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Protein lin-28 homolog A (Lin-28A) (Zinc finger CCHC domain-containing protein 1)

 LN28A_HUMAN             Reviewed;         209 AA.
Q9H9Z2;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-DEC-2017, entry version 150.
RecName: Full=Protein lin-28 homolog A;
Short=Lin-28A;
AltName: Full=Zinc finger CCHC domain-containing protein 1;
Name=LIN28A; Synonyms=CSDD1, LIN28, ZCCHC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12798299; DOI=10.1016/S0012-1606(03)00126-X;
Moss E.G., Tang L.;
"Conservation of the heterochronic regulator Lin-28, its developmental
expression and microRNA complementary sites.";
Dev. Biol. 258:432-442(2003).
[2]
ERRATUM.
Moss E.G., Tang L.;
Dev. Biol. 262:361-361(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[6]
INDUCTION.
PubMed=15003116; DOI=10.1186/gb-2004-5-3-r13;
Sempere L.F., Freemantle S., Pitha-Rowe I., Moss E.G., Dmitrovsky E.,
Ambros V.;
"Expression profiling of mammalian microRNAs uncovers a subset of
brain-expressed microRNAs with possible roles in murine and human
neuronal differentiation.";
Genome Biol. 5:R13.1-R13.11(2004).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=14688391; DOI=10.1634/stemcells.22-1-51;
Richards M., Tan S.-P., Tan J.-H., Chan W.-K., Bongso A.;
"The transcriptome profile of human embryonic stem cells as defined by
SAGE.";
Stem Cells 22:51-64(2004).
[8]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15614775; DOI=10.1002/dvdy.20247;
Gerecht-Nir S., Dazard J.-E., Golan-Mashiach M., Osenberg S.,
Botvinnik A., Amariglio N., Domany E., Rechavi G., Givol D.,
Itskovitz-Eldor J.;
"Vascular gene expression and phenotypic correlation during
differentiation of human embryonic stem cells.";
Dev. Dyn. 232:487-497(2005).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15722555; DOI=10.1074/jbc.M412247200;
Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.;
"Depletion of human micro-RNA miR-125b reveals that it is critical for
the proliferation of differentiated cells but not for the down-
regulation of putative targets during differentiation.";
J. Biol. Chem. 280:16635-16641(2005).
[10]
INDUCTION.
PubMed=16227573; DOI=10.1128/MCB.25.21.9198-9208.2005;
Wu L., Belasco J.G.;
"Micro-RNA regulation of the mammalian lin-28 gene during neuronal
differentiation of embryonal carcinoma cells.";
Mol. Cell. Biol. 25:9198-9208(2005).
[11]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-46; PHE-55; PHE-73;
HIS-147 AND HIS-169.
PubMed=17617744; DOI=10.4161/rna.4.1.4364;
Balzer E., Moss E.G.;
"Localization of the developmental timing regulator Lin28 to mRNP
complexes, P-bodies and stress granules.";
RNA Biol. 4:16-25(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND MUTAGENESIS OF
HIS-147 AND HIS-169.
PubMed=18951094; DOI=10.1016/j.molcel.2008.09.014;
Heo I., Joo C., Cho J., Ha M., Han J., Kim V.N.;
"Lin28 mediates the terminal uridylation of let-7 precursor
MicroRNA.";
Mol. Cell 32:276-284(2008).
[13]
FUNCTION IN PRE-MIRNA URIDYLATION, RNA-BINDING, AND INTERACTION WITH
ZCCHC11.
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
[14]
POSSIBLE INVOLVEMENT IN CANCERS.
PubMed=19483683; DOI=10.1038/ng.392;
Viswanathan S.R., Powers J.T., Einhorn W., Hoshida Y., Ng T.L.,
Toffanin S., O'Sullivan M., Lu J., Phillips L.A., Lockhart V.L.,
Shah S.P., Tanwar P.S., Mermel C.H., Beroukhim R., Azam M.,
Teixeira J., Meyerson M., Hughes T.P., Llovet J.M., Radich J.,
Mullighan C.G., Golub T.R., Sorensen P.H., Daley G.Q.;
"Lin28 promotes transformation and is associated with advanced human
malignancies.";
Nat. Genet. 41:843-848(2009).
[15]
FUNCTION IN PRE-LET-7 URIDYLATION, INTERACTION WITH ZCCHC11,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22118463; DOI=10.1016/j.cell.2011.10.039;
Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J.,
Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.;
"Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct
mechanisms.";
Cell 147:1066-1079(2011).
