ID LMO7_HUMAN Reviewed; 1683 AA. AC Q8WWI1; E9PLH4; O15462; O95346; Q5TBK6; Q9UKC1; Q9UQM5; Q9Y6A7; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 27-MAR-2024, entry version 198. DE RecName: Full=LIM domain only protein 7; DE Short=LMO-7; DE AltName: Full=F-box only protein 20; DE AltName: Full=LOMP; GN Name=LMO7; Synonyms=FBX20, FBXO20, KIAA0858; 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), AND TISSUE SPECIFICITY. RC TISSUE=Brain, and Peripheral blood leukocyte; RX PubMed=11935316; DOI=10.1007/s00439-001-0646-6; RA Rozenblum E., Vahteristo P., Sandberg T., Bergthorsson J.T., Syrjakoski K., RA Weaver D., Haraldsson K., Johannsdottir H.K., Vehmanen P., Nigam S., RA Golberger N., Robbins C., Pak E., Dutra A., Gillander E., Stephan D.A., RA Bailey-Wilson J., Juo S.-H.H., Kainu T., Arason A., Barkardottir R.B., RA Nevanlinna H., Borg A., Kallioniemi O.-P.; RT "A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer RT development: identification and characterization of candidate genes."; RL Hum. Genet. 110:111-121(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 504-758 (ISOFORM 2). RX PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2; RA Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., RA Pagano M.; RT "Identification of a family of human F-box proteins."; RL Curr. Biol. 9:1177-1179(1999). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 763-1683 (ISOFORM 2). RC TISSUE=Brain; RA Mu W., Burt D.R.; RT "LOMP, a novel protein that contains a single LIM domain and PDZ domain."; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1343-1683 (ISOFORM 3), RP ALTERNATIVE SPLICING (ISOFORMS 2; 3 AND 4), AND TISSUE SPECIFICITY. RC TISSUE=Pancreas; RX PubMed=9826547; DOI=10.1006/bbrc.1998.9656; RA Putilina T., Jaworski C., Gentleman S., McDonald B., Kadiri M., Wong P.; RT "Analysis of a human cDNA containing a tissue-specific alternatively RT spliced LIM domain."; RL Biochem. Biophys. Res. Commun. 252:433-439(1998). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-1026 AND SER-1510, RP AND 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-867; THR-949; THR-1048 AND RP SER-1586, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 (ISOFORM 3), RP AND IDENTIFICATION BY 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-873 AND SER-1510, AND 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-276; SER-709; RP SER-867; SER-873; SER-895; THR-913; SER-919; SER-926; THR-932; SER-988; RP SER-991; SER-995; SER-1026; SER-1044; THR-1048; SER-1423; SER-1563; RP SER-1586; SER-1593; SER-1595; SER-1597 AND SER-1601, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-342 AND SER-345 (ISOFORM 3), AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185; SER-704; SER-805; RP THR-956; SER-960; SER-988; SER-1026; SER-1423 AND SER-1586, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-276; SER-704; RP SER-805; SER-867; SER-895; THR-913; SER-919; SER-960; SER-988; SER-991; RP SER-994; SER-1026; SER-1032; THR-1048; SER-1177; SER-1304; SER-1307; RP SER-1510; SER-1516; SER-1593 AND SER-1601, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-342 AND SER-345 (ISOFORM 3), AND IDENTIFICATION BY MASS RP 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-246; SER-704; SER-751; RP SER-805; THR-1048; SER-1423 AND SER-1510, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-342 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 5), AND IDENTIFICATION RP 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-257; SER-276; RP SER-704; SER-706; SER-805; SER-895; THR-913; SER-919; THR-932; THR-956; RP SER-960; SER-988; SER-1026; THR-1048; SER-1423; SER-1454; SER-1493; RP SER-1510; SER-1516; SER-1563; SER-1586 AND SER-1593, AND IDENTIFICATION BY RP 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-704; SER-867; RP SER-879; SER-988; SER-991; SER-1026; SER-1510; SER-1586 AND SER-1593, AND RP IDENTIFICATION BY 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1405, 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 (1.46 ANGSTROMS) OF 1037-1126. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of PDZ domain of KIAA0858 (LIM), ms0793 from homo RT sapiens."; RL Submitted (JUL-2007) to the PDB data bank. RN [23] RP VARIANTS [LARGE SCALE ANALYSIS] ALA-354 AND MET-785. 