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RNA-binding protein with multiple splicing (RBP-MS) (Heart and RRM expressed sequence) (Hermes)

 RBPMS_HUMAN             Reviewed;         196 AA.
Q93062; D3DSU9; Q92516; Q92517; Q92518; Q96J26;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
27-SEP-2017, entry version 164.
RecName: Full=RNA-binding protein with multiple splicing;
Short=RBP-MS;
AltName: Full=Heart and RRM expressed sequence;
Short=Hermes;
Name=RBPMS; Synonyms=HERMES;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E).
TISSUE=Lip;
PubMed=8855282; DOI=10.1073/pnas.93.20.10913;
Shimamoto A., Kitao S., Ichikawa K., Suzuki N., Yamabe Y., Imamura O.,
Tokutake Y., Satoh M., Matsumoto T., Kuromitsu J., Kataoka H.,
Sugawara K., Sugawara M., Sugimoto M., Goto M., Furuichi Y.;
"A unique human gene that spans over 230 kb in the human chromosome
8p11-12 and codes multiple family proteins sharing RNA-binding
motifs.";
Proc. Natl. Acad. Sci. U.S.A. 93:10913-10917(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
TISSUE=Placenta;
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).
[4]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[5]
FUNCTION, INTERACTION WITH SMAD2; SMAD3; SMAD4 AND TGFBR1, SUBCELLULAR
LOCATION, AND RNA-BINDING.
PubMed=17099224; DOI=10.1093/nar/gkl914;
Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J.,
Song H., Ye Q.;
"Potentiation of Smad-mediated transcriptional activation by the RNA-
binding protein RBPMS.";
Nucleic Acids Res. 34:6314-6326(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, 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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[8] {ECO:0000244|PDB:5CYJ, ECO:0000244|PDB:5DET}
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 14-111 OF APOPROTEIN AND IN
COMPLEX WITH RNA, FUNCTION IN RNA-BINDING, SUBUNIT, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF PHE-27; 36-LYS--ARG-38; PHE-65; GLU-97;
LYS-100 AND 103-THR-LYS-104.
PubMed=26347403; DOI=10.1017/S0033583515000207;
Teplova M., Farazi T.A., Tuschl T., Patel D.J.;
"Structural basis underlying CAC RNA recognition by the RRM domain of
dimeric RNA-binding protein RBPMS.";
Q. Rev. Biophys. 2015:1-11(2015).
-!- FUNCTION: Acts as a coactivator of transcriptional activity.
Required to increase TGFB1/Smad-mediated transactivation. Acts
through SMAD2, SMAD3 and SMAD4 to increase transcriptional
activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-
terminal SSXS motif, possibly through recruitment of TGFBR1.
Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4
proteins (PubMed:26347403). Binds to poly(A) RNA (PubMed:17099224,
PubMed:26347403). {ECO:0000269|PubMed:17099224,
ECO:0000269|PubMed:26347403}.
-!- SUBUNIT: Homodimer; each protein chain binds one RNA molecule via
the external surface of the homodimer (PubMed:26347403). Interacts
with SMAD2, SMAD3 and SMAD4; the interactions are direct
(PubMed:17099224). {ECO:0000269|PubMed:17099224,
ECO:0000269|PubMed:26347403}.
