GRSF1_HUMAN
ID GRSF1_HUMAN Reviewed; 480 AA.
AC Q12849; B3KPW0; Q4W5S5; Q6ZST3; Q8IWD6; Q8NBD2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=G-rich sequence factor 1;
DE Short=GRSF-1;
DE Flags: Precursor;
GN Name=GRSF1;
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 [MRNA] (ISOFORM 1).
RX PubMed=8036161; DOI=10.1093/nar/22.12.2334;
RA Qian Z., Wilusz J.;
RT "GRSF-1: a poly(A)+ mRNA binding protein which interacts with a conserved
RT G-rich element.";
RL Nucleic Acids Res. 22:2334-2343(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Caudate nucleus, Cerebellum, Prostate, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-277.
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 177-188; 243-253 AND 318-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=23473033; DOI=10.1016/j.cmet.2013.02.006;
RA Antonicka H., Sasarman F., Nishimura T., Paupe V., Shoubridge E.A.;
RT "The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and
RT is required for posttranscriptional mitochondrial gene expression.";
RL Cell Metab. 17:386-398(2013).
RN [13]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND
RP INTERACTION WITH TRMT10C.
RX PubMed=23473034; DOI=10.1016/j.cmet.2013.02.005;
RA Jourdain A.A., Koppen M., Wydro M., Rodley C.D., Lightowlers R.N.,
RA Chrzanowska-Lightowlers Z.M., Martinou J.C.;
RT "GRSF1 regulates RNA processing in mitochondrial RNA granules.";
RL Cell Metab. 17:399-410(2013).
RN [14]
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 [15]
RP IDENTIFICATION IN A COMPLEX WITH DDX28; DHX30; FASTKD2 AND FASTKD5,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25683715; DOI=10.1016/j.celrep.2015.01.030;
RA Antonicka H., Shoubridge E.A.;
RT "Mitochondrial RNA granules are centers for post-transcriptional RNA
RT processing and ribosome biogenesis.";
RL Cell Rep. 10:920-932(2015).
RN [16]
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).
RN [17]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH PNPT1 AND
RP SUPV3L1, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP GLN-155; TRP-159; GLU-223; ARG-255; TYR-259; GLU-320; ARG-406; PHE-410 AND
RP GLU-470.
RX PubMed=29967381; DOI=10.1038/s41467-018-05007-9;
RA Pietras Z., Wojcik M.A., Borowski L.S., Szewczyk M., Kulinski T.M.,
RA Cysewski D., Stepien P.P., Dziembowski A., Szczesny R.J.;
RT "Dedicated surveillance mechanism controls G-quadruplex forming non-coding
RT RNAs in human mitochondria.";
RL Nat. Commun. 9:2558-2558(2018).
RN [18] {ECO:0007744|PDB:2LMI}
RP STRUCTURE BY NMR OF 140-245.
RA Dutta S.K., Serrano P., Geralt M., Wuthrich K.;
RT "NMR structure of the human RNA binding protein BC040485.";
RL Submitted (DEC-2011) to the PDB data bank.
RN [19] {ECO:0007744|PDB:4QU6, ECO:0007744|PDB:4QU7}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 140-245 IN COMPLEX WITH RNA.
RG Joint Center for Structural Genomics (JCSG), Partnership for T-Cell Biology (TCELL);
RT "Crystal structure of a G-rich RNA sequence binding factor 1 (GRSF1) from
RT Homo sapiens at 1.75 A resolution.";
RL Submitted (JUL-2014) to the PDB data bank.
CC -!- FUNCTION: Regulator of post-transcriptional mitochondrial gene
CC expression, required for assembly of the mitochondrial ribosome and for
CC recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-
CC rich element. Preferentially binds RNAs transcribed from three
CC contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the
CC long non-coding RNAs for MT-CYB and MT-ND5, each of which contains
CC multiple consensus binding sequences (PubMed:23473033, PubMed:23473034,
CC PubMed:29967381). Involved in the degradosome-mediated decay of non-
CC coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules
CC (PubMed:29967381). Acts by unwinding G-quadruplex RNA structures in MT-
CC ncRNA, thus facilitating their degradation by the degradosome
CC (PubMed:29967381). G-quadruplexes (G4) are non-canonical 4 stranded
CC structures formed by transcripts from the light strand of mtDNA
CC (PubMed:29967381). {ECO:0000269|PubMed:23473033,
CC ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:29967381}.
CC -!- SUBUNIT: Monomer. Found in a complex with DDX28, DHX30, FASTKD2 and
CC FASTKD5 (PubMed:25683715). Interacts with the mitochondrial RNase P
CC complex subunit TRMT10C/MRPP1 (PubMed:23473034). Interacts with the 2
CC components of the mitochondrial degradosome complex, PNPT1 and SUPV3L1,
CC in an RNA-dependent manner (PubMed:29967381).
CC {ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:25683715,
CC ECO:0000269|PubMed:29967381}.
CC -!- INTERACTION:
CC Q12849; O75832: PSMD10; NbExp=4; IntAct=EBI-1054150, EBI-752185;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix
CC {ECO:0000269|PubMed:23473033, ECO:0000269|PubMed:23473034,
CC ECO:0000269|PubMed:25683715, ECO:0000269|PubMed:29967381}.
CC Note=Localizes to mitochondrial RNA granules found in close proximity
CC to the mitochondrial nucleoids. {ECO:0000269|PubMed:23473033,
CC ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:25683715}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:23473034}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12849-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12849-5; Sequence=VSP_043118;
CC -!- DOMAIN: The RRM domains mediate RNA-binding.
CC {ECO:0000269|PubMed:29967381}.
CC -!- MISCELLANEOUS: Depletion of GRSF1 by siRNA results in a combined OXPHOS
CC assembly defect, with the prominent loss of complexes I, III, IV, and
CC V. It also leads to altered steady-state levels of mitochondrial rRNAs
CC and mRNAs.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC95399.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=AAH40485.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAY40942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC03513.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAC86863.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=EAX05634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U07231; AAC95399.1; ALT_SEQ; mRNA.
DR EMBL; AK056891; BAG51822.1; -; mRNA.
DR EMBL; AK090755; BAC03513.1; ALT_SEQ; mRNA.
DR EMBL; AK094806; BAG52934.1; -; mRNA.
DR EMBL; AK095799; BAG53131.1; -; mRNA.
DR EMBL; AK097055; BAG53414.1; -; mRNA.
DR EMBL; AK127161; BAC86863.1; ALT_SEQ; mRNA.
DR EMBL; AC021989; AAY40942.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471057; EAX05631.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC040485; AAH40485.1; ALT_SEQ; mRNA.
DR CCDS; CCDS47069.1; -. [Q12849-1]
DR CCDS; CCDS47070.1; -. [Q12849-5]
DR PIR; S48081; S48081.
DR RefSeq; NP_001091947.1; NM_001098477.1. [Q12849-5]
DR RefSeq; NP_002083.3; NM_002092.3. [Q12849-1]
DR RefSeq; XP_011530199.1; XM_011531897.2. [Q12849-5]
DR PDB; 2LMI; NMR; -; A=140-245.
DR PDB; 4QU6; X-ray; 1.75 A; A=140-245.
DR PDB; 4QU7; X-ray; 2.50 A; A/B/C/D=400-480.
DR PDBsum; 2LMI; -.
DR PDBsum; 4QU6; -.
DR PDBsum; 4QU7; -.
DR AlphaFoldDB; Q12849; -.
DR SMR; Q12849; -.
DR BioGRID; 109182; 496.
DR CORUM; Q12849; -.
DR IntAct; Q12849; 30.
DR MINT; Q12849; -.
DR STRING; 9606.ENSP00000254799; -.
DR GlyGen; Q12849; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12849; -.
DR MetOSite; Q12849; -.
DR PhosphoSitePlus; Q12849; -.
DR SwissPalm; Q12849; -.
DR BioMuta; GRSF1; -.
DR DMDM; 215274142; -.
DR EPD; Q12849; -.
DR jPOST; Q12849; -.
DR MassIVE; Q12849; -.
DR MaxQB; Q12849; -.
DR PaxDb; Q12849; -.
DR PeptideAtlas; Q12849; -.
DR PRIDE; Q12849; -.
DR ProteomicsDB; 58982; -. [Q12849-1]
DR ProteomicsDB; 58983; -. [Q12849-5]
DR Antibodypedia; 24367; 160 antibodies from 21 providers.
DR DNASU; 2926; -.
DR Ensembl; ENST00000254799.11; ENSP00000254799.6; ENSG00000132463.15. [Q12849-1]
DR Ensembl; ENST00000502323.5; ENSP00000425430.1; ENSG00000132463.15. [Q12849-5]
DR GeneID; 2926; -.
DR KEGG; hsa:2926; -.
DR MANE-Select; ENST00000254799.11; ENSP00000254799.6; NM_002092.4; NP_002083.4.
DR UCSC; uc010iia.2; human. [Q12849-1]
DR CTD; 2926; -.
DR DisGeNET; 2926; -.
DR GeneCards; GRSF1; -.
DR HGNC; HGNC:4610; GRSF1.
DR HPA; ENSG00000132463; Tissue enhanced (skeletal).
DR MIM; 604851; gene.
DR neXtProt; NX_Q12849; -.
DR OpenTargets; ENSG00000132463; -.
DR PharmGKB; PA29003; -.
