422871}.
COMPBIAS 91 118 Gln/Tyr-rich.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 85 85 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
HELIX 4 14 {ECO:0000244|PDB:5E8J}.
TURN 15 19 {ECO:0000244|PDB:5E8J}.
HELIX 24 30 {ECO:0000244|PDB:5E8J}.
STRAND 39 41 {ECO:0000244|PDB:5E8J}.
SEQUENCE 118 AA; 14381 MW; 266B56E66A73A1AE CRC64;
MTDTAEAVPK FEEMFASRFT ENDKEYQEYL KRPPESPPIV EEWNSRAGGN QRNRGNRLQD
NRQFRGRDNR WGWPSDNRSN QWHGRSWGNN YPQHRQEPYY PQQYGHYGYN QRPPYGYY


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