LC7L2_HUMAN
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 03-AUG-2022, entry version 182.
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};
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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; 267.
DR CORUM; Q9Y383; -.
DR DIP; DIP-32513N; -.
DR IntAct; Q9Y383; 140.
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; Q9Y383; -.
DR PeptideAtlas; Q9Y383; -.
DR PRIDE; Q9Y383; -.
DR ProteomicsDB; 6647; -.
DR ProteomicsDB; 85982; -. [Q9Y383-1]
DR ProteomicsDB; 85983; -. [Q9Y383-2]
DR Antibodypedia; 53629; 143 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 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; AHKADYE; -.
DR PhylomeDB; Q9Y383; -.
DR TreeFam; TF317607; -.
DR PathwayCommons; Q9Y383; -.
DR SignaLink; Q9Y383; -.
DR BioGRID-ORCS; 51631; 97 hits in 1028 CRISPR screens.
DR ChiTaRS; LUC7L2; human.
DR GeneWiki; LUC7L2; -.
DR GenomeRNAi; 51631; -.
DR Pharos; Q9Y383; Tdark.
DR PRO; PR:Q9Y383; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y383; protein.
DR Bgee; ENSG00000146963; Expressed in sural nerve and 189 other tissues.
DR ExpressionAtlas; Q9Y383; baseline and differential.
DR Genevisible; Q9Y383; HS.
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 selection; IBA:GO_Central.
DR InterPro; IPR004882; Luc7-rel.
DR PANTHER; PTHR12375; PTHR12375; 1.
DR Pfam; PF03194; LUC7; 1.
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
