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Q8R3C6 (RBM19_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable RNA-binding protein 19
Alternative name(s):
RNA-binding motif protein 19
Gene names
Name:Rbm19
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length952 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in embryo pre-implantation development. Ref.5

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm. Cytoplasm. Chromosome. Note: Colocalizes with NPM1 during interphase. By late prophase, metaphase, anaphase and telophase, associates with the chromosome periphery. By telophase localizes to nucleolar precursor body (NPB) By similarity. In discrete foci distributed throughout the cytoplasm and nucleoplasm during the 4 to 8 cell stages and the morula stage, but not in the periphery of the NPB. During blastocyst development, becomes increasingly localized to the nucleolus and less to the cytoplasm. At the late blastocyst stage, localized predominantly in the nucleolus. Localized in the nucleolus during interphase and to the perichromosomal sheath during mitosis. Does not colocalize in the cytoplasm with GW182 in P-bodies. May translocate to the nucleolus upon early embryonic development. Ref.3 Ref.5

Tissue specificity

Expressed in the crypts of Lieberkuhn of the intestine (at protein level). Ref.3

Developmental stage

Expressed during early development. Expressed in the epithelium of the embryonic gut tube (at protein level). Ref.3

Disruption phenotype

Arrests embryonic development prior to implantation. Embryos at 3.5 dpc lack the mature, tripartite nucleoli, but instead, contain spheres resembling nucleolar precursor body (NPB), indicating arrest of nucleologenesis. Ref.5

Sequence similarities

Belongs to the RRM MRD1 family.

Contains 6 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmulticellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of embryonic development

Inferred from mutant phenotype Ref.3. Source: UniProtKB

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.3. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R3C6-1)

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: Q8R3C6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     485-521: EANAPGSSYKKKKEAMDKANSSSSHNWNTLFMGPNAV → APAALSPPQQDCWPVDRAGDSTSSSGPLPCPCDAARF
     522-952: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 952952Probable RNA-binding protein 19
PRO_0000081782

Regions

Domain2 – 7978RRM 1
Domain293 – 36876RRM 2
Domain400 – 47879RRM 3
Domain584 – 65673RRM 4
Domain722 – 80382RRM 5
Domain824 – 90481RRM 6
Compositional bias182 – 25069Asp/Glu-rich
Compositional bias389 – 3946Poly-Glu
Compositional bias671 – 71747Glu-rich

Amino acid modifications

Modified residue1771Phosphoserine By similarity
Modified residue1791Phosphoserine By similarity
Modified residue1831Phosphoserine By similarity
Modified residue6931Phosphoserine Ref.4
Modified residue9281Phosphoserine By similarity
Modified residue9441Phosphoserine Ref.6

Natural variations

Alternative sequence485 – 52137EANAP…GPNAV → APAALSPPQQDCWPVDRAGD STSSSGPLPCPCDAARF in isoform 2.
VSP_015005
Alternative sequence522 – 952431Missing in isoform 2.
VSP_015006

Secondary structure

............................................................... 952
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2002. Version 1.
Checksum: 91C45ADB66F8CDB2

FASTA952106,083
        10         20         30         40         50         60 
MSRLIVKNLP NGMKEERFRQ LFAAFGTLTD CSLKFTKDGK FRKFGFIGFK SEEEAQAALN 

        70         80         90        100        110        120 
HFHRSFIDTT RITVEFCKSF GDPSKPRAWS KHAQKSSQPK QPSQDSVPSD TKKDKKKKGP 

       130        140        150        160        170        180 
SDLEKLKEDA KFQEFLSIHQ KRTQVATWAN DALEAKLPKA KTKASSDYLN FDSDSNSDSG 

       190        200        210        220        230        240 
QESEEEPARE DPEEEQGLQP KAAVQKELSD MDYLKSKMVR AEVSSEDEDE EDSEDEAVNC 

       250        260        270        280        290        300 
EEGSEEEEEE GSPASPAKQG GVSRGAVPGV LRPQEAAGKV EKPVSQKEPT TPYTVKLRGA 

       310        320        330        340        350        360 
PFNVTEKNVI EFLAPLKPVA IRIVRNAHGN KTGYVFVDLS SEEEVKKALK CNRDYMGGRY 

       370        380        390        400        410        420 
IEVFREKQAP TARGPPKSTT PWQGRTLGEN EEEEDLADSG RLFVRNLSYT SSEEDLEKLF 

       430        440        450        460        470        480 
SAYGPLSELH YPIDSLTKKP KGFAFVTFMF PEHAVKAYAE VDGQVFQGRM LHVLPSTIKK 

