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Protein

RNA binding motif protein, X-linked-like-1

Gene

Rbmxl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

RNA-binding protein which may be involved in pre-mRNA splicing.By similarity

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA binding motif protein, X-linked-like-1
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein G-like 1
RNA binding motif protein, X chromosome retrogene
Cleaved into the following chain:
Gene namesi
Name:Rbmxl1
Synonyms:Rbmxrt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1343045. Rbmxl1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388RNA binding motif protein, X-linked-like-1PRO_0000408006Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 388387RNA binding motif protein, X-linked-like-1, N-terminally processedPRO_0000434382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in RNA binding motif protein, X-linked-like-1, N-terminally processedBy similarity
Modified residuei30 – 301N6-acetyllysineBy similarity
Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei88 – 881PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91VM5.
MaxQBiQ91VM5.
PaxDbiQ91VM5.
PRIDEiQ91VM5.

PTM databases

iPTMnetiQ91VM5.
PhosphoSiteiQ91VM5.

Expressioni

Gene expression databases

BgeeiQ91VM5.
GenevisibleiQ91VM5. MM.

Interactioni

Protein-protein interaction databases

BioGridi202825. 2 interactions.
IntActiQ91VM5. 4 interactions.
MINTiMINT-1868507.
STRINGi10090.ENSMUSP00000048153.

Structurei

3D structure databases

ProteinModelPortaliQ91VM5.
SMRiQ91VM5. Positions 1-95.
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

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiQ91VM5.
KOiK12885.
OMAiRDGYGAP.
OrthoDBiEOG780RPD.
TreeFamiTF331833.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q91VM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG
60 70 80 90 100
FAFVTFESPA DAKDAARDMN 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 DGYGRDRDYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS
310 320 330 340 350
YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM
360 370 380
ERGYPPPRDS YSSSSRGAPR GGGRGGSRSD RGGGRSRY
Length:388
Mass (Da):42,162
Last modified:December 1, 2001 - v1
Checksum:iF4532F545E431A59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381L → I in AAB86639 (PubMed:9457683).Curated
Sequence conflicti56 – 561F → L in AAB86639 (PubMed:9457683).Curated
Sequence conflicti88 – 881S → F in AAB86639 (PubMed:9457683).Curated
Sequence conflicti232 – 2321A → T in AAB86639 (PubMed:9457683).Curated
Sequence conflicti244 – 2441S → C in AAB86639 (PubMed:9457683).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031568 mRNA. Translation: AAB86639.1.
AK041927 mRNA. Translation: BAC31099.1.
BC011441 mRNA. Translation: AAH11441.1.
BC089350 mRNA. Translation: AAH89350.1.
CCDSiCCDS22430.1.
RefSeqiNP_001239018.1. NM_001252089.1.
NP_033059.2. NM_009033.2.
XP_006530838.1. XM_006530775.1.
XP_006530839.1. XM_006530776.1.
UniGeneiMm.24718.

Genome annotation databases

EnsembliENSMUST00000049245; ENSMUSP00000048153; ENSMUSG00000037070.
GeneIDi19656.
KEGGimmu:19656.
UCSCiuc009mhz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF031568 mRNA. Translation: AAB86639.1.
AK041927 mRNA. Translation: BAC31099.1.
BC011441 mRNA. Translation: AAH11441.1.
BC089350 mRNA. Translation: AAH89350.1.
CCDSiCCDS22430.1.
RefSeqiNP_001239018.1. NM_001252089.1.
NP_033059.2. NM_009033.2.
XP_006530838.1. XM_006530775.1.
XP_006530839.1. XM_006530776.1.
UniGeneiMm.24718.

3D structure databases

ProteinModelPortaliQ91VM5.
SMRiQ91VM5. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202825. 2 interactions.
IntActiQ91VM5. 4 interactions.
MINTiMINT-1868507.
STRINGi10090.ENSMUSP00000048153.

PTM databases

iPTMnetiQ91VM5.
PhosphoSiteiQ91VM5.

Proteomic databases

EPDiQ91VM5.
MaxQBiQ91VM5.
PaxDbiQ91VM5.
PRIDEiQ91VM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049245; ENSMUSP00000048153; ENSMUSG00000037070.
GeneIDi19656.
KEGGimmu:19656.
UCSCiuc009mhz.1. mouse.

Organism-specific databases

CTDi494115.
MGIiMGI:1343045. Rbmxl1.

Phylogenomic databases

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiQ91VM5.
KOiK12885.
OMAiRDGYGAP.
OrthoDBiEOG780RPD.
TreeFamiTF331833.

Miscellaneous databases

NextBioi296934.
PROiQ91VM5.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VM5.
GenevisibleiQ91VM5. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evolution of mammalian HNRPG and its relationship with the putative azoospermia factor RBM."
    Delbridge M.L., Ma K., Subbarao M.N., Cooke H.J., Bhasin S., Graves J.A.M.
    Mamm. Genome 9:168-170(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Thymus.
  3. "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].
    Strain: 129 and C57BL/6.
    Tissue: Brain and Mammary tumor.

Entry informationi

Entry nameiRMXL1_MOUSE
AccessioniPrimary (citable) accession number: Q91VM5
Secondary accession number(s): O35479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 118 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.