RBM3_HUMAN
ID RBM3_HUMAN Reviewed; 157 AA.
AC P98179;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=RNA-binding protein 3;
DE AltName: Full=RNA-binding motif protein 3;
DE AltName: Full=RNPL;
GN Name=RBM3; Synonyms=RNPL;
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].
RX PubMed=8634703; DOI=10.1093/hmg/4.12.2307;
RA Derry J.M., Kerns J.A., Francke U.;
RT "RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain.";
RL Hum. Mol. Genet. 4:2307-2311(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
RP PROTEIN SEQUENCE OF 48-75 AND 102-131, METHYLATION AT ARG-105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP INDUCTION BY HYPOXIA.
RX PubMed=15075239; DOI=10.1242/jcs.01026;
RA Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R., Koehne P.,
RA Fujita J., Seeger K.;
RT "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a
RT HIF-1-independent mechanism.";
RL J. Cell Sci. 117:1785-1794(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-47; ARG-105; ARG-121 AND ARG-131,
RP AND 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).
CC -!- FUNCTION: Cold-inducible mRNA binding protein that enhances global
CC protein synthesis at both physiological and mild hypothermic
CC temperatures. Reduces the relative abundance of microRNAs, when
CC overexpressed. Enhances phosphorylation of translation initiation
CC factors and active polysome formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal
CC subunits in an RNA-independent manner. Associates with ribosomes (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P98179; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-2949699, EBI-11984237;
CC P98179; P61978: HNRNPK; NbExp=6; IntAct=EBI-2949699, EBI-304185;
CC P98179; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-2949699, EBI-7060731;
CC P98179; Q9Y6M1: IGF2BP2; NbExp=6; IntAct=EBI-2949699, EBI-1024419;
CC P98179; Q5VWX1: KHDRBS2; NbExp=8; IntAct=EBI-2949699, EBI-742808;
CC P98179; O75525: KHDRBS3; NbExp=3; IntAct=EBI-2949699, EBI-722504;
CC P98179; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-2949699, EBI-2858213;
CC P98179; Q15365: PCBP1; NbExp=3; IntAct=EBI-2949699, EBI-946095;
CC P98179; P79522: PRR3; NbExp=3; IntAct=EBI-2949699, EBI-2803328;
CC P98179; P38159: RBMX; NbExp=7; IntAct=EBI-2949699, EBI-743526;
CC P98179; P0DJD3: RBMY1A1; NbExp=4; IntAct=EBI-2949699, EBI-8638511;
CC P98179; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-2949699, EBI-11994018;
CC P98179; Q15415: RBMY1J; NbExp=6; IntAct=EBI-2949699, EBI-8642021;
CC P98179; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-2949699, EBI-11987469;
CC P98179; P09012: SNRPA; NbExp=8; IntAct=EBI-2949699, EBI-607085;
CC P98179; P84103: SRSF3; NbExp=3; IntAct=EBI-2949699, EBI-372557;
CC P98179; P68318: VLTF3; Xeno; NbExp=2; IntAct=EBI-2949699, EBI-7366338;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}. Note=Localizes in mRNA
CC granules in dentrites. {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by hypoxia. {ECO:0000269|PubMed:15075239}.
CC -!- PTM: Arg-105 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; U28686; AAB17212.1; -; mRNA.
DR EMBL; AF196969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006825; AAH06825.1; -; mRNA.
DR CCDS; CCDS14301.1; -.
DR PIR; G01859; G01859.
DR RefSeq; NP_006734.1; NM_006743.4.
DR PDB; 7EB1; NMR; -; A=1-84.
DR PDBsum; 7EB1; -.
DR AlphaFoldDB; P98179; -.
DR BMRB; P98179; -.
DR SMR; P98179; -.
DR BioGRID; 111870; 153.
DR IntAct; P98179; 55.
DR MINT; P98179; -.
DR STRING; 9606.ENSP00000365950; -.
DR ChEMBL; CHEMBL4295793; -.
DR iPTMnet; P98179; -.
DR MetOSite; P98179; -.
DR PhosphoSitePlus; P98179; -.
DR BioMuta; RBM3; -.
DR DMDM; 1710620; -.
DR EPD; P98179; -.
DR jPOST; P98179; -.
DR MassIVE; P98179; -.
DR MaxQB; P98179; -.
DR PaxDb; P98179; -.
DR PeptideAtlas; P98179; -.
DR PRIDE; P98179; -.
DR ProteomicsDB; 57816; -.
DR TopDownProteomics; P98179; -.
DR Antibodypedia; 25719; 298 antibodies from 32 providers.
DR DNASU; 5935; -.
DR Ensembl; ENST00000376755.1; ENSP00000365946.1; ENSG00000102317.18.
DR Ensembl; ENST00000376759.8; ENSP00000365950.3; ENSG00000102317.18.
DR GeneID; 5935; -.
DR KEGG; hsa:5935; -.
DR MANE-Select; ENST00000376759.8; ENSP00000365950.3; NM_006743.5; NP_006734.1.
DR UCSC; uc004dkf.3; human.
DR CTD; 5935; -.
DR DisGeNET; 5935; -.
DR GeneCards; RBM3; -.
DR HGNC; HGNC:9900; RBM3.
DR HPA; ENSG00000102317; Low tissue specificity.
DR MIM; 300027; gene.
DR neXtProt; NX_P98179; -.
DR OpenTargets; ENSG00000102317; -.
DR PharmGKB; PA34265; -.
DR VEuPathDB; HostDB:ENSG00000102317; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153524; -.
DR HOGENOM; CLU_012062_28_1_1; -.
DR InParanoid; P98179; -.
DR OMA; WHTTDDA; -.
DR OrthoDB; 1507330at2759; -.
DR PhylomeDB; P98179; -.
DR TreeFam; TF354331; -.
DR PathwayCommons; P98179; -.
DR SignaLink; P98179; -.
DR BioGRID-ORCS; 5935; 9 hits in 704 CRISPR screens.
DR ChiTaRS; RBM3; human.
DR GeneWiki; RBM3; -.
DR GenomeRNAi; 5935; -.
DR Pharos; P98179; Tbio.
DR PRO; PR:P98179; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P98179; protein.
DR Bgee; ENSG00000102317; Expressed in endometrium epithelium and 198 other tissues.
DR ExpressionAtlas; P98179; baseline and differential.
DR Genevisible; P98179; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR CDD; cd12449; RRM_CIRBP_RBM3; 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; IPR034278; RBM3/CIRBP_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; Cell projection; Cytoplasm; Direct protein sequencing;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Stress response.
FT CHAIN 1..157
FT /note="RNA-binding protein 3"
FT /id="PRO_0000081752"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 81..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O89086"
FT MOD_RES 105
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 105
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 121
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 131
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:7EB1"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:7EB1"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:7EB1"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:7EB1"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:7EB1"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:7EB1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7EB1"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:7EB1"
SQ SEQUENCE 157 AA; 17170 MW; 91C12E2A3E32CFA4 CRC64;
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA
SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG RSYSRGGGDQ GYGSGRYYDS
RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN YRDNYDN