       490        500        510        520        530        540 
EASQEANAPG SSYKKKKEAM DKANSSSSHN WNTLFMGPNA VADAIAQKYN ATKSQVFDHE 

       550        560        570        580        590        600 
TRGSVAVRVA LGETQLVQEV RSFLIDNGVC LDSFSQAAAE RSKTVILAKN LPAGTLAAEI 

       610        620        630        640        650        660 
QETFSRFGSL GRVLLPEGGI TAIVEFLEPL EARKAFRHLA YSKFHHVPLY LEWAPIGVFG 

       670        680        690        700        710        720 
AAPQKKDSQH EQPAEKAEVE QETVLDPEGE KASVEGAEAS TGKMEEEEEE EEEEEEESIP 

       730        740        750        760        770        780 
GCTLFIKNLN FSTTEETLKG VFSKVGAIKS CTISKKKNKA GVLLSMGFGF VEYKKPEQAQ 

       790        800        810        820        830        840 
KALKQLQGHT VDGHKLEVRI SERATKPALT STRKKQVPKK QTTSKILVRN IPFQANQREI 

       850        860        870        880        890        900 
RELFSTFGEL KTVRLPKKMT GTGAHRGFGF VDFITKQDAK KAFNALCHST HLYGRRLVLE 

       910        920        930        940        950 
WADSEVTVQT LRRKTARHFQ EPPKKKRSAV LDGILEQLED EDNSDGEQAL QL 

« Hide

Isoform 2 [UniParc].

Checksum: 83C0C09AD3AB0BB2
Show »

FASTA52157,940

References

« Hide 'large scale' references
[1]"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 1).
Strain: FVB/N.
Tissue: Colon and Mammary cancer.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 363-952 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Eye and Lung.
[3]"Rbm19 is a nucleolar protein expressed in crypt/progenitor cells of the intestinal epithelium."
Lorenzen J.A., Bonacci B.B., Palmer R.E., Wells C., Zhang J., Haber D.A., Goldstein A.M., Mayer A.N.
Gene Expr. Patterns 6:45-56(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"RBM19 is essential for preimplantation development in the mouse."
Zhang J., Tomasini A.J., Mayer A.N.
BMC Dev. Biol. 8:115-115(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Solution structure of the second RNA binding domain from hypothetical protein BAB23448."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 581-678.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC025619 mRNA. Translation: AAH25619.1.
BC034010 mRNA. Translation: AAH34010.1.
AK004657 mRNA. Translation: BAB23448.1.
AK053511 mRNA. Translation: BAC35411.1.
CCDSCCDS19616.1. [Q8R3C6-1]
RefSeqNP_083038.1. NM_028762.1. [Q8R3C6-1]
UniGeneMm.41022.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHWNMR-A399-484[»]
1WHXNMR-A581-678[»]
2CPFNMR-A724-808[»]
2CPHNMR-A816-909[»]
ProteinModelPortalQ8R3C6.
SMRQ8R3C6. Positions 290-490, 583-678, 724-910.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216500. 2 interactions.
IntActQ8R3C6. 1 interaction.
MINTMINT-4118964.
STRING10090.ENSMUSP00000031590.

PTM databases

PhosphoSiteQ8R3C6.

Proteomic databases

PaxDbQ8R3C6.
PRIDEQ8R3C6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031590; ENSMUSP00000031590; ENSMUSG00000029594. [Q8R3C6-1]
GeneID74111.
KEGGmmu:74111.
UCSCuc008zha.1. mouse. [Q8R3C6-1]

Organism-specific databases

CTD9904.
MGIMGI:1921361. Rbm19.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00700000104575.
HOGENOMHOG000211156.
HOVERGENHBG055637.
InParanoidQ8R3C6.
KOK14787.
OMAQRERGNT.
OrthoDBEOG7K0ZBH.
PhylomeDBQ8R3C6.
TreeFamTF105725.

Gene expression databases

BgeeQ8R3C6.
CleanExMM_RBM19.
GenevestigatorQ8R3C6.

Family and domain databases

Gene3D3.30.70.330. 6 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 4 hits.
[Graphical view]
SMARTSM00360. RRM. 6 hits.
[Graphical view]
PROSITEPS50102. RRM. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM19. mouse.
EvolutionaryTraceQ8R3C6.
NextBio339804.
PROQ8R3C6.
SOURCESearch...

Entry information

Entry nameRBM19_MOUSE
AccessionPrimary (citable) accession number: Q8R3C6
Secondary accession number(s): Q8BHR0, Q9CW63
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot