ID LC7L2_HUMAN Reviewed; 392 AA. AC Q9Y383; B7Z500; Q8IUP9; Q9NVL3; Q9NVN7; Q9UQN1; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 27-MAR-2024, entry version 191. DE RecName: Full=Putative RNA-binding protein Luc7-like 2; GN Name=LUC7L2; ORFNames=CGI-59, CGI-74; 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 [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Skin, and Uterus; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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 [6] RP HYDROXYLATION AT LYS-266 AND LYS-269, AND MUTAGENESIS OF LYS-266 AND RP LYS-269. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, 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 [11] 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). CC -!- FUNCTION: May bind to RNA via its Arg/Ser-rich domain. CC -!- SUBUNIT: Interacts with SCNM1. {ECO:0000250|UniProtKB:Q7TNC4}. CC -!- INTERACTION: CC Q9Y383; Q92624: APPBP2; NbExp=6; IntAct=EBI-352851, EBI-743771; CC Q9Y383; Q86YF9: DZIP1; NbExp=3; IntAct=EBI-352851, EBI-998108; CC Q9Y383; P42858: HTT; NbExp=9; IntAct=EBI-352851, EBI-466029; CC Q9Y383; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-352851, EBI-373144; CC Q9Y383; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-352851, EBI-16439278; CC Q9Y383; P23511: NFYA; NbExp=4; IntAct=EBI-352851, EBI-389739; CC Q9Y383; P23511-2: NFYA; NbExp=3; IntAct=EBI-352851, EBI-11061759; CC Q9Y383; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-352851, EBI-539478; CC Q9Y383; P78362: SRPK2; NbExp=3; IntAct=EBI-352851, EBI-593303; CC Q9Y383; A7MD48: SRRM4; NbExp=6; IntAct=EBI-352851, EBI-3867173; CC Q9Y383; Q13247: SRSF6; NbExp=7; IntAct=EBI-352851, EBI-745230; CC Q9Y383; Q16629: SRSF7; NbExp=7; IntAct=EBI-352851, EBI-398885; CC Q9Y383; Q15696: ZRSR2; NbExp=3; IntAct=EBI-352851, EBI-6657923; CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q7TNC4}. CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7TNC4}. Note=Colocalizes CC with SCNM1 and SNRNP70 in nuclear speckles. CC {ECO:0000250|UniProtKB:Q7TNC4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y383-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y383-2; Sequence=VSP_010217; CC Name=3; CC IsoId=Q9Y383-3; Sequence=VSP_044896; CC -!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD34069.1; 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; AF151817; AAD34054.1; -; mRNA. DR EMBL; AF151832; AAD34069.1; ALT_FRAME; mRNA. DR EMBL; AK001476; BAA91713.1; -; mRNA. DR EMBL; AK001519; BAA91737.1; -; mRNA. DR EMBL; AK022895; BAB14297.1; -; mRNA. DR EMBL; AK298166; BAH12736.1; -; mRNA. DR EMBL; BC017163; AAH17163.1; -; mRNA. DR EMBL; BC042625; AAH42625.1; -; mRNA. DR EMBL; BC050708; AAH50708.1; -; mRNA. DR EMBL; BC056886; AAH56886.1; -; mRNA. DR CCDS; CCDS43656.1; -. [Q9Y383-1] DR CCDS; CCDS59085.1; -. [Q9Y383-3] DR CCDS; CCDS59510.1; -. [Q9Y383-2] DR RefSeq; NP_001231514.1; NM_001244585.1. [Q9Y383-3] DR RefSeq; NP_001257572.1; NM_001270643.1. [Q9Y383-2] DR RefSeq; NP_057103.2; NM_016019.4. [Q9Y383-1] DR AlphaFoldDB; Q9Y383; -. DR SMR; Q9Y383; -. DR BioGRID; 119646; 353. DR CORUM; Q9Y383; -. DR DIP; DIP-32513N; -. DR IntAct; Q9Y383; 142. DR MINT; Q9Y383; -. DR STRING; 9606.ENSP00000347005; -. DR GlyGen; Q9Y383; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y383; -. DR MetOSite; Q9Y383; -. DR PhosphoSitePlus; Q9Y383; -. DR SwissPalm; Q9Y383; -. DR BioMuta; LUC7L2; -. DR DMDM; 47116960; -. DR EPD; Q9Y383; -. DR jPOST; Q9Y383; -. DR MassIVE; Q9Y383; -. DR MaxQB; Q9Y383; -. DR PaxDb; 9606-ENSP00000347005; -. DR PeptideAtlas; Q9Y383; -. DR ProteomicsDB; 6647; -. DR ProteomicsDB; 85982; -. [Q9Y383-1] DR ProteomicsDB; 85983; -. [Q9Y383-2] DR Pumba; Q9Y383; -. DR Antibodypedia; 53629; 155 antibodies from 26 providers. DR DNASU; 51631; -. DR Ensembl; ENST00000263545.7; ENSP00000263545.7; ENSG00000146963.18. [Q9Y383-3] DR