LS14A_HUMAN
ID LS14A_HUMAN Reviewed; 463 AA.
AC Q8ND56; B4DTG6; Q76LX7; Q96AR3; Q96K73; Q96SN5; Q9UFR3;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein LSM14 homolog A {ECO:0000303|PubMed:26339800};
DE AltName: Full=Protein FAM61A;
DE AltName: Full=Protein SCD6 homolog;
DE AltName: Full=Putative alpha-synuclein-binding protein {ECO:0000303|Ref.1};
DE Short=AlphaSNBP {ECO:0000303|Ref.1};
DE AltName: Full=RNA-associated protein 55A {ECO:0000303|PubMed:17074753};
DE Short=hRAP55 {ECO:0000303|PubMed:17074753};
DE Short=hRAP55A;
GN Name=LSM14A {ECO:0000303|PubMed:26339800, ECO:0000312|HGNC:HGNC:24489};
GN Synonyms=C19orf13, FAM61A, RAP55 {ECO:0000303|PubMed:17074753}, RAP55A;
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] (ISOFORMS 1 AND 2).
RA Takeda K., Araki W., Tabira T.;
RT "Possible alpha synuclein binding protein.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP GLN-238.
RC TISSUE=Mammary gland, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-238.
RC TISSUE=Brain, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, 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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17074753; DOI=10.1074/jbc.m609059200;
RA Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.;
RT "RAP55, a cytoplasmic mRNP component, represses translation in Xenopus
RT oocytes.";
RL J. Biol. Chem. 281:40096-40106(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=16484376; DOI=10.1261/rna.2302706;
RA Yang W.H., Yu J.H., Gulick T., Bloch K.D., Bloch D.B.;
RT "RNA-associated protein 55 (RAP55) localizes to mRNA processing bodies and
RT stress granules.";
RL RNA 12:547-554(2006).
RN [9]
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; SER-192;
RP THR-194 AND SER-216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP REVIEW.
RX PubMed=18723115; DOI=10.1016/j.biocel.2008.06.015;
RA Marnef A., Sommerville J., Ladomery M.R.;
RT "RAP55: insights into an evolutionarily conserved protein family.";
RL Int. J. Biochem. Cell Biol. 41:977-981(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-192 AND SER-216, AND
RP IDENTIFICATION BY 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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-216, 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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-183; SER-192;
RP SER-216 AND SER-227, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP 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 [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26339800; DOI=10.18388/abp.2015_1107;
RA Mili D., Georgesse D., Kenani A.;
RT "Localization and role of RAP55/LSM14 in HeLa cells: a new finding on the
RT mitotic spindle assembly.";
RL Acta Biochim. Pol. 62:613-619(2015).
RN [25]
RP INTERACTION WITH EIF4ENIF1.
RX PubMed=26027925; DOI=10.1016/j.celrep.2015.04.065;
RA Nishimura T., Padamsi Z., Fakim H., Milette S., Dunham W.H., Gingras A.C.,
RA Fabian M.R.;
RT "The eIF4E-Binding protein 4E-T is a component of the mRNA decay machinery
RT that bridges the 5' and 3' termini of target mRNAs.";
RL Cell Rep. 11:1425-1436(2015).
RN [26]
RP INTERACTION WITH DDX6.
RX PubMed=31422817; DOI=10.1016/j.ajhg.2019.07.010;
RA Balak C., Benard M., Schaefer E., Iqbal S., Ramsey K., Ernoult-Lange M.,
RA Mattioli F., Llaci L., Geoffroy V., Courel M., Naymik M., Bachman K.K.,
RA Pfundt R., Rump P., Ter Beest J., Wentzensen I.M., Monaghan K.G.,
RA McWalter K., Richholt R., Le Bechec A., Jepsen W., De Both M., Belnap N.,
RA Boland A., Piras I.S., Deleuze J.F., Szelinger S., Dollfus H., Chelly J.,
RA Muller J., Campbell A., Lal D., Rangasamy S., Mandel J.L., Narayanan V.,
RA Huentelman M., Weil D., Piton A.;
RT "Rare de novo missense variants in RNA helicase DDX6 cause intellectual
RT disability and dysmorphic features and lead to P-body defects and RNA
RT dysregulation.";
RL Am. J. Hum. Genet. 105:509-525(2019).
RN [27]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4ENIF1.
RX PubMed=32354837; DOI=10.1101/gad.336073.119;
RA Raesch F., Weber R., Izaurralde E., Igreja C.;
RT "4E-T-bound mRNAs are stored in a silenced and deadenylated form.";
RL Genes Dev. 34:847-860(2020).
RN [28]
RP INTERACTION WITH DDX6.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
RN [29] {ECO:0007744|PDB:6F9W}
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 1-84 IN COMPLEX WITH EIF4ENIF1,
RP FUNCTION, INTERACTION WITH EIF4ENIF1; EDC4 AND DDX6, AND MUTAGENESIS OF
RP TYR-22; ILE-29; 296-PHE--PHE-298; PHE-305; 369-PHE--ASP-371;
RP 394-GLU--GLY-397 AND PHE-396.
