Q96T37 (RBM15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	RBM15
Synonyms:	OTT, OTT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	977 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Membrane Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of myeloid cell differentiation Inferred from electronic annotation. Source: Ensembl patterning of blood vessels Inferred from electronic annotation. Source: Ensembl placenta blood vessel development Inferred from electronic annotation. Source: Ensembl positive regulation of transcription of Notch receptor target Inferred from electronic annotation. Source: Ensembl spleen development Inferred from electronic annotation. Source: Ensembl ventricular septum morphogenesis Inferred from electronic annotation. Source: Ensembl viral process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB protein binding Inferred from physical interaction Ref.7. Source: UniProtKB
Complete GO annotation...

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 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.19 Ref.21
	Modified residue	210	1	Phosphoserine Ref.19
	Modified residue	257	1	Phosphoserine Ref.14 Ref.19
	Modified residue	259	1	Phosphoserine Ref.14 Ref.19
	Modified residue	292	1	Phosphoserine Ref.14
	Modified residue	294	1	Phosphoserine Ref.10 Ref.14 Ref.19 Ref.21
	Modified residue	365	1	Phosphoserine Ref.19
	Modified residue	450	1	N6-acetyllysine Ref.18
	Modified residue	568	1	Phosphothreonine Ref.8 Ref.12 Ref.14 Ref.19 Ref.21
	Modified residue	622	1	Phosphoserine Ref.8 Ref.19
	Modified residue	670	1	Phosphoserine Ref.12 Ref.14 Ref.17 Ref.19
	Modified residue	674	1	Phosphoserine Ref.12 Ref.14 Ref.17
	Modified residue	700	1	Phosphoserine Ref.8
	Modified residue	741	1	Phosphoserine Ref.14 Ref.21
	Modified residue	765	1	Phosphoserine Ref.19 Ref.21
	Modified residue	935	1	Phosphoserine Ref.14 Ref.19
Natural variations
	Alternative sequence	1 – 44	44	Missing in isoform 4.		VSP_053877
	Alternative sequence	955 – 977	23	GFGFQ…ALTLL → AKLVEQRMKIWNSKL in isoform 3.		VSP_005812
	Alternative sequence	956 – 977	22	FGFQI…ALTLL → AS in isoform 2 and isoform 4.		VSP_005811
Experimental info
	Mutagenesis	795	1	K → A: Disrupts interaction with SETD1B. Ref.22
	Mutagenesis	898	1	K → A: Disrupts interaction with SETD1B. Ref.22
	Mutagenesis	923	1	F → A: Disrupts interaction with SETD1B. Ref.22
	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	227	1	D → N in AAI03494. Ref.6
	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

