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Putative RNA-binding protein Luc7-like 2

 LC7L2_HUMAN             Reviewed;         392 AA.
Q9Y383; B7Z500; Q8IUP9; Q9NVL3; Q9NVN7; Q9UQN1;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Putative RNA-binding protein Luc7-like 2;
Name=LUC7L2; ORFNames=CGI-59, CGI-74;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
HYDROXYLATION AT LYS-266 AND LYS-269, AND MUTAGENESIS OF LYS-266 AND
LYS-269.
PubMed=19574390; DOI=10.1126/science.1175865;
Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,
Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,
Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,
Boettger A.;
"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated
with RNA splicing.";
Science 325:90-93(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: May bind to RNA via its Arg/Ser-rich domain.
-!- SUBUNIT: Interacts with SCNM1. {ECO:0000250}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=5; IntAct=EBI-352851, EBI-743771;
Q9GZQ8:MAP1LC3B; NbExp=3; IntAct=EBI-352851, EBI-373144;
P23511:NFYA; NbExp=3; IntAct=EBI-352851, EBI-389739;
Q96SB4:SRPK1; NbExp=2; IntAct=EBI-352851, EBI-539478;
P78362:SRPK2; NbExp=2; IntAct=EBI-352851, EBI-593303;
Q13247:SRSF6; NbExp=5; IntAct=EBI-352851, EBI-745230;
Q16629:SRSF7; NbExp=5; IntAct=EBI-352851, EBI-398885;
-!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus,
nucleoplasm {ECO:0000250}. Note=Colocalizes with SCNM1 and SNRNP70
in nuclear speckles. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y383-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y383-2; Sequence=VSP_010217;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9Y383-3; Sequence=VSP_044896;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the Luc7 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD34069.1; Type=Frameshift; Positions=388; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF151817; AAD34054.1; -; mRNA.
EMBL; AF151832; AAD34069.1; ALT_FRAME; mRNA.
EMBL; AK001476; BAA91713.1; -; mRNA.
EMBL; AK001519; BAA91737.1; -; mRNA.
EMBL; AK022895; BAB14297.1; -; mRNA.
EMBL; AK298166; BAH12736.1; -; mRNA.
EMBL; BC017163; AAH17163.1; -; mRNA.
EMBL; BC042625; AAH42625.1; -; mRNA.
EMBL; BC050708; AAH50708.1; -; mRNA.
EMBL; BC056886; AAH56886.1; -; mRNA.
CCDS; CCDS43656.1; -. [Q9Y383-1]
CCDS; CCDS59085.1; -. [Q9Y383-3]
CCDS; CCDS59510.1; -. [Q9Y383-2]
RefSeq; NP_001231514.1; NM_001244585.1. [Q9Y383-3]
RefSeq; NP_001257572.1; NM_001270643.1. [Q9Y383-2]
RefSeq; NP_057103.2; NM_016019.4. [Q9Y383-1]
UniGene; Hs.731488; -.
ProteinModelPortal; Q9Y383; -.
SMR; Q9Y383; -.
BioGrid; 119646; 173.
CORUM; Q9Y383; -.
DIP; DIP-32513N; -.
IntAct; Q9Y383; 65.
MINT; MINT-5006732; -.
STRING; 9606.ENSP00000347005; -.
iPTMnet; Q9Y383; -.
PhosphoSitePlus; Q9Y383; -.
SwissPalm; Q9Y383; -.
BioMuta; LUC7L2; -.
DMDM; 47116960; -.
EPD; Q9Y383; -.
PaxDb; Q9Y383; -.
PeptideAtlas; Q9Y383; -.
PRIDE; Q9Y383; -.
DNASU; 51631; -.
Ensembl; ENST00000263545; ENSP00000263545; ENSG00000146963. [Q9Y383-3]
Ensembl; ENST00000354926; ENSP00000347005; ENSG00000146963. [Q9Y383-1]
Ensembl; ENST00000541170; ENSP00000441604; ENSG00000146963. [Q9Y383-3]
Ensembl; ENST00000619796; ENSP00000483438; ENSG00000146963. [Q9Y383-2]
GeneID; 51631; -.
KEGG; hsa:51631; -.
UCSC; uc003vux.5; human. [Q9Y383-1]
CTD; 51631; -.
EuPathDB; HostDB:ENSG00000146963.17; -.
GeneCards; LUC7L2; -.
HGNC; HGNC:21608; LUC7L2.
HPA; HPA051631; -.
MIM; 613056; gene.
neXtProt; NX_Q9Y383; -.
OpenTargets; ENSG00000146963; -.
PharmGKB; PA134873425; -.
eggNOG; KOG0796; Eukaryota.
eggNOG; COG5200; LUCA.
GeneTree; ENSGT00730000110670; -.
HOVERGEN; HBG062167; -.
InParanoid; Q9Y383; -.
KO; K13212; -.
OrthoDB; EOG091G0PSO; -.
PhylomeDB; Q9Y383; -.
TreeFam; TF317607; -.
ChiTaRS; LUC7L2; human.
GeneWiki; LUC7L2; -.
GenomeRNAi; 51631; -.
PMAP-CutDB; Q9Y383; -.
PRO; PR:Q9Y383; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000146963; -.
CleanEx; HS_LUC7L2; -.
ExpressionAtlas; Q9Y383; baseline and differential.
Genevisible; Q9Y383; HS.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
InterPro; IPR004882; Luc7-rel.
PANTHER; PTHR12375; PTHR12375; 1.
Pfam; PF03194; LUC7; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Hydroxylation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 392 Putative RNA-binding protein Luc7-like 2.
/FTId=PRO_0000187282.
COILED 102 177 {ECO:0000255}.
COMPBIAS 239 388 Arg/Ser-rich.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 266 266 5-hydroxylysine; by JMJD6.
{ECO:0000269|PubMed:19574390}.
MOD_RES 269 269 5-hydroxylysine; by JMJD6.
{ECO:0000269|PubMed:19574390}.
VAR_SEQ 1 21 MSAQAQMRAMLDQLMGTSRDG -> MPAYLNLQGSVRKAPH
SPSR (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010217.
VAR_SEQ 1 20 MSAQAQMRAMLDQLMGTSRD -> MVIHSQLKKIQGASERM
(in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044896.
VARIANT 361 361 D -> E (in dbSNP:rs3757435).
/FTId=VAR_034067.
MUTAGEN 266 266 K->R: Induces a decrease in lysyl-
hydroxylation. Abolishes lysyl-
hydroxylation; when associated with R-
269. {ECO:0000269|PubMed:19574390}.
MUTAGEN 269 269 K->R: Induces a decrease in lysyl-
hydroxylation. Abolishes lysyl-
hydroxylation; when associated with R-
266. {ECO:0000269|PubMed:19574390}.
CONFLICT 27 27 R -> Q (in Ref. 2; BAA91737).
{ECO:0000305}.
CONFLICT 389 390 AG -> QR (in Ref. 1; AAD34054).
{ECO:0000305}.
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


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