RBPS2_HUMAN
ID RBPS2_HUMAN Reviewed; 209 AA.
AC Q6ZRY4; A2RRG0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA-binding protein with multiple splicing 2;
DE AltName: Full=RNA binding protein, mRNA processing factor 2;
GN Name=RBPMS2;
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 [MRNA] (ISOFORM 1).
RA Huang C.Q., Wu S.L., Liu S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [6]
RP STRUCTURE BY NMR OF 27-117, FUNCTION, RNA-BINDING, SUBUNIT, INTERACTION
RP WITH EEF2, AND MUTAGENESIS OF LEU-49.
RX PubMed=25064856; DOI=10.1093/nar/gku692;
RA Sagnol S., Yang Y., Bessin Y., Allemand F., Hapkova I., Notarnicola C.,
RA Guichou J.F., Faure S., Labesse G., de Santa Barbara P.;
RT "Homodimerization of RBPMS2 through a new RRM-interaction motif is
RT necessary to control smooth muscle plasticity.";
RL Nucleic Acids Res. 42:10173-10184(2014).
CC -!- FUNCTION: RNA-binding protein involved in the regulation of smooth
CC muscle cell differentiation and proliferation in the gastrointestinal
CC system (PubMed:25064856). Binds NOG mRNA, the major inhibitor of the
CC bone morphogenetic protein (BMP) pathway. Mediates an increase of NOG
CC mRNA levels, thereby contributing to the negative regulation of BMP
CC signaling pathway and promoting reversible dedifferentiation and
CC proliferation of smooth muscle cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9W6I1, ECO:0000269|PubMed:25064856}.
CC -!- SUBUNIT: Homodimer (PubMed:25064856). Interacts with EEF2
CC (PubMed:25064856). {ECO:0000269|PubMed:25064856}.
CC -!- INTERACTION:
CC Q6ZRY4; P19801: AOC1; NbExp=3; IntAct=EBI-11987469, EBI-12826295;
CC Q6ZRY4; Q03989: ARID5A; NbExp=3; IntAct=EBI-11987469, EBI-948603;
CC Q6ZRY4; O14503: BHLHE40; NbExp=3; IntAct=EBI-11987469, EBI-711810;
CC Q6ZRY4; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-11987469, EBI-11983447;
CC Q6ZRY4; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-11987469, EBI-12809220;
CC Q6ZRY4; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-11987469, EBI-11976299;
CC Q6ZRY4; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11987469, EBI-1383687;
CC Q6ZRY4; Q14781-2: CBX2; NbExp=3; IntAct=EBI-11987469, EBI-11974585;
CC Q6ZRY4; Q9BZC1-2: CELF4; NbExp=3; IntAct=EBI-11987469, EBI-12818201;
CC Q6ZRY4; Q8IYX4: DND1; NbExp=3; IntAct=EBI-11987469, EBI-12071340;
CC Q6ZRY4; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-11987469, EBI-10213520;
CC Q6ZRY4; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-11987469, EBI-11978259;
CC Q6ZRY4; Q9NU39: FOXD4L1; NbExp=4; IntAct=EBI-11987469, EBI-11320806;
CC Q6ZRY4; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-11987469, EBI-11961494;
CC Q6ZRY4; O75593: FOXH1; NbExp=3; IntAct=EBI-11987469, EBI-1759806;
CC Q6ZRY4; Q96I24-2: FUBP3; NbExp=3; IntAct=EBI-11987469, EBI-12267436;
CC Q6ZRY4; P07910: HNRNPC; NbExp=3; IntAct=EBI-11987469, EBI-357966;
CC Q6ZRY4; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-11987469, EBI-7060731;
CC Q6ZRY4; Q00839-2: HNRNPU; NbExp=3; IntAct=EBI-11987469, EBI-351143;
CC Q6ZRY4; Q8IZ03: IFIT2; NbExp=3; IntAct=EBI-11987469, EBI-746217;
CC Q6ZRY4; Q13351: KLF1; NbExp=3; IntAct=EBI-11987469, EBI-8284732;
CC Q6ZRY4; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-11987469, EBI-9478422;
CC Q6ZRY4; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-11987469, EBI-1052037;
CC Q6ZRY4; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-11987469, EBI-1048945;
CC Q6ZRY4; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-11987469, EBI-12805508;
CC Q6ZRY4; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-11987469, EBI-10241353;
