RBM26_MOUSE
ID RBM26_MOUSE Reviewed; 1012 AA.
AC Q6NZN0; Q3TA77; Q3UTU9; Q8BQ22; Q8C7W9; Q8K101; Q921K4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RNA-binding protein 26;
DE AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 393;
DE Short=MLZ-393;
DE AltName: Full=RNA-binding motif protein 26;
GN Name=Rbm26;
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), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 723-1012 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 780-1012 (ISOFORM 5).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-746 (ISOFORM 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 24-999 (ISOFORM 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Spinal ganglion, 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 [3]
RP PROTEIN SEQUENCE OF 692-701, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-621, 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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT "Screening of genes involved in chromosome segregation during meiosis I:
RT toward the identification of genes responsible for infertility in humans.";
RL J. Hum. Genet. 55:293-299(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-515, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6NZN0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NZN0-2; Sequence=VSP_022535;
CC Name=3;
CC IsoId=Q6NZN0-3; Sequence=VSP_022533, VSP_022535;
CC Name=4;
CC IsoId=Q6NZN0-4; Sequence=VSP_022533;
CC Name=5;
CC IsoId=Q6NZN0-5; Sequence=VSP_022534;
CC -!- TISSUE SPECIFICITY: Expressed in testis and ovary.
CC {ECO:0000269|PubMed:20339383}.
CC -!- DEVELOPMENTAL STAGE: Expressed in testis and ovary at 15.5 dpc.
CC {ECO:0000269|PubMed:20339383}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29079.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC33537.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC34721.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE23881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE42792.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC066051; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC011531; AAH11531.1; -; mRNA.
DR EMBL; BC029079; AAH29079.1; ALT_INIT; mRNA.
DR EMBL; BC066051; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK049083; BAC33537.1; ALT_FRAME; mRNA.
DR EMBL; AK051686; BAC34721.1; ALT_FRAME; mRNA.
DR EMBL; AK139077; BAE23881.1; ALT_INIT; mRNA.
DR EMBL; AK172039; BAE42792.1; ALT_INIT; mRNA.
DR CCDS; CCDS88725.1; -. [Q6NZN0-4]
DR RefSeq; NP_598838.3; NM_134077.4.
DR AlphaFoldDB; Q6NZN0; -.
DR SMR; Q6NZN0; -.
DR BioGRID; 216580; 4.
DR STRING; 10090.ENSMUSP00000097901; -.
DR iPTMnet; Q6NZN0; -.
DR PhosphoSitePlus; Q6NZN0; -.
DR EPD; Q6NZN0; -.
DR jPOST; Q6NZN0; -.
DR MaxQB; Q6NZN0; -.
DR PaxDb; Q6NZN0; -.
DR PeptideAtlas; Q6NZN0; -.
DR PRIDE; Q6NZN0; -.
DR ProteomicsDB; 255124; -. [Q6NZN0-1]
DR ProteomicsDB; 255125; -. [Q6NZN0-2]
DR ProteomicsDB; 255126; -. [Q6NZN0-3]
DR ProteomicsDB; 255127; -. [Q6NZN0-4]
DR ProteomicsDB; 255128; -. [Q6NZN0-5]
DR Antibodypedia; 24703; 248 antibodies from 29 providers.
DR DNASU; 74213; -.
DR Ensembl; ENSMUST00000022715; ENSMUSP00000022715; ENSMUSG00000022119. [Q6NZN0-4]
DR GeneID; 74213; -.
DR KEGG; mmu:74213; -.
DR UCSC; uc007uxl.2; mouse. [Q6NZN0-4]
DR UCSC; uc007uxn.1; mouse. [Q6NZN0-3]
DR CTD; 64062; -.
DR MGI; MGI:1921463; Rbm26.
DR VEuPathDB; HostDB:ENSMUSG00000022119; -.
DR eggNOG; KOG2135; Eukaryota.
DR GeneTree; ENSGT00510000046929; -.
DR InParanoid; Q6NZN0; -.
DR OrthoDB; 741871at2759; -.
DR PhylomeDB; Q6NZN0; -.
DR BioGRID-ORCS; 74213; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rbm26; mouse.
DR PRO; PR:Q6NZN0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6NZN0; protein.
DR Bgee; ENSMUSG00000022119; Expressed in animal zygote and 247 other tissues.
