RBM33_MOUSE
ID RBM33_MOUSE Reviewed; 1231 AA.
AC Q9CXK9; Q3U5Z3; Q8C5J6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=RNA-binding protein 33;
DE AltName: Full=Proline-rich protein 8;
DE AltName: Full=RNA-binding motif protein 33;
GN Name=Rbm33; Synonyms=Prr8;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 576-1231 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Olfactory bulb;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-816; SER-1002 AND
RP SER-1032, AND IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-243; SER-792; SER-816
RP AND SER-1002, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-520, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CXK9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CXK9-2; Sequence=VSP_030148, VSP_030149;
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DR EMBL; AK014289; BAB29246.1; -; mRNA.
DR EMBL; AK078210; BAC37175.1; -; mRNA.
DR EMBL; AK153360; BAE31932.1; -; mRNA.
DR EMBL; AC134530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51448.1; -. [Q9CXK9-1]
DR RefSeq; NP_082510.1; NM_028234.1. [Q9CXK9-1]
DR AlphaFoldDB; Q9CXK9; -.
DR SMR; Q9CXK9; -.
DR BioGRID; 238016; 3.
DR IntAct; Q9CXK9; 1.
DR STRING; 10090.ENSMUSP00000062449; -.
DR iPTMnet; Q9CXK9; -.
DR PhosphoSitePlus; Q9CXK9; -.
DR EPD; Q9CXK9; -.
DR jPOST; Q9CXK9; -.
DR MaxQB; Q9CXK9; -.
DR PaxDb; Q9CXK9; -.
DR PeptideAtlas; Q9CXK9; -.
DR PRIDE; Q9CXK9; -.
DR ProteomicsDB; 255037; -. [Q9CXK9-1]
DR ProteomicsDB; 255038; -. [Q9CXK9-2]
DR Antibodypedia; 18863; 51 antibodies from 11 providers.
DR Ensembl; ENSMUST00000030920; ENSMUSP00000030920; ENSMUSG00000048271. [Q9CXK9-2]
DR Ensembl; ENSMUST00000059644; ENSMUSP00000062449; ENSMUSG00000048271. [Q9CXK9-1]
DR GeneID; 381626; -.
DR KEGG; mmu:381626; -.
DR UCSC; uc008wty.1; mouse. [Q9CXK9-2]
DR UCSC; uc008wtz.1; mouse. [Q9CXK9-1]
DR CTD; 155435; -.
DR MGI; MGI:1919670; Rbm33.
DR VEuPathDB; HostDB:ENSMUSG00000048271; -.
DR eggNOG; ENOG502QR1Z; Eukaryota.
DR GeneTree; ENSGT00530000063891; -.
DR InParanoid; Q9CXK9; -.
DR OMA; ETHFMPA; -.
DR OrthoDB; 287384at2759; -.
DR PhylomeDB; Q9CXK9; -.
DR TreeFam; TF332363; -.
DR BioGRID-ORCS; 381626; 20 hits in 72 CRISPR screens.
DR ChiTaRS; Rbm33; mouse.
DR PRO; PR:Q9CXK9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CXK9; protein.
DR Bgee; ENSMUSG00000048271; Expressed in manus and 225 other tissues.
DR ExpressionAtlas; Q9CXK9; baseline and differential.
DR Genevisible; Q9CXK9; MM.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039878; RBM33.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR22014; PTHR22014; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96EV2"
FT CHAIN 2..1231
FT /note="RNA-binding protein 33"
FT /id="PRO_0000285045"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..891
FT /evidence="ECO:0000255"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV2"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV2"
FT MOD_RES 520
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV2"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EV2"
FT CROSSLNK 1019
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96EV2"
FT VAR_SEQ 285..320
FT /note="ELSAEAKAALLEFEERERQHKQGRYGSRRGGRRGGS -> GNSWFWPVGKLI
FT KFPHPFLACFLDLYFHFRSLHIFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030148"
FT VAR_SEQ 321..1231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030149"
FT CONFLICT 794
FT /note="P -> S (in Ref. 1; BAE31932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1231 AA; 137325 MW; 6A85C1D1D122B27C CRC64;
MAAALGAGGG AGAGDDDFDQ FDKPGAERSW RRRAADEDWD SELEDDLLGE DLLSGKKNQS
DLSDEELNDD LLQSDNEEEE NFSSQGVTIS LNTTSGIVTS FELSDNTNDQ SGEQESEYEQ
GDDELAYHKP EEQELYTQEY PEEGQYEGHD AELTEDQIEY GDEPEEEQLY SDEVLDIEIN
EPLDEFTDEE YLQAYGGQQG LQVREDCEAE DDLDEITDSQ VASETHEGGM ETLELQKDIK
EESDEEDDDD EESGRLRFKT ERKEGTIIRL SDVTRERRNI PETLELSAEA KAALLEFEER
ERQHKQGRYG SRRGGRRGGS LMCRGMGDQR RDNSERGRMK EHRPALLPTQ PSVVAHSPRL
IPPPQPQPPP PPPPPPPQQQ PIRSLFQQQQ LQPLLPLQHP HHPSPPQGVH MPPQIETPRM
MLTPPPVTPQ QPKNIHINPH FKGTVVTPVQ VPLLPVPSQP RPAVGPQRFP GPPEFPQHTP
GPVPNSFNQP PRLPLQDQWR APPPPQERDP FFLGVSGEPR FPSHLFLEQR SPPPPPPPPT
LLNSSHPVPT QSPLPFTQPG PAFNQQGQQP VFPRERPVRP ALQPPGPVGI LHFSQPGSAT
ARPFIPPRQP FLPSPGQPFL PTHAQPNLQG PLHPPLPPPH QPQPQPQQPQ QQPQHHQHQP
PLQPPLQPPH QPPPQHQPPP QHQPQQHQHH HHLSAPPPPL MPMSQPQFRP HVQTAQPQPS
SSRMQCTPHQ GLRHNAASQN ISKRPMQQMQ PTAPRNSNLR ELPIAPSHVL EMSGNRCSST
PVAQVKSIVN TSPPCRAVVS SRSSQGNTDA KAKPLSPEAQ PKEEAKPEAE FPDEDEETRL
YRLKIEEQKR LREEILKQKE LRRQQQAGAR KKELLERLAQ QQQQQQQQQH QPQQQQQQPQ
QIYGSQTSME QEELAATPSP TNGNPLLPFP GAQCRQNVKT RLLVKNQDIT TASVQPKAVN
FVPPGANVQH QGQHLRPLKH LRQLPHKVLQ VKPMDMEETP HSPQAARVTS LQGRPQDTKP
GVKRTVMHRA NSGGGGDGPH VSSKVRVIKL SGGQGGESDG FSHTEGQPQR LPQPPDMRQQ
PTRKVTLTKG VPQQPQHLPV GPHMYPAIPP GIKSIQGIHP AKKAIMHGRG RGVAGPMGRG
RLMPNKQNLR VVECKPQPCV VSVEGLSSST TDVQLKSLLM SVGPIQSLQM LPQQRKAIAK
FKEPAHALAF QQKFHRHMID LSHINVALIV E