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 -!- INTERACTION: CC Q8WWI1-3; Q6UXM1-1: LRIG3; NbExp=3; IntAct=EBI-4400717, EBI-25412632; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q8WWI1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WWI1-2; Sequence=VSP_009719; CC Name=3; CC IsoId=Q8WWI1-3; Sequence=VSP_009718; CC Name=4; CC IsoId=Q8WWI1-4; Sequence=VSP_009720; CC Name=5; CC IsoId=Q8WWI1-5; Sequence=VSP_055683, VSP_055684, VSP_055685; CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 and isoform 4 are CC predominantly expressed in brain. {ECO:0000269|PubMed:11935316, CC ECO:0000269|PubMed:9826547}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC96299.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAC96300.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAD33924.1; 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; AF330045; AAL37480.1; -; mRNA. DR EMBL; AL137121; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137782; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB020665; BAA74881.2; -; mRNA. DR EMBL; AF174600; AAF04521.1; -; mRNA. DR EMBL; AF144237; AAD33924.1; ALT_SEQ; mRNA. DR EMBL; U90654; AAB86592.1; -; mRNA. DR EMBL; AF092557; AAC96299.1; ALT_INIT; Genomic_DNA. DR EMBL; AF092554; AAC96299.1; JOINED; Genomic_DNA. DR EMBL; AF092555; AAC96299.1; JOINED; Genomic_DNA. DR EMBL; AF092556; AAC96299.1; JOINED; Genomic_DNA. DR EMBL; AF092557; AAC96300.1; ALT_INIT; Genomic_DNA. DR EMBL; AF092554; AAC96300.1; JOINED; Genomic_DNA. DR CCDS; CCDS53876.1; -. [Q8WWI1-5] DR CCDS; CCDS9454.1; -. [Q8WWI1-3] DR PIR; JE0325; JE0325. DR RefSeq; NP_001293009.1; NM_001306080.1. DR RefSeq; NP_001317512.1; NM_001330583.1. DR RefSeq; NP_005349.3; NM_005358.5. [Q8WWI1-3] DR RefSeq; NP_056667.2; NM_015842.2. DR PDB; 2EAQ; X-ray; 1.46 A; A=1037-1126. DR PDBsum; 2EAQ; -. DR AlphaFoldDB; Q8WWI1; -. DR SMR; Q8WWI1; -. DR BioGRID; 110193; 193. DR ComplexPortal; CPX-7929; SCF E3 ubiquitin ligase complex, LMO7 variant. DR CORUM; Q8WWI1; -. DR DIP; DIP-33107N; -. DR IntAct; Q8WWI1; 53. DR MINT; Q8WWI1; -. DR STRING; 9606.ENSP00000366757; -. DR GlyCosmos; Q8WWI1; 11 sites, 2 glycans. DR GlyGen; Q8WWI1; 40 sites, 2 O-linked glycans (40 sites). DR iPTMnet; Q8WWI1; -. DR MetOSite; Q8WWI1; -. DR PhosphoSitePlus; Q8WWI1; -. DR SwissPalm; Q8WWI1; -. DR BioMuta; LMO7; -. DR DMDM; 308153585; -. DR EPD; Q8WWI1; -. DR jPOST; Q8WWI1; -. DR MassIVE; Q8WWI1; -. DR MaxQB; Q8WWI1; -. DR PaxDb; 9606-ENSP00000433352; -. DR PeptideAtlas; Q8WWI1; -. DR ProteomicsDB; 21797; -. DR ProteomicsDB; 74888; -. [Q8WWI1-1] DR ProteomicsDB; 74889; -. [Q8WWI1-2] DR ProteomicsDB; 74890; -. [Q8WWI1-3] DR ProteomicsDB; 74891; -. [Q8WWI1-4] DR Pumba; Q8WWI1; -. DR Antibodypedia; 10122; 139 antibodies from 27 providers. DR DNASU; 4008; -. DR Ensembl; ENST00000341547.8; ENSP00000342112.4; ENSG00000136153.20. [Q8WWI1-3] DR GeneID; 4008; -. DR KEGG; hsa:4008; -. DR UCSC; uc010thv.4; human. [Q8WWI1-1] DR AGR; HGNC:6646; -. DR DisGeNET; 4008; -. DR GeneCards; LMO7; -. DR HGNC; HGNC:6646; LMO7. DR HPA; ENSG00000136153; Tissue enhanced (heart). DR MIM; 604362; gene. DR neXtProt; NX_Q8WWI1; -. DR OpenTargets; ENSG00000136153; -. DR PharmGKB; PA30412; -. DR VEuPathDB; HostDB:ENSG00000136153; -. DR eggNOG; KOG1704; Eukaryota. DR GeneTree; ENSGT00950000183159; -. DR InParanoid; Q8WWI1; -. DR OrthoDB; 6462at2759; -. DR PhylomeDB; Q8WWI1; -. DR TreeFam; TF332155; -. DR PathwayCommons; Q8WWI1; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q8WWI1; -. DR BioGRID-ORCS; 4008; 16 hits in 1196 CRISPR screens. DR ChiTaRS; LMO7; human. DR EvolutionaryTrace; Q8WWI1; -. DR GeneWiki; LMO7; -. DR GenomeRNAi; 4008; -. DR Pharos; Q8WWI1; Tbio. DR PRO; PR:Q8WWI1; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q8WWI1; Protein. DR Bgee; ENSG00000136153; Expressed in sural nerve and 132 other cell types or tissues. DR ExpressionAtlas; Q8WWI1; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; NAS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro. DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro. DR CDD; cd08368; LIM; 1. DR CDD; cd00136; PDZ; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR031865; DUF4757. DR InterPro; IPR029978; LMO-7. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR003096; SM22_calponin. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR46767; LIM DOMAIN ONLY PROTEIN 7; 1. DR PANTHER; PTHR46767:SF1; LIM DOMAIN ONLY PROTEIN 7; 1. DR Pfam; PF00307; CH; 1. DR Pfam; PF15949; DUF4757; 2. DR Pfam; PF00412; LIM; 1. DR Pfam; PF00595; PDZ; 1. DR PRINTS; PR00888; SM22CALPONIN. DR SMART; SM00033; CH; 1. DR SMART; SM00132; LIM; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q8WWI1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; KW Ubl conjugation; Zinc. FT CHAIN 1..1683 FT /note="LIM domain only protein 7" FT /id="PRO_0000075824" FT DOMAIN 64..181 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 1042..1128 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 1612..1678 FT /note="LIM zinc-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT REGION 312..343 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 749..901 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 947..1037 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1255..1604 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 328..343 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 749..789 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 827..859 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 860..901 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 949..977 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 984..1017 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1255..1276 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1278..1305 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1306..1392 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1428..1456 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1469..1483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1514..1604 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 185 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 704 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 706 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 751 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 805 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 867 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 873 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976" FT MOD_RES 879 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 895 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 913 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 919 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 926 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 932 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 949 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 956 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 960 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 988 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 991 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 994 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 995 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1026 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1032 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1044 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1048 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1307 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1423 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1493 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1510 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1563 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1586 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1593 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1595 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1597 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1601 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT CROSSLNK 1405 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..285 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10048485" FT /id="VSP_055683" FT VAR_SEQ 357..690 