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Protein

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

Gene

RBMXL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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
Cleaved into the following chain:
Gene namesi
Name:RBMXL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25073. RBMXL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165752300.

Polymorphism and mutation databases

BioMutaiRBMXL1.
DMDMi74760797.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390RNA binding motif protein, X-linked-like-1PRO_0000408005Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 390389RNA binding motif protein, X-linked-like-1, N-terminally processedPRO_0000434381Add
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)Combined sources
Modified residuei88 – 881PhosphoserineCombined sources
Modified residuei161 – 1611PhosphoserineCombined sources
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96E39.
MaxQBiQ96E39.
PaxDbiQ96E39.
PRIDEiQ96E39.

PTM databases

iPTMnetiQ96E39.
PhosphoSiteiQ96E39.

Expressioni

Gene expression databases

BgeeiQ96E39.
GenevisibleiQ96E39. HS.

Organism-specific databases

HPAiHPA057707.

Interactioni

Protein-protein interaction databases

BioGridi138936. 18 interactions.
IntActiQ96E39. 10 interactions.
MINTiMINT-4992845.
STRINGi9606.ENSP00000318415.

Structurei

3D structure databases

ProteinModelPortaliQ96E39.
SMRiQ96E39. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi273 – 36795Ser-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiQ96E39.
KOiK12885.
OMAiYSANGGH.
OrthoDBiEOG780RPD.
PhylomeDBiQ96E39.
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.

Q96E39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEADRPGKL FIGGLNTETN EKALETVFGK YGRIVEVLLI KDRETNKSRG
60 70 80 90 100
FAFVTFESPA DAKDAARDMN GKSLDGKAIK VEQATKPSFE RGRHGPPPPP
110 120 130 140 150
RSRGPPRGFG AGRGGSGGTR GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK
160 170 180 190 200
RGPPPRSGGP SPKRSAPSGL VRSSSGMGGR APLSRGRDSY GGPPRREPLP
210 220 230 240 250
SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD YTYRDYGHSS
260 270 280 290 300
SRDDYPSRGY GDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPLTRGP
310 320 330 340 350
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSCDR VGRQERGLPP
360 370 380 390
SVERGYPSSR DSYSSSSRGA PRGAGPGGSR SDRGGGRSRY
Length:390
Mass (Da):42,142
Last modified:December 1, 2001 - v1
Checksum:iE8D74676C3AE6420
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832554 mRNA. Translation: CAI46148.1.
AL139416 Genomic DNA. Translation: CAI21693.1.
CH471097 Genomic DNA. Translation: EAW73155.1.
CH471097 Genomic DNA. Translation: EAW73156.1.
BC012942 mRNA. Translation: AAH12942.1.
CCDSiCCDS716.1.
RefSeqiNP_001156008.1. NM_001162536.2.
NP_062556.2. NM_019610.5.
UniGeneiHs.481898.

Genome annotation databases

EnsembliENST00000321792; ENSP00000318415; ENSG00000213516.
ENST00000399794; ENSP00000446099; ENSG00000213516.
GeneIDi494115.
KEGGihsa:494115.
UCSCiuc001dms.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832554 mRNA. Translation: CAI46148.1.
AL139416 Genomic DNA. Translation: CAI21693.1.
CH471097 Genomic DNA. Translation: EAW73155.1.
CH471097 Genomic DNA. Translation: EAW73156.1.
BC012942 mRNA. Translation: AAH12942.1.
CCDSiCCDS716.1.
RefSeqiNP_001156008.1. NM_001162536.2.
NP_062556.2. NM_019610.5.
UniGeneiHs.481898.

3D structure databases

ProteinModelPortaliQ96E39.
SMRiQ96E39. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi138936. 18 interactions.
IntActiQ96E39. 10 interactions.
MINTiMINT-4992845.
STRINGi9606.ENSP00000318415.

PTM databases

iPTMnetiQ96E39.
PhosphoSiteiQ96E39.

Polymorphism and mutation databases

BioMutaiRBMXL1.
DMDMi74760797.

Proteomic databases

EPDiQ96E39.
MaxQBiQ96E39.
PaxDbiQ96E39.
PRIDEiQ96E39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321792; ENSP00000318415; ENSG00000213516.
ENST00000399794; ENSP00000446099; ENSG00000213516.
GeneIDi494115.
KEGGihsa:494115.
UCSCiuc001dms.4. human.

Organism-specific databases

CTDi494115.
GeneCardsiRBMXL1.
HGNCiHGNC:25073. RBMXL1.
HPAiHPA057707.
neXtProtiNX_Q96E39.
PharmGKBiPA165752300.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHG3. Eukaryota.
ENOG4111GI6. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276235.
HOVERGENiHBG063314.
InParanoidiQ96E39.
KOiK12885.
OMAiYSANGGH.
OrthoDBiEOG780RPD.
PhylomeDBiQ96E39.
TreeFamiTF331833.

Miscellaneous databases

GenomeRNAii494115.
NextBioi255993.
PROiQ96E39.

Gene expression databases

BgeeiQ96E39.
GenevisibleiQ96E39. HS.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Eye.
  5. "Emergence of young human genes after a burst of retroposition in primates."
    Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.
    PLoS Biol. 3:E357-E357(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETROGENE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRMXL1_HUMAN
AccessioniPrimary (citable) accession number: Q96E39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 129 of the entry and version 1 of the sequence. [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

Miscellaneous

According to some authors, RBMXL1 is a RBMX retrogene on chromosome X which is likely to be functional.1 Publication

Caution

The first non-coding exon of RBMXL1 is in common with that of CCBL2.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  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.