Full text data of RBM3
RBM3
(RNPL)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Putative RNA-binding protein 3 (RNA-binding motif protein 3; RNPL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Putative RNA-binding protein 3 (RNA-binding motif protein 3; RNPL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00024320
IPI00024320 Putative RNA-binding protein 3 RNA binding and processing soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00024320 Putative RNA-binding protein 3 RNA binding and processing soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P98179
ID RBM3_HUMAN Reviewed; 157 AA.
AC P98179;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Putative 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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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
RT project: 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 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 MASS
RP SPECTROMETRY.
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem 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.,
RA Koehne P., Fujita J., Seeger K.;
RT "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP
RT by a HIF-1-independent mechanism.";
RL J. Cell Sci. 117:1785-1794(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASS
RP SPECTROMETRY.
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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).
CC -!- SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal
CC subunits in an RNA-independent manner. Associates with ribosomes
CC (By similarity).
CC -!- INTERACTION:
CC P68318:VLTF3 (xeno); NbExp=2; IntAct=EBI-2949699, EBI-7366338;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). Cell projection, dendrite (By similarity).
CC Note=Localizes in mRNA granules in dentrites (By similarity).
CC -!- INDUCTION: Up-regulated by hypoxia.
CC -!- PTM: Arg-105 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: Phosphorylated (By similarity).
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U28686; AAB17212.1; -; mRNA.
DR EMBL; AF196969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006825; AAH06825.1; -; mRNA.
DR PIR; G01859; G01859.
DR RefSeq; NP_006734.1; NM_006743.4.
DR UniGene; Hs.301404; -.
DR ProteinModelPortal; P98179; -.
DR SMR; P98179; 1-126.
DR IntAct; P98179; 4.
DR MINT; MINT-5002714; -.
DR STRING; 9606.ENSP00000365946; -.
DR PhosphoSite; P98179; -.
DR DMDM; 1710620; -.
DR PaxDb; P98179; -.
DR PeptideAtlas; P98179; -.
DR PRIDE; P98179; -.
DR DNASU; 5935; -.
DR Ensembl; ENST00000376755; ENSP00000365946; ENSG00000102317.
DR Ensembl; ENST00000376759; ENSP00000365950; ENSG00000102317.
DR Ensembl; ENST00000598825; ENSP00000470199; ENSG00000268489.
DR Ensembl; ENST00000600134; ENSP00000471507; ENSG00000268489.
DR GeneID; 5935; -.
DR KEGG; hsa:5935; -.
DR UCSC; uc004dkf.2; human.
DR CTD; 5935; -.
DR GeneCards; GC0XP048432; -.
DR HGNC; HGNC:9900; RBM3.
DR HPA; HPA003624; -.
DR MIM; 300027; gene.
DR neXtProt; NX_P98179; -.
DR PharmGKB; PA34265; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000276232; -.
DR HOVERGEN; HBG107480; -.
DR InParanoid; P98179; -.
DR KO; K13186; -.
DR OMA; SDAMRAM; -.
DR PhylomeDB; P98179; -.
DR ChiTaRS; RBM3; human.
DR GeneWiki; RBM3; -.
DR GenomeRNAi; 5935; -.
DR NextBio; 23136; -.
DR PRO; PR:P98179; -.
DR ArrayExpress; P98179; -.
DR Bgee; P98179; -.
DR CleanEx; HS_RBM3; -.
DR Genevestigator; P98179; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0006412; P:translation; IEA:Ensembl.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cell projection; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Stress response.
FT CHAIN 1 157 Putative RNA-binding protein 3.
FT /FTId=PRO_0000081752.
FT DOMAIN 6 84 RRM.
FT COMPBIAS 88 149 Gly-rich.
FT MOD_RES 105 105 Dimethylated arginine; in A2780 ovarian
FT carcinoma cell line.
FT MOD_RES 105 105 Omega-N-methylated arginine.
FT MOD_RES 147 147 Phosphoserine.
FT MOD_RES 155 155 Phosphotyrosine.
SQ SEQUENCE 157 AA; 17170 MW; 91C12E2A3E32CFA4 CRC64;
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA
SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG RSYSRGGGDQ GYGSGRYYDS
RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN YRDNYDN
//
ID RBM3_HUMAN Reviewed; 157 AA.
AC P98179;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Putative 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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT 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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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
RT project: 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 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 MASS
RP SPECTROMETRY.
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem 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.,
RA Koehne P., Fujita J., Seeger K.;
RT "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP
RT by a HIF-1-independent mechanism.";
RL J. Cell Sci. 117:1785-1794(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASS
RP SPECTROMETRY.
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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).
CC -!- SUBUNIT: Interacts with RPL4. Associates with the 60S ribosomal
CC subunits in an RNA-independent manner. Associates with ribosomes
CC (By similarity).
CC -!- INTERACTION:
CC P68318:VLTF3 (xeno); NbExp=2; IntAct=EBI-2949699, EBI-7366338;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC similarity). Cell projection, dendrite (By similarity).
CC Note=Localizes in mRNA granules in dentrites (By similarity).
CC -!- INDUCTION: Up-regulated by hypoxia.
CC -!- PTM: Arg-105 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: Phosphorylated (By similarity).
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U28686; AAB17212.1; -; mRNA.
DR EMBL; AF196969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006825; AAH06825.1; -; mRNA.
DR PIR; G01859; G01859.
DR RefSeq; NP_006734.1; NM_006743.4.
DR UniGene; Hs.301404; -.
DR ProteinModelPortal; P98179; -.
DR SMR; P98179; 1-126.
DR IntAct; P98179; 4.
DR MINT; MINT-5002714; -.
DR STRING; 9606.ENSP00000365946; -.
DR PhosphoSite; P98179; -.
DR DMDM; 1710620; -.
