Q8NDT2 (RB15B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative RNA-binding protein 15B

Alternative name(s):
One-twenty two protein 3
Short name=HuOTT3
RNA-binding motif protein 15B

Gene names

Name:	RBM15B
Synonyms:	OTT3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function in the regulation of alternative or illicit splicing. Ref.5
Subunit structure	Interacts (via the SPOC domain) with Epstein-Barr virus BMLF1 (via the N-terminus); the interaction is direct. May interact with NCOR2. Ref.5
Subcellular location	Nucleus › nucleoplasm. Note: Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. Ref.5
Tissue specificity	Ubiquitously expressed. Ref.5
Sequence similarities	Belongs to the RRM Spen family. Contains 3 RRM (RNA recognition motif) domains. Contains 1 SPOC domain.
Sequence caution	The sequence AAH01367.2 differs from that shown. Reason: Erroneous initiation. The sequence AAS50153.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part. The sequence CAD38547.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of alternative mRNA splicing, via spliceosome Inferred from direct assay Ref.5. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	RNA binding Non-traceable author statement Ref.5. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 890	890	Putative RNA-binding protein 15B		PRO_0000081778
Regions
	Domain	139 – 219	81	RRM 1
	Domain	337 – 414	78	RRM 2
	Domain	418 – 492	75	RRM 3
	Domain	711 – 889	179	SPOC
	Region	722 – 890	169	Interaction with Epstein-Barr virus BMLF1
	Motif	593 – 597	5	Nuclear localization signal Potential
	Compositional bias	658 – 677	20	His-rich
Amino acid modifications
	Modified residue	109	1	Phosphoserine Ref.11 Ref.12
	Modified residue	267	1	Phosphoserine Ref.10
	Modified residue	552	1	Phosphoserine Ref.11 Ref.12
	Modified residue	562	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q8NDT2 [UniParc]. Last modified May 5, 2009. Version 3. Checksum: 276C94252F036C83	FASTA	890	97,205
	10 20 30 40 50 60 MKRQSERDSS PSGRGSSSSA KRPREREREA EAGGRRAAHK ASGGAKHPVP ARARDKPRGS 70 80 90 100 110 120 GSGGGGHRDG RGTGDANHRA SSGRSSGSGA GGGGRGGKAS GDPGASGMSP RASPLPPPPP 130 140 150 160 170 180 PPGAEPACPG SSAAAPEYKT LLISSLSPAL PAEHLEDRLF HQFKRFGEIS LRLSHTPELG 190 200 210 220 230 240 RVAYVNFRHP QDAREARQHA LARQLLLYDR PLKVEPVYLR GGGGSSRRSS SSSAAASTPP 250 260 270 280 290 300 PGPPAPADPL GYLPLHGGYQ YKQRSLSPVA APPLREPRAR HAAAAFALDA AAAAAVGLSR 310 320 330 340 350 360 ERALDYYGLY DDRGRPYGYP AVCEEDLMPE DDQRATRNLF IGNLDHSVSE VELRRAFEKY 370 380 390 400 410 420 GIIEEVVIKR PARGQGGAYA FLKFQNLDMA HRAKVAMSGR VIGRNPIKIG YGKANPTTRL 430 440 450 460 470 480 WVGGLGPNTS LAALAREFDR FGSIRTIDHV KGDSFAYIQY ESLDAAQAAC AKMRGFPLGG 490 500 510 520 530 540 PDRRLRVDFA KAEETRYPQQ YQPSPLPVHY ELLTDGYTRH RNLDADLVRD RTPPHLLYSD 550 560 570 580 590 600 RDRTFLEGDW TSPSKSSDRR NSLEGYSRSV RSRSGERWGA DGDRGLPKPW EERRKRRSLS 610 620 630 640 650 660 SDRGRTTHSP YEERSRTKGS GQQSERGSDR TPERSRKENH SSEGTKESSS NSLSNSRHGA 670 680 690 700 710 720 EERGHHHHHH EAADSSHGKK ARDSERNHRT TEAEPKPLEE PKHETKKLKN LSEYAQTLQL 730 740 750 760 770 780 GWNGLLVLKN SCFPTSMHIL EGDQGVISSL LKDHTSGSKL TQLKIAQRLR LDQPKLDEVT 790 800 810 820 830 840 RRIKQGSPNG YAVLLATQAT PSGLGTEGMP TVEPGLQRRL LRNLVSYLKQ KQAAGVISLP 850 860 870 880 890 VGGSKGRDGT GMLYAFPPCD FSQQYLQSAL RTLGKLEEEH MVIVIVRDTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-890. Tissue: Brain.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 443-890. Tissue: Colon.
[4]	Sales M.M., Ferrasi A.C., Pereira A.A., Pardini M.I.M.C., Camargo A.A. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 633-780. Tissue: Head.
[5]	"Interaction of the Epstein-Barr virus mRNA export factor EB2 with human Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links Spen proteins with splicing regulation and mRNA export." Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P., Mercher T., Bernard O.A., Sergeant A., Manet E. J. Biol. Chem. 280:36935-36945(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EPSTEIN-BARR VIRUS BMLF1 AND NCOR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-552, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-552 AND SER-562, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC092037 Genomic DNA. No translation available. AL831838 mRNA. Translation: CAD38547.2. Different initiation. BC001367 mRNA. Translation: AAH01367.2. Different initiation. AY545557 mRNA. Translation: AAS50153.1. Sequence problems.
IPI	IPI00175136.
RefSeq	NP_037418.3. NM_013286.4.
UniGene	Hs.118738. Hs.731737.
3D structure databases
ProteinModelPortal	Q8NDT2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NDT2. 5 interactions.
STRING	9606.ENSP00000313890.
PTM databases
PhosphoSite	Q8NDT2.
Polymorphism databases
DMDM	229463030.
Proteomic databases
PaxDb	Q8NDT2.
PeptideAtlas	Q8NDT2.
PRIDE	Q8NDT2.
Protocols and materials databases
DNASU	29890.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323686; ENSP00000313890; ENSG00000179837. ENST00000563281; ENSP00000454545; ENSG00000259956.
GeneID	29890.
KEGG	hsa:29890.
UCSC	uc003dbd.3. human.
Organism-specific databases
CTD	29890.
GeneCards	GC03P051428.
HGNC	HGNC:24303. RBM15B.
HPA	HPA036645.
MIM	612602. gene.
neXtProt	NX_Q8NDT2.
PharmGKB	PA134870079.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG250829.
HOGENOM	HOG000006547.
HOVERGEN	HBG058366.
InParanoid	Q8NDT2.
KO	K13190.
OMA	KRDSERN.
OrthoDB	EOG42RD6Z.
Gene expression databases
Bgee	Q8NDT2.
CleanEx	HS_RBM15B.
Genevestigator	Q8NDT2.
GermOnline	ENSG00000179837. Homo sapiens.
Family and domain databases
Gene3D	2.40.290.10. 1 hit. 3.30.70.330. 3 hits.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR012921. SPOC_C. IPR016194. SPOC_like_C_dom. IPR010912. SPOC_met. [Graphical view]
Pfam	PF00076. RRM_1. 2 hits. PF07744. SPOC. 1 hit. [Graphical view]
SMART	SM00360. RRM. 3 hits. [Graphical view]
SUPFAM	SSF100939. SPOC-like. 1 hit.
PROSITE	PS50102. RRM. 3 hits. PS50917. SPOC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	29890.
NextBio	52441.
SOURCE	Search...

Entry information

Entry name

RB15B_HUMAN

Accession

Primary (citable) accession number: Q8NDT2
Secondary accession number(s): Q6QE19, Q9BV96

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.