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P84586 (RMXRL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding motif protein, X chromosome retrogene-like
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein G retrogene-like
Short name=hnRNP G
RNA-binding motif protein, X chromosome retrogene
Gene names
Name:Rbmxrtl
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of pre-mRNAs. Associates with chromatin. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Binds non-specifically to pre-mRNAs By similarity.

Subcellular location

Nucleus By similarity. Note: Component of ribonucleosomes By similarity.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
   Cellular componentNucleus
Spliceosome
   LigandRNA-binding
   Molecular functionDevelopmental protein
Ribonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to interleukin-1

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA splice site selection

Inferred from direct assay PubMed 19282290. Source: UniProtKB

membrane protein ectodomain proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay PubMed 15009664. Source: UniProtKB

positive regulation of mRNA splicing, via spliceosome

Inferred from direct assay PubMed 19282290. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from direct assay PubMed 19282290. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from direct assay PubMed 19282290. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcatalytic step 2 spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear euchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

supraspliceosomal complex

Inferred from direct assay PubMed 19282290. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay PubMed 19282290. Source: UniProtKB

mRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388RNA-binding motif protein, X chromosome retrogene-like
PRO_0000081856
Initiator methionine11Removed; alternate By similarity
Chain2 – 388387RNA-binding motif protein, X chromosome retrogene-like, N-terminally processed
PRO_0000414744

Regions

Domain8 – 8679RRM

Amino acid modifications

Modified residue11N-acetylmethionine; in RNA binding motif protein, X-linked-like-1; alternate By similarity
Modified residue21N-acetylvaline; in RNA binding motif protein, X-linked-like-1, N-terminally processed By similarity
Modified residue2051Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P84586 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: AFE8746592E44CF4

FASTA38842,204
        10         20         30         40         50         60 
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG FAFVTFESPA 

        70         80         90        100        110        120 
DAKDVARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGSGGTRGPP 

       130        140        150        160        170        180 
SRGGYMDDGG YSMNFNMSSS RGPLPVKRGP PPRSGGPPPK RSTPSGPVRS SSGMGGRTPV 

       190        200        210        220        230        240 
SRGRDSYGGP PRREPLPSRR DVYLSPRDDG YSTKDSYSSR DYPSSRDTRD YAPPPRDYTY 

       250        260        270        280        290        300 
RDYSHSSSRD DYPSRGYGDR DGYGRDREYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS 

       310        320        330        340        350        360 
YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM ERGYPPPRDS 

       370        380 
YSSSSRGAPR GGGRGGSRSD RGGGRSRY 

« Hide

References

[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03113401 Genomic DNA. No translation available.
RefSeqNP_001100890.1. NM_001107420.1.
UniGeneRn.19966.

3D structure databases

ProteinModelPortalP84586.
SMRP84586. Positions 1-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000016184.

PTM databases

PhosphoSiteP84586.

Proteomic databases

PaxDbP84586.
PRIDEP84586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID307779.
KEGGrno:307779.
UCSCRGD:1306751. rat.

Organism-specific databases

CTD307779.
RGD1306751. Rbmxrtl.

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000276235.
HOVERGENHBG063314.
InParanoidP84586.
KOK12885.
PhylomeDBP84586.
TreeFamTF331833.

Gene expression databases

GenevestigatorP84586.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio657858.
PROP84586.

Entry information

Entry nameRMXRL_RAT
AccessionPrimary (citable) accession number: P84586
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 83 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