RBM28_MOUSE
ID RBM28_MOUSE Reviewed; 750 AA.
AC Q8CGC6; E9QKF8; Q3U0K5; Q8BG25; Q8VEJ8; Q9CS22; Q9CSE6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=RNA-binding protein 28;
DE AltName: Full=RNA-binding motif protein 28;
GN Name=Rbm28;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Embryonic head, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
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-231 AND SER-239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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 [5]
RP STRUCTURE BY NMR OF 317-414.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in RNA-binding protein 28.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Nucleolar component of the spliceosomal ribonucleoprotein
CC complexes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with U1, U2, U4, U5, and U6 spliceosomal small
CC nuclear RNAs (snRNAs). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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DR EMBL; AK012408; BAC25367.1; -; mRNA.
DR EMBL; AK013047; BAB28620.1; -; mRNA.
DR EMBL; AK019296; BAB31653.3; -; mRNA.
DR EMBL; AK019436; BAC25592.1; -; mRNA.
DR EMBL; AK156773; BAE33848.1; -; mRNA.
DR EMBL; AC153909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018373; AAH18373.1; -; mRNA.
DR EMBL; BC040811; AAH40811.1; -; mRNA.
DR CCDS; CCDS51733.1; -.
DR RefSeq; NP_598686.2; NM_133925.2.
DR PDB; 1X4H; NMR; -; A=317-414.
DR PDBsum; 1X4H; -.
DR AlphaFoldDB; Q8CGC6; -.
DR SMR; Q8CGC6; -.
DR BioGRID; 212775; 30.
DR DIP; DIP-58949N; -.
DR IntAct; Q8CGC6; 1.
DR STRING; 10090.ENSMUSP00000007993; -.
DR iPTMnet; Q8CGC6; -.
DR PhosphoSitePlus; Q8CGC6; -.
DR SwissPalm; Q8CGC6; -.
DR EPD; Q8CGC6; -.
DR MaxQB; Q8CGC6; -.
DR PaxDb; Q8CGC6; -.
DR PeptideAtlas; Q8CGC6; -.
DR PRIDE; Q8CGC6; -.
DR ProteomicsDB; 300265; -.
DR Antibodypedia; 17763; 149 antibodies from 26 providers.
DR DNASU; 68272; -.
DR Ensembl; ENSMUST00000007993; ENSMUSP00000007993; ENSMUSG00000029701.
DR GeneID; 68272; -.
DR KEGG; mmu:68272; -.
DR UCSC; uc009bcx.2; mouse.
DR CTD; 55131; -.
DR MGI; MGI:2655711; Rbm28.
DR VEuPathDB; HostDB:ENSMUSG00000029701; -.
DR eggNOG; KOG0127; Eukaryota.
DR GeneTree; ENSGT00550000074976; -.
DR HOGENOM; CLU_011608_2_0_1; -.
DR InParanoid; Q8CGC6; -.
DR OMA; RNLPWSV; -.
DR OrthoDB; 1181291at2759; -.
DR PhylomeDB; Q8CGC6; -.
DR TreeFam; TF312798; -.
DR BioGRID-ORCS; 68272; 18 hits in 76 CRISPR screens.
DR ChiTaRS; Rbm28; mouse.
DR EvolutionaryTrace; Q8CGC6; -.
DR PRO; PR:Q8CGC6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CGC6; protein.
DR Bgee; ENSMUSG00000029701; Expressed in embryonic post-anal tail and 262 other tissues.
DR ExpressionAtlas; Q8CGC6; baseline and differential.
DR Genevisible; Q8CGC6; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NW13"
FT CHAIN 2..750
FT /note="RNA-binding protein 28"
FT /id="PRO_0000081786"
FT DOMAIN 4..80
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 114..191
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 325..409
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 477..582
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW13"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW13"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW13"
FT CROSSLNK 643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW13"
FT CONFLICT 239
FT /note="S -> I (in Ref. 1; BAB31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..243
FT /note="DE -> GR (in Ref. 1; BAB31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="L -> P (in Ref. 3; AAH40811)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="L -> F (in Ref. 3; AAH40811)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="V -> A (in Ref. 1; BAE33848 and 3; AAH18373/
FT AAH40811)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="S -> T (in Ref. 1; BAE33848 and 3; AAH18373)"
FT /evidence="ECO:0000305"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:1X4H"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:1X4H"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1X4H"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1X4H"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:1X4H"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:1X4H"
FT TURN 388..392
FT /evidence="ECO:0007829|PDB:1X4H"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:1X4H"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:1X4H"
SQ SEQUENCE 750 AA; 84214 MW; C767D7C6333E9944 CRC64;
MAGLTLFVGR LPPSARSDQL EELFSQVGPV KQCFVVTEKG SKACRGFGYV TFSMLEDVQR
ALKEITTFEG CKIDVTVAKK KLRNKSKETR KNENAESPKK EPKHKKAKVA DKKARLIIRN
LSFKCSEDDL KAVFTHYGTV LEVNIPKKPD GKMRGFAFVQ FKNLLEAGKA LKGANMKEIK
GRTVAVDWAV AKDKYKDAQH ASAPGVKKSS DRKPKESGKK NCRVEEQVED SDDEEDDDSH
DDEEERESTI ASPVSVHKRA VKRAAPEESI EEDDSYEDSD LEEGGSSYDE GTVDSESSAE
DQEDEDVPVS EKKKRKLPSD VTEGKTVFIR NLSFDSEEEA LGEVLQQFGD LKYVRVVLHP
DTEHSKGCAF AQFMTQEAAQ KCLAAASLEA EGGGLKLDGR QLKVDLAVTR DEAAKLQTKK
VKKPTGTRNL YLAREGLIRA GTKAAEGVSA ADMAKRERFE LLKHQKLKNQ NIFVSQTRLC
LHNLPKAVDD KQLRKLLLEA TRGEKGVRIK ECRVMRDLKG VHGKMKGQSL GYAFAEFQKH
EHALRALRHF NNNPEIFGSQ KRPIVEFSLE DRRKLKVKEL RIQRSLQKME SKPVTSKPQK
EQKEVGKDKQ QKVVQSATQD QSKAPGEQKG KAGSTSWSGF QTKAEVEQVE LPDGKKRRKV
LALPSHRGPK IRLRDKGKVK SLPSRKPKPQ MGQRKQKKQQ LASSVQAPKR KAKENKAEAR
FNQLVEQYKQ KLLGPSKGAP LMKRSKWFDS