Ensembl; ENST00000354926.9; ENSP00000347005.4; ENSG00000146963.18. [Q9Y383-1] DR Ensembl; ENST00000541170.7; ENSP00000441604.1; ENSG00000146963.18. [Q9Y383-3] DR Ensembl; ENST00000619796.4; ENSP00000483438.1; ENSG00000146963.18. [Q9Y383-2] DR GeneID; 51631; -. DR KEGG; hsa:51631; -. DR MANE-Select; ENST00000354926.9; ENSP00000347005.4; NM_016019.5; NP_057103.2. DR UCSC; uc003vux.5; human. [Q9Y383-1] DR AGR; HGNC:21608; -. DR CTD; 51631; -. DR DisGeNET; 51631; -. DR GeneCards; LUC7L2; -. DR HGNC; HGNC:21608; LUC7L2. DR HPA; ENSG00000146963; Low tissue specificity. DR MIM; 613056; gene. DR neXtProt; NX_Q9Y383; -. DR OpenTargets; ENSG00000146963; -. DR PharmGKB; PA134873425; -. DR VEuPathDB; HostDB:ENSG00000146963; -. DR eggNOG; KOG0796; Eukaryota. DR GeneTree; ENSGT00950000183213; -. DR HOGENOM; CLU_030397_3_0_1; -. DR InParanoid; Q9Y383; -. DR OMA; CENEIDQ; -. DR PhylomeDB; Q9Y383; -. DR TreeFam; TF317607; -. DR PathwayCommons; Q9Y383; -. DR SignaLink; Q9Y383; -. DR BioGRID-ORCS; 51631; 103 hits in 1089 CRISPR screens. DR ChiTaRS; LUC7L2; human. DR GeneWiki; LUC7L2; -. DR GenomeRNAi; 51631; -. DR Pharos; Q9Y383; Tbio. DR PRO; PR:Q9Y383; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9Y383; Protein. DR Bgee; ENSG00000146963; Expressed in sural nerve and 191 other cell types or tissues. DR ExpressionAtlas; Q9Y383; baseline and differential. DR GO; GO:0016607; C:nuclear speck; ISS: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:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006376; P:mRNA splice site recognition; IBA:GO_Central. DR InterPro; IPR004882; Luc7-rel. DR PANTHER; PTHR12375:SF28; RNA-BINDING PROTEIN LUC7-LIKE 2-RELATED; 1. DR PANTHER; PTHR12375; RNA-BINDING PROTEIN LUC7-RELATED; 1. DR Pfam; PF03194; LUC7; 1. DR Genevisible; Q9Y383; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Hydroxylation; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..392 FT /note="Putative RNA-binding protein Luc7-like 2" FT /id="PRO_0000187282" FT REGION 235..392 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 102..177 FT /evidence="ECO:0000255" FT COMPBIAS 235..261 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 262..328 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 329..392 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 266 FT /note="5-hydroxylysine; by JMJD6" FT /evidence="ECO:0000269|PubMed:19574390" FT MOD_RES 269 FT /note="5-hydroxylysine; by JMJD6" FT /evidence="ECO:0000269|PubMed:19574390" FT VAR_SEQ 1..21 FT /note="MSAQAQMRAMLDQLMGTSRDG -> MPAYLNLQGSVRKAPHSPSR (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010217" FT VAR_SEQ 1..20 FT /note="MSAQAQMRAMLDQLMGTSRD -> MVIHSQLKKIQGASERM (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044896" FT VARIANT 361 FT /note="D -> E (in dbSNP:rs3757435)" FT /id="VAR_034067" FT MUTAGEN 266 FT /note="K->R: Induces a decrease in lysyl-hydroxylation. FT Abolishes lysyl-hydroxylation; when associated with R-269." FT /evidence="ECO:0000269|PubMed:19574390" FT MUTAGEN 269 FT /note="K->R: Induces a decrease in lysyl-hydroxylation. FT Abolishes lysyl-hydroxylation; when associated with R-266." FT /evidence="ECO:0000269|PubMed:19574390" FT CONFLICT 27 FT /note="R -> Q (in Ref. 2; BAA91737)" FT /evidence="ECO:0000305" FT CONFLICT 389..390 FT /note="AG -> QR (in Ref. 1; AAD34054)" FT /evidence="ECO:0000305" SQ SEQUENCE 392 AA; 46514 MW; 1C559CCE0F23F693 CRC64; MSAQAQMRAM LDQLMGTSRD GDTTRQRIKF SDDRVCKSHL LNCCPHDVLS GTRMDLGECL KVHDLALRAD YEIASKEQDF FFELDAMDHL QSFIADCDRR TEVAKKRLAE TQEEISAEVA AKAERVHELN EEIGKLLAKV EQLGAEGNVE ESQKVMDEVE KARAKKREAE EVYRNSMPAS SFQQQKLRVC EVCSAYLGLH DNDRRLADHF GGKLHLGFIE IREKLEELKR VVAEKQEKRN QERLKRREER EREEREKLRR SRSHSKNPKR SRSREHRRHR SRSMSRERKR RTRSKSREKR HRHRSRSSSR SRSRSHQRSR HSSRDRSRER SKRRSSKERF RDQDLASCDR DRSSRDRSPR DRDRKDKKRS YESANGRSED RRSSEEREAG EI //