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Q96T37 - RBM15_HUMAN

UniProt

Q96T37 - RBM15_HUMAN

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Protein

Putative RNA-binding protein 15

Gene

RBM15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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. nucleoplasm Source: HPA
Complete GO annotation...

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

BgeeiQ96T37.
ExpressionAtlasiQ96T37. baseline and differential.
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. 27 interactions.
IntActiQ96T37. 6 interactions.
MINTiMINT-4131981.

Structurei

3D structure databases

ProteinModelPortaliQ96T37.
SMRiQ96T37. Positions 172-271, 358-532, 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.
GeneTreeiENSGT00530000063730.
HOVERGENiHBG058366.
InParanoidiQ96T37.
KOiK13190.
OMAiHPTSKKM.
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

        10         20         30         40         50
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER 
        60         70         80         90        100
SPVKAKRSRG GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL 
       110        120        130        140        150
DKSSSRGGSR EYDTGGGSSS SRLHSYSSPS TKNSSGGGES RSSSRGGGGE 
       160        170        180        190        200
SRSSGAASSA PGGGDGAEYK TLKISELGSQ LSDEAVEDGL FHEFKRFGDV 
       210        220        230        240        250
SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL YDRPLKIEAV 
       260        270        280        290        300
YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL 
       310        320        330        340        350
GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG 
       360        370        380        390        400
AGAGAAPFRE VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI 
       410        420        430        440        450
TEVDIKRPSR GQTSTYGFLK FENLDMSHRA KLAMSGKIII RNPIKIGYGK 
       460        470        480        490        500
ATPTTRLWVG GLGPWVPLAA LAREFDRFGT IRTIDYRKGD SWAYIQYESL 
       510        520        530        540        550
DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP LPLTHYELVT 
       560        570        580        590        600
DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT 
       610        620        630        640        650
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG 
       660        670        680        690        700
RHLDRSPESD RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS 
       710        720        730        740        750
PIRDRRGSLE KSQGDKRDRK NSASAERDRK HRTTAPTEGK SPLKKEDRSD 
       760        770        780        790        800
GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA SPKLCLAWQG MLLLKNSNFP 
       810        820        830        840        850
SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP KLDEVTRRIK 
       860        870        880        890        900
VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA 
       910        920        930        940        950
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM 
       960        970 
IIVRGFGFQI GVRYENKKRE NLALTLL
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.Curated
The sequence BAB15185.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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]
ENST00000618772; ENSP00000483133; ENSG00000162775. [Q96T37-1]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ96T37.
SMRiQ96T37. Positions 172-271, 358-532, 783-943.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122293. 27 interactions.
IntActiQ96T37. 6 interactions.
MINTiMINT-4131981.

PTM databases

PhosphoSiteiQ96T37.

Polymorphism databases

DMDMi32363506.

Proteomic databases

MaxQBiQ96T37.
PaxDbiQ96T37.
PRIDEiQ96T37.

Protocols and materials databases

DNASUi64783.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369784; ENSP00000358799; ENSG00000162775. [Q96T37-1]
ENST00000487146; ENSP00000473552; ENSG00000162775. [Q96T37-3]
ENST00000602849; ENSP00000473638; ENSG00000162775. [Q96T37-2]
ENST00000618772; ENSP00000483133; ENSG00000162775. [Q96T37-1]
GeneIDi64783.
KEGGihsa:64783.
UCSCiuc001dzl.1. human. [Q96T37-1]
uc001dzm.1. human. [Q96T37-3]
uc021orn.1. human. [Q96T37-2]

Organism-specific databases

CTDi64783.
GeneCardsiGC01P110882.
HGNCiHGNC:14959. RBM15.
HPAiCAB015201.
HPA019824.
HPA049642.
MIMi606077. gene.
neXtProtiNX_Q96T37.
PharmGKBiPA34264.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250829.
GeneTreeiENSGT00530000063730.
HOVERGENiHBG058366.
InParanoidiQ96T37.
KOiK13190.
OMAiHPTSKKM.
OrthoDBiEOG7QZG9W.
PhylomeDBiQ96T37.
TreeFamiTF315637.

Miscellaneous databases

ChiTaRSiRBM15. human.
GeneWikiiRBM15.
GenomeRNAii64783.
NextBioi35460349.
PROiQ96T37.
SOURCEiSearch...

Gene expression databases

BgeeiQ96T37.
ExpressionAtlasiQ96T37. baseline and differential.
GenevestigatoriQ96T37.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.