	Sequence		Length	Mass (Da)
	Isoform 1 (RBM15s+ae) [UniParc]. Last modified June 27, 2003. Version 2. Checksum: FB26AFE246E40282	FASTA	977	107,189
	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
	Isoform 2 (RBM15L) [UniParc]. Checksum: 72893E069306B4E0	FASTA	957	104,755
	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 AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM IIVRGAS
	Isoform 3 (RBM15S) [UniParc]. Checksum: E2E52058E76FE38D	FASTA	969	106,366
	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 IIVRAKLVEQ RMKIWNSKL
	Isoform 4 [UniParc]. Checksum: 1B4E29CDD062A5AC	FASTA	913	99,701
	10 20 30 40 50 60 MKGKERSPVK AKRSRGGEDS TSRGERSKKL GGSGGSNGSS SGKTDSGGGS RRSLHLDKSS 70 80 90 100 110 120 SRGGSREYDT GGGSSSSRLH SYSSPSTKNS SGGGESRSSS RGGGGESRSS GAASSAPGGG 130 140 150 160 170 180 DGAEYKTLKI SELGSQLSDE AVEDGLFHEF KRFGDVSVKI SHLSGSGSGD ERVAFVNFRR 190 200 210 220 230 240 PEDARAAKHA RGRLVLYDRP LKIEAVYVSR RRSRSPLDKD TYPPSASVVG ASVGGHRHPP 250 260 270 280 290 300 GGGGGQRSLS PGGAALGYRD YRLQQLALGR LPPPPPPPLP RDLERERDYP FYERVRPAYS 310 320 330 340 350 360 LEPRVGAGAG AAPFREVDEI SPEDDQRANR TLFLGNLDIT VTESDLRRAF DRFGVITEVD 370 380 390 400 410 420 IKRPSRGQTS TYGFLKFENL DMSHRAKLAM SGKIIIRNPI KIGYGKATPT TRLWVGGLGP 430 440 450 460 470 480 WVPLAALARE FDRFGTIRTI DYRKGDSWAY IQYESLDAAH AAWTHMRGFP LGGPDRRLRV 490 500 510 520 530 540 DFADTEHRYQ QQYLQPLPLT HYELVTDAFG HRAPDPLRGA RDRTPPLLYR DRDRDLYPDS 550 560 570 580 590 600 DWVPPPPPVR ERSTRTAATS VPAYEPLDSL DRRRDGWSLD RDRGDRDLPS SRDQPRKRRL 610 620 630 640 650 660 PEESGGRHLD RSPESDRPRK RHCAPSPDRS PELSSSRDRY NSDNDRSSRL LLERPSPIRD 670 680 690 700 710 720 RRGSLEKSQG DKRDRKNSAS AERDRKHRTT APTEGKSPLK KEDRSDGSAP STSTASSKLK 730 740 750 760 770 780 SPSQKQDGGT APVASASPKL CLAWQGMLLL KNSNFPSNMH LLQGDLQVAS SLLVEGSTGG 790 800 810 820 830 840 KVAQLKITQR LRLDQPKLDE VTRRIKVAGP NGYAILLAVP GSSDSRSSSS SAASDTATST 850 860 870 880 890 900 QRPLRNLVSY LKQKQAAGVI SLPVGGNKDK ENTGVLHAFP PCEFSQQFLD SPAKALAKSE 910 EDYLVMIIVR GAS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
CCDS	CCDS59198.1. [Q96T37-3] CCDS822.1. [Q96T37-1]
RefSeq	NP_001188474.1. NM_001201545.1. [Q96T37-3] NP_073605.4. NM_022768.4. [Q96T37-1]
UniGene	Hs.435947. Hs.708172.
3D structure databases
ProteinModelPortal	Q96T37.
SMR	Q96T37. Positions 374-529, 783-943.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	122293. 22 interactions.
IntAct	Q96T37. 6 interactions.
MINT	MINT-4131981.
PTM databases
PhosphoSite	Q96T37.
Polymorphism databases
DMDM	32363506.
Proteomic databases
MaxQB	Q96T37.
PaxDb	Q96T37.
PRIDE	Q96T37.
Protocols and materials databases
DNASU	64783.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369784; ENSP00000358799; ENSG00000162775. [Q96T37-1] ENST00000487146; ENSP00000473552; ENSG00000162775. [Q96T37-3] ENST00000602849; ENSP00000473638; ENSG00000162775. [Q96T37-2]
GeneID	64783.
KEGG	hsa:64783.
UCSC	uc001dzl.1. human. [Q96T37-1] uc001dzm.1. human. [Q96T37-3] uc021orn.1. human. [Q96T37-2]
Organism-specific databases
CTD	64783.
GeneCards	GC01P110882.
HGNC	HGNC:14959. RBM15.
HPA	CAB015201. HPA019824. HPA049642.
MIM	606077. gene.
neXtProt	NX_Q96T37.
PharmGKB	PA34264.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG250829.
HOVERGEN	HBG058366.
InParanoid	Q96T37.
KO	K13190.
OMA	VMIIVRV.
OrthoDB	EOG7QZG9W.
PhylomeDB	Q96T37.
TreeFam	TF315637.
Gene expression databases
ArrayExpress	Q96T37.
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. SSF100939. 1 hit.
PROSITE	PS50102. RRM. 3 hits. PS50917. SPOC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RBM15. human.
GeneWiki	RBM15.
GenomeRNAi	64783.
NextBio	35460349.
PRO	Q96T37.
SOURCE	Search...

Entry information

Entry name

RBM15_HUMAN

Accession

Primary (citable) accession number: Q96T37
Secondary accession number(s): A1A693 , 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 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.