CC Q6ZRY4; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-11987469, EBI-12111050;
CC Q6ZRY4; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11987469, EBI-11962084;
CC Q6ZRY4; Q8IUC2: KRTAP8-1; NbExp=5; IntAct=EBI-11987469, EBI-10261141;
CC Q6ZRY4; Q14847-2: LASP1; NbExp=3; IntAct=EBI-11987469, EBI-9088686;
CC Q6ZRY4; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-11987469, EBI-716006;
CC Q6ZRY4; Q13064: MKRN3; NbExp=3; IntAct=EBI-11987469, EBI-2340269;
CC Q6ZRY4; P35548: MSX2; NbExp=3; IntAct=EBI-11987469, EBI-6447480;
CC Q6ZRY4; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-11987469, EBI-2858213;
CC Q6ZRY4; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-11987469, EBI-11022007;
CC Q6ZRY4; Q15365: PCBP1; NbExp=4; IntAct=EBI-11987469, EBI-946095;
CC Q6ZRY4; O75864: PPP1R37; NbExp=3; IntAct=EBI-11987469, EBI-5235692;
CC Q6ZRY4; P86480: PRR20D; NbExp=3; IntAct=EBI-11987469, EBI-12754095;
CC Q6ZRY4; Q9UKA9-2: PTBP2; NbExp=3; IntAct=EBI-11987469, EBI-12255608;
CC Q6ZRY4; Q53GL6: RALY; NbExp=3; IntAct=EBI-11987469, EBI-9512693;
CC Q6ZRY4; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-11987469, EBI-12123390;
CC Q6ZRY4; O43251-10: RBFOX2; NbExp=5; IntAct=EBI-11987469, EBI-11963050;
CC Q6ZRY4; P98179: RBM3; NbExp=3; IntAct=EBI-11987469, EBI-2949699;
CC Q6ZRY4; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-11987469, EBI-740773;
CC Q6ZRY4; Q9BTD8: RBM42; NbExp=3; IntAct=EBI-11987469, EBI-746862;
CC Q6ZRY4; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-11987469, EBI-12068216;
CC Q6ZRY4; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-11987469, EBI-740343;
CC Q6ZRY4; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-11987469, EBI-11987469;
CC Q6ZRY4; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-11987469, EBI-372094;
CC Q6ZRY4; Q13214-2: SEMA3B; NbExp=3; IntAct=EBI-11987469, EBI-11017428;
CC Q6ZRY4; P09012: SNRPA; NbExp=6; IntAct=EBI-11987469, EBI-607085;
CC Q6ZRY4; Q96SI9: STRBP; NbExp=3; IntAct=EBI-11987469, EBI-740355;
CC Q6ZRY4; Q96A09: TENT5B; NbExp=3; IntAct=EBI-11987469, EBI-752030;
CC Q6ZRY4; Q96LM6: TEX37; NbExp=3; IntAct=EBI-11987469, EBI-743976;
CC Q6ZRY4; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-11987469, EBI-11064654;
CC Q6ZRY4; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-11987469, EBI-12068150;
CC Q6ZRY4; Q13432: UNC119; NbExp=3; IntAct=EBI-11987469, EBI-711260;
CC Q6ZRY4; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-11987469, EBI-11975223;
CC Q6ZRY4; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-11987469, EBI-2559305;
CC Q6ZRY4; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-11987469, EBI-10188476;
CC Q6ZRY4; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-11987469, EBI-742550;
CC Q6ZRY4; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-11987469, EBI-7850213;
CC Q6ZRY4; Q66K41-2: ZNF385C; NbExp=3; IntAct=EBI-11987469, EBI-12055653;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25064856}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZRY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZRY4-2; Sequence=VSP_056896;
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DR EMBL; AY369207; AAQ73311.1; -; mRNA.
DR EMBL; AK127873; BAC87172.1; -; mRNA.
DR EMBL; AC091582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131612; AAI31613.1; -; mRNA.
DR CCDS; CCDS32271.1; -. [Q6ZRY4-1]
DR RefSeq; NP_919248.1; NM_194272.2. [Q6ZRY4-1]
DR PDB; 2M9K; NMR; -; A/B=27-117.
DR PDBsum; 2M9K; -.
DR AlphaFoldDB; Q6ZRY4; -.
DR BMRB; Q6ZRY4; -.
DR SMR; Q6ZRY4; -.
DR BioGRID; 131505; 94.
DR IntAct; Q6ZRY4; 66.