RX PubMed=29510985; DOI=10.15252/embj.201797869;
RA Brandmann T., Fakim H., Padamsi Z., Youn J.Y., Gingras A.C., Fabian M.R.,
RA Jinek M.;
RT "Molecular architecture of LSM14 interactions involved in the assembly of
RT mRNA silencing complexes.";
RL EMBO J. 37:0-0(2018).
CC -!- FUNCTION: Essential for formation of P-bodies, cytoplasmic structures
CC that provide storage sites for translationally inactive mRNAs and
CC protect them from degradation (PubMed:16484376, PubMed:17074753,
CC PubMed:29510985). Acts as a repressor of mRNA translation
CC (PubMed:29510985). May play a role in mitotic spindle assembly
CC (PubMed:26339800). {ECO:0000269|PubMed:16484376,
CC ECO:0000269|PubMed:17074753, ECO:0000269|PubMed:26339800,
CC ECO:0000269|PubMed:29510985}.
CC -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex (By
CC similarity). Interacts with DDX6 (PubMed:31422817, PubMed:29510985,
CC PubMed:31439631). Interacts with EIF4ENIF1/4E-T; promoting
CC EIF4ENIF1/4E-T localization to P-bodies (PubMed:26027925,
CC PubMed:32354837, PubMed:29510985). Interacts (via FFD box) with EDC4
CC (PubMed:29510985). {ECO:0000250|UniProtKB:A0A8M2,
CC ECO:0000269|PubMed:26027925, ECO:0000269|PubMed:29510985,
CC ECO:0000269|PubMed:31422817, ECO:0000269|PubMed:31439631,
CC ECO:0000269|PubMed:32354837}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16484376,
CC ECO:0000269|PubMed:17074753, ECO:0000269|PubMed:32354837}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:26339800}. Cytoplasm, Stress
CC granule {ECO:0000269|PubMed:16484376}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=AlphaSNBP(A);
CC IsoId=Q8ND56-1; Sequence=Displayed;
CC Name=2; Synonyms=AlphaSNBP(B);
CC IsoId=Q8ND56-2; Sequence=VSP_014650;
CC Name=3;
CC IsoId=Q8ND56-3; Sequence=VSP_057232;
CC -!- DOMAIN: The LSM14 domain and the RGG repeats are required for
CC accumulation in P-bodies, and the region containing the FDF motif is
CC responsible for cytoplasmic retention. {ECO:0000269|PubMed:16484376}.
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55066.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB069974; BAC99045.1; -; mRNA.
DR EMBL; AB069975; BAC99046.1; -; mRNA.
DR EMBL; AK027369; BAB55066.1; ALT_INIT; mRNA.
DR EMBL; AK027643; BAB55259.1; -; mRNA.
DR EMBL; AK300208; BAG61978.1; -; mRNA.
DR EMBL; AL834398; CAD39060.2; -; mRNA.
DR EMBL; AL117499; CAB55964.1; -; mRNA.
DR EMBL; AC010614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016842; AAH16842.1; -; mRNA.
DR CCDS; CCDS12435.1; -. [Q8ND56-2]
DR CCDS; CCDS46040.1; -. [Q8ND56-1]
DR PIR; T17274; T17274.
DR RefSeq; NP_001107565.1; NM_001114093.1. [Q8ND56-1]
DR RefSeq; NP_056393.2; NM_015578.2. [Q8ND56-2]
DR PDB; 6F9W; X-ray; 2.62 A; A=1-84.
DR PDBsum; 6F9W; -.
DR AlphaFoldDB; Q8ND56; -.
DR SMR; Q8ND56; -.
DR BioGRID; 117527; 175.
DR IntAct; Q8ND56; 46.
DR MINT; Q8ND56; -.
DR STRING; 9606.ENSP00000446271; -.
DR GlyGen; Q8ND56; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8ND56; -.
DR PhosphoSitePlus; Q8ND56; -.
DR BioMuta; LSM14A; -.
DR EPD; Q8ND56; -.
DR jPOST; Q8ND56; -.
DR MassIVE; Q8ND56; -.
DR MaxQB; Q8ND56; -.
DR PaxDb; Q8ND56; -.
DR PeptideAtlas; Q8ND56; -.
DR PRIDE; Q8ND56; -.
DR ProteomicsDB; 5108; -.
DR ProteomicsDB; 72979; -. [Q8ND56-1]
DR ProteomicsDB; 72980; -. [Q8ND56-2]
DR Antibodypedia; 47950; 170 antibodies from 29 providers.
DR DNASU; 26065; -.
DR Ensembl; ENST00000433627.9; ENSP00000413964.3; ENSG00000257103.9. [Q8ND56-1]
DR Ensembl; ENST00000540746.6; ENSP00000446451.1; ENSG00000257103.9. [Q8ND56-3]
DR Ensembl; ENST00000544216.8; ENSP00000446271.2; ENSG00000257103.9. [Q8ND56-2]
DR Ensembl; ENST00000570462.5; ENSP00000459843.1; ENSG00000262860.5. [Q8ND56-1]
DR Ensembl; ENST00000575811.5; ENSP00000461225.1; ENSG00000262860.5. [Q8ND56-2]
DR GeneID; 26065; -.
