RB15B_HUMAN
ID RB15B_HUMAN Reviewed; 890 AA.
AC Q8NDT2; A4QPG7; Q6QE19; Q9BV96;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Putative RNA-binding protein 15B {ECO:0000305};
DE AltName: Full=One-twenty two protein 3 {ECO:0000303|PubMed:16129689, ECO:0000303|PubMed:19586903};
DE Short=HsOTT3 {ECO:0000303|PubMed:19586903};
DE Short=HuOTT3 {ECO:0000303|PubMed:16129689};
DE AltName: Full=RNA-binding motif protein 15B {ECO:0000303|PubMed:19586903};
GN Name=RBM15B {ECO:0000303|PubMed:16129689, ECO:0000303|PubMed:19586903,
GN ECO:0000312|HGNC:HGNC:24303};
GN Synonyms=OTT3 {ECO:0000303|PubMed:16129689, ECO:0000303|PubMed:19586903};
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-890 (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 633-780.
RC TISSUE=Head;
RA Sales M.M., Ferrasi A.C., Pereira A.A., Pardini M.I.M.C., Camargo A.A.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH EPSTEIN-BARR VIRUS BMLF1 (MICROBIAL INFECTION)
RP AND NCOR2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16129689; DOI=10.1074/jbc.m501725200;
RA Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P.,
RA Mercher T., Bernard O.A., Sergeant A., Manet E.;
RT "Interaction of the Epstein-Barr virus mRNA export factor EB2 with human
RT Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links
RT Spen proteins with splicing regulation and mRNA export.";
RL J. Biol. Chem. 280:36935-36945(2005).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP IDENTIFICATION BY 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 [8]
RP IDENTIFICATION BY 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 [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALYREF AND NXF1.
RX PubMed=19586903; DOI=10.1074/jbc.m109.040113;
RA Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J.,
RA Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.;
RT "The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the
RT nuclear export receptor NXF1.";
RL J. Biol. Chem. 284:26106-26116(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-552, AND
RP IDENTIFICATION BY 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 FUNCTION.
RX PubMed=21044963; DOI=10.1074/jbc.m110.192518;
RA Loyer P., Busson A., Trembley J.H., Hyle J., Grenet J., Zhao W.,
RA Ribault C., Montier T., Kidd V.J., Lahti J.M.;
RT "The RNA binding motif protein 15B (RBM15B/OTT3) is a functional competitor
RT of serine-arginine (SR) proteins and antagonizes the positive effect of the
RT CDK11p110-cyclin L2alpha complex on splicing.";
RL J. Biol. Chem. 286:147-159(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-552 AND SER-562, AND
RP IDENTIFICATION BY 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 THR-532; SER-556 AND SER-562, 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-109, AND IDENTIFICATION BY
RP 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-213 AND LYS-702, AND
RP IDENTIFICATION BY MASS 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 [18]
RP FUNCTION, RNA-BINDING, AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=27602518; DOI=10.1038/nature19342;
RA Patil D.P., Chen C.K., Pickering B.F., Chow A., Jackson C., Guttman M.,
RA Jaffrey S.R.;
RT "m(6)A RNA methylation promotes XIST-mediated transcriptional repression.";
RL Nature 537:369-373(2016).
CC -!- FUNCTION: RNA-binding protein that acts as a key regulator of N6-
CC methyladenosine (m6A) methylation of RNAs, thereby regulating different
CC processes, such as alternative splicing of mRNAs and X chromosome
CC inactivation mediated by Xist RNA (PubMed:16129689, PubMed:27602518).
CC Associated component of the WMM complex, a complex that mediates N6-
CC methyladenosine (m6A) methylation of RNAs, a modification that plays a
CC role in the efficiency of mRNA splicing and RNA processing
CC (PubMed:27602518). Plays a key role in m6A methylation, possibly by
CC binding target RNAs and recruiting the WMM complex (PubMed:27602518).
CC Involved in random X inactivation mediated by Xist RNA: acts by binding
CC Xist RNA and recruiting the WMM complex, which mediates m6A
CC methylation, leading to target YTHDC1 reader on Xist RNA and promoting
CC transcription repression activity of Xist (PubMed:27602518). Functions
CC in the regulation of alternative or illicit splicing, possibly by
CC regulating m6A methylation (PubMed:16129689). Inhibits pre-mRNA
CC splicing (PubMed:21044963). Also functions as a mRNA export factor by
CC acting as a cofactor for the nuclear export receptor NXF1
CC (PubMed:19586903). {ECO:0000269|PubMed:19586903,
CC ECO:0000269|PubMed:21044963, ECO:0000269|PubMed:27602518,
CC ECO:0000305|PubMed:16129689}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:27602518). The MAC subcomplex is
CC composed of METTL3 and METTL14 (PubMed:27602518). The MACOM subcomplex
CC is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of
CC RBM15 (RBM15 or RBM15B) (PubMed:27602518). May interact with NCOR2
CC (PubMed:16129689). Interacts with NXF1, the interaction is required to
CC promote mRNA export (PubMed:19586903). {ECO:0000269|PubMed:16129689,
CC ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:27602518}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via the SPOC domain) with
CC Epstein-Barr virus BMLF1 (via the N-terminus); the interaction is
CC direct. {ECO:0000269|PubMed:16129689}.
CC -!- INTERACTION:
CC Q8NDT2; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-726721, EBI-741200;
CC Q8NDT2-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10269922, EBI-396137;
CC Q8NDT2-2; Q92997: DVL3; NbExp=3; IntAct=EBI-10269922, EBI-739789;
CC Q8NDT2-2; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-10269922, EBI-741200;
CC Q8NDT2-2; O76024: WFS1; NbExp=3; IntAct=EBI-10269922, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16129689}. Nucleus speckle
CC {ECO:0000269|PubMed:19586903}. Nucleus envelope
CC {ECO:0000269|PubMed:19586903}. Note=Colocalizes with BMLF1 in the
CC nucleus. Localized in the nucleoplasm with a granular staining pattern
CC and excluded from the nucleoli. {ECO:0000269|PubMed:16129689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NDT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDT2-2; Sequence=VSP_053878;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16129689}.
CC -!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01367.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS50153.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC Sequence=CAD38547.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC092037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001367; AAH01367.2; ALT_INIT; mRNA.
DR EMBL; BC139836; AAI39837.1; -; mRNA.
DR EMBL; AL831838; CAD38547.2; ALT_INIT; mRNA.
DR EMBL; AY545557; AAS50153.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33764.1; -. [Q8NDT2-1]
DR RefSeq; NP_037418.3; NM_013286.4. [Q8NDT2-1]
DR AlphaFoldDB; Q8NDT2; -.
DR SMR; Q8NDT2; -.
DR BioGRID; 118943; 87.
DR IntAct; Q8NDT2; 41.
DR MINT; Q8NDT2; -.
DR STRING; 9606.ENSP00000454545; -.
DR iPTMnet; Q8NDT2; -.
DR PhosphoSitePlus; Q8NDT2; -.
DR BioMuta; RBM15B; -.
DR DMDM; 229463030; -.
DR EPD; Q8NDT2; -.
DR jPOST; Q8NDT2; -.
DR MassIVE; Q8NDT2; -.
DR MaxQB; Q8NDT2; -.
DR PaxDb; Q8NDT2; -.
DR PeptideAtlas; Q8NDT2; -.
DR PRIDE; Q8NDT2; -.
DR ProteomicsDB; 73053; -. [Q8NDT2-1]
DR Antibodypedia; 59712; 58 antibodies from 18 providers.
DR DNASU; 29890; -.
DR Ensembl; ENST00000563281.2; ENSP00000454545.1; ENSG00000259956.2. [Q8NDT2-1]
DR GeneID; 29890; -.
DR KEGG; hsa:29890; -.
DR MANE-Select; ENST00000563281.2; ENSP00000454545.1; NM_013286.5; NP_037418.3.
DR UCSC; uc003dbd.4; human. [Q8NDT2-1]
DR CTD; 29890; -.
DR DisGeNET; 29890; -.
DR GeneCards; RBM15B; -.
DR HGNC; HGNC:24303; RBM15B.
DR HPA; ENSG00000259956; Low tissue specificity.
DR MIM; 612602; gene.
DR neXtProt; NX_Q8NDT2; -.
