RBM47_HUMAN
ID RBM47_HUMAN Reviewed; 593 AA.
AC A0AV96; A0PJK2; B5MED4; Q8NI52; Q8NI53; Q9NXG3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=RNA-binding protein 47;
DE AltName: Full=RNA-binding motif protein 47;
GN Name=RBM47;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RA Wang A., Gonzalez-Santos J.M., Hu J.;
RT "SPICE cloning and characterization of a human cDNA encoding a novel RNA-
RT binding protein.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-565.
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-565.
RC TISSUE=Brain;
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-332; ARG-394 AND ARG-405, AND
RP IDENTIFICATION BY MASS 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 [6]
RP STRUCTURE BY NMR OF 150-245.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RRM domain of unnamed protein product.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- INTERACTION:
CC A0AV96; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-2823850, EBI-12809220;
CC A0AV96; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-2823850, EBI-946029;
CC A0AV96; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-2823850, EBI-1383687;
CC A0AV96; Q8N6W0: CELF5; NbExp=3; IntAct=EBI-2823850, EBI-12139335;
CC A0AV96; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-2823850, EBI-10220102;
CC A0AV96; P32243-2: OTX2; NbExp=3; IntAct=EBI-2823850, EBI-9087860;
CC A0AV96; P57721-2: PCBP3; NbExp=3; IntAct=EBI-2823850, EBI-11983983;
CC A0AV96; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-2823850, EBI-740924;
CC A0AV96; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-2823850, EBI-12123390;
CC A0AV96; Q66K41-2: ZNF385C; NbExp=3; IntAct=EBI-2823850, EBI-12055653;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0AV96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0AV96-2; Sequence=VSP_028839;
CC -!- SIMILARITY: Belongs to the RRM RBM47 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM21973.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF261889; AAM21972.1; -; Genomic_DNA.
DR EMBL; AF262323; AAM21973.1; ALT_FRAME; mRNA.
DR EMBL; AK000280; BAA91049.1; -; mRNA.
DR EMBL; AC098869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034402; AAH34402.1; -; mRNA.
DR EMBL; BC126261; AAI26262.1; -; mRNA.
DR CCDS; CCDS3460.1; -. [A0AV96-2]
DR CCDS; CCDS43223.1; -. [A0AV96-1]
DR RefSeq; NP_001092104.1; NM_001098634.1. [A0AV96-1]
DR RefSeq; NP_061900.2; NM_019027.3. [A0AV96-2]
DR RefSeq; XP_005248160.1; XM_005248103.3. [A0AV96-1]
DR RefSeq; XP_005248164.1; XM_005248107.3.
DR RefSeq; XP_005248165.1; XM_005248108.3. [A0AV96-1]
DR RefSeq; XP_005248166.1; XM_005248109.4. [A0AV96-1]
DR RefSeq; XP_011512006.1; XM_011513704.2.
DR RefSeq; XP_011512009.1; XM_011513707.2. [A0AV96-1]
DR RefSeq; XP_011512010.1; XM_011513708.2. [A0AV96-1]
DR RefSeq; XP_016863793.1; XM_017008304.1. [A0AV96-1]
DR RefSeq; XP_016863794.1; XM_017008305.1.
DR RefSeq; XP_016863795.1; XM_017008306.1. [A0AV96-1]
DR RefSeq; XP_016863796.1; XM_017008307.1. [A0AV96-1]
DR RefSeq; XP_016863797.1; XM_017008308.1. [A0AV96-1]
DR RefSeq; XP_016863799.1; XM_017008310.1. [A0AV96-2]
DR PDB; 2DIS; NMR; -; A=150-245.
DR PDBsum; 2DIS; -.
DR AlphaFoldDB; A0AV96; -.
DR SMR; A0AV96; -.
DR BioGRID; 119998; 210.
DR IntAct; A0AV96; 22.
DR STRING; 9606.ENSP00000371212; -.
DR GlyGen; A0AV96; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A0AV96; -.
DR PhosphoSitePlus; A0AV96; -.
DR BioMuta; RBM47; -.
DR EPD; A0AV96; -.
DR jPOST; A0AV96; -.
DR MassIVE; A0AV96; -.
DR MaxQB; A0AV96; -.
DR PaxDb; A0AV96; -.
DR PeptideAtlas; A0AV96; -.
DR PRIDE; A0AV96; -.
DR ProteomicsDB; 14; -. [A0AV96-1]
DR ProteomicsDB; 15; -. [A0AV96-2]
DR Antibodypedia; 1338; 46 antibodies from 20 providers.
DR DNASU; 54502; -.