DR VEuPathDB; HostDB:ENSG00000132463; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000158529; -.
DR HOGENOM; CLU_032003_0_0_1; -.
DR InParanoid; Q12849; -.
DR OMA; DIINFFM; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; Q12849; -.
DR TreeFam; TF316157; -.
DR PathwayCommons; Q12849; -.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR SignaLink; Q12849; -.
DR SIGNOR; Q12849; -.
DR BioGRID-ORCS; 2926; 202 hits in 1091 CRISPR screens.
DR ChiTaRS; GRSF1; human.
DR GenomeRNAi; 2926; -.
DR Pharos; Q12849; Tbio.
DR PRO; PR:Q12849; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q12849; protein.
DR Bgee; ENSG00000132463; Expressed in parotid gland and 213 other tissues.
DR ExpressionAtlas; Q12849; baseline and differential.
DR Genevisible; Q12849; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0006378; P:mRNA polyadenylation; TAS:ProtInc.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd12730; RRM1_GRSF1; 1.
DR CDD; cd12505; RRM2_GRSF1; 1.
DR CDD; cd12733; RRM3_GRSF1; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034424; GRSF-1_RRM2.
DR InterPro; IPR033106; GRSF1.
DR InterPro; IPR034425; GRSF1_RRM1.
DR InterPro; IPR034426; GRSF1_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR13976:SF42; PTHR13976:SF42; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Mitochondrion; mRNA processing; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transit peptide; tRNA processing.
FT TRANSIT 1..117
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 118..480
FT /note="G-rich sequence factor 1"
FT /id="PRO_0000081597"
FT DOMAIN 122..246
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 250..326
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 401..480
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043118"
FT VARIANT 277
FT /note="D -> Y (in dbSNP:rs17854012)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047537"
FT MUTAGEN 155
FT /note="Q->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-159; A-
FT 223; A-255; A-259; A-320; A-406; A-410 and A-470."
FT MUTAGEN 159
FT /note="W->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 223; A-255; A-259; A-320; A-406; A-410 and A-470."
FT MUTAGEN 223
FT /note="E->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-255; A-259; A-320; A-406; A-410 and A-470."
FT MUTAGEN 255
FT /note="R->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-223; A-259; A-320; A-406; A-410 and A-470."
FT MUTAGEN 259
FT /note="Y->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-223; A-255; A-320; A-406; A-410 and A-470."
FT MUTAGEN 320
FT /note="E->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-223; A-255; A-259; A-406; A-410 and A-470."
FT MUTAGEN 406
FT /note="R->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-223; A-255; A-259; A-320; A-410 and A-470."
FT MUTAGEN 410
FT /note="F->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-223; A-255; A-259; A-320; A-406 and A-470."
FT MUTAGEN 470
FT /note="E->A: Impairs RNA-binding and melting of G-
FT quadruplex RNA structures; when associated with A-155; A-
FT 159; A-223; A-255; A-259; A-320; A-406 and A-410."
FT CONFLICT 264
FT /note="K -> E (in Ref. 2; BAC86863)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="DI -> VF (in Ref. 1; AAC95399)"
FT /evidence="ECO:0000305"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:4QU6"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:4QU6"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4QU6"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:4QU6"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4QU6"
FT STRAND 192..202
FT /evidence="ECO:0007829|PDB:4QU6"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:4QU6"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:4QU6"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4QU6"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:4QU6"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:4QU6"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:4QU7"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:4QU7"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:4QU7"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:4QU7"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:4QU7"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:4QU7"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:4QU7"
SQ SEQUENCE 480 AA; 53126 MW; E09EE4E70212A70F CRC64;
MAGTRWVLGA LLRGCGCNCS SCRRTGAACL PFYSAAGSIP SGVSGRRRLL LLLGAAAAAA
SQTRGLQTGP VPPGRLAGPP AVATSAAAAA AASYSALRAS LLPQSLAAAA AVPTRSYSQE
SKTTYLEDLP PPPEYELAPS KLEEEVDDVF LIRAQGLPWS CTMEDVLNFF SDCRIRNGEN
GIHFLLNRDG KRRGDALIEM ESEQDVQKAL EKHRMYMGQR YVEVYEINNE DVDALMKSLQ
VKSSPVVNDG VVRLRGLPYS CNEKDIVDFF AGLNIVDITF VMDYRGRRKT GEAYVQFEEP
EMANQALLKH REEIGNRYIE IFPSRRNEVR THVGSYKGKK IASFPTAKYI TEPEMVFEEH
EVNEDIQPMT AFESEKEIEL PKEVPEKLPE AADFGTTSSL HFVHMRGLPF QANAQDIINF
FAPLKPVRIT MEYSSSGKAT GEADVHFETH EDAVAAMLKD RSHVHHRYIE LFLNSCPKGK
