LMO7_HUMAN
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 03-AUG-2022, entry version 189.
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};
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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; 159.
DR CORUM; Q8WWI1; -.
DR DIP; DIP-33107N; -.
DR IntAct; Q8WWI1; 48.
DR MINT; Q8WWI1; -.
DR STRING; 9606.ENSP00000433352; -.
DR GlyGen; Q8WWI1; 11 sites, 2 O-linked glycans (11 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; Q8WWI1; -.
DR PeptideAtlas; Q8WWI1; -.
DR PRIDE; 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 Antibodypedia; 10122; 122 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 CTD; 4008; -.
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; 38375at2759; -.
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 1120 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 130 other tissues.
DR ExpressionAtlas; Q8WWI1; baseline and differential.
DR Genevisible; Q8WWI1; HS.
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; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001715; CH-domain.
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; PTHR46767; 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; SSF47576; 1.
DR SUPFAM; SSF50156; SSF50156; 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.
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
