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Q96T37

- RBM15_HUMAN

UniProt

Q96T37 - RBM15_HUMAN

Protein

Putative RNA-binding protein 15

Gene

RBM15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (27 Jun 2003)
      Previous versions | rss
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    Functioni

    May function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing. High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing. May be implicated in HOX gene regulation.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei954 – 9552Breakpoint for translocation to form RBM15-MKL1

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of myeloid cell differentiation Source: Ensembl
    2. patterning of blood vessels Source: Ensembl
    3. placenta blood vessel development Source: Ensembl
    4. positive regulation of transcription of Notch receptor target Source: Ensembl
    5. spleen development Source: Ensembl
    6. ventricular septum morphogenesis Source: Ensembl
    7. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative RNA-binding protein 15
    Alternative name(s):
    One-twenty two protein 1
    RNA-binding motif protein 15
    Gene namesi
    Name:RBM15
    Synonyms:OTT, OTT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:14959. RBM15.

    Subcellular locationi

    Nucleus. Nucleus membrane; Peripheral membrane protein
    Note: Colocalizes at the nuclear pore with DBP5 and NXF1.

    GO - Cellular componenti

    1. nuclear membrane Source: UniProtKB-SubCell
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi795 – 7951K → A: Disrupts interaction with SETD1B. 1 Publication
    Mutagenesisi898 – 8981K → A: Disrupts interaction with SETD1B. 1 Publication
    Mutagenesisi923 – 9231F → A: Disrupts interaction with SETD1B. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA34264.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 977977Putative RNA-binding protein 15PRO_0000081777Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei109 – 1091Phosphoserine2 Publications
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphoserine2 Publications
    Modified residuei259 – 2591Phosphoserine2 Publications
    Modified residuei292 – 2921Phosphoserine1 Publication
    Modified residuei294 – 2941Phosphoserine4 Publications
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei450 – 4501N6-acetyllysine1 Publication
    Modified residuei568 – 5681Phosphothreonine5 Publications
    Modified residuei622 – 6221Phosphoserine2 Publications
    Modified residuei670 – 6701Phosphoserine4 Publications
    Modified residuei674 – 6741Phosphoserine3 Publications
    Modified residuei700 – 7001Phosphoserine1 Publication
    Modified residuei741 – 7411Phosphoserine2 Publications
    Modified residuei765 – 7651Phosphoserine2 Publications
    Modified residuei935 – 9351Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96T37.
    PaxDbiQ96T37.
    PRIDEiQ96T37.

    PTM databases

    PhosphoSiteiQ96T37.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96T37.
    BgeeiQ96T37.
    GenevestigatoriQ96T37.

    Organism-specific databases

    HPAiCAB015201.
    HPA019824.
    HPA049642.

    Interactioni

    Subunit structurei

    Interacts with Epstein-Barr virus BSFL2/BMLF1. Interacts (via SPOC domain) with SETD1B. Interacts with NXF1, the interaction is required to promote mRNA export.4 Publications

    Protein-protein interaction databases

    BioGridi122293. 22 interactions.
    IntActiQ96T37. 6 interactions.
    MINTiMINT-4131981.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96T37.
    SMRiQ96T37. Positions 374-529, 783-943.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini170 – 25283RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini374 – 45178RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini455 – 52975RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini777 – 956180SPOCPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 166107Gly/Ser-richAdd
    BLAST
    Compositional biasi616 – 732117Arg-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RRM Spen family.Curated
    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation
    Contains 1 SPOC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG250829.
    HOVERGENiHBG058366.
    InParanoidiQ96T37.
    KOiK13190.
    OMAiVMIIVRV.
    OrthoDBiEOG7QZG9W.
    PhylomeDBiQ96T37.
    TreeFamiTF315637.

