LC7L3_HUMAN
ID LC7L3_HUMAN Reviewed; 432 AA.
AC O95232; B3KN54; D3DTY1; Q6PHR9; Q9NUY0; Q9P2S7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Luc7-like protein 3;
DE AltName: Full=Cisplatin resistance-associated-overexpressed protein;
DE AltName: Full=Luc7A;
DE AltName: Full=Okadaic acid-inducible phosphoprotein OA48-18;
DE AltName: Full=cAMP regulatory element-associated protein 1;
DE Short=CRE-associated protein 1;
DE Short=CREAP-1;
GN Name=LUC7L3; Synonyms=CREAP1, CROP, O48;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10631324; DOI=10.1016/s0014-5793(99)01744-5;
RA Nishii Y., Morishima M., Kakehi Y., Umehara K., Kioka N., Terano Y.,
RA Amachi T., Ueda K.;
RT "CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated from
RT cisplatin-resistant cell line.";
RL FEBS Lett. 465:153-156(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=16462885; DOI=10.1139/o05-139;
RA Shipman K.L., Robinson P.J., King B.R., Smith R., Nicholson R.C.;
RT "Identification of a family of DNA-binding proteins with homology to RNA
RT splicing factors.";
RL Biochem. Cell Biol. 84:9-19(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [MRNA] OF 378-432.
RC TISSUE=Fetal brain;
RX PubMed=10754390; DOI=10.1007/bf02256622;
RA Chin L.S., Singh S.K., Wang Q., Murray S.F.;
RT "Identification of okadaic-acid-induced genes by mRNA differential display
RT in glioma cells.";
RL J. Biomed. Sci. 7:152-159(2000).
RN [7]
RP INTERACTION WITH SFRS1, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12565863; DOI=10.1016/s0006-291x(02)03017-6;
RA Umehara H., Nishii Y., Morishima M., Kakehi Y., Kioka N., Amachi T.,
RA Koizumi J., Hagiwara M., Ueda K.;
RT "Effect of cisplatin treatment on speckled distribution of a
RT serine/arginine-rich nuclear protein CROP/Luc7A.";
RL Biochem. Biophys. Res. Commun. 301:324-329(2003).
RN [8]
RP INTERACTION WITH RSRC1.
RX PubMed=15798186; DOI=10.1128/mcb.25.8.2969-2980.2005;
RA Cazalla D., Newton K., Caceres J.F.;
RT "A novel SR-related protein is required for the second step of pre-mRNA
RT splicing.";
RL Mol. Cell. Biol. 25:2969-2980(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP INTERACTION WITH RBM25.
RX PubMed=18663000; DOI=10.1128/mcb.00560-08;
RA Zhou A., Ou A.C., Cho A., Benz E.J. Jr., Huang S.C.;
RT "Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site
RT selection.";
RL Mol. Cell. Biol. 28:5924-5936(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-431, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP INTERACTION WITH JMJD6.
RX PubMed=19574390; DOI=10.1126/science.1175865;
RA Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,
RA Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,
RA Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,
RA Boettger A.;
RT "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with
RT RNA splicing.";
RL Science 325:90-93(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3; SER-425 AND SER-431, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-115; SER-425 AND
RP SER-431, 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 [22]
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 [23]
RP INTERACTION WITH RRP1B.
RX PubMed=23604122; DOI=10.1038/onc.2013.133;
RG NISC Comparative Sequencing Program;
RA Lee M., Dworkin A.M., Gildea D., Trivedi N.S., Moorhead G.B.,
RA Crawford N.P.;
RT "RRP1B is a metastasis modifier that regulates the expression of
RT alternative mRNA isoforms through interactions with SRSF1.";
RL Oncogene 33:1818-1827(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-424, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-424, 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).
CC -!- FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role
CC in RNA splicing. {ECO:0000269|PubMed:16462885}.
CC -!- SUBUNIT: May interact with SFRS1 and form homodimers (PubMed:12565863).
CC Interacts with JMJD6 (PubMed:19574390). Interacts with RBM25
CC (PubMed:18663000). Interacts with RSRC1 (via Arg/Ser-rich domain)
CC (PubMed:15798186). Interacts with RRP1B (PubMed:23604122).
CC {ECO:0000269|PubMed:12565863, ECO:0000269|PubMed:15798186,
CC ECO:0000269|PubMed:18663000, ECO:0000269|PubMed:19574390,
CC ECO:0000269|PubMed:23604122}.
CC -!- INTERACTION:
CC O95232-2; P40692: MLH1; NbExp=3; IntAct=EBI-19157865, EBI-744248;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10631324,
CC ECO:0000269|PubMed:12565863}. Note=The subnuclear localization is
CC affected by cisplatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95232-2; Sequence=VSP_018136, VSP_018137;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, brain,
CC pancreas, thymus, ovary, small intestine and peripheral blood
CC leukocytes, as well as cerebellum, putamen and pituitary gland. Lowest
CC levels in lung, liver and kidney. Also expressed in fetal tissues,
CC including brain, heart, kidney, thymus and lung.
CC {ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:16462885}.
CC -!- PTM: Phosphorylated in vitro by SRPK1, SRPK2 and CLK1.
CC {ECO:0000269|PubMed:12565863}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79807.1; Type=Erroneous translation; Note=Erroneous CDS prediction.; Evidence={ECO:0000305};
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DR EMBL; AB034205; BAA90542.1; -; mRNA.
