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Protein

RNA-binding motif protein, X chromosome retrogene-like

Gene

Rbmxrtl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following chain:
Gene namesi
Name:Rbmxrtl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306751. Rbmxrtl.

Subcellular locationi

  • Nucleus By similarity

  • Note: Component of ribonucleosomes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388RNA-binding motif protein, X chromosome retrogene-likePRO_0000081856Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 388387RNA-binding motif protein, X chromosome retrogene-like, N-terminally processedPRO_0000414744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in RNA binding motif protein, X-linked-like-1; alternateBy similarity
Modified residuei2 – 21N-acetylvaline; in RNA binding motif protein, X-linked-like-1, N-terminally processedBy similarity
Modified residuei30 – 301N6-acetyllysineBy similarity
Modified residuei88 – 881PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP84586.
PRIDEiP84586.

PTM databases

PhosphoSiteiP84586.

Expressioni

Gene expression databases

GenevisibleiP84586. RN.

Interactioni

Protein-protein interaction databases

BioGridi258804. 1 interaction.
STRINGi10116.ENSRNOP00000057432.

Structurei

3D structure databases

ProteinModelPortaliP84586.
SMRiP84586. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 8679RRMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiP84586.
KOiK12885.
PhylomeDBiP84586.
TreeFamiTF331833.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P84586-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG
60 70 80 90 100
FAFVTFESPA DAKDVARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP
110 120 130 140 150
RSRGPPRGLR GGSGGTRGPP SRGGYMDDGG YSMNFNMSSS RGPLPVKRGP
160 170 180 190 200
PPRSGGPPPK RSTPSGPVRS SSGMGGRTPV SRGRDSYGGP PRREPLPSRR
210 220 230 240 250
DVYLSPRDDG YSTKDSYSSR DYPSSRDTRD YAPPPRDYTY RDYSHSSSRD
260 270 280 290 300
DYPSRGYGDR DGYGRDREYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS
310 320 330 340 350
YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM
360 370 380
ERGYPPPRDS YSSSSRGAPR GGGRGGSRSD RGGGRSRY
Length:388
Mass (Da):42,204
Last modified:July 19, 2005 - v1
Checksum:iAFE8746592E44CF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03113401 Genomic DNA. No translation available.
RefSeqiNP_001100890.1. NM_001107420.1.
UniGeneiRn.19966.

Genome annotation databases

GeneIDi307779.
KEGGirno:307779.
UCSCiRGD:1306751. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03113401 Genomic DNA. No translation available.
RefSeqiNP_001100890.1. NM_001107420.1.
UniGeneiRn.19966.

3D structure databases

ProteinModelPortaliP84586.
SMRiP84586. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi258804. 1 interaction.
STRINGi10116.ENSRNOP00000057432.

PTM databases

PhosphoSiteiP84586.

Proteomic databases

PaxDbiP84586.
PRIDEiP84586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi307779.
KEGGirno:307779.
UCSCiRGD:1306751. rat.

Organism-specific databases

CTDi307779.
RGDi1306751. Rbmxrtl.

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiP84586.
KOiK12885.
PhylomeDBiP84586.
TreeFamiTF331833.

Miscellaneous databases

NextBioi657858.
PROiP84586.

Gene expression databases

GenevisibleiP84586. RN.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiRMXRL_RAT
AccessioniPrimary (citable) accession number: P84586
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 22, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.