    Family and domain databases

    Gene3Di2.40.290.10. 1 hit.
    3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012921. SPOC_C.
    IPR016194. SPOC_like_C_dom.
    IPR010912. SPOC_met.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    PF07744. SPOC. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    PROSITEiPS50102. RRM. 3 hits.
    PS50917. SPOC. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q96T37-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER    50
    SPVKAKRSRG GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL 100
    DKSSSRGGSR EYDTGGGSSS SRLHSYSSPS TKNSSGGGES RSSSRGGGGE 150
    SRSSGAASSA PGGGDGAEYK TLKISELGSQ LSDEAVEDGL FHEFKRFGDV 200
    SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL YDRPLKIEAV 250
    YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL 300
    GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG 350
    AGAGAAPFRE VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI 400
    TEVDIKRPSR GQTSTYGFLK FENLDMSHRA KLAMSGKIII RNPIKIGYGK 450
    ATPTTRLWVG GLGPWVPLAA LAREFDRFGT IRTIDYRKGD SWAYIQYESL 500
    DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP LPLTHYELVT 550
    DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT 600
    AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG 650
    RHLDRSPESD RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS 700
    PIRDRRGSLE KSQGDKRDRK NSASAERDRK HRTTAPTEGK SPLKKEDRSD 750
    GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA SPKLCLAWQG MLLLKNSNFP 800
    SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP KLDEVTRRIK 850
    VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA 900
    AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM 950
    IIVRGFGFQI GVRYENKKRE NLALTLL 977
    Length:977
    Mass (Da):107,189
    Last modified:June 27, 2003 - v2
    Checksum:iFB26AFE246E40282
    GO
    Isoform 2 (identifier: Q96T37-2) [UniParc]FASTAAdd to Basket

    Also known as: RBM15L

    The sequence of this isoform differs from the canonical sequence as follows:
         956-977: FGFQIGVRYENKKRENLALTLL → AS

    Show »
    Length:957
    Mass (Da):104,755
    Checksum:i72893E069306B4E0
    GO
    Isoform 3 (identifier: Q96T37-3) [UniParc]FASTAAdd to Basket

    Also known as: RBM15S

    The sequence of this isoform differs from the canonical sequence as follows:
         955-977: GFGFQIGVRYENKKRENLALTLL → AKLVEQRMKIWNSKL

    Show »
    Length:969
    Mass (Da):106,366
    Checksum:iE2E52058E76FE38D
    GO
    Isoform 4 (identifier: Q96T37-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: Missing.
         956-977: FGFQIGVRYENKKRENLALTLL → AS

    Note: Produced by alternative initiation of isoform 2.

    Show »
    Length:913
    Mass (Da):99,701
    Checksum:i1B4E29CDD062A5AC
    GO

    Sequence cautioni

    The sequence BAB14088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB15185.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991H → L in AAK54722. (PubMed:11431691)Curated
    Sequence conflicti99 – 991H → L in AAK54723. (PubMed:11431691)Curated
    Sequence conflicti99 – 991H → L in AAK54724. (PubMed:11431691)Curated
    Sequence conflicti99 – 991H → L in BAB14088. 1 PublicationCurated
    Sequence conflicti227 – 2271D → N in AAI03494. (PubMed:15489334)Curated
    Sequence conflicti705 – 7051R → G in AAK54722. (PubMed:11431691)Curated
    Sequence conflicti705 – 7051R → G in AAK54723. (PubMed:11431691)Curated
    Sequence conflicti705 – 7051R → G in AAK54724. (PubMed:11431691)Curated
    Sequence conflicti705 – 7051R → G in BAB14088. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444Missing in isoform 4. CuratedVSP_053877Add
    BLAST
    Alternative sequencei955 – 97723GFGFQ…ALTLL → AKLVEQRMKIWNSKL in isoform 3. 2 PublicationsVSP_005812Add
    BLAST
    Alternative sequencei956 – 97722FGFQI…ALTLL → AS in isoform 2 and isoform 4. 1 PublicationVSP_005811Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    BC047479 mRNA. Translation: AAH47479.1.
    BC062316 mRNA. Translation: AAH62316.1.
    BC098140 mRNA. Translation: AAH98140.1.
    BC103493 mRNA. Translation: AAI03494.1.
    BC103507 mRNA. Translation: AAI03508.1.
    BK005915 mRNA. Translation: DAA05818.1.
    CCDSiCCDS59198.1. [Q96T37-3]
    CCDS822.1. [Q96T37-1]
    RefSeqiNP_001188474.1. NM_001201545.1. [Q96T37-3]
    NP_073605.4. NM_022768.4. [Q96T37-1]
    UniGeneiHs.435947.
    Hs.708172.