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11935316, FT ECO:0000303|PubMed:9826547" FT /id="VSP_009718" FT VAR_SEQ 1606..1683 FT /note="RSVSGKRICSYCNNILGKGAAMIIESLGLCYHLHCFKCVACECDLGGSSSGA FT EVRIRNHQLYCNDCYLRFKSGRPTAM -> SVLPVSVTSEALPQELKSGSETTNCTATT FT AISDSNLDGQPPCDVSLHTKALLQIEEEVVAAHVDL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10531035, ECO:0000303|Ref.6" FT /id="VSP_009719" FT VAR_SEQ 1606..1683 FT /note="RSVSGKRICSYCNNILGKGAAMIIESLGLCYHLHCFKCVACECDLGGSSSGA FT EVRIRNHQLYCNDCYLRFKSGRPTAM -> SWTANRHVM (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_009720" FT VAR_SEQ 1606..1670 FT /note="RSVSGKRICSYCNNILGKGAAMIIESLGLCYHLHCFKCVACECDLGGSSSGA FT EVRIRNHQLYCND -> SVLPVSVTSEALPQELKSGSETTNCTATTAISDSNLDGQPPC FT DVSLHTKALLQIEEEVVAAHVDL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10048485" FT /id="VSP_055684" FT VAR_SEQ 1671..1683 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10048485" FT /id="VSP_055685" FT VARIANT 354 FT /note="T -> A (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036189" FT VARIANT 785 FT /note="L -> M (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036190" FT VARIANT 1547 FT /note="P -> Q (in dbSNP:rs7988661)" FT /id="VAR_056163" FT CONFLICT 522 FT /note="V -> A (in Ref. 5; AAF04521)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="F -> L (in Ref. 5; AAF04521)" FT /evidence="ECO:0000305" FT CONFLICT 891 FT /note="R -> C (in Ref. 6; AAD33924)" FT /evidence="ECO:0000305" FT CONFLICT 943 FT /note="V -> I (in Ref. 1; AAL37480 and 6; AAD33924)" FT /evidence="ECO:0000305" FT CONFLICT 1447 FT /note="M -> T (in Ref. 6; AAD33924/AAB86592)" FT /evidence="ECO:0000305" FT STRAND 1038..1046 FT /evidence="ECO:0007829|PDB:2EAQ" FT STRAND 1056..1062 FT /evidence="ECO:0007829|PDB:2EAQ" FT STRAND 1065..1071 FT /evidence="ECO:0007829|PDB:2EAQ" FT HELIX 1076..1079 FT /evidence="ECO:0007829|PDB:2EAQ" FT STRAND 1087..1091 FT /evidence="ECO:0007829|PDB:2EAQ" FT HELIX 1101..1114 FT /evidence="ECO:0007829|PDB:2EAQ" FT STRAND 1116..1124 FT /evidence="ECO:0007829|PDB:2EAQ" FT MOD_RES Q8WWI1-3:342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES Q8WWI1-3:345 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES Q8WWI1-5:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 1683 AA; 192696 MW; 3E79B2AEAC67F6F5 CRC64; MKKIRICHIF TFYSWMSYDV LFQRTELGAL EIWRQLICAH VCICVGWLYL RDRVCSKKDI ILRTEQNSGR TILIKAVTEK NFETKDFRAS LENGVLLCDL INKLKPGVIK KINRLSTPIA GLDNINVFLK ACEQIGLKEA QLFHPGDLQD LSNRVTVKQE ETDRRVKNVL ITLYWLGRKA QSNPYYNGPH LNLKAFENLL GQALTKALED SSFLKRSGRD SGYGDIWCPE RGEFLAPPRH HKREDSFESL DSLGSRSLTS CSSDITLRGG REGFESDTDS EFTFKMQDYN KDDMSYRRIS AVEPKTALPF NRFLPNKSRQ PSYVPAPLRK KKPDKHEDNR RSWASPVYTE ADGTFSSNQR RIWGTNVENW PTVQGTSKSS CYLEEEKAKT RSIPNIVKDD LYVRKLSPVM PNPGNAFDQF LPKCWTPEDV NWKRIKRETY KPWYKEFQGF SQFLLLQALQ TYSDDILSSE THTKIDPTSG PRLITRRKNL SYAPGYRRDD LEMAALDPDL ENDDFFVRKT GVFHANPYVL RAFEDFRKFS EQDDSVERDI ILQCREGELV LPDLEKDDMI VRRIPAQKKE VPLSGAPDRY HPVPFPEPWT LPPEIQAKFL CVFERTCPSK EKSNSCRILV PSYRQKKDDM LTRKIQSWKL GTTVPPISFT PGPCSEADLK RWEAIREASR LRHKKRLMVE RLFQKIYGEN GSKSMSDVSA EDVQNLRQLR YEEMQKIKSQ LKEQDQKWQD DLAKWKDRRK SYTSDLQKKK EEREEIEKQA LEKSKRSSKT FKEMLQDRES QNQKSTVPSR RRMYSFDDVL EEGKRPPTMT VSEASYQSER VEEKGATYPS EIPKEDSTTF AKREDRVTTE IQLPSQSPVE EQSPASLSSL RSRSTQMEST RVSASLPRSY RKTDTVRLTS VVTPRPFGSQ TRGISSLPRS YTMDDAWKYN GDVEDIKRTP NNVVSTPAPS PDASQLASSL SSQKEVAATE EDVTRLPSPT SPFSSLSQDQ AATSKATLSS TSGLDLMSES GEGEISPQRE VSRSQDQFSD MRISINQTPG KSLDFGFTIK WDIPGIFVAS VEAGSPAEFS QLQVDDEIIA INNTKFSYND SKEWEEAMAK AQETGHLVMD VRRYGKAGSP ETKWIDATSG IYNSEKSSNL SVTTDFSESL QSSNIESKEI NGIHDESNAF ESKASESISL KNLKRRSQFF EQGSSDSVVP DLPVPTISAP SRWVWDQEEE RKRQERWQKE QDRLLQEKYQ REQEKLREEW QRAKQEAERE NSKYLDEELM VLSSNSMSLT TREPSLATWE ATWSEGSKSS DREGTRAGEE ERRQPQEEVV HEDQGKKPQD QLVIERERKW EQQLQEEQEQ KRLQAEAEEQ KRPAEEQKRQ AEIERETSVR IYQYRRPVDS YDIPKTEEAS SGFLPGDRNK SRSTTELDDY STNKNGNNKY LDQIGNMTSS QRRSKKEQVP SGAELERQQI LQEMRKRTPL HNDNSWIRQR SASVNKEPVS LPGIMRRGES LDNLDSPRSN SWRQPPWLNQ PTGFYASSSV QDFSRPPPQL VSTSNRAYMR NPSSSVPPPS AGSVKTSTTG VATTQSPTPR SHSPSASQSG SQLRNRSVSG KRICSYCNNI LGKGAAMIIE SLGLCYHLHC FKCVACECDL GGSSSGAEVR IRNHQLYCND CYLRFKSGRP TAM //