ID LRIF1_HUMAN Reviewed; 769 AA. AC Q5T3J3; Q86XS4; Q8N3B6; Q96HT4; Q9NUM5; Q9NV32; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=Ligand-dependent nuclear receptor-interacting factor 1 {ECO:0000305}; DE AltName: Full=HP1-binding protein enriched in inactive X chromosome protein 1 {ECO:0000303|PubMed:23542155}; DE Short=HBiX1 {ECO:0000303|PubMed:23542155}; DE AltName: Full=Receptor-interacting factor 1 {ECO:0000303|PubMed:17455211}; GN Name=LRIF1 {ECO:0000312|HGNC:HGNC:30299}; GN Synonyms=C1orf103 {ECO:0000312|HGNC:HGNC:30299}, RIF1 GN {ECO:0000303|PubMed:17455211}; 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). RA Li H., Leo C., Chen A., Chen J.D.; RT "Identification of a transcriptional inhibitory factor for retinoic acid RT receptor."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 269-769 (ISOFORM 1). RC TISSUE=Placenta; 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., 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., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., 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., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-769 (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, MUTAGENESIS, NUCLEAR LOCALIZATION SIGNAL, AND RP INTERACTION WITH RARA. RX PubMed=17455211; DOI=10.1002/jcb.21340; RA Li H.J., Haque Z.K., Chen A., Mendelsohn M.; RT "RIF-1, a novel nuclear receptor corepressor that associates with the RT nuclear matrix."; RL J. Cell. Biochem. 102:1021-1035(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-769 (ISOFORM 1). RC TISSUE=Placenta; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-769 (ISOFORM 1). RC TISSUE=Melanoma; 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-599 AND THR-732, AND 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 [9] RP IDENTIFICATION 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 [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-436; SER-502 AND RP SER-599, AND 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 [12] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBX1; CBX3; CBX5 AND RP SMCHD1, AND MUTAGENESIS OF 582-VAL--LEU-584. RX PubMed=23542155; DOI=10.1038/nsmb.2532; RA Nozawa R.S., Nagao K., Igami K.T., Shibata S., Shirai N., Nozaki N., RA Sado T., Kimura H., Obuse C.; RT "Human inactive X chromosome is compacted through a PRC2-independent RT SMCHD1-HBiX1 pathway."; RL Nat. Struct. Mol. Biol. 20:566-573(2013). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-702, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-259; LYS-279; LYS-446 AND RP LYS-605, AND IDENTIFICATION BY MASS 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 [15] RP FUNCTION, AND INVOLVEMENT IN FSHD3. RX PubMed=32467133; DOI=10.1212/wnl.0000000000009617; RA Hamanaka K., Sikrova D., Mitsuhashi S., Masuda H., Sekiguchi Y., RA Sugiyama A., Shibuya K., Lemmers R.J.L.F., Goossens R., Ogawa M., Nagao K., RA Obuse C., Noguchi S., Hayashi Y.K., Kuwabara S., Balog J., Nishino I., RA van der Maarel S.M.; RT "Homozygous nonsense variant in LRIF1 associated with facioscapulohumeral RT muscular dystrophy."; RL Neurology 94:e2441-e2447(2020). CC -!- FUNCTION: Together with SMCHD1, involved in chromosome X inactivation CC in females by promoting the compaction of heterochromatin CC (PubMed:23542155). Also able to repress the ligand-induced CC transcriptional activity of retinoic acid receptor alpha (RARA), CC possibly through direct recruitment of histone deacetylases CC (PubMed:17455211). Also required for silencing of the DUX4 locus in CC somatic cells (PubMed:32467133). {ECO:0000269|PubMed:17455211, CC ECO:0000269|PubMed:23542155, ECO:0000269|PubMed:32467133}. CC -!- SUBUNIT: Interacts with RARA (PubMed:17455211). Interacts with SMCHD1; CC leading to recruitment to inactivated chromosome X in females CC (PubMed:23542155). Interacts (via PxVxL motif) with HP1 (CBX1/HP1-beta, CC CBX3/HP1-gamma and CBX5/HP1-alpha) (PubMed:23542155). CC {ECO:0000269|PubMed:17455211, ECO:0000269|PubMed:23542155}. CC -!- INTERACTION: CC Q5T3J3; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-473196, EBI-11524452; CC Q5T3J3; Q13185: CBX3; NbExp=8; IntAct=EBI-473196, EBI-78176; CC Q5T3J3; P45973: CBX5; NbExp=11; IntAct=EBI-473196, EBI-78219; CC Q5T3J3; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-473196, EBI-739773; CC Q5T3J3; O75575-2: CRCP; NbExp=3; IntAct=EBI-473196, EBI-12880830; CC Q5T3J3; Q14192: FHL2; NbExp=3; IntAct=EBI-473196, EBI-701903; CC Q5T3J3; P15408: FOSL2; NbExp=3; IntAct=EBI-473196, EBI-3893419; CC Q5T3J3; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-473196, EBI-6425864; CC Q5T3J3; O95257: GADD45G; NbExp=4; IntAct=EBI-473196, EBI-448202; CC Q5T3J3; Q9Y2X7: GIT1; NbExp=2; IntAct=EBI-473196, EBI-466061; CC Q5T3J3; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-473196, EBI-743960; CC Q5T3J3; P57682: KLF3; NbExp=3; IntAct=EBI-473196, EBI-8472267; CC Q5T3J3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-473196, EBI-741158; CC Q5T3J3; O15160: POLR1C; NbExp=3; IntAct=EBI-473196, EBI-1055079; CC Q5T3J3; O43741: PRKAB2; NbExp=3; IntAct=EBI-473196, EBI-1053424; CC Q5T3J3; P13861-2: PRKAR2A; NbExp=3; IntAct=EBI-473196, EBI-11752137; CC Q5T3J3; P08195-4: SLC3A2; NbExp=3; IntAct=EBI-473196, EBI-12832276; CC Q5T3J3; A6NHR9: SMCHD1; NbExp=9; IntAct=EBI-473196, EBI-2801919; CC Q5T3J3; Q8TC71: SPATA18; NbExp=3; IntAct=EBI-473196, EBI-11334239; CC Q5T3J3; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-473196, EBI-372432; CC Q5T3J3; Q13432: UNC119; NbExp=3; IntAct=EBI-473196, EBI-711260; CC Q5T3J3; O14972: VPS26C; NbExp=3; IntAct=EBI-473196, EBI-7207091; CC Q5T3J3; P58304: VSX2; NbExp=3; IntAct=EBI-473196, EBI-6427899; CC Q5T3J3; O43829: ZBTB14; NbExp=3; IntAct=EBI-473196, EBI-10176632; CC Q5T3J3; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-473196, EBI-11741890; CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:23542155}. Nucleus CC matrix {ECO:0000269|PubMed:17455211}. Note=Localizes to Barr body; CC recruited by SMCHD1. {ECO:0000269|PubMed:23542155}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5T3J3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5T3J3-2; Sequence=VSP_020721; CC -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression CC levels in heart, liver and placenta. {ECO:0000269|PubMed:17455211}. CC -!- DOMAIN: The Pro-Xaa-Val-Xaa-Leu (PxVxL) motif mediates interaction with CC HP1 (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-alpha). CC {ECO:0000269|PubMed:23542155}. CC -!- DISEASE: Facioscapulohumeral muscular dystrophy 3, digenic (FSHD3) CC [MIM:619477]: A form of facioscapulohumeral muscular dystrophy, a CC degenerative muscle disease characterized by slowly progressive CC weakness of the muscles of the face, upper-arm, and shoulder girdle. CC FSHD3 is a digenic form characterized by adult onset of proximal muscle CC weakness affecting the face, neck, scapular muscles, and upper and CC lower limbs. Muscle involvement is usually asymmetric, and other muscle CC groups may become involved with progression of the disease. CC {ECO:0000269|PubMed:32467133}. Note=The disease is caused by variants CC affecting distinct genetic loci, including the gene represented in this CC entry. The disease is caused by a LRIF1 homozygous variant resulting in CC loss of isoform 1, in the presence of an haplotype on chromosome 4 CC permissive for chromatin relaxation of the D4Z4 macrosatellite and CC inappropriate DUX4 expression. Deregulated expression of DUX4 in CC skeletal muscle can lead to cell death. {ECO:0000269|PubMed:32467133}. CC -!- SIMILARITY: Belongs to the LRIF1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH08115.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAO43631.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA92097.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY190122; AAO43631.1; ALT_FRAME; mRNA. DR EMBL; AK001826; BAA91928.1; -; mRNA. DR EMBL; AK002131; BAA92097.1; ALT_FRAME; mRNA. DR EMBL; AL360270; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008115; AAH08115.1; ALT_INIT; mRNA. DR EMBL; AL834466; CAD39125.1; -; mRNA. DR CCDS; CCDS30800.1; -. [Q5T3J3-1] DR CCDS; CCDS41366.1; -. [Q5T3J3-2] DR RefSeq; NP_001006946.1; NM_001006945.1. [Q5T3J3-2] DR RefSeq; NP_060842.3; NM_018372.3. [Q5T3J3-1] DR AlphaFoldDB; Q5T3J3; -. DR SMR; Q5T3J3; -. DR BioGRID; 120905; 239. DR IntAct; Q5T3J3; 104. DR MINT; Q5T3J3; -. DR STRING; 9606.ENSP00000358778; -. DR GlyCosmos; Q5T3J3; 7 sites, 2 glycans. DR GlyGen; Q5T3J3; 11 sites, 2 O-linked glycans (11 sites). DR iPTMnet; Q5T3J3; -. DR PhosphoSitePlus; Q5T3J3; -. DR BioMuta; LRIF1; -. DR DMDM; 74744778; -. DR EPD; Q5T3J3; -. DR jPOST; Q5T3J3; -. DR MassIVE; Q5T3J3; -. DR MaxQB; Q5T3J3; -. DR PaxDb; 9606-ENSP00000358778; -. DR PeptideAtlas; Q5T3J3; -. DR ProteomicsDB; 64403; -. [Q5T3J3-1] DR ProteomicsDB; 64404; -. [Q5T3J3-2] DR Pumba; Q5T3J3; -. DR Antibodypedia; 33789; 130 antibodies from 19 providers. DR DNASU; 55791; -. DR Ensembl; ENST00000369763.5; ENSP00000358778.4; ENSG00000121931.16. [Q5T3J3-1] DR Ensembl; ENST00000485275.2; ENSP00000432290.1; ENSG00000121931.16. [Q5T3J3-2] DR Ensembl; ENST00000494675.5; ENSP00000435259.1; ENSG00000121931.16. [Q5T3J3-2] DR GeneID; 55791; -. DR KEGG; hsa:55791; -. DR MANE-Select; ENST00000369763.5; ENSP00000358778.4; NM_018372.4; NP_060842.3. DR UCSC; uc001dzz.4; human. [Q5T3J3-1] DR AGR; HGNC:30299; -. DR CTD; 55791; -. DR DisGeNET; 55791; -. DR GeneCards; LRIF1; -. DR HGNC; HGNC:30299; LRIF1. DR HPA; ENSG00000121931; Low tissue specificity. DR MalaCards; LRIF1; -. DR MIM; 615354; gene. DR MIM; 619477; phenotype. DR neXtProt; NX_Q5T3J3; -. DR OpenTargets; ENSG00000121931; -. DR PharmGKB; PA142672487; -. DR VEuPathDB; HostDB:ENSG00000121931; -. DR eggNOG; ENOG502QU1A; Eukaryota. DR GeneTree; ENSGT00390000017353; -. DR HOGENOM; CLU_020634_0_0_1; -. DR InParanoid; Q5T3J3; -. DR OMA; ERNDKNH; -. DR OrthoDB; 5357329at2759; -. DR PhylomeDB; Q5T3J3; -. DR TreeFam; TF336147; -. DR PathwayCommons; Q5T3J3; -. DR SignaLink; Q5T3J3; -. DR BioGRID-ORCS; 55791; 19 hits in 1158 CRISPR screens. DR ChiTaRS; LRIF1; human. DR GeneWiki; C1orf103; -. DR GenomeRNAi; 55791; -. DR Pharos; Q5T3J3; Tdark. DR PRO; PR:Q5T3J3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5T3J3; Protein. DR Bgee; ENSG00000121931; Expressed in calcaneal tendon and 187 other cell types or tissues. DR GO; GO:0001740; C:Barr body; IDA:UniProtKB. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IEA:InterPro. DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR InterPro; IPR026191; LRIF1. DR PANTHER; PTHR16131:SF2; LIGAND-DEPENDENT NUCLEAR RECEPTOR-INTERACTING FACTOR 1; 1. DR PANTHER; PTHR16131; UNCHARACTERIZED; 1. DR Pfam; PF15741; LRIF1; 1. DR Genevisible; Q5T3J3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromosome; Coiled coil; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..769 FT /note="Ligand-dependent nuclear receptor-interacting factor FT 1" FT /id="PRO_0000250686" FT REGION 378..400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 528..562 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 740..769 FT /evidence="ECO:0000255" FT MOTIF 580..584 FT /note="PxVxL motif" FT /evidence="ECO:0000269|PubMed:23542155" FT MOTIF 628..631 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:17455211" FT MOTIF 642..645 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:17455211" FT COMPBIAS 545..562 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 402 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 436 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 502 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 599 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 732 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 259 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 279 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 446 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 605 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 702 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT VAR_SEQ 1..536 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020721" FT VARIANT 438 FT /note="A -> T (in dbSNP:rs2232041)" FT /id="VAR_050703" FT VARIANT 599 FT /note="S -> P (in dbSNP:rs2232045)" FT /id="VAR_027599" FT VARIANT 641 FT /note="I -> M (in dbSNP:rs2232047)" FT /id="VAR_027600" FT MUTAGEN 582..584 FT /note="VCL->DCE: Abolishes interaction with HP1 FT (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-alpha)." FT /evidence="ECO:0000269|PubMed:23542155" FT MUTAGEN 628..630 FT /note="KKR->AAA: Slightly reduces nuclear localization." FT /evidence="ECO:0000269|PubMed:17455211" FT MUTAGEN 642..644 FT /note="KKR->AAA: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:17455211" FT CONFLICT 66..68 FT /note="DAL -> NA (in Ref. 1; AAO43631)" FT /evidence="ECO:0000305" FT CONFLICT 72..80 FT /note="TGKPVQVTF -> PGNQFSY (in Ref. 1; AAO43631)" FT /evidence="ECO:0000305" FT CONFLICT 108..111 FT /note="LTRT -> PSRP (in Ref. 1; AAO43631)" FT /evidence="ECO:0000305" FT CONFLICT 666 FT /note="Missing (in Ref. 2; BAA92097)" FT /evidence="ECO:0000305" SQ SEQUENCE 769 AA; 84568 MW; D39A2BB494F16AAA CRC64; MSNNLRRVFL KPAEENSGNA SRCVSGCMYQ VVQTIGSDGK NLLQLLPIPK SSGNLIPLVQ SSVMSDALKG NTGKPVQVTF QTQISSSSTS ASVQLPIFQP ASSSNYFLTR TVDTSEKGRV TSVGTGNFSS SVSKVQSHGV KIDGLTMQTF AVPPSTQKDS SFIVVNTQSL PVTVKSPVLP SGHHLQIPAH AEVKSVPASS LPPSVQQKIL ATATTSTSGM VEASQMPTVI YVSPVNTVKN VVTKNFQNIY PKPVTEIAKP VILNTTQIPK NVATETQLKG GQHSQAAPVK WIFQDNLQPF TPSLVPVKSS NNVASKILKT FVDRKNLGDN TINMPPLSTI DPSGTRSKNM PIKDNALVMF NGKVYLLAKK GTDVLPSQID QQNSVSPDTP VRKDTLQTVS SSPVTEISRE VVNIVLAKSK SSQMETKSLS NTQLASMANL RAEKNKVEKP SPSTTNPHMN QSSNYLKQSK TLFTNPIFPV GFSTGHNAPR KVTAVIYARK GSVLQSIEKI SSSVDATTVT SQQCVFRDQE PKIHNEMAST SDKGAQGRND KKDSQGRSNK ALHLKSDAEF KKIFGLTKDL RVCLTRIPDH LTSGEGFDSF SSLVKSGTYK ETEFMVKEGE RKQQNFDKKR KAKTNKKMDH IKKRKTENAY NAIINGEANV TGSQLLSSIL PTSDVSQHNI LTSHSKTRQE KRTEMEYYTH EKQEKGTLNS NAAYEQSHFF NKNYTEDIFP VTPPELEETI RDEKIRRLKQ VLREKEAALE EMRKKMHQK //