-!- INTERACTION:
B2R550:-; NbExp=3; IntAct=EBI-740322, EBI-10175488;
Q96EJ4:-; NbExp=3; IntAct=EBI-740322, EBI-750454;
Q13444:ADAM15; NbExp=3; IntAct=EBI-740322, EBI-77818;
Q08117:AES; NbExp=3; IntAct=EBI-740322, EBI-717810;
Q08117-2:AES; NbExp=4; IntAct=EBI-740343, EBI-11741437;
Q9Y4X0:AMMECR1; NbExp=3; IntAct=EBI-740322, EBI-8583355;
P54253:ATXN1; NbExp=6; IntAct=EBI-740322, EBI-930964;
Q8N9N5:BANP; NbExp=3; IntAct=EBI-740322, EBI-744695;
Q9BXC9:BBS2; NbExp=3; IntAct=EBI-740322, EBI-748297;
A8KA13:BCL6B; NbExp=3; IntAct=EBI-740322, EBI-10174813;
O14503:BHLHE40; NbExp=3; IntAct=EBI-740322, EBI-711810;
Q8N9W6:BOLL; NbExp=3; IntAct=EBI-740322, EBI-998198;
Q6NUJ2:C11orf87; NbExp=3; IntAct=EBI-740322, EBI-6660291;
Q6P1W5:C1orf94; NbExp=4; IntAct=EBI-740322, EBI-946029;
Q6P5X5:C22orf39; NbExp=3; IntAct=EBI-740322, EBI-7317823;
Q13554:CAMK2B; NbExp=3; IntAct=EBI-740322, EBI-1058722;
P51959:CCNG1; NbExp=3; IntAct=EBI-740322, EBI-3905829;
O75909:CCNK; NbExp=4; IntAct=EBI-740322, EBI-739806;
Q9UJX2:CDC23; NbExp=4; IntAct=EBI-740322, EBI-396137;
Q96SW2:CRBN; NbExp=3; IntAct=EBI-740322, EBI-2510250;
Q02930-3:CREB5; NbExp=3; IntAct=EBI-740322, EBI-10192698;
P05813:CRYBA1; NbExp=3; IntAct=EBI-740322, EBI-7043337;
P07498:CSN3; NbExp=3; IntAct=EBI-740322, EBI-2602175;
Q15038:DAZAP2; NbExp=6; IntAct=EBI-740322, EBI-724310;
Q5TAQ9:DCAF8; NbExp=3; IntAct=EBI-740322, EBI-740686;
A2VCK2:DCDC2B; NbExp=3; IntAct=EBI-740322, EBI-10173222;
Q9BTE1:DCTN5; NbExp=3; IntAct=EBI-740322, EBI-747324;
Q9NQL9:DMRT3; NbExp=3; IntAct=EBI-740322, EBI-9679045;
Q7L591:DOK3; NbExp=3; IntAct=EBI-740322, EBI-2834978;
Q6PKX4:DOK6; NbExp=3; IntAct=EBI-740322, EBI-2880244;
O14531:DPYSL4; NbExp=3; IntAct=EBI-740322, EBI-719542;
Q86UW9:DTX2; NbExp=7; IntAct=EBI-740322, EBI-740376;
O95967:EFEMP2; NbExp=3; IntAct=EBI-740322, EBI-743414;
Q9H5Z6:FAM124B; NbExp=3; IntAct=EBI-740322, EBI-741626;
Q92567:FAM168A; NbExp=5; IntAct=EBI-740322, EBI-7957930;
Q92567-2:FAM168A; NbExp=4; IntAct=EBI-740343, EBI-11978259;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-740322, EBI-10244131;
Q96D16:FBXL18; NbExp=3; IntAct=EBI-740322, EBI-744419;
Q9BVV2:FNDC11; NbExp=3; IntAct=EBI-740322, EBI-744935;
Q99958:FOXC2; NbExp=3; IntAct=EBI-740322, EBI-3956892;
Q9BZS1:FOXP3; NbExp=4; IntAct=EBI-740322, EBI-983719;
O75603:GCM2; NbExp=3; IntAct=EBI-740322, EBI-10188645;
Q8IVS8:GLYCTK; NbExp=3; IntAct=EBI-740322, EBI-748515;
Q9NWQ4:GPATCH2L; NbExp=3; IntAct=EBI-740322, EBI-5666657;
Q13227:GPS2; NbExp=3; IntAct=EBI-740322, EBI-713355;
Q13588:GRAP; NbExp=3; IntAct=EBI-740322, EBI-2847510;
P40956:GTS1 (xeno); NbExp=3; IntAct=EBI-740343, EBI-7968;
Q8N4W5:hCG_2008078; NbExp=6; IntAct=EBI-740343, EBI-11746188;
B4DNA4:hCG_20425; NbExp=3; IntAct=EBI-740322, EBI-7399002;
Q9UBP5:HEY2; NbExp=3; IntAct=EBI-740322, EBI-750630;
Q9NQ87:HEYL; NbExp=4; IntAct=EBI-740322, EBI-751092;
Q8WVV9:HNRNPLL; NbExp=3; IntAct=EBI-740322, EBI-535849;
P49639:HOXA1; NbExp=3; IntAct=EBI-740322, EBI-740785;
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-740322, EBI-3957603;
P01344:IGF2; NbExp=3; IntAct=EBI-740322, EBI-7178764;
Q9NXX0:ILF3; NbExp=3; IntAct=EBI-740322, EBI-743980;
Q0VD86:INCA1; NbExp=3; IntAct=EBI-740322, EBI-6509505;
Q9NRY2:INIP; NbExp=3; IntAct=EBI-740322, EBI-2881520;
Q9UHH9:IP6K2; NbExp=3; IntAct=EBI-740322, EBI-747509;
Q03020:ISU1 (xeno); NbExp=3; IntAct=EBI-740343, EBI-29901;
Q7L273:KCTD9; NbExp=3; IntAct=EBI-740322, EBI-4397613;
Q96HR4:KIAA1305; NbExp=3; IntAct=EBI-740322, EBI-10288524;
Q99706:KIR2DL4; NbExp=3; IntAct=EBI-740322, EBI-10294579;
P52292:KPNA2; NbExp=3; IntAct=EBI-740322, EBI-349938;
P59991:KRTAP12-2; NbExp=3; IntAct=EBI-740322, EBI-10176379;
P60329:KRTAP12-4; NbExp=4; IntAct=EBI-740343, EBI-10176396;
Q3LI72:KRTAP19-5; NbExp=4; IntAct=EBI-740322, EBI-1048945;
Q3SYF9:KRTAP19-7; NbExp=3; IntAct=EBI-740322, EBI-10241353;
A1A580:KRTAP23-1; NbExp=3; IntAct=EBI-740322, EBI-10171734;
Q6PEX3:KRTAP26-1; NbExp=4; IntAct=EBI-740343, EBI-3957672;
Q8IUC2:KRTAP8-1; NbExp=3; IntAct=EBI-740322, EBI-10261141;
Q14847-2:LASP1; NbExp=6; IntAct=EBI-740343, EBI-9088686;
Q6DKI2:LGALS9C; NbExp=3; IntAct=EBI-740322, EBI-9088829;
Q8N8I6:LINC00482; NbExp=3; IntAct=EBI-740322, EBI-10267998;
Q9Y4M8:LINC00588; NbExp=4; IntAct=EBI-740343, EBI-10039207;
P61968:LMO4; NbExp=3; IntAct=EBI-740322, EBI-2798728;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-740322, EBI-2341787;
Q8N1F1:LRRC75A-AS1; NbExp=3; IntAct=EBI-740322, EBI-2872544;
Q9Y5V3:MAGED1; NbExp=3; IntAct=EBI-740322, EBI-716006;
B1AHB0:MCM5; NbExp=3; IntAct=EBI-740322, EBI-10175425;
P32902:MRP4 (xeno); NbExp=3; IntAct=EBI-740343, EBI-16248;
P25566:MXR2 (xeno); NbExp=3; IntAct=EBI-740343, EBI-21713;
Q9NPC6:MYOZ2; NbExp=3; IntAct=EBI-740322, EBI-746712;
Q6XQN6:NAPRT; NbExp=3; IntAct=EBI-740322, EBI-10254872;
Q6XQN6-2:NAPRT; NbExp=3; IntAct=EBI-740322, EBI-10254820;
Q14511:NEDD9; NbExp=3; IntAct=EBI-740322, EBI-2108053;
Q6NSM0:NR1D2; NbExp=3; IntAct=EBI-740322, EBI-10250949;
P32242:OTX1; NbExp=4; IntAct=EBI-740322, EBI-740446;
Q6PIY7:PAPD4; NbExp=3; IntAct=EBI-740322, EBI-2802204;
Q9HBE1-4:PATZ1; NbExp=5; IntAct=EBI-740343, EBI-11022007;
J3QSH9:PER1; NbExp=3; IntAct=EBI-740322, EBI-10178671;
Q6IN51:PER1; NbExp=3; IntAct=EBI-740322, EBI-10250187;
O43189:PHF1; NbExp=4; IntAct=EBI-740322, EBI-530034;
Q9NWS0:PIH1D1; NbExp=3; IntAct=EBI-740322, EBI-357318;
Q13526:PIN1; NbExp=4; IntAct=EBI-740322, EBI-714158;
P78337:PITX1; NbExp=4; IntAct=EBI-740322, EBI-748265;
P40473:POG1 (xeno); NbExp=3; IntAct=EBI-740343, EBI-25207;
Q7Z3K3:POGZ; NbExp=4; IntAct=EBI-740343, EBI-1389308;
Q96HA1:POM121; NbExp=4; IntAct=EBI-740322, EBI-739990;
P09565:PP9974; NbExp=3; IntAct=EBI-740322, EBI-10196507;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-740322, EBI-1181405;
P54646:PRKAA2; NbExp=3; IntAct=EBI-740322, EBI-1383852;
P86479:PRR20C; NbExp=3; IntAct=EBI-740322, EBI-10172814;
