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Protein

RNA-binding protein 15

Gene

RBM15

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

Functioni

RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also 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 (PubMed:17001072, PubMed:19786495). 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 (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311).By similarity1 Publication4 Publications

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • nucleic acid binding Source: GO_Central
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processHost-virus interaction

Enzyme and pathway databases

SIGNORiQ96T37

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein 15Curated
Alternative name(s):
One-twenty two protein 11 Publication
RNA-binding motif protein 151 Publication
Gene namesi
Name:RBM151 PublicationImported
Synonyms:OTT1 Publication, OTT11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000162775.14
HGNCiHGNC:14959 RBM15
MIMi606077 gene
neXtProtiNX_Q96T37

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi574 – 578RDRDR → KDKDK: Decreased, but not abolished methylation by PRMT1. 1 Publication5
Mutagenesisi578R → K: Decreased methylation by PRMT1, leading to decreased ubiquitination by CNOT4. 1 Publication1
Mutagenesisi795K → A: Disrupts interaction with SETD1B. 1 Publication1
Mutagenesisi898K → A: Disrupts interaction with SETD1B. 1 Publication1
Mutagenesisi923F → A: Disrupts interaction with SETD1B. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei954 – 955Breakpoint for translocation to form RBM15-MKL12 Publications2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi64783
MalaCardsiRBM15
OpenTargetsiENSG00000162775
Orphaneti402023 'Megakaryoblastic acute myeloid leukemia with t(1;22)(p13;q13)'
PharmGKBiPA34264

Polymorphism and mutation databases

BioMutaiRBM15
DMDMi32363506

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000817771 – 977RNA-binding protein 15Add BLAST977

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei109PhosphoserineCombined sources1
Modified residuei179PhosphoserineCombined sources1
Modified residuei208PhosphoserineCombined sources1
Modified residuei210PhosphoserineCombined sources1
Cross-linki246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei253PhosphoserineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei266PhosphotyrosineCombined sources1
Modified residuei292PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1
Modified residuei365PhosphoserineCombined sources1
Cross-linki406Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei450N6-acetyllysineCombined sources1
Modified residuei568PhosphothreonineCombined sources1
Modified residuei578Asymmetric dimethylarginine; alternate; by PRMT11 Publication1
Modified residuei578Omega-N-methylarginine; alternate; by PRMT11 Publication1
Modified residuei622PhosphoserineCombined sources1
Modified residuei656PhosphoserineCombined sources1
Modified residuei670PhosphoserineCombined sources1
Modified residuei674PhosphoserineCombined sources1
Modified residuei700PhosphoserineCombined sources1
Modified residuei741PhosphoserineCombined sources1
Cross-linki744Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei765PhosphoserineCombined sources1
Modified residuei767PhosphoserineCombined sources1
Modified residuei781PhosphoserineCombined sources1
Modified residuei935PhosphoserineCombined sources1

Post-translational modificationi

Methylated at Arg-578 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.1 Publication
Ubiquitinated by CNOT4 following methylation at Arg-578 by PRMT1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96T37
MaxQBiQ96T37
PaxDbiQ96T37
PeptideAtlasiQ96T37
PRIDEiQ96T37
ProteomicsDBi78180
78181 [Q96T37-2]
78182 [Q96T37-3]

PTM databases

iPTMnetiQ96T37
PhosphoSitePlusiQ96T37
SwissPalmiQ96T37

Expressioni

Gene expression databases

BgeeiENSG00000162775
ExpressionAtlasiQ96T37 baseline and differential
GenevisibleiQ96T37 HS

Organism-specific databases

HPAiCAB015201
HPA019824
HPA049642

Interactioni

Subunit structurei

Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:27602518). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:27602518). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:27602518). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (PubMed:24100041). Interacts with RBPJ (By similarity). Interacts (via SPOC domain) with SETD1B (PubMed:22927943). Interacts with NXF1, the interaction is required to promote mRNA export (PubMed:17001072). Interacts with SF3B1 (PubMed:26575292).By similarity5 Publications
(Microbial infection) Interacts with Epstein-Barr virus BSFL2/BMLF1.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi122293, 49 interactors
CORUMiQ96T37
IntActiQ96T37, 21 interactors
MINTiQ96T37
STRINGi9606.ENSP00000358799

Structurei

3D structure databases

ProteinModelPortaliQ96T37
SMRiQ96T37
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini170 – 252RRM 1PROSITE-ProRule annotationAdd BLAST83
Domaini374 – 451RRM 2PROSITE-ProRule annotationAdd BLAST78
Domaini455 – 529RRM 3PROSITE-ProRule annotationAdd BLAST75
Domaini777 – 956SPOCPROSITE-ProRule annotationAdd BLAST180

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi60 – 166Gly/Ser-richAdd BLAST107
Compositional biasi616 – 732Arg-richAdd BLAST117

Sequence similaritiesi

Belongs to the RRM Spen family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0112 Eukaryota
ENOG410XSAC LUCA
GeneTreeiENSGT00530000063730
HOVERGENiHBG058366
InParanoidiQ96T37
KOiK13190
OMAiYVCFRTP
OrthoDBiEOG091G0615
PhylomeDBiQ96T37
TreeFamiTF315637

Family and domain databases

CDDicd12553 RRM1_RBM15, 1 hit
cd12555 RRM2_RBM15, 1 hit
cd12557 RRM3_RBM15, 1 hit
Gene3Di2.40.290.10, 1 hit
3.30.70.330, 3 hits
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR034470 RBM15_RRM1
IPR034472 RBM15_RRM2
IPR034473 RBM15_RRM3
IPR000504 RRM_dom
IPR016194 SPOC-like_C_dom_sf
IPR012921 SPOC_C
IPR010912 SPOC_met
PfamiView protein in Pfam
PF00076 RRM_1, 2 hits
PF07744 SPOC, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 3 hits
SUPFAMiSSF100939 SSF100939, 1 hit
SSF54928 SSF54928, 2 hits
PROSITEiView protein in PROSITE
PS50102 RRM, 3 hits
PS50917 SPOC, 1 hit

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti99H → L in AAK54722 (PubMed:11431691).Curated1
Sequence conflicti99H → L in AAK54723 (PubMed:11431691).Curated1
Sequence conflicti99H → L in AAK54724 (PubMed:11431691).Curated1
Sequence conflicti99H → L in BAB14088 (Ref. 3) Curated1
Sequence conflicti227D → N in AAI03494 (PubMed:15489334).Curated1
Sequence conflicti705R → G in AAK54722 (PubMed:11431691).Curated1
Sequence conflicti705R → G in AAK54723 (PubMed:11431691).Curated1
Sequence conflicti705R → G in AAK54724 (PubMed:11431691).Curated1
Sequence conflicti705R → G in BAB14088 (Ref. 3) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0538771 – 44Missing in isoform 4. CuratedAdd BLAST44
Alternative sequenceiVSP_005812955 – 977GFGFQ…ALTLL → AKLVEQRMKIWNSKL in isoform 3. 2 PublicationsAdd BLAST23
Alternative sequenceiVSP_005811956 – 977FGFQI…ALTLL → AS in isoform 2 and isoform 4. 1 PublicationAdd BLAST22

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 No translation available.
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
Hs.732334

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]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Chromosomal rearrangement

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 27, 2003
Last modified: July 18, 2018
This is version 173 of the entry and version 2 of the sequence. See 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

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