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Q96T37 (RBM15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative RNA-binding protein 15
Alternative name(s):
One-twenty two protein 1
RNA-binding motif protein 15
Gene names
Name:RBM15
Synonyms:OTT, OTT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length977 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.16

Subunit structure

Interacts with Epstein-Barr virus BSFL2/BMLF1. Interacts (via SPOC domain) with SETD1B. Interacts with NXF1, the interaction is required to promote mRNA export. Ref.7 Ref.9 Ref.16 Ref.22

Subcellular location

Nucleus. Nucleus membrane; Peripheral membrane protein. Note: Colocalizes at the nuclear pore with DBP5 and NXF1. Ref.9 Ref.16

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. Translation N-terminally extended.

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [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
Isoform 4 (identifier: Q96T37-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 977977Putative RNA-binding protein 15
PRO_0000081777

Regions

Domain170 – 25283RRM 1
Domain374 – 45178RRM 2
Domain455 – 52975RRM 3
Domain777 – 956180SPOC
Compositional bias60 – 166107Gly/Ser-rich
Compositional bias616 – 732117Arg-rich

Sites

Site954 – 9552Breakpoint for translocation to form RBM15-MKL1

Amino acid modifications

Modified residue1091Phosphoserine Ref.19 Ref.21
Modified residue2101Phosphoserine Ref.19
Modified residue2571Phosphoserine Ref.14 Ref.19
Modified residue2591Phosphoserine Ref.14 Ref.19
Modified residue2921Phosphoserine Ref.14
Modified residue2941Phosphoserine Ref.10 Ref.14 Ref.19 Ref.21
Modified residue3651Phosphoserine Ref.19
Modified residue4501N6-acetyllysine Ref.18
Modified residue5681Phosphothreonine Ref.8 Ref.12 Ref.14 Ref.19 Ref.21
Modified residue6221Phosphoserine Ref.8 Ref.19
Modified residue6701Phosphoserine Ref.12 Ref.14 Ref.17 Ref.19
Modified residue6741Phosphoserine Ref.12 Ref.14 Ref.17
Modified residue7001Phosphoserine Ref.8
Modified residue7411Phosphoserine Ref.14 Ref.21
Modified residue7651Phosphoserine Ref.19 Ref.21
Modified residue9351Phosphoserine Ref.14 Ref.19

Natural variations

Alternative sequence1 – 4444Missing in isoform 4.
VSP_053877
Alternative sequence955 – 97723GFGFQ…ALTLL → AKLVEQRMKIWNSKL in isoform 3.
VSP_005812
Alternative sequence956 – 97722FGFQI…ALTLL → AS in isoform 2 and isoform 4.
VSP_005811

Experimental info

Mutagenesis7951K → A: Disrupts interaction with SETD1B. Ref.22
Mutagenesis8981K → A: Disrupts interaction with SETD1B. Ref.22
Mutagenesis9231F → A: Disrupts interaction with SETD1B. Ref.22
Sequence conflict991H → L in AAK54722. Ref.1
Sequence conflict991H → L in AAK54723. Ref.1
Sequence conflict991H → L in AAK54724. Ref.1
Sequence conflict991H → L in BAB14088. Ref.3
Sequence conflict2271D → N in AAI03494. Ref.6
Sequence conflict7051R → G in AAK54722. Ref.1
Sequence conflict7051R → G in AAK54723. Ref.1
Sequence conflict7051R → G in AAK54724. Ref.1
Sequence conflict7051R → G in BAB14088. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RBM15s+ae) [UniParc].

Last modified June 27, 2003. Version 2.
Checksum: FB26AFE246E40282

FASTA977107,189
        10         20         30         40         50         60 
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER SPVKAKRSRG 

        70         80         90        100        110        120 
GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL DKSSSRGGSR EYDTGGGSSS 

       130        140        150        160        170        180 
SRLHSYSSPS TKNSSGGGES RSSSRGGGGE SRSSGAASSA PGGGDGAEYK TLKISELGSQ 

       190        200        210        220        230        240 
LSDEAVEDGL FHEFKRFGDV SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL 

       250        260        270        280        290        300 
YDRPLKIEAV YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL 

       310        320        330        340        350        360 
GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG AGAGAAPFRE 

