LN28B_HUMAN
ID LN28B_HUMAN Reviewed; 250 AA.
AC Q6ZN17; A1L165; B2RPN6; Q5TCM4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein lin-28 homolog B;
DE Short=Lin-28B;
GN Name=LIN28B; Synonyms=CSDD2;
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] (ISOFORM 1).
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] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 1).
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 ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=16971064; DOI=10.1016/j.gene.2006.07.011;
RA Guo Y., Chen Y., Ito H., Watanabe A., Ge X., Kodama T., Aburatani H.;
RT "Identification and characterization of lin-28 homolog B (LIN28B) in human
RT hepatocellular carcinoma.";
RL Gene 384:51-61(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=18951094; DOI=10.1016/j.molcel.2008.09.014;
RA Heo I., Joo C., Cho J., Ha M., Han J., Kim V.N.;
RT "Lin28 mediates the terminal uridylation of let-7 precursor MicroRNA.";
RL Mol. Cell 32:276-284(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
RA Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J.,
RA Kim V.N.;
RT "TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-
RT microRNA uridylation.";
RL Cell 138:696-708(2009).
RN [10]
RP POSSIBLE INVOLVEMENT IN CANCERS.
RX PubMed=19483683; DOI=10.1038/ng.392;
RA Viswanathan S.R., Powers J.T., Einhorn W., Hoshida Y., Ng T.L.,
RA Toffanin S., O'Sullivan M., Lu J., Phillips L.A., Lockhart V.L., Shah S.P.,
RA Tanwar P.S., Mermel C.H., Beroukhim R., Azam M., Teixeira J., Meyerson M.,
RA Hughes T.P., Llovet J.M., Radich J., Mullighan C.G., Golub T.R.,
RA Sorensen P.H., Daley G.Q.;
RT "Lin28 promotes transformation and is associated with advanced human
RT malignancies.";
RL Nat. Genet. 41:843-848(2009).
RN [11]
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 [12]
RP FUNCTION IN PRE-LET-7 REPRESSION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
RA Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
RA Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
RT "Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
RT mechanisms.";
RL Cell 147:1066-1079(2011).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-96; SER-105; SER-110
RP AND SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=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 [15]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 24-111, AND ZINC KNUCKLE DOMAIN.
RX PubMed=22570413; DOI=10.1093/nar/gks355;
RA Mayr F., Schutz A., Doge N., Heinemann U.;
RT "The Lin28 cold-shock domain remodels pre-let-7 microRNA.";
RL Nucleic Acids Res. 40:7492-7506(2012).
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 (PubMed:22118463).
CC Does not act on pri-miR21 (PubMed:22118463). The repression of let-7
CC expression is required for normal development and contributes to
CC maintain the pluripotent state of embryonic stem cells by preventing
CC let-7-mediated differentiation. When overexpressed, recruits
CC ZCCHC11/TUT4 uridylyltransferase to pre-let-7 transcripts, leading to
CC their terminal uridylation and degradation (PubMed:19703396). This
CC activity might not be relevant in vivo, as LIN28B-mediated inhibition
CC of let-7 miRNA maturation appears to be ZCCHC11-independent
CC (PubMed:22118463). Interaction with target pre-miRNAs occurs via an 5'-
CC GGAG-3' motif in the pre-miRNA terminal loop. Mediates MYC-induced let-
CC 7 repression (By similarity). When overexpressed, isoform 1 stimulates
CC growth of the breast adenocarcinoma cell line MCF-7. Isoform 2 has no
CC effect on cell growth. {ECO:0000250|UniProtKB:Q45KJ6,
CC ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:18951094,
CC ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22118463}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus
CC {ECO:0000269|PubMed:22118463}. Cytoplasm {ECO:0000269|PubMed:16971064}.
CC Note=Predominantly nucleolar (PubMed:22118463). In Huh7 cells,
CC predominantly cytoplasmic, with only a subset of cells exhibiting
CC strong nuclear staining; however, the specificity of the polyclonal
CC antibody used in these experiments has not been not documented
CC (PubMed:16971064). {ECO:0000269|PubMed:16971064,
CC ECO:0000269|PubMed:22118463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZN17-1; Sequence=Displayed;
CC Name=2; Synonyms=LIN28BS;
CC IsoId=Q6ZN17-2; Sequence=VSP_027207;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the placenta and, at
CC mucher lower, in testis and fetal liver (PubMed:16971064). Isoform 1 is
CC only detected in placenta and in moderately and poorly differentiated
CC hepatocellular carcinoma cells (at protein level). Isoform 2 is
CC detected in fetal liver, non-tumor liver tissues, as well as well-
CC differentiated tumor tissues (at protein level). Tends to be up-
CC regulated in triple-negative (ER-,PR-,HER2-) breast tumors, as well as
CC in liver, ovarian, and thyroid carcinomas (PubMed:22118463).
CC {ECO:0000269|PubMed:16971064, ECO:0000269|PubMed:22118463}.
CC -!- INDUCTION: Might be negatively regulated by the microRNA let-7b.
CC {ECO:0000269|PubMed:16971064}.
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.
CC -!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LIN28BID45723ch6q16.html";
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DR EMBL; DQ127228; AAZ38897.1; -; mRNA.
DR EMBL; AK131411; BAD18558.1; -; mRNA.
