Q96T37 (RBM15_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 122.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Putative RNA-binding protein 15 Alternative name(s): One-twenty two protein 1 RNA-binding motif protein 15 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 977 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May be implicated in HOX gene regulation. |
| Subunit structure | Interacts with Epstein-Barr virus BSFL2/BMLF1. Ref.7 |
| Subcellular location | |
| Involvement in disease | A chromosomal aberration involving RBM15 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with MKL1. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene. |
| Sequence similarities | Belongs to the RRM Spen family. Contains 3 RRM (RNA recognition motif) domains. Contains 1 SPOC domain. |
| Sequence caution | The sequence BAB14088.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB15185.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q96T37-1) Also known as: RBM15s+ae; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q96T37-2) Also known as: RBM15L; The sequence of this isoform differs from the canonical sequence as follows: 956-977: FGFQIGVRYENKKRENLALTLL → AS | ||||||
| Isoform 3 (identifier: Q96T37-3) Also known as: RBM15S; The sequence of this isoform differs from the canonical sequence as follows: 955-977: GFGFQIGVRYENKKRENLALTLL → AKLVEQRMKIWNSKL |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 977 | 977 | Putative RNA-binding protein 15 | PRO_0000081777 | |||||
Regions | |||||||||
| Domain | 170 – 252 | 83 | RRM 1 | ||||||
| Domain | 374 – 451 | 78 | RRM 2 | ||||||
| Domain | 455 – 529 | 75 | RRM 3 | ||||||
| Domain | 777 – 956 | 180 | SPOC | ||||||
| Compositional bias | 60 – 166 | 107 | Gly/Ser-rich | ||||||
| Compositional bias | 616 – 732 | 117 | Arg-rich | ||||||
Sites | |||||||||
| Site | 954 – 955 | 2 | Breakpoint for translocation to form RBM15-MKL1 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 109 | 1 | Phosphoserine Ref.16 Ref.18 | ||||||
| Modified residue | 210 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 257 | 1 | Phosphoserine Ref.13 Ref.16 | ||||||
| Modified residue | 259 | 1 | Phosphoserine Ref.13 Ref.16 | ||||||
| Modified residue | 292 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 294 | 1 | Phosphoserine Ref.9 Ref.13 Ref.16 Ref.18 | ||||||
| Modified residue | 365 | 1 | Phosphoserine Ref.16 | ||||||
| Modified residue | 450 | 1 | N6-acetyllysine Ref.15 | ||||||
| Modified residue | 568 | 1 | Phosphothreonine Ref.8 Ref.11 Ref.13 Ref.16 Ref.18 | ||||||
| Modified residue | 622 | 1 | Phosphoserine Ref.8 Ref.16 | ||||||
| Modified residue | 670 | 1 | Phosphoserine Ref.11 Ref.13 Ref.14 Ref.16 | ||||||
| Modified residue | 674 | 1 | Phosphoserine Ref.11 Ref.13 Ref.14 | ||||||
| Modified residue | 700 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 741 | 1 | Phosphoserine Ref.13 Ref.18 | ||||||
| Modified residue | 765 | 1 | Phosphoserine Ref.16 Ref.18 | ||||||
| Modified residue | 935 | 1 | Phosphoserine Ref.13 Ref.16 | ||||||
Natural variations | |||||||||
| Alternative sequence | 955 – 977 | 23 | GFGFQ…ALTLL → AKLVEQRMKIWNSKL in isoform 3. | VSP_005812 | |||||
| Alternative sequence | 956 – 977 | 22 | FGFQI…ALTLL → AS in isoform 2. | VSP_005811 | |||||
Experimental info | |||||||||
| Sequence conflict | 99 | 1 | H → L in AAK54722. Ref.1 | ||||||
| Sequence conflict | 99 | 1 | H → L in AAK54723. Ref.1 | ||||||
| Sequence conflict | 99 | 1 | H → L in AAK54724. Ref.1 | ||||||
| Sequence conflict | 99 | 1 | H → L in BAB14088. Ref.3 | ||||||
| Sequence conflict | 705 | 1 | R → G in AAK54722. Ref.1 | ||||||
| Sequence conflict | 705 | 1 | R → G in AAK54723. Ref.1 | ||||||
| Sequence conflict | 705 | 1 | R → G in AAK54724. Ref.1 | ||||||
| Sequence conflict | 705 | 1 | R → G in BAB14088. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Fusion of two novel genes, RBM15 and MKL1, in the t(1;22)(p13;q13) of acute megakaryoblastic leukemia." Ma Z., Morris S.W., Valentine V., Li M., Herbrick J.-A., Cui X., Bouman D., Li Y., Mehta P.K., Nizetic D., Kaneko Y., Chan G.C.F., Chan L.C., Squire J., Scherer S.W., Hitzler J.K. Nat. Genet. 28:220-221(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), CHROMOSOMAL TRANSLOCATION WITH MKL1. |
