RBM26_HUMAN
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 03-AUG-2022, entry version 167.
DE RecName: Full=RNA-binding protein 26;
DE AltName: Full=CTCL tumor antigen se70-2;
DE AltName: Full=RNA-binding motif protein 26;
GN Name=RBM26; Synonyms=C13orf10; 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.
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).
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; Evidence={ECO:0000305};
CC Sequence=BAB14933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55125.1; Type=Erroneous initiation; 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; 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. [Q5T8P6-1]
DR RefSeq; XP_011533494.1; XM_011535192.2. [Q5T8P6-2]
DR RefSeq; XP_011533495.1; XM_011535193.2. [Q5T8P6-3]
DR AlphaFoldDB; Q5T8P6; -.
DR SMR; Q5T8P6; -.
DR BioGRID; 122035; 123.
DR IntAct; Q5T8P6; 57.
DR MINT; Q5T8P6; -.
DR STRING; 9606.ENSP00000483408; -.
DR GlyGen; Q5T8P6; 7 sites, 2 O-linked glycans (7 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; Q5T8P6; -.
DR PeptideAtlas; Q5T8P6; -.
DR PRIDE; 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 Antibodypedia; 24703; 248 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 CTD; 64062; -.
DR DisGeNET; 64062; -.
DR GeneCards; RBM26; -.
DR HGNC; HGNC:20327; RBM26.
DR HPA; ENSG00000139746; Low tissue specificity.
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; 741871at2759; -.
DR PhylomeDB; Q5T8P6; -.
DR TreeFam; TF319253; -.
DR PathwayCommons; Q5T8P6; -.
DR SignaLink; Q5T8P6; -.
DR BioGRID-ORCS; 64062; 36 hits in 1083 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 214 other tissues.
DR ExpressionAtlas; Q5T8P6; baseline and differential.
DR Genevisible; Q5T8P6; HS.
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 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; 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