DR EMBL; AL135911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48434.1; -; Genomic_DNA.
DR EMBL; BC127712; AAI27713.1; -; mRNA.
DR EMBL; BC127713; AAI27714.1; -; mRNA.
DR EMBL; BC137526; AAI37527.1; -; mRNA.
DR EMBL; BC137527; AAI37528.1; -; mRNA.
DR EMBL; BC141960; AAI41961.1; -; mRNA.
DR CCDS; CCDS34504.1; -. [Q6ZN17-1]
DR RefSeq; NP_001004317.1; NM_001004317.3. [Q6ZN17-1]
DR PDB; 4A4I; X-ray; 1.95 A; A/B=24-111.
DR PDBsum; 4A4I; -.
DR AlphaFoldDB; Q6ZN17; -.
DR SMR; Q6ZN17; -.
DR BioGRID; 133142; 342.
DR IntAct; Q6ZN17; 10.
DR STRING; 9606.ENSP00000344401; -.
DR ChEMBL; CHEMBL4295873; -.
DR iPTMnet; Q6ZN17; -.
DR PhosphoSitePlus; Q6ZN17; -.
DR BioMuta; LIN28B; -.
DR DMDM; 74758701; -.
DR EPD; Q6ZN17; -.
DR jPOST; Q6ZN17; -.
DR MassIVE; Q6ZN17; -.
DR MaxQB; Q6ZN17; -.
DR PaxDb; Q6ZN17; -.
DR PeptideAtlas; Q6ZN17; -.
DR PRIDE; Q6ZN17; -.
DR ProteomicsDB; 67959; -. [Q6ZN17-1]
DR ProteomicsDB; 67960; -. [Q6ZN17-2]
DR Antibodypedia; 32105; 324 antibodies from 36 providers.
DR DNASU; 389421; -.
DR Ensembl; ENST00000345080.5; ENSP00000344401.4; ENSG00000187772.8. [Q6ZN17-1]
DR GeneID; 389421; -.
DR KEGG; hsa:389421; -.
DR MANE-Select; ENST00000345080.5; ENSP00000344401.4; NM_001004317.4; NP_001004317.1.
DR UCSC; uc003pqv.2; human. [Q6ZN17-1]
DR CTD; 389421; -.
DR DisGeNET; 389421; -.
DR GeneCards; LIN28B; -.
DR HGNC; HGNC:32207; LIN28B.
DR HPA; ENSG00000187772; Tissue enriched (placenta).
DR MalaCards; LIN28B; -.
DR MIM; 611044; gene.
DR neXtProt; NX_Q6ZN17; -.
DR OpenTargets; ENSG00000187772; -.
DR Orphanet; 635; Neuroblastoma.
DR PharmGKB; PA142671543; -.
DR VEuPathDB; HostDB:ENSG00000187772; -.
DR eggNOG; KOG3070; Eukaryota.
DR GeneTree; ENSGT00940000153295; -.
DR HOGENOM; CLU_089169_1_1_1; -.
DR InParanoid; Q6ZN17; -.
DR OMA; GPWGNMA; -.
DR PhylomeDB; Q6ZN17; -.
DR TreeFam; TF316240; -.
DR PathwayCommons; Q6ZN17; -.
DR SignaLink; Q6ZN17; -.
DR SIGNOR; Q6ZN17; -.
DR BioGRID-ORCS; 389421; 42 hits in 1102 CRISPR screens.
DR ChiTaRS; LIN28B; human.
DR GenomeRNAi; 389421; -.
DR Pharos; Q6ZN17; Tbio.
DR PRO; PR:Q6ZN17; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6ZN17; protein.
DR Bgee; ENSG00000187772; Expressed in placenta and 36 other tissues.
DR ExpressionAtlas; Q6ZN17; baseline and differential.
DR Genevisible; Q6ZN17; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; IDA:CACAO.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; IDA:CACAO.
DR GO; GO:2000627; P:positive regulation of miRNA catabolic process; IMP:CACAO.
DR GO; GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0050779; P:RNA destabilization; IDA:CACAO.
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 3D-structure; Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing; Zinc; Zinc-finger.
FT CHAIN 1..250
FT /note="Protein lin-28 homolog B"
FT /id="PRO_0000253793"
FT DOMAIN 29..102
FT /note="CSD"
FT ZN_FING 127..144
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 149..166
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 112..125
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22118463"
FT MOTIF 239..250
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:22118463"
FT COMPBIAS 169..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027207"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:4A4I"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:4A4I"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:4A4I"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:4A4I"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4A4I"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4A4I"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4A4I"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4A4I"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4A4I"
SQ SEQUENCE 250 AA; 27084 MW; DEF2920C5F1D0BBD CRC64;
MAEGGASKGG GEEPGKLPEP AEEESQVLRG TGHCKWFNVR MGFGFISMIN REGSPLDIPV
DVFVHQSKLF MEGFRSLKEG EPVEFTFKKS SKGLESIRVT GPGGSPCLGS ERRPKGKTLQ
KRKPKGDRCY NCGGLDHHAK ECSLPPQPKK CHYCQSIMHM VANCPHKNVA QPPASSQGRQ
EAESQPCTST LPREVGGGHG CTSPPFPQEA RAEISERSGR SPQEASSTKS SIAPEEQSKK
GPSVQKRKKT