       370        380        390        400        410        420 
VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI TEVDIKRPSR GQTSTYGFLK 

       430        440        450        460        470        480 
FENLDMSHRA KLAMSGKIII RNPIKIGYGK ATPTTRLWVG GLGPWVPLAA LAREFDRFGT 

       490        500        510        520        530        540 
IRTIDYRKGD SWAYIQYESL DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP 

       550        560        570        580        590        600 
LPLTHYELVT DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT 

       610        620        630        640        650        660 
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG RHLDRSPESD 

       670        680        690        700        710        720 
RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS PIRDRRGSLE KSQGDKRDRK 

       730        740        750        760        770        780 
NSASAERDRK HRTTAPTEGK SPLKKEDRSD GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA 

       790        800        810        820        830        840 
SPKLCLAWQG MLLLKNSNFP SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP 

       850        860        870        880        890        900 
KLDEVTRRIK VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA 

       910        920        930        940        950        960 
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM IIVRGFGFQI 

       970 
GVRYENKKRE NLALTLL 

« Hide

Isoform 2 (RBM15L) [UniParc].

Checksum: 72893E069306B4E0
Show »

FASTA957104,755
Isoform 3 (RBM15S) [UniParc].

Checksum: E2E52058E76FE38D
Show »

FASTA969106,366
Isoform 4 [UniParc].

Checksum: 1B4E29CDD062A5AC
Show »

FASTA91399,701

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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[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]"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, 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]"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].
[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.

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.
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.
CCDSCCDS59198.1. [Q96T37-3]
CCDS822.1. [Q96T37-1]
RefSeqNP_001188474.1. NM_001201545.1. [Q96T37-3]
NP_073605.4. NM_022768.4. [Q96T37-1]
UniGeneHs.435947.
Hs.708172.

3D structure databases

ProteinModelPortalQ96T37.
SMRQ96T37. Positions 374-529, 783-943.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122293. 22 interactions.
IntActQ96T37. 6 interactions.
MINTMINT-4131981.

PTM databases

PhosphoSiteQ96T37.

Polymorphism databases

DMDM32363506.

Proteomic databases

MaxQBQ96T37.
PaxDbQ96T37.
PRIDEQ96T37.

Protocols and materials databases

DNASU64783.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369784; ENSP00000358799; ENSG00000162775. [Q96T37-1]
ENST00000487146; ENSP00000473552; ENSG00000162775. [Q96T37-3]
ENST00000602849; ENSP00000473638; ENSG00000162775. [Q96T37-2]
GeneID64783.
KEGGhsa:64783.
UCSCuc001dzl.1. human. [Q96T37-1]
uc001dzm.1. human. [Q96T37-3]
uc021orn.1. human. [Q96T37-2]

Organism-specific databases

CTD64783.
GeneCardsGC01P110882.
HGNCHGNC:14959. RBM15.
HPACAB015201.
HPA019824.
HPA049642.
MIM606077. gene.
neXtProtNX_Q96T37.
PharmGKBPA34264.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250829.
HOVERGENHBG058366.
InParanoidQ96T37.
KOK13190.
OMAVMIIVRV.
OrthoDBEOG7QZG9W.
PhylomeDBQ96T37.
TreeFamTF315637.

Gene expression databases

ArrayExpressQ96T37.
BgeeQ96T37.
GenevestigatorQ96T37.

Family and domain databases

Gene3D2.40.290.10. 1 hit.
3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR012921. SPOC_C.
IPR016194. SPOC_like_C_dom.
IPR010912. SPOC_met.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
PF07744. SPOC. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMSSF100939. SSF100939. 1 hit.
PROSITEPS50102. RRM. 3 hits.
PS50917. SPOC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM15. human.
GeneWikiRBM15.
GenomeRNAi64783.
NextBio35460349.
PROQ96T37.
SOURCESearch...

Entry information

Entry nameRBM15_HUMAN
AccessionPrimary (citable) accession number: Q96T37
Secondary accession number(s): A1A693 expand/collapse secondary AC list , Q3ZB86, Q4V760, Q5D058, Q5T613, Q86VW9, Q96PE4, Q96SC5, Q96SC6, Q96SC9, Q96SD0, Q96T38, Q9BRA5, Q9H6R8, Q9H9Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 27, 2003
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM