LUC7L_HUMAN
ID LUC7L_HUMAN Reviewed; 371 AA.
AC Q9NQ29; B8ZZ13; Q96S32; Q9NPH4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Putative RNA-binding protein Luc7-like 1;
DE AltName: Full=Putative SR protein LUC7B1;
DE AltName: Full=SR+89;
GN Name=LUC7L; Synonyms=LUC7L1;
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 (ISOFORM 2).
RA Utsch B., Albers N., Wickert L., Bidlingmaier F., Ludwig M.;
RT "SR+89, a gene encoding a serine/arginine-rich protein, is widely
RT transcribed from human chromosome 16p13.3 proximal to the alpha-globin
RT cluster. Exclusion of this new gene as a candidate gene for the hypospadic
RT phenotype associated with homozygous SEA-alpha-thalassaemia.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11170747; DOI=10.1006/geno.2000.6394;
RA Tufarelli C., Frischauf A.-M., Hardison R., Flint J., Higgs D.R.;
RT "Characterization of a widely expressed gene (LUC7-LIKE; LUC7L) defining
RT the centromeric boundary of the human alpha-globin domain.";
RL Genomics 71:307-314(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
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=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Blood, and Lung;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION BY
RP 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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-336 AND SER-363, AND
RP 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).
CC -!- FUNCTION: May bind to RNA via its Arg/Ser-rich domain.
CC {ECO:0000269|PubMed:11170747}.
CC -!- INTERACTION:
CC Q9NQ29; Q8IWX8: CHERP; NbExp=2; IntAct=EBI-473747, EBI-2555370;
CC Q9NQ29; Q9NQ29: LUC7L; NbExp=2; IntAct=EBI-473747, EBI-473747;
CC Q9NQ29; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-473747, EBI-5235340;
CC Q9NQ29; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-473747, EBI-539478;
CC Q9NQ29; P78362: SRPK2; NbExp=3; IntAct=EBI-473747, EBI-593303;
CC Q9NQ29-3; Q13247: SRSF6; NbExp=3; IntAct=EBI-6654742, EBI-745230;
CC Q9NQ29-3; Q16629: SRSF7; NbExp=3; IntAct=EBI-6654742, EBI-398885;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQ29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ29-2; Sequence=VSP_010215;
CC Name=3;
CC IsoId=Q9NQ29-3; Sequence=VSP_010214;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11170747}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
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DR EMBL; AJ404326; CAB93981.1; -; mRNA.
DR EMBL; AJ404326; CAB93982.1; -; mRNA.
DR EMBL; AY005111; AAG22846.1; -; mRNA.
DR EMBL; AE006462; AAK61218.1; -; Genomic_DNA.
DR EMBL; AK001093; BAA91500.1; -; mRNA.
DR EMBL; Z69890; CAM26671.1; -; Genomic_DNA.
DR EMBL; Z69706; CAM26671.1; JOINED; Genomic_DNA.
DR EMBL; CH471112; EAW85853.1; -; Genomic_DNA.
DR EMBL; BC003194; AAH03194.1; -; mRNA.
DR EMBL; BC065198; AAH65198.1; -; mRNA.
DR CCDS; CCDS10401.1; -. [Q9NQ29-2]
DR CCDS; CCDS32348.1; -. [Q9NQ29-1]
DR RefSeq; NP_001307155.1; NM_001320226.1. [Q9NQ29-2]
DR RefSeq; NP_001317349.1; NM_001330420.1.
DR RefSeq; NP_060502.1; NM_018032.4. [Q9NQ29-2]
DR RefSeq; NP_958815.1; NM_201412.2. [Q9NQ29-1]
DR AlphaFoldDB; Q9NQ29; -.
DR SMR; Q9NQ29; -.
DR BioGRID; 120818; 231.
DR IntAct; Q9NQ29; 90.
DR MINT; Q9NQ29; -.
DR STRING; 9606.ENSP00000293872; -.
DR iPTMnet; Q9NQ29; -.
DR MetOSite; Q9NQ29; -.
DR PhosphoSitePlus; Q9NQ29; -.
DR BioMuta; LUC7L; -.
DR DMDM; 47116932; -.
DR EPD; Q9NQ29; -.
DR jPOST; Q9NQ29; -.
DR MassIVE; Q9NQ29; -.
