LRIF1_HUMAN
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 03-AUG-2022, entry version 141.
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},
GN RIF1 {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};
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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; 230.
DR IntAct; Q5T3J3; 104.
DR MINT; Q5T3J3; -.
DR STRING; 9606.ENSP00000358778; -.
DR GlyGen; Q5T3J3; 7 sites, 2 O-linked glycans (7 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; Q5T3J3; -.
DR PeptideAtlas; Q5T3J3; -.
DR PRIDE; Q5T3J3; -.
DR ProteomicsDB; 64403; -. [Q5T3J3-1]
DR ProteomicsDB; 64404; -. [Q5T3J3-2]
DR Antibodypedia; 33789; 98 antibodies from 18 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 CTD; 55791; -.
DR DisGeNET; 55791; -.
DR GeneCards; LRIF1; -.
DR HGNC; HGNC:30299; LRIF1.
DR HPA; ENSG00000121931; Low tissue specificity.
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; AVTSQQC; -.
DR OrthoDB; 277572at2759; -.
DR PhylomeDB; Q5T3J3; -.
DR TreeFam; TF336147; -.
DR PathwayCommons; Q5T3J3; -.
DR SignaLink; Q5T3J3; -.
DR BioGRID-ORCS; 55791; 19 hits in 1080 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 185 other tissues.
DR Genevisible; Q5T3J3; HS.
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 transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR026191; LRIF1.
DR PANTHER; PTHR16131; PTHR16131; 1.
DR Pfam; PF15741; LRIF1; 1.
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 (CBX1/HP1-
FT 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