DR STRING; 9606.ENSP00000300069; -.
DR iPTMnet; Q6ZRY4; -.
DR PhosphoSitePlus; Q6ZRY4; -.
DR BioMuta; RBPMS2; -.
DR DMDM; 74762401; -.
DR EPD; Q6ZRY4; -.
DR jPOST; Q6ZRY4; -.
DR MassIVE; Q6ZRY4; -.
DR MaxQB; Q6ZRY4; -.
DR PaxDb; Q6ZRY4; -.
DR PeptideAtlas; Q6ZRY4; -.
DR PRIDE; Q6ZRY4; -.
DR ProteomicsDB; 467; -.
DR ProteomicsDB; 68173; -. [Q6ZRY4-1]
DR Antibodypedia; 25848; 91 antibodies from 17 providers.
DR DNASU; 348093; -.
DR Ensembl; ENST00000300069.5; ENSP00000300069.4; ENSG00000166831.9. [Q6ZRY4-1]
DR Ensembl; ENST00000560606.5; ENSP00000456720.1; ENSG00000166831.9. [Q6ZRY4-2]
DR GeneID; 348093; -.
DR KEGG; hsa:348093; -.
DR MANE-Select; ENST00000300069.5; ENSP00000300069.4; NM_194272.3; NP_919248.1.
DR UCSC; uc002anq.4; human. [Q6ZRY4-1]
DR CTD; 348093; -.
DR DisGeNET; 348093; -.
DR GeneCards; RBPMS2; -.
DR HGNC; HGNC:19098; RBPMS2.
DR HPA; ENSG00000166831; Tissue enhanced (heart).
DR MIM; 619034; gene.
DR neXtProt; NX_Q6ZRY4; -.
DR OpenTargets; ENSG00000166831; -.
DR PharmGKB; PA134871904; -.
DR VEuPathDB; HostDB:ENSG00000166831; -.
DR eggNOG; KOG1457; Eukaryota.
DR GeneTree; ENSGT00940000158086; -.
DR HOGENOM; CLU_099973_3_0_1; -.
DR InParanoid; Q6ZRY4; -.
DR OMA; MRWFPSS; -.
DR OrthoDB; 1368991at2759; -.
DR PhylomeDB; Q6ZRY4; -.
DR TreeFam; TF351070; -.
DR PathwayCommons; Q6ZRY4; -.
DR SignaLink; Q6ZRY4; -.
DR BioGRID-ORCS; 348093; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; RBPMS2; human.
DR GenomeRNAi; 348093; -.
DR Pharos; Q6ZRY4; Tbio.
DR PRO; PR:Q6ZRY4; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6ZRY4; protein.
DR Bgee; ENSG00000166831; Expressed in cardiac muscle of right atrium and 124 other tissues.
DR Genevisible; Q6ZRY4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR CDD; cd12683; RRM_RBPMS2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034787; RBPMS2_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..209
FT /note="RNA-binding protein with multiple splicing 2"
FT /id="PRO_0000274909"
FT DOMAIN 31..108
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..51
FT /note="Important for homodimerization"
FT /evidence="ECO:0000269|PubMed:25064856"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056896"
FT MUTAGEN 49
FT /note="L->E: Strongly reduces homodimerization and
FT interaction with EEF2. Strongly reduces NOG mRNA binding.
FT Loss of function in gastrointestinal smooth muscle cell
FT differentiation."
FT /evidence="ECO:0000269|PubMed:25064856"
FT MUTAGEN 49
FT /note="L->Q: No effect on homodimerization. No effect on
FT function in gastrointestinal smooth muscle cell
FT differentiation."
FT /evidence="ECO:0000269|PubMed:25064856"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2M9K"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2M9K"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2M9K"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2M9K"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2M9K"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:2M9K"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2M9K"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2M9K"
SQ SEQUENCE 209 AA; 22497 MW; E7924D0CD3AD860C CRC64;
MSNLKPDGEH GGSTGTGSGA GSGGALEEEV RTLFVSGLPV DIKPRELYLL FRPFKGYEGS
LIKLTARQPV GFVIFDSRAG AEAAKNALNG IRFDPENPQT LRLEFAKANT KMAKSKLMAT
PNPSNVHPAL GAHFIARDPY DLMGAALIPA SPEAWAPYPL YTTELTPAIS HAAFTYPTAT
AAAAALHAQV RWYPSSDTTQ QGWKYRQFC