DR MaxQB; Q9NQ29; -.
DR PaxDb; Q9NQ29; -.
DR PeptideAtlas; Q9NQ29; -.
DR PRIDE; Q9NQ29; -.
DR ProteomicsDB; 82058; -. [Q9NQ29-1]
DR ProteomicsDB; 82059; -. [Q9NQ29-2]
DR ProteomicsDB; 82060; -. [Q9NQ29-3]
DR Antibodypedia; 22529; 210 antibodies from 23 providers.
DR DNASU; 55692; -.
DR Ensembl; ENST00000293872.13; ENSP00000293872.8; ENSG00000007392.17. [Q9NQ29-1]
DR Ensembl; ENST00000337351.8; ENSP00000337507.4; ENSG00000007392.17. [Q9NQ29-2]
DR Ensembl; ENST00000397783.5; ENSP00000380885.1; ENSG00000007392.17. [Q9NQ29-2]
DR GeneID; 55692; -.
DR KEGG; hsa:55692; -.
DR MANE-Select; ENST00000293872.13; ENSP00000293872.8; NM_201412.3; NP_958815.1.
DR UCSC; uc002cga.2; human. [Q9NQ29-1]
DR CTD; 55692; -.
DR DisGeNET; 55692; -.
DR GeneCards; LUC7L; -.
DR HGNC; HGNC:6723; LUC7L.
DR HPA; ENSG00000007392; Low tissue specificity.
DR MIM; 607782; gene.
DR neXtProt; NX_Q9NQ29; -.
DR OpenTargets; ENSG00000007392; -.
DR PharmGKB; PA30485; -.
DR VEuPathDB; HostDB:ENSG00000007392; -.
DR eggNOG; KOG0796; Eukaryota.
DR GeneTree; ENSGT00950000183213; -.
DR HOGENOM; CLU_030397_3_1_1; -.
DR InParanoid; Q9NQ29; -.
DR OMA; LGYVKMR; -.
DR OrthoDB; 1499212at2759; -.
DR PhylomeDB; Q9NQ29; -.
DR TreeFam; TF317607; -.
DR PathwayCommons; Q9NQ29; -.
DR SignaLink; Q9NQ29; -.
DR BioGRID-ORCS; 55692; 10 hits in 1081 CRISPR screens.
DR ChiTaRS; LUC7L; human.
DR GeneWiki; LUC7L; -.
DR GenomeRNAi; 55692; -.
DR Pharos; Q9NQ29; Tbio.
DR PRO; PR:Q9NQ29; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NQ29; protein.
DR Bgee; ENSG00000007392; Expressed in tendon of biceps brachii and 191 other tissues.
DR ExpressionAtlas; Q9NQ29; baseline and differential.
DR Genevisible; Q9NQ29; HS.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0050733; F:RS domain binding; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..371
FT /note="Putative RNA-binding protein Luc7-like 1"
FT /id="PRO_0000187280"
FT REGION 232..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..177
FT /evidence="ECO:0000255"
FT COILED 218..259
FT /evidence="ECO:0000255"
FT COMPBIAS 232..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..321
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..20
FT /note="MSAQAQMRALLDQLMGTARD -> MQM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010214"
FT VAR_SEQ 326..371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010215"
FT CONFLICT 171
FT /note="E -> V (in Ref. 3; AAK61218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 43728 MW; C277F424F5F5659C CRC64;
MSAQAQMRAL LDQLMGTARD GDETRQRVKF TDDRVCKSHL LDCCPHDILA GTRMDLGECT
KIHDLALRAD YEIASKERDL FFELDAMDHL ESFIAECDRR TELAKKRLAE TQEEISAEVS
AKAEKVHELN EEIGKLLAKA EQLGAEGNVD ESQKILMEVE KVRAKKKEAE EEYRNSMPAS
SFQQQKLRVC EVCSAYLGLH DNDRRLADHF GGKLHLGFIQ IREKLDQLRK TVAEKQEKRN
QDRLRRREER EREERLSRRS GSRTRDRRRS RSRDRRRRRS RSTSRERRKL SRSRSRDRHR
RHRSRSRSHS RGHRRASRDR SAKYKFSRER ASREESWESG RSERGPPDWR LESSNGKMAS
RRSEEKEAGE I