DR Ensembl; ENST00000295971.12; ENSP00000295971.7; ENSG00000163694.15. [A0AV96-1]
DR Ensembl; ENST00000381793.6; ENSP00000371212.2; ENSG00000163694.15. [A0AV96-1]
DR Ensembl; ENST00000381795.10; ENSP00000371214.6; ENSG00000163694.15. [A0AV96-2]
DR GeneID; 54502; -.
DR KEGG; hsa:54502; -.
DR MANE-Select; ENST00000295971.12; ENSP00000295971.7; NM_001098634.2; NP_001092104.1.
DR UCSC; uc003gvc.3; human. [A0AV96-1]
DR CTD; 54502; -.
DR DisGeNET; 54502; -.
DR GeneCards; RBM47; -.
DR HGNC; HGNC:30358; RBM47.
DR HPA; ENSG00000163694; Low tissue specificity.
DR MIM; 619104; gene.
DR neXtProt; NX_A0AV96; -.
DR OpenTargets; ENSG00000163694; -.
DR PharmGKB; PA162400825; -.
DR VEuPathDB; HostDB:ENSG00000163694; -.
DR eggNOG; KOG0117; Eukaryota.
DR GeneTree; ENSGT00940000156979; -.
DR InParanoid; A0AV96; -.
DR OMA; APNIQRI; -.
DR OrthoDB; 1384330at2759; -.
DR PhylomeDB; A0AV96; -.
DR TreeFam; TF314932; -.
DR PathwayCommons; A0AV96; -.
DR SignaLink; A0AV96; -.
DR BioGRID-ORCS; 54502; 28 hits in 1081 CRISPR screens.
DR ChiTaRS; RBM47; human.
DR EvolutionaryTrace; A0AV96; -.
DR GenomeRNAi; 54502; -.
DR Pharos; A0AV96; Tbio.
DR PRO; PR:A0AV96; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; A0AV96; protein.
DR Bgee; ENSG00000163694; Expressed in renal medulla and 173 other tissues.
DR ExpressionAtlas; A0AV96; baseline and differential.
DR Genevisible; A0AV96; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR CDD; cd12491; RRM2_RBM47; 1.
DR CDD; cd12497; RRM3_RBM47; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034442; RBM47.
DR InterPro; IPR034440; RBM47_RRM2.
DR InterPro; IPR034445; RBM47_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR21245:SF6; PTHR21245:SF6; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Methylation; Nucleus;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..593
FT /note="RNA-binding protein 47"
FT /id="PRO_0000307855"
FT DOMAIN 71..149
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 151..233
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 246..318
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 394
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 394
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 405
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 405
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 375..443
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028839"
FT VARIANT 538
FT /note="G -> R (in dbSNP:rs35529250)"
FT /id="VAR_061832"
FT VARIANT 565
FT /note="M -> V (in dbSNP:rs278981)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054770"
FT CONFLICT 9
FT /note="A -> T (in Ref. 1; AAM21973)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> T (in Ref. 2; BAA91049)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="G -> V (in Ref. 1; AAM21972)"
FT /evidence="ECO:0000305"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2DIS"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:2DIS"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2DIS"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2DIS"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:2DIS"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:2DIS"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:2DIS"
FT TURN 212..216
FT /evidence="ECO:0007829|PDB:2DIS"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:2DIS"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2DIS"
SQ SEQUENCE 593 AA; 64099 MW; AEA061F89A68010B CRC64;
MTAEDSTAAM SSDSAAGSSA KVPEGVAGAP NEAALLALME RTGYSMVQEN GQRKYGGPPP
GWEGPHPQRG CEVFVGKIPR DVYEDELVPV FEAVGRIYEL RLMMDFDGKN RGYAFVMYCH
KHEAKRAVRE LNNYEIRPGR LLGVCCSVDN CRLFIGGIPK MKKREEILEE IAKVTEGVLD
VIVYASAADK MKNRGFAFVE YESHRAAAMA RRKLMPGRIQ LWGHQIAVDW AEPEIDVDED
VMETVKILYV RNLMIETTED TIKKSFGQFN PGCVERVKKI RDYAFVHFTS REDAVHAMNN
LNGTELEGSC LEVTLAKPVD KEQYSRYQKA ARGGGAAEAA QQPSYVYSCD PYTLAYYGYP
YNALIGPNRD YFVKAGSIRG RGRGAAGNRA PGPRGSYLGG YSAGRGIYSR YHEGKGKQQE
KGYELVPNLE IPTVNPVAIK PGTVAIPAIG AQYSMFPAAP APKMIEDGKI HTVEHMISPI
AVQPDPASAA AAAAAAAAAA AAVIPTVSTP PPFQGRPITP VYTVAPNVQR IPTAGIYGAS
YVPFAAPATA TIATLQKNAA AAAAMYGGYA GYIPQAFPAA AIQVPIPDVY QTY
