ID   RB15B_HUMAN             Reviewed;         890 AA.
AC   Q8NDT2; Q6QE19; Q9BV96;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   05-OCT-2010, entry version 71.
DE   RecName: Full=Putative RNA-binding protein 15B;
DE   AltName: Full=One-twenty two protein 3;
DE            Short=HuOTT3;
DE   AltName: Full=RNA-binding motif protein 15B;
GN   Name=RBM15B; Synonyms=OTT3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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] OF 155-890.
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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-890.
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.,
RA   Camargo A.A.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH EPSTEIN-BARR VIRUS BMLF1 AND NCOR2,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16129689; DOI=10.1074/jbc.M501725200;
RA   Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S.,
RA   Meresse P., Mercher T., Bernard O.A., Sergeant A., Manet E.;
RT   "Interaction of the Epstein-Barr virus mRNA export factor EB2 with
RT   human Spen proteins SHARP, OTT1, and a novel member of the family,
RT   OTT3, links Spen proteins with splicing regulation and mRNA export.";
RL   J. Biol. Chem. 280:36935-36945(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, AND MASS
RP   SPECTROMETRY.
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598; SER-600; SER-601
RP   AND SER-609, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17287340; DOI=10.1073/pnas.0611217104;
RA   Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
RT   "Global proteomic profiling of phosphopeptides using electron transfer
RT   dissociation tandem mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532 AND SER-562, AND
RP   MASS SPECTROMETRY.
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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=T-cell;
RX   PubMed=19367720; DOI=10.1021/pr800500r;
RA   Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT   "Phosphorylation analysis of primary human T lymphocytes using
RT   sequential IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 AND SER-552, AND
RP   MASS SPECTROMETRY.
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).
CC   -!- FUNCTION: May function in the regulation of alternative or illicit
CC       splicing.
CC   -!- SUBUNIT: Interacts (via the SPOC domain) with Epstein-Barr virus
CC       BMLF1 (via the N-terminus); the interaction is direct. May
CC       interact with NCOR2.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Colocalizes with
CC       BMLF1 in the nucleus. Localized in the nucleoplasm with a granular
CC       staining pattern and excluded from the nucleoli.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the RRM Spen family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SIMILARITY: Contains 1 SPOC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH01367.2; Type=Erroneous initiation;
CC       Sequence=AAS50153.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part;
CC       Sequence=CAD38547.2; Type=Erroneous initiation;
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DR   EMBL; AC092037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL831838; CAD38547.2; ALT_INIT; mRNA.
DR   EMBL; BC001367; AAH01367.2; ALT_INIT; mRNA.
DR   EMBL; AY545557; AAS50153.1; ALT_SEQ; mRNA.
DR   IPI; IPI00175136; -.
DR   RefSeq; NP_037418.3; -.
DR   UniGene; Hs.118738; -.
DR   ProteinModelPortal; Q8NDT2; -.
DR   IntAct; Q8NDT2; 1.
DR   STRING; Q8NDT2; -.
DR   PhosphoSite; Q8NDT2; -.
DR   PeptideAtlas; Q8NDT2; -.
DR   PRIDE; Q8NDT2; -.
DR   Ensembl; ENST00000323686; ENSP00000313890; ENSG00000179837.
DR   GeneID; 29890; -.
DR   KEGG; hsa:29890; -.
DR   UCSC; uc003dbd.1; human.
DR   CTD; 29890; -.
DR   GeneCards; GC03P051405; -.
DR   HGNC; HGNC:24303; RBM15B.
DR   MIM; 612602; gene.
DR   PharmGKB; PA134870079; -.
DR   HOGENOM; HBG717522; -.
DR   HOVERGEN; HBG058366; -.
DR   InParanoid; Q8NDT2; -.
DR   OMA; HRDGRGA; -.
DR   OrthoDB; EOG9Z0DRC; -.
DR   NextBio; 52441; -.
DR   ArrayExpress; Q8NDT2; -.
DR   Bgee; Q8NDT2; -.
DR   CleanEx; HS_RBM15B; -.
DR   Genevestigator; Q8NDT2; -.
DR   GermOnline; ENSG00000179837; Homo sapiens.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative nuclear mRNA spli...; IDA:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; a_b_plait_nuc-bd.
DR   InterPro; IPR000504; RRM_RNP1.
DR   InterPro; IPR016194; SPOC-like.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR010912; SPOC_met.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   Pfam; PF07744; SPOC; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF100939; SPOC-like; 1.
DR   PROSITE; PS50102; RRM; 3.
DR   PROSITE; PS50917; SPOC; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Host-virus interaction; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    890       Putative RNA-binding protein 15B.
FT                                /FTId=PRO_0000081778.
FT   DOMAIN      139    219       RRM 1.
FT   DOMAIN      337    414       RRM 2.
FT   DOMAIN      418    492       RRM 3.
FT   DOMAIN      711    889       SPOC.
FT   REGION      722    890       Interaction with Epstein-Barr virus
FT                                BMLF1.
FT   MOTIF       593    597       Nuclear localization signal (Potential).
FT   COMPBIAS    658    677       His-rich.
FT   MOD_RES     267    267       Phosphoserine.
FT   MOD_RES     532    532       Phosphothreonine.
FT   MOD_RES     552    552       Phosphoserine.
FT   MOD_RES     562    562       Phosphoserine.
FT   MOD_RES     598    598       Phosphoserine.
FT   MOD_RES     600    600       Phosphoserine.
FT   MOD_RES     601    601       Phosphoserine.
FT   MOD_RES     609    609       Phosphoserine.
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
//