Q96PU8:QKI; NbExp=5; IntAct=EBI-740322, EBI-945792;
Q9Y2K5-2:R3HDM2; NbExp=3; IntAct=EBI-740322, EBI-10326419;
Q9NWB1:RBFOX1; NbExp=3; IntAct=EBI-740322, EBI-945906;
Q6ZRY4:RBPMS2; NbExp=4; IntAct=EBI-740343, EBI-11987469;
Q96NR8:RDH12; NbExp=3; IntAct=EBI-740322, EBI-3916363;
O94955:RHOBTB3; NbExp=3; IntAct=EBI-740322, EBI-2367123;
Q9BQY4:RHOXF2; NbExp=6; IntAct=EBI-740322, EBI-372094;
Q0D2K3:RIPPLY1; NbExp=3; IntAct=EBI-740322, EBI-10226430;
A1L4F5:ROR2; NbExp=3; IntAct=EBI-740322, EBI-10172778;
Q04307:RPC11 (xeno); NbExp=3; IntAct=EBI-740343, EBI-15858;
Q14D33:RTP5; NbExp=3; IntAct=EBI-740322, EBI-10217913;
Q9BVN2:RUSC1; NbExp=3; IntAct=EBI-740322, EBI-6257312;
Q86WG5:SBF2; NbExp=3; IntAct=EBI-740322, EBI-2683289;
Q9NTN9-3:SEMA4G; NbExp=3; IntAct=EBI-740322, EBI-9089805;
Q08AM8:SH3RF2; NbExp=3; IntAct=EBI-740322, EBI-10225873;
O00241-2:SIRPB1; NbExp=3; IntAct=EBI-740322, EBI-10179231;
Q8NCR6:SMRP1; NbExp=3; IntAct=EBI-740322, EBI-10269322;
Q53HV7:SMUG1; NbExp=2; IntAct=EBI-740322, EBI-749970;
Q53HV7-2:SMUG1; NbExp=4; IntAct=EBI-740343, EBI-12275818;
P14678-2:SNRPB; NbExp=3; IntAct=EBI-740322, EBI-372475;
Q5TAL4:SNRPC; NbExp=3; IntAct=EBI-740322, EBI-10246938;
Q5T0L3:SPATA46; NbExp=3; IntAct=EBI-740322, EBI-750105;
Q6RVD6:SPATA8; NbExp=4; IntAct=EBI-740322, EBI-8635958;
Q9UQ90:SPG7; NbExp=3; IntAct=EBI-740322, EBI-717201;
P35184:SQT1 (xeno); NbExp=3; IntAct=EBI-740343, EBI-17971;
Q96SI9:STRBP; NbExp=4; IntAct=EBI-740322, EBI-740355;
P38340:TAE1 (xeno); NbExp=3; IntAct=EBI-740343, EBI-21116;
O95947:TBX6; NbExp=4; IntAct=EBI-740343, EBI-2824328;
Q96LM6:TEX37; NbExp=4; IntAct=EBI-740322, EBI-743976;
Q92734:TFG; NbExp=3; IntAct=EBI-740322, EBI-357061;
P35590:TIE1; NbExp=3; IntAct=EBI-740322, EBI-2256865;
Q9GZM7-3:TINAGL1; NbExp=3; IntAct=EBI-740322, EBI-10303636;
Q0P5Q0:TMSB4X; NbExp=3; IntAct=EBI-740322, EBI-10226570;
Q6FIE9:TOLLIP; NbExp=3; IntAct=EBI-740322, EBI-10249783;
Q9H0E2:TOLLIP; NbExp=4; IntAct=EBI-740322, EBI-74615;
Q9H496:TOR1AIP2; NbExp=3; IntAct=EBI-740322, EBI-2510146;
Q6ZVT0:TTLL10; NbExp=3; IntAct=EBI-740322, EBI-7844656;
O75896:TUSC2; NbExp=3; IntAct=EBI-740322, EBI-1052725;
O95231:VENTX; NbExp=3; IntAct=EBI-740322, EBI-10191303;
Q6RSH7:VHLL; NbExp=3; IntAct=EBI-740322, EBI-10254232;
A5D8V6:VPS37C; NbExp=3; IntAct=EBI-740322, EBI-2559305;
Q96KV7:WDR90; NbExp=3; IntAct=EBI-740322, EBI-9478492;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-740322, EBI-741158;
Q8TGQ8:YOL085W-A (xeno); NbExp=3; IntAct=EBI-740343, EBI-11537679;
Q12484:YOR343C (xeno); NbExp=3; IntAct=EBI-740343, EBI-29987;
A0A0C4DGF1:ZBTB32; NbExp=5; IntAct=EBI-740322, EBI-10188476;
Q96K80:ZC3H10; NbExp=4; IntAct=EBI-740322, EBI-742550;
Q66K41:ZNF385C; NbExp=3; IntAct=EBI-740322, EBI-10219231;
Q96MN9:ZNF488; NbExp=3; IntAct=EBI-740322, EBI-948288;
Q9P0T4:ZNF581; NbExp=6; IntAct=EBI-740343, EBI-745520;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17099224}.