DR KEGG; hsa:26065; -.
DR MANE-Select; ENST00000544216.8; ENSP00000446271.2; NM_015578.4; NP_056393.2. [Q8ND56-2]
DR UCSC; uc002nva.5; human. [Q8ND56-1]
DR CTD; 26065; -.
DR DisGeNET; 26065; -.
DR GeneCards; LSM14A; -.
DR HGNC; HGNC:24489; LSM14A.
DR HPA; ENSG00000257103; Low tissue specificity.
DR MIM; 610677; gene.
DR neXtProt; NX_Q8ND56; -.
DR OpenTargets; ENSG00000257103; -.
DR PharmGKB; PA134989467; -.
DR VEuPathDB; HostDB:ENSG00000257103; -.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000154415; -.
DR InParanoid; Q8ND56; -.
DR OMA; WYPPPGH; -.
DR OrthoDB; 1569369at2759; -.
DR PhylomeDB; Q8ND56; -.
DR TreeFam; TF313514; -.
DR PathwayCommons; Q8ND56; -.
DR SignaLink; Q8ND56; -.
DR BioGRID-ORCS; 26065; 93 hits in 1076 CRISPR screens.
DR ChiTaRS; LSM14A; human.
DR GenomeRNAi; 26065; -.
DR Pharos; Q8ND56; Tbio.
DR PRO; PR:Q8ND56; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8ND56; protein.
DR Bgee; ENSG00000257103; Expressed in ventricular zone and 105 other tissues.
DR ExpressionAtlas; Q8ND56; baseline and differential.
DR Genevisible; Q8ND56; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IDA:UniProtKB.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0039529; P:RIG-I signaling pathway; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR CDD; cd01736; LSm14_N; 1.
DR InterPro; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR025761; FFD_box.
DR InterPro; IPR025609; Lsm14-like_N.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR025768; TFG_box.
DR Pfam; PF09532; FDF; 1.
DR Pfam; PF12701; LSM14; 1.
DR SMART; SM01199; FDF; 1.
DR SMART; SM01271; LSM14; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51513; FFD; 1.
DR PROSITE; PS51536; TFG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Developmental protein; Methylation; Phosphoprotein; Reference proteome;
KW Repressor; Ribonucleoprotein; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..463
FT /note="Protein LSM14 homolog A"
FT /id="PRO_0000187090"
FT DOMAIN 284..320
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 147..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 361..377
FT /note="FFD box"
FT MOTIF 380..400
FT /note="TFG box"
FT COMPBIAS 147..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 192
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 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 401
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2F8"
FT VAR_SEQ 139..179
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057232"
FT VAR_SEQ 458..463
FT /note="TTAFGP -> DNKVAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_014650"
FT VARIANT 238
FT /note="R -> Q (in dbSNP:rs36006556)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_057532"
FT VARIANT 448
FT /note="R -> Q (in dbSNP:rs2274896)"
FT /id="VAR_022884"
FT MUTAGEN 22
FT /note="Y->E: Abolished interaction with EIF4ENIF1/4E-T
FT without affecting interaction with DDX6; when associated
FT with E-29."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 29
FT /note="I->E: Abolished interaction with EIF4ENIF1/4E-T
FT without affecting interaction with DDX6; when associated
FT with E-22."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 296..298
FT /note="FDF->ADA: Abolished interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 305
FT /note="F->A: Abolished interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 369..371
FT /note="FFD->AAA: Does not affect interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 394..397
FT /note="ETFG->AAAA: Abolished interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:29510985"
FT MUTAGEN 396
FT /note="F->A: Abolished interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:29510985"
FT CONFLICT 17
FT /note="K -> Q (in Ref. 3; CAD39060)"
FT /evidence="ECO:0000305"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:6F9W"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:6F9W"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:6F9W"
FT STRAND 35..46
FT /evidence="ECO:0007829|PDB:6F9W"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:6F9W"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6F9W"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6F9W"
SQ SEQUENCE 463 AA; 50530 MW; 703BE8E8C54799DF CRC64;
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS STSSFQSMGS YGPFGRMPTY
SQFSPSSLVG QQFGAVGVAG SSLTSFGTET SNSGTLPQSS AVGSAFTQDT RSLKTQLSQG
RSSPQLDPLR KSPTMEQAVQ TASAHLPAPA AVGRRSPVST RPLPSASQKA GENQEHRRAE
VHKVSRPENE QLRNDNKRQV APGAPSAPRR GRGGHRGGRG RFGIRRDGPM KFEKDFDFES
ANAQFNKEEI DREFHNKLKL KEDKLEKQEK PVNGEDKGDS GVDTQNSEGN ADEEDPLGPN
CYYDKTKSFF DNISCDDNRE RRPTWAEERR LNAETFGIPL RPNRGRGGYR GRGGLGFRGG
RGRGGGRGGT FTAPRGFRGG FRGGRGGREF ADFEYRKTTA FGP