| [2] | "Involvement of a human gene related to the Drosophila spen gene in the recurrent t(1;22) translocation of acute megakaryocytic leukemia." Mercher T., Coniat M.B.-L., Monni R., Mauchauffe M., Khac F.N., Gressin L., Mugneret F., Leblanc T., Dastugue N., Berger R., Bernard O.A. Proc. Natl. Acad. Sci. U.S.A. 98:5776-5779(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHROMOSOMAL TRANSLOCATION WITH MKL1. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Hepatoma and Teratocarcinoma. |
| [5] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-977 (ISOFORM 1). Tissue: Melanoma. |
| [7] | "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: INTERACTION WITH EBV BSFL2/BMLF1. |
| [8] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-568; SER-622 AND SER-700, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney. |
| [11] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-568; SER-670 AND SER-674, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma. |
| [13] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-259; SER-292; SER-294; THR-568; SER-670; SER-674; SER-741 AND SER-935, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "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-670 AND SER-674, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [15] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-450, MASS SPECTROMETRY. |
| [16] | "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; SER-210; SER-257; SER-259; SER-294; SER-365; THR-568; SER-622; SER-670; SER-765 AND SER-935, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [18] | "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-294; THR-568; SER-741 AND SER-765, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF368062 mRNA. Translation: AAK54722.1. AF368063 mRNA. Translation: AAK54723.1. AF368064 mRNA. Translation: AAK54724.1. AF364035 mRNA. Translation: AAK56920.1. Different termination. AJ303089 mRNA. Translation: CAC38828.1. Different termination. AJ303090 mRNA. Translation: CAC38829.1. Different termination. AJ297259 Genomic DNA. Translation: CAC38861.1. AJ297259 Genomic DNA. Translation: CAC38862.1. AK022541 mRNA. Translation: BAB14088.1. Different initiation. AK025596 mRNA. Translation: BAB15185.1. Different initiation. AL355488 Genomic DNA. Translation: CAI19077.1. CH471122 Genomic DNA. Translation: EAW56439.1. BC006397 mRNA. Translation: AAH06397.2. BC062316 mRNA. Translation: AAH62316.1. BC098140 mRNA. Translation: AAH98140.1. BC103507 mRNA. Translation: AAI03508.1. |
| IPI | IPI00102752. IPI00220716. IPI00220717. |
| RefSeq | NP_001188474.1. NM_001201545.1. NP_073605.4. NM_022768.4. |
| UniGene | Hs.435947. Hs.708172. |
3D structure databases | |
| ProteinModelPortal | Q96T37. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q96T37. 2 interactions. |
PTM databases | |
| PhosphoSite | Q96T37. |
Polymorphism databases | |
| DMDM | 32363506. |
Proteomic databases | |
| PaxDb | Q96T37. |
| PRIDE | Q96T37. |
Protocols and materials databases | |
| DNASU | 64783. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000369784; ENSP00000358799; ENSG00000162775. |
| GeneID | 64783. |
| KEGG | hsa:64783. |
| UCSC | uc001dzl.1. human. uc001dzm.1. human. uc021orn.1. human. |
Organism-specific databases | |
| CTD | 64783. |
| GeneCards | GC01P110876. |
| HGNC | HGNC:14959. RBM15. |
| HPA | CAB015201. HPA019824. |
| MIM | 606077. gene. |
| neXtProt | NX_Q96T37. |
| PharmGKB | PA34264. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG250829. |
| HOVERGEN | HBG058366. |
| InParanoid | Q96T37. |
| KO | K13190. |
| OMA | DYLVMIV. |
| OrthoDB | EOG41ZF99. |
| PhylomeDB | Q96T37. |
Gene expression databases | |
| Bgee | Q96T37. |
| Genevestigator | Q96T37. |
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. 1 hit. 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 | |
| ChiTaRS | RBM15. human. |
| GenomeRNAi | 64783. |
| NextBio | 66822. |
| SOURCE | Search... |
Entry information
| Entry name | RBM15_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96T37 Secondary accession number(s): Q4V760 Q9H9Y0 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