Cytoplasm {ECO:0000269|PubMed:17099224}. Cytoplasm, P-body
{ECO:0000269|PubMed:26347403}. Note=Translocates into cytoplasmic
stress granules that probably correspond to P-bodies in response
to oxidative stress. {ECO:0000269|PubMed:26347403}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=A;
IsoId=Q93062-1; Sequence=Displayed;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=B;
IsoId=Q93062-2; Sequence=VSP_005813;
Name=C;
IsoId=Q93062-3; Sequence=VSP_005814;
Name=D;
IsoId=Q93062-4; Sequence=VSP_005815;
Name=E;
IsoId=Q93062-5; Sequence=VSP_005816;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, at various levels
depending on the isoform and the tissue.
-!- DOMAIN: The RRM domain is necessary for interaction with SMAD4.
Both the RRM domain and the C-terminus are required for
TGFB1/Smad-mediated transactivation activity.
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EMBL; D84110; BAA12228.1; -; mRNA.
EMBL; D84107; BAA12225.1; -; mRNA.
EMBL; D84108; BAA12226.1; -; mRNA.
EMBL; D84109; BAA12227.1; -; mRNA.
EMBL; D84111; BAA12229.1; -; mRNA.
EMBL; CH471080; EAW63451.1; -; Genomic_DNA.
EMBL; CH471080; EAW63453.1; -; Genomic_DNA.
EMBL; BC003608; AAH03608.1; -; mRNA.
CCDS; CCDS34875.1; -. [Q93062-2]
CCDS; CCDS34876.1; -. [Q93062-3]
CCDS; CCDS6077.1; -. [Q93062-1]
PIR; JC6127; JC6127.
RefSeq; NP_001008710.1; NM_001008710.2. [Q93062-1]
RefSeq; NP_001008711.1; NM_001008711.2. [Q93062-2]
RefSeq; NP_001008712.1; NM_001008712.2. [Q93062-3]
RefSeq; NP_006858.1; NM_006867.3. [Q93062-1]
RefSeq; XP_016868475.1; XM_017012986.1. [Q93062-1]
UniGene; Hs.334587; -.
PDB; 1BNY; Model; -; A=15-111.
PDB; 5CYJ; X-ray; 1.79 A; A/B=14-111.
PDB; 5DET; X-ray; 1.95 A; A/B=14-111.
PDBsum; 1BNY; -.
PDBsum; 5CYJ; -.
PDBsum; 5DET; -.
ProteinModelPortal; Q93062; -.
SMR; Q93062; -.
BioGrid; 116220; 197.
IntAct; Q93062; 268.
MINT; MINT-1434067; -.
STRING; 9606.ENSP00000340176; -.
iPTMnet; Q93062; -.
PhosphoSitePlus; Q93062; -.
DMDM; 13124469; -.
MaxQB; Q93062; -.
PaxDb; Q93062; -.
PeptideAtlas; Q93062; -.
PRIDE; Q93062; -.
Ensembl; ENST00000287771; ENSP00000287771; ENSG00000157110. [Q93062-2]
Ensembl; ENST00000320203; ENSP00000318102; ENSG00000157110. [Q93062-1]
Ensembl; ENST00000339877; ENSP00000340176; ENSG00000157110. [Q93062-3]
Ensembl; ENST00000397323; ENSP00000380486; ENSG00000157110. [Q93062-1]
GeneID; 11030; -.
KEGG; hsa:11030; -.
UCSC; uc003xib.5; human. [Q93062-1]
CTD; 11030; -.
DisGeNET; 11030; -.
EuPathDB; HostDB:ENSG00000157110.15; -.
GeneCards; RBPMS; -.
HGNC; HGNC:19097; RBPMS.
HPA; HPA056999; -.
MIM; 601558; gene.
neXtProt; NX_Q93062; -.
