RBM5_MOUSE
ID RBM5_MOUSE Reviewed; 815 AA.
AC Q91YE7; Q3UZ19; Q99KV9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=RNA-binding protein 5;
DE AltName: Full=Putative tumor suppressor LUCA15;
DE AltName: Full=RNA-binding motif protein 5;
GN Name=Rbm5; Synonyms=Luca15;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Heath E., Morgan G.T., Sablitzky F.;
RT "Def-3 defines a novel sub-nuclear domain and co-localises with LUCA15.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Eye, Fetal brain, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-621 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 484-491 IN COMPLEX WITH B2M AND
RP H2-K1.
RX PubMed=16761314; DOI=10.1002/eji.200635895;
RA Auphan-Anezin N., Mazza C., Guimezanes A., Barrett-Wilt G.A.,
RA Montero-Julian F., Roussel A., Hunt D.F., Malissen B.,
RA Schmitt-Verhulst A.-M.;
RT "Distinct orientation of the alloreactive monoclonal CD8 T cell activation
RT program by three different peptide/MHC complexes.";
RL Eur. J. Immunol. 36:1856-1866(2006).
CC -!- FUNCTION: Component of the spliceosome A complex. Regulates alternative
CC splicing of a number of mRNAs. May modulate splice site pairing after
CC recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of
CC the intron. May both positively and negatively regulate apoptosis by
CC regulating the alternative splicing of several genes involved in this
CC process, including FAS and CASP2/caspase-2. In the case of FAS,
CC promotes production of a soluble form of FAS that inhibits apoptosis.
CC In the case of CASP2/caspase-2, promotes production of a catalytically
CC active form of CASP2/Caspase-2 that induces apoptosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the spliceosome A complex (also known as the
CC prespliceosome). Appears to dissociate from the spliceosome upon
CC formation of the spliceosome B complex (also known as the precatalytic
CC spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound.
CC Interacts with U2AF2; this interaction is direct. Also interacts with
CC ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these
CC interactions may be indirect (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91YE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91YE7-2; Sequence=VSP_021003;
CC -!- SIMILARITY: Belongs to the RBM5/RBM10 family. {ECO:0000305}.
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DR EMBL; AJ309168; CAC69136.1; -; mRNA.
DR EMBL; AK134183; BAE22042.1; -; mRNA.
DR EMBL; AK146880; BAE27501.1; -; mRNA.
DR EMBL; BC003988; AAH03988.1; -; mRNA.
DR EMBL; BC023854; AAH23854.1; -; mRNA.
DR EMBL; BC031899; AAH31899.1; -; mRNA.
DR EMBL; BC043058; AAH43058.1; -; mRNA.
DR EMBL; BC054729; AAH54729.1; -; mRNA.
DR CCDS; CCDS23506.1; -. [Q91YE7-1]
DR CCDS; CCDS90660.1; -. [Q91YE7-2]
DR RefSeq; NP_683732.1; NM_148930.3. [Q91YE7-1]
DR RefSeq; XP_006511933.1; XM_006511870.3.
DR RefSeq; XP_006511934.1; XM_006511871.3.
DR RefSeq; XP_006511935.1; XM_006511872.2. [Q91YE7-1]
DR RefSeq; XP_011241223.1; XM_011242921.2.
DR PDB; 2CLV; X-ray; 1.90 A; C/M=484-491.
DR PDB; 2OL3; X-ray; 2.90 A; P=484-491.
DR PDBsum; 2CLV; -.
DR PDBsum; 2OL3; -.
DR AlphaFoldDB; Q91YE7; -.
DR BMRB; Q91YE7; -.
DR SMR; Q91YE7; -.
DR BioGRID; 219933; 5.
DR IntAct; Q91YE7; 3.
DR MINT; Q91YE7; -.
DR STRING; 10090.ENSMUSP00000138379; -.
DR iPTMnet; Q91YE7; -.
DR PhosphoSitePlus; Q91YE7; -.
DR EPD; Q91YE7; -.
DR jPOST; Q91YE7; -.
DR MaxQB; Q91YE7; -.
DR PaxDb; Q91YE7; -.
DR PeptideAtlas; Q91YE7; -.
DR PRIDE; Q91YE7; -.
DR ProteomicsDB; 300323; -. [Q91YE7-1]
DR ProteomicsDB; 300324; -. [Q91YE7-2]
DR Antibodypedia; 1962; 258 antibodies from 30 providers.
DR DNASU; 83486; -.
DR Ensembl; ENSMUST00000035199; ENSMUSP00000035199; ENSMUSG00000032580. [Q91YE7-2]
DR Ensembl; ENSMUST00000182659; ENSMUSP00000138379; ENSMUSG00000032580. [Q91YE7-1]
DR GeneID; 83486; -.
DR KEGG; mmu:83486; -.
DR UCSC; uc009rmv.2; mouse. [Q91YE7-2]
DR UCSC; uc009rmw.2; mouse. [Q91YE7-1]
DR CTD; 10181; -.
DR MGI; MGI:1933204; Rbm5.
DR VEuPathDB; HostDB:ENSMUSG00000032580; -.
DR eggNOG; KOG0154; Eukaryota.
DR GeneTree; ENSGT00940000156617; -.
DR HOGENOM; CLU_010527_0_0_1; -.
DR InParanoid; Q91YE7; -.
DR OMA; TIMGVIR; -.
DR OrthoDB; 786674at2759; -.
DR PhylomeDB; Q91YE7; -.
DR TreeFam; TF315789; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 83486; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Rbm5; mouse.
DR EvolutionaryTrace; Q91YE7; -.
DR PRO; PR:Q91YE7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91YE7; protein.
DR Bgee; ENSMUSG00000032580; Expressed in rostral migratory stream and 255 other tissues.
DR ExpressionAtlas; Q91YE7; baseline and differential.
DR Genevisible; Q91YE7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; ISS:UniProtKB.
DR CDD; cd12752; RRM1_RBM5; 1.
DR CDD; cd12755; RRM2_RBM5; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033094; RBM5.
DR InterPro; IPR034991; RBM5_RRM1.
DR InterPro; IPR034993; RBM5_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF21; PTHR13948:SF21; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..815
FT /note="RNA-binding protein 5"
FT /id="PRO_0000253050"
FT DOMAIN 98..178
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 231..315
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 743..789
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 181..210
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 647..672
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..809
FT /note="Required for interaction with U2AF2"
FT /evidence="ECO:0000250"
FT REGION 385..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..535
FT /note="Sufficient for interaction with ACIN1, PRPF8, SFRS3,
FT SNRPB, SNRPN, SNRNP70 and SNRNP200"
FT /evidence="ECO:0000250"
FT REGION 508..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52756"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 455
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021003"
FT CONFLICT 272
FT /note="Q -> K (in Ref. 2; BAE22042)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="E -> G (in Ref. 2; BAE22042)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="F -> L (in Ref. 2; BAE22042)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="S -> P (in Ref. 2; BAE22042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 815 AA; 92311 MW; BCDADD4A8FB4EAC9 CRC64;
MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP
ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES
FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP
KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESAQSVDYYC DTIILRNIAP
HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP
LKIDGKTIGV DFAKSARKDL VLPDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGSVDYSY
MQPGQDGYTQ YTQYSQDYQQ FYQQQAGGLE SDTSATSGTT VTTTSAAVVS QSPQLYNQTS
NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY
DPNSQYYYNS LTQQYLYWDG EKETYVPAAE ASSNQQTGLP STKEGKEKKE KPKSKTAQQI
AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLLP
ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNRD
ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP
KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK
GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME
