SLIRP_HUMAN
ID SLIRP_HUMAN Reviewed; 109 AA.
AC Q9GZT3; J3KMY7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=SRA stem-loop-interacting RNA-binding protein, mitochondrial;
DE Flags: Precursor;
GN Name=SLIRP; Synonyms=C14orf156; ORFNames=DC23, DC50, PD04872;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), FUNCTION, RNA-BINDING,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-7;
RP 13-ARG-ARG-14; 24-ARG-ARG-25 AND LEU-62.
RX PubMed=16762838; DOI=10.1016/j.molcel.2006.05.024;
RA Hatchell E.C., Colley S.M., Beveridge D.J., Epis M.R., Stuart L.M.,
RA Giles K.M., Redfern A.D., Miles L.E.C., Barker A., Macdonald L.M.,
RA Arthur P.G., Lui J.C.K., Golding J.L., McCulloch R.K., Metcalf C.B.,
RA Wilce J.A., Wilce M.C., Lanz R.B., O'malley B.W., Leedman P.J.;
RT "SLIRP, a small SRA binding protein, is a nuclear receptor corepressor.";
RL Mol. Cell 22:657-668(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Lanfranchi G.;
RT "Study of 100 skeletal muscle full length mRNA.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Prostate;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: RNA-binding protein that acts as a nuclear receptor
CC corepressor. Probably acts by binding the SRA RNA, and repressing the
CC SRA-mediated nuclear receptor coactivation. Binds the STR7 loop of SRA
CC RNA. Also able to repress glucocorticoid (GR), androgen (AR), thyroid
CC (TR) and VDR-mediated transactivation. {ECO:0000269|PubMed:16762838}.
CC -!- INTERACTION:
CC Q9GZT3; A2BDD9: AMOT; NbExp=3; IntAct=EBI-1050793, EBI-17286414;
CC Q9GZT3; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-1050793, EBI-10171570;
CC Q9GZT3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1050793, EBI-5916454;
CC Q9GZT3; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1050793, EBI-3044087;
CC Q9GZT3; Q6A162: KRT40; NbExp=3; IntAct=EBI-1050793, EBI-10171697;
CC Q9GZT3; P42704: LRPPRC; NbExp=3; IntAct=EBI-1050793, EBI-1050853;
CC Q9GZT3; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1050793, EBI-742948;
CC Q9GZT3; O14561: NDUFAB1; NbExp=4; IntAct=EBI-1050793, EBI-1246261;
CC Q9GZT3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1050793, EBI-79165;
CC Q9GZT3; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-1050793, EBI-302345;
CC Q9GZT3; Q8N2I9: STK40; NbExp=3; IntAct=EBI-1050793, EBI-716112;
CC Q9GZT3; Q15007: WTAP; NbExp=4; IntAct=EBI-1050793, EBI-751647;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16762838}.
CC Nucleus {ECO:0000269|PubMed:16762838}. Note=Predominantly
CC mitochondrial. Some fraction is nuclear. In the nucleus, it is
CC recruited to nuclear receptor target promoters.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZT3-2; Sequence=VSP_047350;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest level in
CC heart, liver, skeletal muscle and testis.
CC {ECO:0000269|PubMed:16762838}.
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DR EMBL; AY860853; AAX58600.1; -; mRNA.
DR EMBL; AJ272055; CAC81241.1; -; mRNA.
DR EMBL; AF253980; AAG44629.1; -; mRNA.
DR EMBL; AF271779; AAG44790.1; -; mRNA.
DR EMBL; BC017895; AAH17895.1; -; mRNA.
DR EMBL; BU535760; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS58331.1; -. [Q9GZT3-2]
DR CCDS; CCDS9866.1; -. [Q9GZT3-1]
DR RefSeq; NP_001254792.1; NM_001267863.1. [Q9GZT3-2]
DR RefSeq; NP_001254793.1; NM_001267864.1.
DR RefSeq; NP_112487.1; NM_031210.5. [Q9GZT3-1]
DR AlphaFoldDB; Q9GZT3; -.
DR SMR; Q9GZT3; -.
DR BioGRID; 123624; 321.
DR IntAct; Q9GZT3; 53.
DR MINT; Q9GZT3; -.
DR STRING; 9606.ENSP00000450909; -.
DR GlyGen; Q9GZT3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZT3; -.
DR PhosphoSitePlus; Q9GZT3; -.
DR SwissPalm; Q9GZT3; -.
DR BioMuta; SLIRP; -.
DR DMDM; 74762723; -.
DR EPD; Q9GZT3; -.
DR jPOST; Q9GZT3; -.
DR MassIVE; Q9GZT3; -.
DR MaxQB; Q9GZT3; -.
DR PaxDb; Q9GZT3; -.
DR PeptideAtlas; Q9GZT3; -.
DR PRIDE; Q9GZT3; -.
DR ProteomicsDB; 80130; -. [Q9GZT3-1]
DR TopDownProteomics; Q9GZT3-1; -. [Q9GZT3-1]
DR Antibodypedia; 13187; 119 antibodies from 21 providers.
DR DNASU; 81892; -.
DR Ensembl; ENST00000238688.9; ENSP00000238688.5; ENSG00000119705.10. [Q9GZT3-2]
DR Ensembl; ENST00000557342.6; ENSP00000450909.1; ENSG00000119705.10. [Q9GZT3-1]
DR GeneID; 81892; -.
DR KEGG; hsa:81892; -.
DR MANE-Select; ENST00000557342.6; ENSP00000450909.1; NM_031210.6; NP_112487.1.
DR UCSC; uc001xue.7; human. [Q9GZT3-1]
DR CTD; 81892; -.
DR DisGeNET; 81892; -.
DR GeneCards; SLIRP; -.
DR HGNC; HGNC:20495; SLIRP.
DR HPA; ENSG00000119705; Low tissue specificity.
DR MIM; 610211; gene.
DR neXtProt; NX_Q9GZT3; -.
DR OpenTargets; ENSG00000119705; -.
DR PharmGKB; PA134892132; -.
DR VEuPathDB; HostDB:ENSG00000119705; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00390000008624; -.
DR InParanoid; Q9GZT3; -.
DR OMA; RNRRPFA; -.
DR OrthoDB; 481670at2759; -.
DR PhylomeDB; Q9GZT3; -.
DR TreeFam; TF319527; -.
DR PathwayCommons; Q9GZT3; -.
DR SignaLink; Q9GZT3; -.
DR BioGRID-ORCS; 81892; 76 hits in 1091 CRISPR screens.
DR ChiTaRS; SLIRP; human.
DR GenomeRNAi; 81892; -.
DR Pharos; Q9GZT3; Tbio.
DR PRO; PR:Q9GZT3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9GZT3; protein.
DR Bgee; ENSG00000119705; Expressed in mucosa of transverse colon and 204 other tissues.
DR ExpressionAtlas; Q9GZT3; baseline and differential.
DR Genevisible; Q9GZT3; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0000961; P:negative regulation of mitochondrial RNA catabolic process; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR CDD; cd12242; RRM_SLIRP; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034152; SLIRP_RRM.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..109
FT /note="SRA stem-loop-interacting RNA-binding protein,
FT mitochondrial"
FT /id="PRO_0000247051"
FT DOMAIN 19..103
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 89..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047350"
FT MUTAGEN 7
FT /note="R->A: Impairs corepressor activity; when associated
FT with 13-A-A-14."
FT /evidence="ECO:0000269|PubMed:16762838"
FT MUTAGEN 13..14
FT /note="RR->AA: Impairs corepressor activity; when
FT associated with A-7."
FT /evidence="ECO:0000269|PubMed:16762838"
FT MUTAGEN 24..25
FT /note="RR->AA: Impairs SRA-mediated repression; when
FT associated with A-62."
FT /evidence="ECO:0000269|PubMed:16762838"
FT MUTAGEN 62
FT /note="L->A: Impairs SRA-mediated repression; when
FT associated with 24-A-A-25."
FT /evidence="ECO:0000269|PubMed:16762838"
FT CONFLICT 44
FT /note="H -> R (in Ref. 5; BU535760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12349 MW; 8BDCB6EA244F17B8 CRC64;
MAASAARGAA ALRRSINQPV AFVRRIPWTA ASSQLKEHFA QFGHVRRCIL PFDKETGFHR
GLGWVQFSSE EGLRNALQQE NHIIDGVKVQ VHTRRPKLPQ TSDDEKKDF