    Genome annotation databases

    EnsembliENST00000369784; ENSP00000358799; ENSG00000162775. [Q96T37-1]
    ENST00000487146; ENSP00000473552; ENSG00000162775. [Q96T37-3]
    ENST00000602849; ENSP00000473638; ENSG00000162775. [Q96T37-2]
    GeneIDi64783.
    KEGGihsa:64783.
    UCSCiuc001dzl.1. human. [Q96T37-1]
    uc001dzm.1. human. [Q96T37-3]
    uc021orn.1. human. [Q96T37-2]

    Polymorphism databases

    DMDMi32363506.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    BC047479 mRNA. Translation: AAH47479.1 .
    BC062316 mRNA. Translation: AAH62316.1 .
    BC098140 mRNA. Translation: AAH98140.1 .
    BC103493 mRNA. Translation: AAI03494.1 .
    BC103507 mRNA. Translation: AAI03508.1 .
    BK005915 mRNA. Translation: DAA05818.1 .
    CCDSi CCDS59198.1. [Q96T37-3 ]
    CCDS822.1. [Q96T37-1 ]
    RefSeqi NP_001188474.1. NM_001201545.1. [Q96T37-3 ]
    NP_073605.4. NM_022768.4. [Q96T37-1 ]
    UniGenei Hs.435947.
    Hs.708172.

    3D structure databases

    ProteinModelPortali Q96T37.
    SMRi Q96T37. Positions 374-529, 783-943.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122293. 22 interactions.
    IntActi Q96T37. 6 interactions.
    MINTi MINT-4131981.

    PTM databases

    PhosphoSitei Q96T37.

    Polymorphism databases

    DMDMi 32363506.

    Proteomic databases

    MaxQBi Q96T37.
    PaxDbi Q96T37.
    PRIDEi Q96T37.

    Protocols and materials databases

    DNASUi 64783.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369784 ; ENSP00000358799 ; ENSG00000162775 . [Q96T37-1 ]
    ENST00000487146 ; ENSP00000473552 ; ENSG00000162775 . [Q96T37-3 ]
    ENST00000602849 ; ENSP00000473638 ; ENSG00000162775 . [Q96T37-2 ]
    GeneIDi 64783.
    KEGGi hsa:64783.
    UCSCi uc001dzl.1. human. [Q96T37-1 ]
    uc001dzm.1. human. [Q96T37-3 ]
    uc021orn.1. human. [Q96T37-2 ]

    Organism-specific databases

    CTDi 64783.
    GeneCardsi GC01P110882.
    HGNCi HGNC:14959. RBM15.
    HPAi CAB015201.
    HPA019824.
    HPA049642.
    MIMi 606077. gene.
    neXtProti NX_Q96T37.
    PharmGKBi PA34264.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250829.
    HOVERGENi HBG058366.
    InParanoidi Q96T37.
    KOi K13190.
    OMAi VMIIVRV.
    OrthoDBi EOG7QZG9W.
    PhylomeDBi Q96T37.
    TreeFami TF315637.

    Miscellaneous databases

    ChiTaRSi RBM15. human.
    GeneWikii RBM15.
    GenomeRNAii 64783.
    NextBioi 35460349.
    PROi Q96T37.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96T37.
    Bgeei Q96T37.
    Genevestigatori Q96T37.

    Family and domain databases

    Gene3Di 2.40.290.10. 1 hit.
    3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR012921. SPOC_C.
    IPR016194. SPOC_like_C_dom.
    IPR010912. SPOC_met.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    PF07744. SPOC. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    PS50917. SPOC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., 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 and Testis.
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway."
      Lindtner S., Zolotukhin A.S., Uranishi H., Bear J., Kulkarni V., Smulevitch S., Samiotaki M., Panayotou G., Felber B.K., Pavlakis G.N.
      J. Biol. Chem. 281:36915-36928(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 4), RNA-BINDING, INTERACTION WITH NXF1.
    10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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.
    14. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA."
      Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N., Felber B.K.
      Nucleic Acids Res. 37:7151-7162(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBP5.
    17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Rbm15-Mkl1 interacts with the Setd1b histone H3-Lys4 methyltransferase via a SPOC domain that is required for cytokine-independent proliferation."
      Lee J.H., Skalnik D.G.
      PLoS ONE 7:E42965-E42965(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETD1B, MUTAGENESIS OF LYS-795; LYS-898 AND PHE-923.

    Entry informationi

    Entry nameiRBM15_HUMAN
    AccessioniPrimary (citable) accession number: Q96T37
    Secondary accession number(s): A1A693
    , Q3ZB86, Q4V760, Q5D058, Q5T613, Q86VW9, Q96PE4, Q96SC5, Q96SC6, Q96SC9, Q96SD0, Q96T38, Q9BRA5, Q9H6R8, Q9H9Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: June 27, 2003
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3