Full text data of RBMXL1
RBMXL1
[Confidence: low (only semi-automatic identification from reviews)]
RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RNA binding motif protein, X-linked-like-1 (Heterogeneous nuclear ribonucleoprotein G-like 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96E39
ID RMXL1_HUMAN Reviewed; 390 AA.
AC Q96E39;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=RNA binding motif protein, X-linked-like-1;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G-like 1;
GN Name=RBMXL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP RETROGENE.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-161, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: RNA-binding protein which may be involved in pre-mRNA
CC splicing (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- MISCELLANEOUS: According to some authors, RBMXL1 is a RBMX
CC retrogene on chromosome X which is likely to be functional
CC (PubMed:16201836).
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- CAUTION: The first non-coding exon of RBMXL1 is in common with
CC that of CCBL2.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL832554; CAI46148.1; -; mRNA.
DR EMBL; AL139416; CAI21693.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73155.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73156.1; -; Genomic_DNA.
DR EMBL; BC012942; AAH12942.1; -; mRNA.
DR RefSeq; NP_001156008.1; NM_001162536.2.
DR RefSeq; NP_062556.2; NM_019610.5.
DR UniGene; Hs.481898; -.
DR ProteinModelPortal; Q96E39; -.
DR SMR; Q96E39; 1-105.
DR IntAct; Q96E39; 1.
DR MINT; MINT-4992845; -.
DR PhosphoSite; Q96E39; -.
DR PaxDb; Q96E39; -.
DR PRIDE; Q96E39; -.
DR Ensembl; ENST00000321792; ENSP00000318415; ENSG00000213516.
DR Ensembl; ENST00000399794; ENSP00000446099; ENSG00000213516.
DR GeneID; 494115; -.
DR KEGG; hsa:494115; -.
DR UCSC; uc001dms.3; human.
DR CTD; 494115; -.
DR GeneCards; GC01M089446; -.
DR HGNC; HGNC:25073; RBMXL1.
DR neXtProt; NX_Q96E39; -.
DR PharmGKB; PA165752300; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000276235; -.
DR HOVERGEN; HBG063314; -.
DR KO; K12885; -.
DR OMA; YSANGGH; -.
DR OrthoDB; EOG780RPD; -.
DR PhylomeDB; Q96E39; -.
DR GenomeRNAi; 494115; -.
DR NextBio; 255993; -.
DR PRO; PR:Q96E39; -.
DR ArrayExpress; Q96E39; -.
DR Bgee; Q96E39; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Complete proteome; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding.
FT CHAIN 1 390 RNA binding motif protein, X-linked-like-
FT 1.
FT /FTId=PRO_0000408005.
FT DOMAIN 8 86 RRM.
FT COMPBIAS 273 367 Ser-rich.
FT MOD_RES 88 88 Phosphoserine.
FT MOD_RES 161 161 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine (By similarity).
SQ SEQUENCE 390 AA; 42142 MW; E8D74676C3AE6420 CRC64;
MVEADRPGKL FIGGLNTETN EKALETVFGK YGRIVEVLLI KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE RGRHGPPPPP RSRGPPRGFG AGRGGSGGTR
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP SPKRSAPSGL VRSSSGMGGR
APLSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY GDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPLTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSCDR VGRQERGLPP SVERGYPSSR
DSYSSSSRGA PRGAGPGGSR SDRGGGRSRY
//
ID RMXL1_HUMAN Reviewed; 390 AA.
AC Q96E39;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=RNA binding motif protein, X-linked-like-1;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G-like 1;
GN Name=RBMXL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP RETROGENE.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-161, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: RNA-binding protein which may be involved in pre-mRNA
CC splicing (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- MISCELLANEOUS: According to some authors, RBMXL1 is a RBMX
CC retrogene on chromosome X which is likely to be functional
CC (PubMed:16201836).
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- CAUTION: The first non-coding exon of RBMXL1 is in common with
CC that of CCBL2.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL832554; CAI46148.1; -; mRNA.
DR EMBL; AL139416; CAI21693.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73155.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73156.1; -; Genomic_DNA.
DR EMBL; BC012942; AAH12942.1; -; mRNA.
DR RefSeq; NP_001156008.1; NM_001162536.2.
DR RefSeq; NP_062556.2; NM_019610.5.
DR UniGene; Hs.481898; -.
DR ProteinModelPortal; Q96E39; -.
DR SMR; Q96E39; 1-105.
DR IntAct; Q96E39; 1.
DR MINT; MINT-4992845; -.
DR PhosphoSite; Q96E39; -.
DR PaxDb; Q96E39; -.
DR PRIDE; Q96E39; -.
DR Ensembl; ENST00000321792; ENSP00000318415; ENSG00000213516.
DR Ensembl; ENST00000399794; ENSP00000446099; ENSG00000213516.
DR GeneID; 494115; -.
DR KEGG; hsa:494115; -.
DR UCSC; uc001dms.3; human.
DR CTD; 494115; -.
DR GeneCards; GC01M089446; -.
DR HGNC; HGNC:25073; RBMXL1.
DR neXtProt; NX_Q96E39; -.
DR PharmGKB; PA165752300; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000276235; -.
DR HOVERGEN; HBG063314; -.
DR KO; K12885; -.
DR OMA; YSANGGH; -.
DR OrthoDB; EOG780RPD; -.
DR PhylomeDB; Q96E39; -.
DR GenomeRNAi; 494115; -.
DR NextBio; 255993; -.
DR PRO; PR:Q96E39; -.
DR ArrayExpress; Q96E39; -.
DR Bgee; Q96E39; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Complete proteome; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding.
FT CHAIN 1 390 RNA binding motif protein, X-linked-like-
FT 1.
FT /FTId=PRO_0000408005.
FT DOMAIN 8 86 RRM.
FT COMPBIAS 273 367 Ser-rich.
FT MOD_RES 88 88 Phosphoserine.
FT MOD_RES 161 161 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine (By similarity).
SQ SEQUENCE 390 AA; 42142 MW; E8D74676C3AE6420 CRC64;
MVEADRPGKL FIGGLNTETN EKALETVFGK YGRIVEVLLI KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE RGRHGPPPPP RSRGPPRGFG AGRGGSGGTR
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP SPKRSAPSGL VRSSSGMGGR
APLSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY GDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPLTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSCDR VGRQERGLPP SVERGYPSSR
DSYSSSSRGA PRGAGPGGSR SDRGGGRSRY
//