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 27-MAR-2024, entry version 174. 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}; 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; 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; 174. DR CORUM; O95232; -. DR IntAct; O95232; 39. DR MINT; O95232; -. DR STRING; 9606.ENSP00000376919; -. DR CarbonylDB; O95232; -. DR GlyGen; O95232; 5 sites, 1 O-linked glycan (5 sites). 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; 9606-ENSP00000425092; -. DR PeptideAtlas; O95232; -. DR ProteomicsDB; 50730; -. [O95232-1] DR ProteomicsDB; 50731; -. [O95232-2] DR Pumba; O95232; -. DR Antibodypedia; 18160; 125 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 AGR; HGNC:24309; -. 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; CTRIHDE; -. DR OrthoDB; 3145682at2759; -. DR PhylomeDB; O95232; -. DR TreeFam; TF354312; -. DR PathwayCommons; O95232; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; O95232; -. DR BioGRID-ORCS; 51747; 819 hits in 1163 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 211 other cell types or tissues. DR ExpressionAtlas; O95232; baseline and differential. 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 recognition; IBA:GO_Central. DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB. DR InterPro; IPR004882; Luc7-rel. DR PANTHER; PTHR12375:SF47; LUC7-LIKE PROTEIN 3; 1. DR PANTHER; PTHR12375; RNA-BINDING PROTEIN LUC7-RELATED; 1. DR Pfam; PF03194; LUC7; 1. DR Genevisible; O95232; HS. 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 //