LN28B_MOUSE
ID LN28B_MOUSE Reviewed; 247 AA.
AC Q45KJ6; Q3UZC6; Q3V444;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein lin-28 homolog B;
DE Short=Lin-28B;
GN Name=Lin28b;
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 [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RA Moss E.G., Kemper K.;
RT "Expression of Lin28A and Lin28B in post-implantation mouse embryos.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 FUNCTION IN MYC-MEDIATED LET-7 REPRESSION.
RX PubMed=19211792; DOI=10.1073/pnas.0808300106;
RA Chang T.-C., Zeitels L.R., Hwang H.-W., Chivukula R.R., Wentzel E.A.,
RA Dews M., Jung J., Gao P., Dang C.V., Beer M.A., Thomas-Tikhonenko A.,
RA Mendell J.T.;
RT "Lin-28B transactivation is necessary for Myc-mediated let-7 repression and
RT proliferation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3384-3389(2009).
CC -!- FUNCTION: Suppressor of microRNA (miRNA) biogenesis, including that of
CC let-7 and possibly of miR107, miR-143 and miR-200c. Binds primary let-7
CC transcripts (pri-let-7), including pri-let-7g and pri-let-7a-1, and
CC sequester them in the nucleolus, away from the microprocessor complex,
CC hence preventing their processing into mature miRNA. Does not act on
CC pri-miR21. The repression of let-7 expression is required for normal
CC development and contributes to maintain the pluripotent state of
CC embryonic stem cells by preventing let-7-mediated differentiation. When
CC overexpressed, recruits ZCCHC11/TUT4 uridylyltransferase to pre-let-7
CC transcripts, leading to their terminal uridylation and degradation.
CC This activity might not be relevant in vivo, as LIN28B-mediated
CC inhibition of let-7 miRNA maturation appears to be ZCCHC11-independent.
CC Interaction with target pre-miRNAs occurs via an 5'-GGAG-3' motif in
CC the pre-miRNA terminal loop (By similarity). Mediates MYC-induced let-7
CC repression (PubMed:19211792). When overexpressed, may stimulate growth
CC of carcinoma cell lines (By similarity). {ECO:0000250|UniProtKB:Q6ZN17,
CC ECO:0000269|PubMed:19211792}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q6ZN17}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q45KJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q45KJ6-2; Sequence=VSP_021119;
CC Name=3;
CC IsoId=Q45KJ6-3; Sequence=VSP_021115, VSP_021119, VSP_021120,
CC VSP_021121;
CC Name=4;
CC IsoId=Q45KJ6-4; Sequence=VSP_021116, VSP_021117, VSP_021118;
CC -!- DOMAIN: The tandem zinc fingers, also referred as zinc knuckle domain
CC (ZKD), mediate specific binding to the GGAG/GGUG motif while the CSD
CC shows only limited pyrimidine-rich sequence specificity. Both domains
CC bind single-stranded nucleic acids (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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DR EMBL; DQ127225; AAZ38894.1; -; mRNA.
DR EMBL; AK133928; BAE21931.1; -; mRNA.
DR EMBL; AK012973; BAE43235.1; -; mRNA.
DR EMBL; AC153847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089037; AAH89037.1; -; mRNA.
DR CCDS; CCDS35895.1; -. [Q45KJ6-2]
DR RefSeq; NP_001026942.1; NM_001031772.2. [Q45KJ6-2]
DR RefSeq; XP_011241490.1; XM_011243188.1. [Q45KJ6-2]
DR AlphaFoldDB; Q45KJ6; -.
DR SMR; Q45KJ6; -.
DR DIP; DIP-48572N; -.
DR IntAct; Q45KJ6; 1.
DR STRING; 10090.ENSMUSP00000078361; -.
DR iPTMnet; Q45KJ6; -.
DR PhosphoSitePlus; Q45KJ6; -.
DR MaxQB; Q45KJ6; -.
DR PeptideAtlas; Q45KJ6; -.
DR PRIDE; Q45KJ6; -.
DR ProteomicsDB; 292346; -. [Q45KJ6-1]
DR ProteomicsDB; 292347; -. [Q45KJ6-2]
DR ProteomicsDB; 292348; -. [Q45KJ6-3]
DR ProteomicsDB; 292349; -. [Q45KJ6-4]
DR Antibodypedia; 32105; 324 antibodies from 36 providers.
DR DNASU; 380669; -.
DR Ensembl; ENSMUST00000079390; ENSMUSP00000078361; ENSMUSG00000063804. [Q45KJ6-2]
DR GeneID; 380669; -.
DR KEGG; mmu:380669; -.
DR UCSC; uc007faa.2; mouse. [Q45KJ6-2]
DR UCSC; uc007fab.1; mouse. [Q45KJ6-3]
DR CTD; 389421; -.
DR MGI; MGI:3584032; Lin28b.
DR VEuPathDB; HostDB:ENSMUSG00000063804; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153295; -.
DR HOGENOM; CLU_089169_1_1_1; -.
DR InParanoid; Q45KJ6; -.
DR OMA; GPWGNMA; -.
DR OrthoDB; 1604809at2759; -.
DR PhylomeDB; Q45KJ6; -.
DR TreeFam; TF316240; -.
DR BioGRID-ORCS; 380669; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lin28b; mouse.
DR PRO; PR:Q45KJ6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q45KJ6; protein.
DR Bgee; ENSMUSG00000063804; Expressed in embryonic post-anal tail and 59 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; ISO:MGI.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:MGI.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISO:MGI.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0050779; P:RNA destabilization; ISO:MGI.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00313; CSD; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS51857; CSD_2; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing; Zinc;
KW Zinc-finger.
FT CHAIN 1..247
FT /note="Protein lin-28 homolog B"
FT /id="PRO_0000253794"
FT DOMAIN 27..100
FT /note="CSD"
FT ZN_FING 125..142
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 147..164
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN17"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN17"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN17"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021115"
FT VAR_SEQ 1..3
FT /note="MAE -> MHLVPLLANILNVLQKMMRSFNQGSSAP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021116"
FT VAR_SEQ 65..71
FT /note="SKLFMEG -> LFPPSHH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021117"
FT VAR_SEQ 72..247
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021118"
FT VAR_SEQ 125
FT /note="D -> DRWRRQDLLMDQMWTVREEESRMIP (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_021119"
FT VAR_SEQ 127..152
FT /note="CYNCGGLDHHAKECSLPPQPKKCHYC -> FVWLGQQERRRDRFPRWGKLQD
FT GLGV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021120"
FT VAR_SEQ 153..247
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021121"
SQ SEQUENCE 247 AA; 26903 MW; 5ECB233AF2FA6DDF CRC64;
MAEGGASKGE EPEKLPGLAE DEPQVLHGTG HCKWFNVRMG FGFISMISRE GNPLDIPVDV
FVHQSKLFME GFRSLKEGEP VEFTFKKSPK GLESIRVTGP GGSPCLGSER RPKGKTLQKR
KPKGDRCYNC GGLDHHAKEC SLPPQPKKCH YCQSIMHMVA NCPHKLAAQL PASSQGRQEA
ESQPCSSAAP REVGGGHGCT VLFPQEVKSE MAEHSDRSPQ EVSSTKAFAA IGEQNKKGPL
IQKRKKT