DR OpenTargets; ENSG00000259956; -.
DR PharmGKB; PA134870079; -.
DR VEuPathDB; HostDB:ENSG00000259956; -.
DR eggNOG; KOG0112; Eukaryota.
DR GeneTree; ENSGT00940000160561; -.
DR HOGENOM; CLU_012724_1_0_1; -.
DR InParanoid; Q8NDT2; -.
DR OMA; NFAYIQY; -.
DR OrthoDB; 367857at2759; -.
DR PhylomeDB; Q8NDT2; -.
DR TreeFam; TF354224; -.
DR PathwayCommons; Q8NDT2; -.
DR SignaLink; Q8NDT2; -.
DR BioGRID-ORCS; 29890; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; RBM15B; human.
DR GenomeRNAi; 29890; -.
DR Pharos; Q8NDT2; Tbio.
DR PRO; PR:Q8NDT2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NDT2; protein.
DR Bgee; ENSG00000259956; Expressed in ganglionic eminence and 189 other tissues.
DR Genevisible; Q8NDT2; HS.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12554; RRM1_RBM15B; 1.
DR CDD; cd12556; RRM2_RBM15B; 1.
DR CDD; cd12558; RRM3_RBM15B; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034475; RBM15B_RRM1.
DR InterPro; IPR034535; RBM15B_RRM2.
DR InterPro; IPR034536; RBM15B_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR010912; SPOC_met.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF07744; SPOC; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
DR PROSITE; PS50917; SPOC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Host-virus interaction; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..890
FT /note="Putative RNA-binding protein 15B"
FT /id="PRO_0000081778"
FT DOMAIN 139..219
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 337..414
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 418..492
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 711..889
FT /note="SPOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00249"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..890
FT /note="Interaction with Epstein-Barr virus BMLF1"
FT MOTIF 593..597
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ5"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ5"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 702
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053878"
FT CONFLICT 593
FT /note="R -> K (in Ref. 2; AAI39837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 890 AA; 97205 MW; 276C94252F036C83 CRC64;
MKRQSERDSS PSGRGSSSSA KRPREREREA EAGGRRAAHK ASGGAKHPVP ARARDKPRGS
GSGGGGHRDG RGTGDANHRA SSGRSSGSGA GGGGRGGKAS GDPGASGMSP RASPLPPPPP
PPGAEPACPG SSAAAPEYKT LLISSLSPAL PAEHLEDRLF HQFKRFGEIS LRLSHTPELG
RVAYVNFRHP QDAREARQHA LARQLLLYDR PLKVEPVYLR GGGGSSRRSS SSSAAASTPP
PGPPAPADPL GYLPLHGGYQ YKQRSLSPVA APPLREPRAR HAAAAFALDA AAAAAVGLSR
ERALDYYGLY DDRGRPYGYP AVCEEDLMPE DDQRATRNLF IGNLDHSVSE VELRRAFEKY
GIIEEVVIKR PARGQGGAYA FLKFQNLDMA HRAKVAMSGR VIGRNPIKIG YGKANPTTRL
WVGGLGPNTS LAALAREFDR FGSIRTIDHV KGDSFAYIQY ESLDAAQAAC AKMRGFPLGG
PDRRLRVDFA KAEETRYPQQ YQPSPLPVHY ELLTDGYTRH RNLDADLVRD RTPPHLLYSD
RDRTFLEGDW TSPSKSSDRR NSLEGYSRSV RSRSGERWGA DGDRGLPKPW EERRKRRSLS
SDRGRTTHSP YEERSRTKGS GQQSERGSDR TPERSRKENH SSEGTKESSS NSLSNSRHGA
EERGHHHHHH EAADSSHGKK ARDSERNHRT TEAEPKPLEE PKHETKKLKN LSEYAQTLQL
GWNGLLVLKN SCFPTSMHIL EGDQGVISSL LKDHTSGSKL TQLKIAQRLR LDQPKLDEVT
RRIKQGSPNG YAVLLATQAT PSGLGTEGMP TVEPGLQRRL LRNLVSYLKQ KQAAGVISLP
VGGSKGRDGT GMLYAFPPCD FSQQYLQSAL RTLGKLEEEH MVIVIVRDTA
