LS14B_MOUSE
ID LS14B_MOUSE Reviewed; 385 AA.
AC Q8CGC4; A2AC71;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein LSM14 homolog B {ECO:0000303|PubMed:28458300};
DE AltName: Full=RNA-associated protein 55B {ECO:0000303|PubMed:18723115};
DE Short=mRAP55B {ECO:0000303|PubMed:18723115};
GN Name=Lsm14b {ECO:0000303|PubMed:28458300, ECO:0000312|MGI:MGI:3040677};
GN Synonyms=Fam61b, Rap55b {ECO:0000303|PubMed:18723115};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-351, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [6]
RP FUNCTION.
RX PubMed=28458300; DOI=10.1262/jrd.2017-018;
RA Zhang T., Li Y., Li H., Ma X.S., Ouyang Y.C., Hou Y., Schatten H.,
RA Sun Q.Y.;
RT "RNA-associated protein LSM family member 14 controls oocyte meiotic
RT maturation through regulating mRNA pools.";
RL J. Reprod. Dev. 63:383-388(2017).
CC -!- FUNCTION: Required for oocyte meiotic maturation (PubMed:28458300). May
CC be involved in the storage of translationally inactive mRNAs and
CC protect them from degradation (PubMed:28458300). Plays a role in
CC control of mRNA translation (By similarity).
CC {ECO:0000250|UniProtKB:Q68FI1, ECO:0000269|PubMed:28458300}.
CC -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex. Interacts with
CC DDX6. {ECO:0000250|UniProtKB:Q68FI1, ECO:0000250|UniProtKB:Q9BX40}.
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40823.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL663067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040823; AAH40823.1; ALT_INIT; mRNA.
DR CCDS; CCDS17165.2; -.
DR RefSeq; NP_808395.2; NM_177727.4.
DR AlphaFoldDB; Q8CGC4; -.
DR SMR; Q8CGC4; -.
DR BioGRID; 232352; 2.
DR STRING; 10090.ENSMUSP00000055036; -.
DR iPTMnet; Q8CGC4; -.
DR PhosphoSitePlus; Q8CGC4; -.
DR EPD; Q8CGC4; -.
DR jPOST; Q8CGC4; -.
DR MaxQB; Q8CGC4; -.
DR PaxDb; Q8CGC4; -.
DR PeptideAtlas; Q8CGC4; -.
DR PRIDE; Q8CGC4; -.
DR ProteomicsDB; 252534; -.
DR Antibodypedia; 52743; 62 antibodies from 13 providers.
DR DNASU; 241846; -.
DR Ensembl; ENSMUST00000055485; ENSMUSP00000055036; ENSMUSG00000039108.
DR GeneID; 241846; -.
DR KEGG; mmu:241846; -.
DR UCSC; uc008ohy.1; mouse.
DR CTD; 149986; -.
DR MGI; MGI:3040677; Lsm14b.
DR VEuPathDB; HostDB:ENSMUSG00000039108; -.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000156010; -.
DR HOGENOM; CLU_019221_0_0_1; -.
DR InParanoid; Q8CGC4; -.
DR OMA; HPRWSPY; -.
DR OrthoDB; 1569369at2759; -.
DR PhylomeDB; Q8CGC4; -.
DR TreeFam; TF313514; -.
DR BioGRID-ORCS; 241846; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q8CGC4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CGC4; protein.
DR Bgee; ENSMUSG00000039108; Expressed in secondary oocyte and 254 other tissues.
DR ExpressionAtlas; Q8CGC4; baseline and differential.
DR Genevisible; Q8CGC4; MM.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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 Acetylation; Developmental protein; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT CHAIN 2..385
FT /note="Protein LSM14 homolog B"
FT /id="PRO_0000187094"
FT DOMAIN 241..277
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 180..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..326
FT /note="FFD box"
FT MOTIF 330..350
FT /note="TFG box"
FT COMPBIAS 180..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT MOD_RES 351
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BX40"
FT CONFLICT 294
FT /note="A -> T (in Ref. 2; AAH40823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42310 MW; FCCD738676405904 CRC64;
MSGSSGTPYL GSKISLISKA QIRYEGILYT IDTDNSTVAL AKVRSFGTED RPTDRPAPPR
EEIYEYIIFR GSDIKDITVC EPPKAQHTLP QDPAIVQSSL GSASASPFQP HVPYSPFRGM
PPYGQLAASS LLSQQYAASL GLGAGFPSTP VGKSPMVEQA VQTSSVDNLN AKKLLPSKVT
SATQLNGRQA QPSSKPASDV VQPAPVHTQG QVNDENRRPP RRRSGNRRTR NRSRGQNRPT
NVKENTIKFE GDFDFESANA QFNREELDKE FKKKLNFKDD KADKGEEKDP AVMAQSEETA
AEEDLLGPNC YYDKSKSFFD NISSELKTSS RRTTWAEERK LNTETFGVSG RFLRGRSSRG
GFRGGRGNGT TRRNPTSHRA GTGRV
