ID   RBM26_HUMAN             Reviewed;        1007 AA.
AC   Q5T8P6; B4DZE0; Q2NKM2; Q2NKQ2; Q5CZH8; Q5T8P5; Q5T8P8; Q5U5P5; Q5W0G7;
AC   Q8N3H5; Q96K92; Q96SZ3; Q9H2F8; Q9H7F9; Q9P1G7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=RNA-binding protein 26 {ECO:0000305};
DE   AltName: Full=CTCL tumor antigen se70-2;
DE   AltName: Full=RNA-binding motif protein 26;
GN   Name=RBM26 {ECO:0000312|HGNC:HGNC:20327}; Synonyms=C13orf10;
GN   ORFNames=PRO1777;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC   TISSUE=Adipose tissue, Embryo, Teratocarcinoma, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA   Liu M., He F.;
RT   "Functional prediction of the coding sequences of 121 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   TISSUE=Lymph;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-911 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 215-869 (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 703-1007 (ISOFORM 1/2/3/4/5).
RC   TISSUE=Testis;
RX   PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA   Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT   "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-616, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-510, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
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., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-496 AND SER-518, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-616, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [19]
RP   FUNCTION.
RX   PubMed=31950173; DOI=10.1093/nar/gkz1238;
RA   Silla T., Schmid M., Dou Y., Garland W., Milek M., Imami K., Johnsen D.,
RA   Polak P., Andersen J.S., Selbach M., Landthaler M., Jensen T.H.;
RT   "The human ZC3H3 and RBM26/27 proteins are critical for PAXT-mediated
RT   nuclear RNA decay.";
RL   Nucleic Acids Res. 48:2518-2530(2020).
CC   -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC       (pA+) RNA. {ECO:0000269|PubMed:31950173}.
CC   -!- INTERACTION:
CC       Q5T8P6; O43639: NCK2; NbExp=3; IntAct=EBI-3232077, EBI-713635;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q5T8P6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5T8P6-2; Sequence=VSP_022532;
CC       Name=3;
CC         IsoId=Q5T8P6-3; Sequence=VSP_022531, VSP_022532;
CC       Name=4;
CC         IsoId=Q5T8P6-4; Sequence=VSP_022528, VSP_022531;
CC       Name=5;
CC         IsoId=Q5T8P6-5; Sequence=VSP_022528, VSP_022531, VSP_022532;
CC       Name=6;
CC         IsoId=Q5T8P6-6; Sequence=VSP_022529, VSP_022530;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG34912.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB14933.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55125.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK024610; BAB14933.1; ALT_INIT; mRNA.
DR   EMBL; AK027339; BAB55046.1; -; mRNA.
DR   EMBL; AK027456; BAB55125.1; ALT_INIT; mRNA.
DR   EMBL; AK302871; BAG64052.1; -; mRNA.
DR   EMBL; AF116667; AAF71087.1; -; mRNA.
DR   EMBL; AL139006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL159974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC041655; AAH41655.1; -; mRNA.
DR   EMBL; BC111697; AAI11698.1; -; mRNA.
DR   EMBL; BC111739; AAI11740.1; -; mRNA.
DR   EMBL; AL834343; CAD39009.3; -; mRNA.
DR   EMBL; BX648672; CAI56708.1; -; mRNA.
DR   EMBL; AF273052; AAG34912.1; ALT_INIT; mRNA.
DR   CCDS; CCDS66566.1; -. [Q5T8P6-2]
DR   CCDS; CCDS91822.1; -. [Q5T8P6-1]
DR   CCDS; CCDS9462.1; -. [Q5T8P6-3]
DR   RefSeq; NP_001273560.1; NM_001286631.1.
DR   RefSeq; NP_001273561.1; NM_001286632.1. [Q5T8P6-2]
DR   RefSeq; NP_071401.3; NM_022118.4. [Q5T8P6-3]
DR   RefSeq; XP_011533490.1; XM_011535188.2.
DR   RefSeq; XP_011533494.1; XM_011535192.2.
DR   RefSeq; XP_011533495.1; XM_011535193.2.
DR   AlphaFoldDB; Q5T8P6; -.
DR   SMR; Q5T8P6; -.
DR   BioGRID; 122035; 147.
DR   ComplexPortal; CPX-2750; Poly(A) tail exosome targeting complex, RBM26 variant.
DR   IntAct; Q5T8P6; 56.
DR   MINT; Q5T8P6; -.
DR   STRING; 9606.ENSP00000483408; -.
DR   GlyCosmos; Q5T8P6; 7 sites, 2 glycans.
DR   GlyGen; Q5T8P6; 14 sites, 2 O-linked glycans (14 sites).
DR   iPTMnet; Q5T8P6; -.
DR   MetOSite; Q5T8P6; -.
DR   PhosphoSitePlus; Q5T8P6; -.
DR   BioMuta; RBM26; -.
DR   DMDM; 124021002; -.
DR   EPD; Q5T8P6; -.
DR   jPOST; Q5T8P6; -.
DR   MassIVE; Q5T8P6; -.
DR   MaxQB; Q5T8P6; -.
DR   PaxDb; 9606-ENSP00000483408; -.
DR   PeptideAtlas; Q5T8P6; -.
DR   ProteomicsDB; 64744; -. [Q5T8P6-1]
DR   ProteomicsDB; 64745; -. [Q5T8P6-2]
DR   ProteomicsDB; 64746; -. [Q5T8P6-3]
DR   ProteomicsDB; 64747; -. [Q5T8P6-4]
DR   ProteomicsDB; 64748; -. [Q5T8P6-5]
DR   ProteomicsDB; 64749; -. [Q5T8P6-6]
DR   Pumba; Q5T8P6; -.
DR   Antibodypedia; 24703; 282 antibodies from 29 providers.
DR   DNASU; 64062; -.
DR   Ensembl; ENST00000267229.11; ENSP00000267229.7; ENSG00000139746.16. [Q5T8P6-3]
DR   Ensembl; ENST00000438724.5; ENSP00000390222.1; ENSG00000139746.16. [Q5T8P6-2]
DR   Ensembl; ENST00000438737.3; ENSP00000387531.2; ENSG00000139746.16. [Q5T8P6-1]
DR   GeneID; 64062; -.
DR   KEGG; hsa:64062; -.
DR   MANE-Select; ENST00000438737.3; ENSP00000387531.2; NM_001366735.2; NP_001353664.1.
DR   UCSC; uc001vky.4; human. [Q5T8P6-1]
DR   AGR; HGNC:20327; -.
DR   CTD; 64062; -.
DR   DisGeNET; 64062; -.
DR   GeneCards; RBM26; -.
DR   HGNC; HGNC:20327; RBM26.
DR   HPA; ENSG00000139746; Low tissue specificity.
DR   MIM; 620081; gene.
DR   neXtProt; NX_Q5T8P6; -.
DR   OpenTargets; ENSG00000139746; -.
DR   PharmGKB; PA134982324; -.
DR   VEuPathDB; HostDB:ENSG00000139746; -.
DR   eggNOG; KOG2135; Eukaryota.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOGENOM; CLU_006190_0_0_1; -.
DR   InParanoid; Q5T8P6; -.
DR   OrthoDB; 5406435at2759; -.
DR   PhylomeDB; Q5T8P6; -.
DR   TreeFam; TF319253; -.
DR   PathwayCommons; Q5T8P6; -.
DR   SignaLink; Q5T8P6; -.
DR   BioGRID-ORCS; 64062; 36 hits in 1163 CRISPR screens.
DR   ChiTaRS; RBM26; human.
DR   GeneWiki; RBM26; -.
DR   GenomeRNAi; 64062; -.
DR   Pharos; Q5T8P6; Tdark.
DR   PRO; PR:Q5T8P6; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q5T8P6; Protein.
DR   Bgee; ENSG00000139746; Expressed in pylorus and 216 other cell types or tissues.
DR   ExpressionAtlas; Q5T8P6; baseline and differential.
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; HDA:UniProtKB.
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   Gene3D; 1.20.1390.10; PWI domain; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
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; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR   PANTHER; PTHR14398:SF2; RNA-BINDING PROTEIN 26; 1.