DR ExpressionAtlas; Q6NZN0; baseline and differential.
DR Genevisible; Q6NZN0; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd12516; RRM1_RBM26; 1.
DR CDD; cd12258; RRM2_RBM26_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034861; RBM26.
DR InterPro; IPR039511; RBM26-like_RRM2.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR034859; RBM26_RRM1.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; PTHR14398; 1.
DR PANTHER; PTHR14398:SF2; PTHR14398:SF2; 1.
DR Pfam; PF01480; PWI; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1012
FT /note="RNA-binding protein 26"
FT /id="PRO_0000273377"
FT DOMAIN 537..611
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 896..965
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 288..316
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 106..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..127
FT /evidence="ECO:0000255"
FT COILED 724..800
FT /evidence="ECO:0000255"
FT COILED 828..852
FT /evidence="ECO:0000255"
FT COMPBIAS 106..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..882
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1004
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8P6"
FT MOD_RES 515
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T8P6"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T8P6"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T8P6"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5T8P6"
FT VAR_SEQ 426..430
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022533"
FT VAR_SEQ 984..1012
FT /note="FQEESLVDDSLLQDDDEEEEDNESRSWRR -> RENITA (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022534"
FT VAR_SEQ 991..1012
FT /note="DDSLLQDDDEEEEDNESRSWRR -> VGFFFFSLVFPSLFIVLL (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_022535"
FT CONFLICT 324
FT /note="N -> K (in Ref. 2; BAC33537)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="S -> Y (in Ref. 2; BAC33537)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="N -> S (in Ref. 2; BAE42792)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="E -> G (in Ref. 2; BAC33537)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="T -> S (in Ref. 2; BAC33537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 114143 MW; EBD1FD8C14BE106F CRC64;
MVSKMIIENF EALKSWLSKT LEPICDADPS ALAKYVLALV KKDKSEKELK ALCIDQLDVF
LQKETQIFVE KLFDAVNTKS YLPPPEQPSS GSLKVDFLQH QEKDIKKEEL TKEEEREKKF
SRRLNHSPPQ SSSRYRDNRS RDERKKDDRS RKRDYDRNPP RRDSYRDRYN RRRGRSRSYS
RSRSRSWSKE RLRDRDRDRS RTRSRSRTRS RERDLVKPKY DLDRTDPLEN NYTPVSSVSN
ISSGHYPVPT LSSTITVIAP THHGNNTTES WSEFHEDQVD HNSYVRPPMP KKRCRDYDEK
GFCMRGDMCP FDHGSDPVVV EDVNLPGMLP FPAQPPVVEG PPPPGLPPPP PILTPPPVNL
RPPVPPPGPL PPSLPPVTGP PPPLPPLQPS GMDAPPNSAT SSVPTVVTTG IHHQPPPAPP
SLFTAVFVLP DTYDTDGYNP EAPSITNTSR PMYRHRVHAQ RPNLIGLTSG DMDLPPREKP
PNKSSMRIVV DSESRKRTIG SGEPGVSTKK TWFDKPNFNR TNSPGFQKKV QFGNENTKLE
LRKVPPELNN ISKLNEHFSR FGTLVNLQVA YNGDPEGALI QFATYEEAKK AISSTEAVLN
NRFIKVYWHR EGTTQQLQTT SPKVIQPLVQ QPILPVVKQS VKERLGPVPS ATTEPAEAQS
ATSELPQNVT KLSVKDRLGF VSKPSVSATE KVLSTSTGLT KTVYNPAALK AAQKTLSVST
PAVDNNEAQK KKQEALKLQQ DVRKRKQEIL EKHIETQKML ISKLEKNKTM KSEDKAEIMK
TLEILTKNIT KLKDEVKSTS PGRCLPKSIK TKTQMQKELL DTELDLYKKM QAGEEVTELR
RKYTELQLEA AKRGILSSGR GRGIHTRGRG TAHGRGRGRG RGRGVPGHAV VDHRPRALEI
SAFTESDRED LLPHFAQYGE IEDCQIDDAS LHAIITFKTR AEAEAAAIHG ARFKGQDLKL
AWNKPIANMS AVDTEEAEPD EEEFQEESLV DDSLLQDDDE EEEDNESRSW RR