DR EMBL; DQ013876; AAY26238.1; -; mRNA.
DR EMBL; AK001925; BAA91981.1; -; mRNA.
DR EMBL; AK023672; BAG51216.1; -; mRNA.
DR EMBL; CH471109; EAW94583.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94585.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94587.1; -; Genomic_DNA.
DR EMBL; BC056409; AAH56409.1; -; mRNA.
DR EMBL; AF069250; AAC79807.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11573.1; -. [O95232-1]
DR RefSeq; NP_006098.2; NM_006107.3. [O95232-1]
DR RefSeq; NP_057508.2; NM_016424.4. [O95232-1]
DR AlphaFoldDB; O95232; -.
DR SMR; O95232; -.
DR BioGRID; 119710; 123.
DR CORUM; O95232; -.
DR IntAct; O95232; 35.
DR MINT; O95232; -.
DR STRING; 9606.ENSP00000425092; -.
DR CarbonylDB; O95232; -.
DR GlyGen; O95232; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95232; -.
DR PhosphoSitePlus; O95232; -.
DR SwissPalm; O95232; -.
DR BioMuta; LUC7L3; -.
DR EPD; O95232; -.
DR jPOST; O95232; -.
DR MassIVE; O95232; -.
DR MaxQB; O95232; -.
DR PaxDb; O95232; -.
DR PeptideAtlas; O95232; -.
DR PRIDE; O95232; -.
DR ProteomicsDB; 50730; -. [O95232-1]
DR ProteomicsDB; 50731; -. [O95232-2]
DR Antibodypedia; 18160; 101 antibodies from 24 providers.
DR DNASU; 51747; -.
DR Ensembl; ENST00000240304.5; ENSP00000240304.1; ENSG00000108848.16. [O95232-1]
DR Ensembl; ENST00000505658.6; ENSP00000425092.1; ENSG00000108848.16. [O95232-1]
DR GeneID; 51747; -.
DR KEGG; hsa:51747; -.
DR MANE-Select; ENST00000505658.6; ENSP00000425092.1; NM_016424.5; NP_057508.2.
DR UCSC; uc002isr.4; human. [O95232-1]
DR CTD; 51747; -.
DR DisGeNET; 51747; -.
DR GeneCards; LUC7L3; -.
DR HGNC; HGNC:24309; LUC7L3.
DR HPA; ENSG00000108848; Low tissue specificity.
DR MIM; 609434; gene.
DR neXtProt; NX_O95232; -.
DR OpenTargets; ENSG00000108848; -.
DR PharmGKB; PA165432062; -.
DR VEuPathDB; HostDB:ENSG00000108848; -.
DR eggNOG; KOG0796; Eukaryota.
DR GeneTree; ENSGT00950000183213; -.
DR HOGENOM; CLU_030397_0_1_1; -.
DR InParanoid; O95232; -.
DR OMA; DNSHYNQ; -.
DR PhylomeDB; O95232; -.
DR TreeFam; TF354312; -.
DR PathwayCommons; O95232; -.
DR SignaLink; O95232; -.
DR BioGRID-ORCS; 51747; 784 hits in 1083 CRISPR screens.
DR ChiTaRS; LUC7L3; human.
DR GeneWiki; CROP_(gene); -.
DR GenomeRNAi; 51747; -.
DR Pharos; O95232; Tbio.
DR PRO; PR:O95232; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O95232; protein.
DR Bgee; ENSG00000108848; Expressed in pylorus and 209 other tissues.
DR ExpressionAtlas; O95232; baseline and differential.
DR Genevisible; O95232; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR InterPro; IPR004882; Luc7-rel.
DR PANTHER; PTHR12375; PTHR12375; 1.
DR Pfam; PF03194; LUC7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; DNA-binding;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..432
FT /note="Luc7-like protein 3"
FT /id="PRO_0000058013"
FT REGION 234..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..181
FT /evidence="ECO:0000255"
FT COMPBIAS 234..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..363
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 56..79
FT /note="GPCEKIHDENLRKQYEKSSRFMKV -> DVFGRGDNISDVSKFLEDDKWMEE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018136"
FT VAR_SEQ 80..432
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018137"
FT CONFLICT 217
FT /note="H -> Y (in Ref. 3; BAA91981)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..379
FT /note="EK -> HE (in Ref. 6; AAC79807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 51466 MW; E75F55EC0137310C CRC64;
MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN TRSDLGPCEK
IHDENLRKQY EKSSRFMKVG YERDFLRYLQ SLLAEVERRI RRGHARLALS QNQQSSGAAG
PTGKNEEKIQ VLTDKIDVLL QQIEELGSEG KVEEAQGMMK LVEQLKEERE LLRSTTSTIE
SFAAQEKQME VCEVCGAFLI VGDAQSRVDD HLMGKQHMGY AKIKATVEEL KEKLRKRTEE
PDRDERLKKE KQEREEREKE REREREERER KRRREEEERE KERARDRERR KRSRSRSRHS
SRTSDRRCSR SRDHKRSRSR ERRRSRSRDR RRSRSHDRSE RKHRSRSRDR RRSKSRDRKS
YKHRSKSRDR EQDRKSKEKE KRGSDDKKSS VKSGSREKQS EDTNTESKES DTKNEVNGTS
EDIKSEGDTQ SN