DR   Pfam; PF01480; PWI; 1.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   Genevisible; Q5T8P6; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW   Metal-binding; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1007
FT                   /note="RNA-binding protein 26"
FT                   /id="PRO_0000273376"
FT   DOMAIN          532..606
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          891..960
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..241
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          460..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          719..795
FT                   /evidence="ECO:0000255"
FT   COILED          823..847
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        861..877
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..999
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         510
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT   CROSSLNK        94
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   VAR_SEQ         1..446
FT                   /note="Missing (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022528"
FT   VAR_SEQ         110..120
FT                   /note="ITKEEEREKKF -> VTICVNTLQVI (in isoform 6)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_022529"
FT   VAR_SEQ         121..1007
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_022530"
FT   VAR_SEQ         619..621
FT                   /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022531"
FT   VAR_SEQ         663..686
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022532"
FT   VARIANT         718
FT                   /note="V -> D (in dbSNP:rs10767)"
FT                   /id="VAR_030137"
FT   CONFLICT        12
FT                   /note="A -> T (in Ref. 5; CAI56708)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="Q -> H (in Ref. 5; CAI56708)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        426
FT                   /note="D -> A (in Ref. 5; CAI56708)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        709
FT                   /note="K -> E (in Ref. 1; BAB55046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        900
FT                   /note="E -> G (in Ref. 1; BAB55046/BAB55125)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        959
FT                   /note="K -> E (in Ref. 1; BAB14933)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1007 AA;  113597 MW;  DCA34DF4A9A42045 CRC64;
     MVSKMIIENF EALKSWLSKT LEPICDADPS ALAKYVLALV KKDKSEKELK ALCIDQLDVF
     LQKETQIFVE KLFDAVNTKS YLPPPEQPSS GSLKVEFFPH QEKDIKKEEI TKEEEREKKF
     SRRLNHSPPQ SSSRYRENRS RDERKKDDRS RKRDYDRNPP RRDSYRDRYN RRRGRSRSYS
     RSRSRSWSKE RLRERDRDRS RTRSRSRTRS RERDLVKPKY DLDRTDPLEN NYTPVSSVPS
     ISSGHYPVPT LSSTITVIAP THHGNNTTES WSEFHEDQVD HNSYVRPPMP KKRCRDYDEK
     GFCMRGDMCP FDHGSDPVVV EDVNLPGMLP FPAQPPVVEG PPPPGLPPPP PILTPPPVNL
     RPPVPPPGPL PPSLPPVTGP PPPLPPLQPS GMDAPPNSAT SSVPTVVTTG IHHQPPPAPP
     SLFTADTYDT DGYNPEAPSI TNTSRPMYRH RVHAQRPNLI GLTSGDMDLP PREKPPNKSS
     MRIVVDSESR KRTIGSGEPG VPTKKTWFDK PNFNRTNSPG FQKKVQFGNE NTKLELRKVP
     PELNNISKLN EHFSRFGTLV NLQVAYNGDP EGALIQFATY EEAKKAISST EAVLNNRFIK
     VYWHREGSTQ QLQTTSPKVM QPLVQQPILP VVKQSVKERL GPVPSSTIEP AEAQSASSDL
     PQNVTKLSVK DRLGFVSKPS VSATEKVLST STGLTKTVYN PAALKAAQKT LLVSTSAVDN
     NEAQKKKQEA LKLQQDVRKR KQEILEKHIE TQKMLISKLE KNKTMKSEDK AEIMKTLEVL
     TKNITKLKDE VKAASPGRCL PKSIKTKTQM QKELLDTELD LYKKMQAGEE VTELRRKYTE
     LQLEAAKRGI LSSGRGRGIH SRGRGAVHGR GRGRGRGRGV PGHAVVDHRP RALEISAFTE
     SDREDLLPHF AQYGEIEDCQ IDDSSLHAVI TFKTRAEAEA AAVHGARFKG QDLKLAWNKP
     VTNISAVETE EVEPDEEEFQ EESLVDDSLL QDDDEEEEDN ESRSWRR
//