DR PaxDb; P98179; -.
DR PeptideAtlas; P98179; -.
DR PRIDE; P98179; -.
DR DNASU; 5935; -.
DR Ensembl; ENST00000376755; ENSP00000365946; ENSG00000102317.
DR Ensembl; ENST00000376759; ENSP00000365950; ENSG00000102317.
DR Ensembl; ENST00000598825; ENSP00000470199; ENSG00000268489.
DR Ensembl; ENST00000600134; ENSP00000471507; ENSG00000268489.
DR GeneID; 5935; -.
DR KEGG; hsa:5935; -.
DR UCSC; uc004dkf.2; human.
DR CTD; 5935; -.
DR GeneCards; GC0XP048432; -.
DR HGNC; HGNC:9900; RBM3.
DR HPA; HPA003624; -.
DR MIM; 300027; gene.
DR neXtProt; NX_P98179; -.
DR PharmGKB; PA34265; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000276232; -.
DR HOVERGEN; HBG107480; -.
DR InParanoid; P98179; -.
DR KO; K13186; -.
DR OMA; SDAMRAM; -.
DR PhylomeDB; P98179; -.
DR ChiTaRS; RBM3; human.
DR GeneWiki; RBM3; -.
DR GenomeRNAi; 5935; -.
DR NextBio; 23136; -.
DR PRO; PR:P98179; -.
DR ArrayExpress; P98179; -.
DR Bgee; P98179; -.
DR CleanEx; HS_RBM3; -.
DR Genevestigator; P98179; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0006412; P:translation; IEA:Ensembl.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cell projection; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Stress response.
FT CHAIN 1 157 Putative RNA-binding protein 3.
FT /FTId=PRO_0000081752.
FT DOMAIN 6 84 RRM.
FT COMPBIAS 88 149 Gly-rich.
FT MOD_RES 105 105 Dimethylated arginine; in A2780 ovarian
FT carcinoma cell line.
FT MOD_RES 105 105 Omega-N-methylated arginine.
FT MOD_RES 147 147 Phosphoserine.
FT MOD_RES 155 155 Phosphotyrosine.
SQ SEQUENCE 157 AA; 17170 MW; 91C12E2A3E32CFA4 CRC64;
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA
SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG RSYSRGGGDQ GYGSGRYYDS
RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN YRDNYDN
//
MIM
300027
*RECORD*
*FIELD* NO
300027
*FIELD* TI
*300027 RNA-BINDING MOTIF PROTEIN 3; RBM3
*FIELD* TX
CLONING
Using cDNA selection with a YAC from the Xp11.2 region, Derry et al.
read more(1995) identified a novel gene, which they designated RBM3 (for
'RNA-binding motif protein 3'), that encodes a polypeptide with high
sequence similarity to a group of proteins that bind to RNA; see also
the Y-chromosome genes RBM1 (400006) and RBM2. The RBM3 gene gave rise
to alternatively spliced transcripts in a variety of human tissues. The
longest open reading frame encodes a 157-amino acid protein with a
predicted molecular weight of 17 kD. Its putative RNA-binding domain
most closely resembles that of 2 previously characterized human
RNA-binding proteins, YRRM and a glycoprotein identified as an
autoantigen. The authors noted that homology of RBM3 in both sequence
and size to an RNA-binding protein from maize, AAIP, suggested it
functions in a fundamental pathway conserved from plants to mammals.
MAPPING
On a YAC contig map, RBM3 was found by Derry et al. (1995) to be located
between OATL1 (311240) and GATA1 (305371)/TFE3 (314310) in subband
Xp11.23.
*FIELD* RF
1. Derry, J. M. J.; Kerns, J. A.; Francke, U.: RBM3, a novel human
gene in Xp11.23 with a putative RNA-binding domain. Hum. Molec. Genet. 4:
2307-2311, 1995.
*FIELD* CD
Victor A. McKusick: 2/19/1996
*FIELD* ED
carol: 02/03/2014
terry: 9/7/2010
psherman: 4/27/1998
mark: 2/5/1997
mark: 2/19/1996
*RECORD*
*FIELD* NO
300027
*FIELD* TI
*300027 RNA-BINDING MOTIF PROTEIN 3; RBM3
*FIELD* TX
CLONING
Using cDNA selection with a YAC from the Xp11.2 region, Derry et al.
read more(1995) identified a novel gene, which they designated RBM3 (for
'RNA-binding motif protein 3'), that encodes a polypeptide with high
sequence similarity to a group of proteins that bind to RNA; see also
the Y-chromosome genes RBM1 (400006) and RBM2. The RBM3 gene gave rise
to alternatively spliced transcripts in a variety of human tissues. The
longest open reading frame encodes a 157-amino acid protein with a
predicted molecular weight of 17 kD. Its putative RNA-binding domain
most closely resembles that of 2 previously characterized human
RNA-binding proteins, YRRM and a glycoprotein identified as an
autoantigen. The authors noted that homology of RBM3 in both sequence
and size to an RNA-binding protein from maize, AAIP, suggested it
functions in a fundamental pathway conserved from plants to mammals.
MAPPING
On a YAC contig map, RBM3 was found by Derry et al. (1995) to be located
between OATL1 (311240) and GATA1 (305371)/TFE3 (314310) in subband
Xp11.23.
*FIELD* RF
1. Derry, J. M. J.; Kerns, J. A.; Francke, U.: RBM3, a novel human
gene in Xp11.23 with a putative RNA-binding domain. Hum. Molec. Genet. 4:
2307-2311, 1995.
*FIELD* CD
Victor A. McKusick: 2/19/1996
*FIELD* ED
carol: 02/03/2014
terry: 9/7/2010
psherman: 4/27/1998
mark: 2/5/1997
mark: 2/19/1996