LRRF1_HUMAN
ID LRRF1_HUMAN Reviewed; 808 AA.
AC Q32MZ4; E9PGZ2; O75766; O75799; Q32MZ5; Q53T49; Q6PKG2; Q9Y607;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Leucine-rich repeat flightless-interacting protein 1;
DE Short=LRR FLII-interacting protein 1;
DE AltName: Full=GC-binding factor 2;
DE AltName: Full=TAR RNA-interacting protein;
GN Name=LRRFIP1; Synonyms=GCF2, TRIP;
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 3), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Ovarian carcinoma;
RX PubMed=9705290; DOI=10.1074/jbc.273.34.21594;
RA Reed A.L., Yamazaki H., Kaufman J.D., Rubinstein Y., Murphy B.A.,
RA Johnson A.C.;
RT "Molecular cloning and characterization of a transcription regulator with
RT homology to GC-binding factor.";
RL J. Biol. Chem. 273:21594-21602(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH FLII, AND DEVELOPMENTAL STAGE.
RC TISSUE=Cervix carcinoma;
RX PubMed=9671805; DOI=10.1093/nar/26.15.3460;
RA Wilson S.A., Brown E.C., Kingsman A.J., Kingsman S.M.;
RT "TRIP: a novel double stranded RNA binding protein which interacts with the
RT leucine rich repeat of flightless I.";
RL Nucleic Acids Res. 26:3460-3467(1998).
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 MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Melanoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-626 (ISOFORM 4).
RC TISSUE=Heart;
RX PubMed=10366446; DOI=10.1006/geno.1999.5817;
RA Fong K.S.K., de Couet H.G.;
RT "Novel proteins interacting with the leucine-rich repeat domain of human
RT flightless-I identified by the yeast two-hybrid system.";
RL Genomics 58:146-157(1999).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=10364563; DOI=10.1161/01.res.84.11.1258;
RA Khachigian L.M., Santiago F.S., Rafty L.A., Chan O.L.-W., Delbridge G.J.,
RA Bobik A., Collins T., Johnson A.C.;
RT "GC factor 2 represses platelet-derived growth factor A-chain gene
RT transcription and is itself induced by arterial injury.";
RL Circ. Res. 84:1258-1267(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14522076; DOI=10.1016/s0167-4781(03)00156-8;
RA Rikiyama T., Curtis J., Oikawa M., Zimonjic D.B., Popescu N., Murphy B.A.,
RA Wilson M.A., Johnson A.C.;
RT "GCF2: expression and molecular analysis of repression.";
RL Biochim. Biophys. Acta 1629:15-25(2003).
RN [8]
RP FUNCTION.
RX PubMed=16199883; DOI=10.1128/mcb.25.20.9073-9081.2005;
RA Suriano A.R., Sanford A.N., Kim N., Oh M., Kennedy S., Henderson M.J.,
RA Dietzmann K., Sullivan K.E.;
RT "GCF2/LRRFIP1 represses tumor necrosis factor alpha expression.";
RL Mol. Cell. Biol. 25:9073-9081(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-581; SER-618;
RP THR-676; SER-714 AND SER-733, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP FUNCTION, AND INTERACTION WITH FLII AND MYD88.
RX PubMed=19265123; DOI=10.4049/jimmunol.0802260;
RA Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.;
RT "Modulation of TLR signaling by multiple MyD88-interacting partners
RT including leucine-rich repeat Fli-I-interacting proteins.";
RL J. Immunol. 182:3450-3460(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-120 AND SER-618, AND
RP IDENTIFICATION BY 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-16; SER-120; SER-555; SER-581; SER-714 AND SER-766,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-116; SER-120;
RP SER-581; SER-714; SER-733; SER-766 AND SER-768, AND IDENTIFICATION BY MASS
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-606, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 162-249, DOMAIN, COILED COIL,
RP DNA-BINDING, AND SUBUNIT.
RX PubMed=23099021; DOI=10.1016/j.jsb.2012.10.006;
RA Nguyen J.B., Modis Y.;
RT "Crystal structure of the dimeric coiled-coil domain of the cytosolic
RT nucleic acid sensor LRRFIP1.";
RL J. Struct. Biol. 181:82-88(2013).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-68.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcriptional repressor which preferentially binds to the
CC GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate
CC expression of TNF, EGFR and PDGFA. May control smooth muscle cells
CC proliferation following artery injury through PDGFA repression. May
CC also bind double-stranded RNA. Positively regulates Toll-like receptor
CC (TLR) signaling in response to agonist probably by competing with the
CC negative FLII regulator for MYD88-binding.
CC {ECO:0000269|PubMed:10364563, ECO:0000269|PubMed:14522076,
CC ECO:0000269|PubMed:16199883, ECO:0000269|PubMed:19265123,
CC ECO:0000269|PubMed:9705290}.
CC -!- SUBUNIT: Homodimer. May also form higher oligomers. Interacts with
CC FLII. Interacts with MYD88. Competes with FLII for MyD88-binding, even
CC in the absence of LPS. {ECO:0000269|PubMed:19265123,
CC ECO:0000269|PubMed:23099021, ECO:0000269|PubMed:9671805}.
CC -!- INTERACTION:
CC Q32MZ4; Q13045: FLII; NbExp=2; IntAct=EBI-1369100, EBI-351549;
CC Q32MZ4; P42858: HTT; NbExp=3; IntAct=EBI-1369100, EBI-466029;
CC Q32MZ4-4; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-10240044, EBI-744115;
CC Q32MZ4-4; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-10240044, EBI-394607;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q32MZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32MZ4-2; Sequence=VSP_020265;
CC Name=3;
CC IsoId=Q32MZ4-3; Sequence=VSP_020264, VSP_020265;
CC Name=4;
CC IsoId=Q32MZ4-4; Sequence=VSP_046809, VSP_046810, VSP_046811,
CC VSP_046812, VSP_046813, VSP_046814;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9671805, ECO:0000269|PubMed:9705290}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in fetal tissues.
CC {ECO:0000269|PubMed:9671805}.
CC -!- DOMAIN: The DNA-binding domain is intrinsically unstructured.
CC {ECO:0000269|PubMed:23099021}.
CC -!- DOMAIN: The coiled coil mediates dimerization.
CC {ECO:0000269|PubMed:23099021}.
CC -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01385.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAY14672.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U69609; AAC32037.1; -; mRNA.
DR EMBL; AJ223075; CAA11076.1; -; mRNA.
DR EMBL; AC012076; AAY14672.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC096574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001385; AAH01385.1; ALT_SEQ; mRNA.
DR EMBL; BC108913; AAI08914.1; -; mRNA.
DR EMBL; BC108914; AAI08915.1; -; mRNA.
DR EMBL; AF115510; AAD41258.1; -; mRNA.
DR CCDS; CCDS2521.1; -. [Q32MZ4-2]
DR CCDS; CCDS46551.1; -. [Q32MZ4-4]
DR CCDS; CCDS46552.1; -. [Q32MZ4-1]
DR CCDS; CCDS46553.1; -. [Q32MZ4-3]
DR RefSeq; NP_001131022.1; NM_001137550.1. [Q32MZ4-4]
DR RefSeq; NP_001131024.1; NM_001137552.1. [Q32MZ4-1]
DR RefSeq; NP_001131025.1; NM_001137553.1. [Q32MZ4-3]
DR RefSeq; NP_004726.2; NM_004735.3. [Q32MZ4-2]
DR PDB; 4H22; X-ray; 2.89 A; A/B/C/D=162-249.
DR PDBsum; 4H22; -.
DR AlphaFoldDB; Q32MZ4; -.
DR SMR; Q32MZ4; -.
DR BioGRID; 114642; 69.
DR IntAct; Q32MZ4; 37.
DR MINT; Q32MZ4; -.
DR STRING; 9606.ENSP00000375857; -.
DR ChEMBL; CHEMBL4295838; -.
DR GlyGen; Q32MZ4; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q32MZ4; -.
DR MetOSite; Q32MZ4; -.
DR PhosphoSitePlus; Q32MZ4; -.
DR SwissPalm; Q32MZ4; -.
DR BioMuta; LRRFIP1; -.
DR DMDM; 114149995; -.
DR EPD; Q32MZ4; -.
DR jPOST; Q32MZ4; -.
DR MassIVE; Q32MZ4; -.
DR MaxQB; Q32MZ4; -.
DR PaxDb; Q32MZ4; -.
DR PeptideAtlas; Q32MZ4; -.
DR PRIDE; Q32MZ4; -.
DR ProteomicsDB; 20424; -.
DR ProteomicsDB; 61609; -. [Q32MZ4-1]
DR ProteomicsDB; 61610; -. [Q32MZ4-2]
DR ProteomicsDB; 61611; -. [Q32MZ4-3]
DR Antibodypedia; 1000; 349 antibodies from 31 providers.
DR DNASU; 9208; -.
DR Ensembl; ENST00000244815.9; ENSP00000244815.5; ENSG00000124831.19. [Q32MZ4-2]
DR Ensembl; ENST00000289175.10; ENSP00000289175.6; ENSG00000124831.19. [Q32MZ4-3]
DR Ensembl; ENST00000308482.14; ENSP00000310109.9; ENSG00000124831.19. [Q32MZ4-4]
DR Ensembl; ENST00000392000.4; ENSP00000375857.4; ENSG00000124831.19. [Q32MZ4-1]
DR GeneID; 9208; -.
DR KEGG; hsa:9208; -.
DR MANE-Select; ENST00000308482.14; ENSP00000310109.9; NM_001137550.2; NP_001131022.1. [Q32MZ4-4]
DR UCSC; uc002vxc.4; human. [Q32MZ4-1]
DR CTD; 9208; -.
DR DisGeNET; 9208; -.
DR GeneCards; LRRFIP1; -.
DR HGNC; HGNC:6702; LRRFIP1.
DR HPA; ENSG00000124831; Low tissue specificity.
DR MIM; 603256; gene.
DR neXtProt; NX_Q32MZ4; -.
DR OpenTargets; ENSG00000124831; -.
DR PharmGKB; PA30465; -.
DR VEuPathDB; HostDB:ENSG00000124831; -.
DR eggNOG; KOG2010; Eukaryota.
DR GeneTree; ENSGT00530000063564; -.
DR HOGENOM; CLU_018871_2_1_1; -.
DR InParanoid; Q32MZ4; -.
DR OMA; WPNTERE; -.
DR OrthoDB; 1434475at2759; -.
DR PhylomeDB; Q32MZ4; -.
DR TreeFam; TF314109; -.
DR PathwayCommons; Q32MZ4; -.
DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
DR Reactome; R-HSA-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR SignaLink; Q32MZ4; -.
DR SIGNOR; Q32MZ4; -.
DR BioGRID-ORCS; 9208; 15 hits in 1082 CRISPR screens.
DR ChiTaRS; LRRFIP1; human.
DR GeneWiki; LRRFIP1; -.
DR GenomeRNAi; 9208; -.
DR Pharos; Q32MZ4; Tbio.
DR PRO; PR:Q32MZ4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q32MZ4; protein.
DR Bgee; ENSG00000124831; Expressed in renal medulla and 211 other tissues.
DR ExpressionAtlas; Q32MZ4; baseline and differential.
DR Genevisible; Q32MZ4; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003725; F:double-stranded RNA binding; TAS:ProtInc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR IDEAL; IID00479; -.
DR InterPro; IPR019139; LRRFIP1/2.
DR PANTHER; PTHR19212; PTHR19212; 3.
DR Pfam; PF09738; LRRFIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT CHAIN 2..808
FT /note="Leucine-rich repeat flightless-interacting protein
FT 1"
FT /id="PRO_0000248392"
FT REGION 41..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..584
FT /note="DNA-binding"
FT COILED 128..250
FT /evidence="ECO:0000269|PubMed:23099021"
FT COMPBIAS 41..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..680
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ39"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ39"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ39"
FT MOD_RES 676
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 606
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..22
FT /note="MTSPAAAQSREIDCLSPEAQKL -> MDMGTQGSGRKRLPNRERLTAEDDAL
FT NQIARE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366446"
FT /id="VSP_046809"
FT VAR_SEQ 51
FT /note="E -> EIYQVQKKYYGLDTKWGDIEQWM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366446"
FT /id="VSP_046810"
FT VAR_SEQ 52..83
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9705290"
FT /id="VSP_020264"
FT VAR_SEQ 83
FT /note="R -> RSQPDLEYGGPYAWTNGYDGELYGSQSLNRRSGRPSCLYSAARPSGS
FT YRASVLDEGSFGGTRRGSTSGSRAPSEYSGHLNSSSRASSRASSARASPV (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366446"
FT /id="VSP_046811"
FT VAR_SEQ 137..160
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9671805, ECO:0000303|PubMed:9705290"
FT /id="VSP_020265"
FT VAR_SEQ 249
FT /note="E -> EEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSE
FT RDDLREEVVMLKEELK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366446"
FT /id="VSP_046812"
FT VAR_SEQ 297..450
FT /note="GRASEVEVKNEIVANVGKREILHNTEKEQHTEDTVKDCVDIEVFPAGENTED
FT QKSSEDTAPFLGTLAGATYEEQVQSQILESSSLPENTVQVESNEVMGAPDDRTRTPLEP
FT SNCWSDLDGGNHTENVGEAAVTQVEEQAGTVASCPLGHSDDTV -> DIRLKKLVDERE
FT CLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLA
FT KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE
FT VSNGHLVKRLEKMKANRSALLSQQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366446"
FT /id="VSP_046813"
FT VAR_SEQ 451..808
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366446"
FT /id="VSP_046814"
FT VARIANT 68
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036037"
FT VARIANT 275
FT /note="Q -> R (in dbSNP:rs3213869)"
FT /id="VAR_027291"
FT VARIANT 418
FT /note="N -> S (in dbSNP:rs2001301)"
FT /id="VAR_027292"
FT VARIANT 609
FT /note="E -> K (in dbSNP:rs761312145)"
FT /id="VAR_027293"
FT VARIANT 633
FT /note="K -> E (in dbSNP:rs3739041)"
FT /id="VAR_056111"
FT VARIANT 645
FT /note="P -> L (in dbSNP:rs3739040)"
FT /id="VAR_027294"
FT VARIANT 779
FT /note="R -> G (in dbSNP:rs3739039)"
FT /id="VAR_027295"
FT VARIANT 783
FT /note="H -> D (in dbSNP:rs3739038)"
FT /id="VAR_027296"
FT CONFLICT 17
FT /note="P -> L (in Ref. 1; AAC32037)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="R -> W (in Ref. 1; AAC32037)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="I -> F (in Ref. 2; CAA11076)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="T -> A (in Ref. 1; AAC32037)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="L -> F (in Ref. 4; AAI08915)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="T -> P (in Ref. 1; AAC32037)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="V -> A (in Ref. 1; AAC32037)"
FT /evidence="ECO:0000305"
FT HELIX 171..242
FT /evidence="ECO:0007829|PDB:4H22"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:4H22"
SQ SEQUENCE 808 AA; 89253 MW; 4E6140DF2471A7C9 CRC64;
MTSPAAAQSR EIDCLSPEAQ KLAEARLAAK RAARAEAREI RMKELERQQK EEDSERYSRR
SRRNTSASDE DERMSVGSRG SLRVEERPEK DFTEKGSRNM PGLSAATLAS LGGTSSRRGS
GDTSISIDTE ASIREIKELN ELKDQIQDVE GKYMQGLKEM KDSLAEVEEK YKKAMVSNAQ
LDNEKTNFMY QVDTLKDMLL ELEEQLAESR RQYEEKNKEF EREKHAHSIL QFQFAEVKEA
LKQREEMLEK HGIILNSEIA TNGETSDTLN NVGYQGPTKM TKEELNALKS TGDGTLGRAS
EVEVKNEIVA NVGKREILHN TEKEQHTEDT VKDCVDIEVF PAGENTEDQK SSEDTAPFLG
TLAGATYEEQ VQSQILESSS LPENTVQVES NEVMGAPDDR TRTPLEPSNC WSDLDGGNHT
ENVGEAAVTQ VEEQAGTVAS CPLGHSDDTV YHDDKCMVEV PQELETSTGH SLEKEFTNQE
AAEPKEVPAH STEVGRDHNE EEGEETGLRD EKPIKTEVPG SPAGTEGNCQ EATGPSTVDT
QNEPLDMKEP DEEKSDQQGE ALDSSQKKTK NKKKKNKKKK SPVPVETLKD VKKELTYQNT
DLSEIKEEEQ VKSTDRKSAV EAQNEVTENP KQKIAAESSE NVDCPENPKI KLDGKLDQEG
DDVQTAAEEV LADGDTLDFE DDTVQSSGPR AGGEELDEGV AKDNAKIDGA TQSSPAEPKS
EDADRCTLPE HESPSQDISD ACEAESTERC EMSEHPSQTV RKALDSNSLE NDDLSAPGRE
PGHFNPESRE DTRGGNEKGK SKEDCTMS