OpenTargets; ENSG00000157110; -.
PharmGKB; PA134985584; -.
eggNOG; KOG1457; Eukaryota.
eggNOG; ENOG410XSBT; LUCA.
GeneTree; ENSGT00500000044861; -.
HOGENOM; HOG000017369; -.
HOVERGEN; HBG069897; -.
InParanoid; Q93062; -.
OMA; FITREPY; -.
PhylomeDB; Q93062; -.
TreeFam; TF351070; -.
ChiTaRS; RBPMS; human.
GeneWiki; RBPMS; -.
GenomeRNAi; 11030; -.
PRO; PR:Q93062; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000157110; -.
CleanEx; HS_RBPMS; -.
ExpressionAtlas; Q93062; baseline and differential.
Genevisible; Q93062; HS.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035614; F:snRNA stem-loop binding; IBA:GO_Central.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Transcription;
Transcription regulation.
CHAIN 1 196 RNA-binding protein with multiple
splicing.
/FTId=PRO_0000081793.
DOMAIN 24 101 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 98 105 Interaction with RNA.
{ECO:0000269|PubMed:26347403}.
SITE 27 27 Interaction with RNA.
{ECO:0000269|PubMed:26347403}.
SITE 61 61 Interaction with RNA.
{ECO:0000269|PubMed:26347403}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 12 12 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WVB0}.
MOD_RES 113 113 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 133 196 YELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASL
HAQMRWLPPSEATSQGWKSRQFC -> LGGANEHGERQ
(in isoform D).
{ECO:0000303|PubMed:8855282}.
/FTId=VSP_005815.
VAR_SEQ 133 176 Missing (in isoform E).
{ECO:0000303|PubMed:8855282}.
/FTId=VSP_005816.
VAR_SEQ 177 196 MRWLPPSEATSQGWKSRQFC -> LCEGQTVRRSHPLSAPS
PDSASLAWFPV (in isoform B).
{ECO:0000303|PubMed:8855282}.
/FTId=VSP_005813.
VAR_SEQ 177 196 MRWLPPSEATSQGWKSRQFC -> CFSPEAKPNTPVFCPLL
QQIRFVSGNVFVTYQPTADQQRELPC (in isoform
C). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8855282}.
/FTId=VSP_005814.
MUTAGEN 27 27 F->A: Abolishes RNA binding.
{ECO:0000269|PubMed:26347403}.
MUTAGEN 36 38 KPR->EPE: Impairs dimerization and RNA
binding. {ECO:0000269|PubMed:26347403}.
MUTAGEN 65 65 F->A: Abolishes RNA binding.
{ECO:0000269|PubMed:26347403}.
MUTAGEN 97 97 E->A: Abolishes RNA binding; when
associated with A-100.
{ECO:0000269|PubMed:26347403}.
MUTAGEN 100 100 K->A: Abolishes RNA binding; when
associated with A-97.
{ECO:0000269|PubMed:26347403}.
MUTAGEN 100 100 K->E: Abolishes RNA binding.
{ECO:0000269|PubMed:26347403}.
MUTAGEN 103 104 TK->AA: Abolishes RNA binding.
{ECO:0000269|PubMed:26347403}.
STRAND 25 29 {ECO:0000244|PDB:5CYJ}.
HELIX 37 44 {ECO:0000244|PDB:5CYJ}.
STRAND 50 56 {ECO:0000244|PDB:5CYJ}.
STRAND 59 61 {ECO:0000244|PDB:5CYJ}.
STRAND 63 70 {ECO:0000244|PDB:5CYJ}.
HELIX 71 81 {ECO:0000244|PDB:5CYJ}.
STRAND 85 87 {ECO:0000244|PDB:5CYJ}.
STRAND 95 98 {ECO:0000244|PDB:5CYJ}.
HELIX 107 109 {ECO:0000244|PDB:5CYJ}.
SEQUENCE 196 AA; 21802 MW; 05DD964E62F8F88C CRC64;
MNNGGKAEKE NTPSEANLQE EEVRTLFVSG LPLDIKPREL YLLFRPFKGY EGSLIKLTSK
QPVGFVSFDS RSEAEAAKNA LNGIRFDPEI PQTLRLEFAK ANTKMAKNKL VGTPNPSTPL
PNTVPQFIAR EPYELTVPAL YPSSPEVWAP YPLYPAELAP ALPPPAFTYP ASLHAQMRWL
PPSEATSQGW KSRQFC


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