[16]
FUNCTION IN MRNA TRANSLATION, AND INTERACTION WITH DHX9.
PubMed=21247876; DOI=10.1093/nar/gkq1350;
Jin J., Jing W., Lei X.X., Feng C., Peng S., Boris-Lawrie K.,
Huang Y.;
"Evidence that Lin28 stimulates translation by recruiting RNA helicase
A to polysomes.";
Nucleic Acids Res. 39:3724-3734(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3; SER-120 AND SER-200, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[19]
FUNCTION IN PRE-LET-7 URIDYLATION.
PubMed=22898984; DOI=10.1261/rna.034538.112;
Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
"Lin28-mediated control of let-7 microRNA expression by alternative
TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RNA 18:1875-1885(2012).
[20]
STRUCTURE BY NMR OF 134-186.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the zinc-finger domain in LIN-28.";
Submitted (NOV-2005) to the PDB data bank.
[21]
STRUCTURE BY NMR OF 124-186 IN COMPLEX WITH SHORT RNA, AND CONSENSUS
MOTIF.
PubMed=22157959; DOI=10.1038/nsmb.2202;
Loughlin F.E., Gebert L.F., Towbin H., Brunschweiger A., Hall J.,
Allain F.H.;
"Structural basis of pre-let-7 miRNA recognition by the zinc knuckles
of pluripotency factor Lin28.";
Nat. Struct. Mol. Biol. 19:84-89(2012).
-!- FUNCTION: RNA-binding protein that inhibits processing of pre-let-
7 miRNAs and regulates translation of mRNAs that control
developmental timing, pluripotency and metabolism
(PubMed:21247876). Seems to recognize a common structural G-
quartet (G4) feature in its miRNA and mRNA targets (Probable).
'Translational enhancer' that drives specific mRNAs to polysomes
and increases the efficiency of protein synthesis. Its association
with the translational machinery and target mRNAs results in an
increased number of initiation events per molecule of mRNA and,
indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA,
ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for
skeletal muscle differentiation program through the translational
up-regulation of IGF2 expression. Suppressor of microRNA (miRNA)
biogenesis, including that of let-7, miR107, miR-143 and miR-200c.
Specifically binds the miRNA precursors (pre-miRNAs), recognizing
an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits
ZCCHC11/TUT4 uridylyltransferase. This results in the terminal
uridylation of target pre-miRNAs. Uridylated pre-miRNAs fail to be
processed by Dicer and undergo degradation. The repression of let-
7 expression is required for normal development and contributes to
maintain the pluripotent state by preventing let-7-mediated
differentiation of embryonic stem cells (PubMed:18951094,
PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to
the periendoplasmic reticulum area, binds to a large number of
spliced mRNAs and inhibits the translation of mRNAs destined for
the ER, reducing the synthesis of transmembrane proteins, ER or
Golgi lumen proteins, and secretory proteins. Binds to and
enhances the translation of mRNAs for several metabolic enzymes,
such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative
phosphorylation. Which, with the let-7 repression may enhance
tissue repair in adult tissue (By similarity).
{ECO:0000250|UniProtKB:Q8K3Y3, ECO:0000269|PubMed:18951094,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:21247876,
ECO:0000269|PubMed:22118463, ECO:0000269|PubMed:22898984,
ECO:0000305}.
-!- SUBUNIT: Monomer (By similarity). During skeletal muscle
differentiation, associated with translation initiation complexes
in the polysomal compartment (PubMed:21247876). Directly interacts
with EIF3S2 (By similarity). Interacts with NCL in an RNA-
dependent manner (By similarity). Interacts (via C-terminus) with
DHX9 (via N- and C-terminus); this interaction occurs in a RNA-
independent manner (PubMed:21247876). Interacts with ZCCHC11/TUT4
in the presence of pre-let-7 RNA (PubMed:19703396,
PubMed:22118463). {ECO:0000250, ECO:0000250|UniProtKB:Q8K3Y3,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:21247876,
ECO:0000269|PubMed:22118463, ECO:0000269|PubMed:22157959}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18951094,
ECO:0000269|PubMed:22118463}. Rough endoplasmic reticulum
{ECO:0000250|UniProtKB:Q8K3Y3}. Cytoplasm, P-body
{ECO:0000269|PubMed:17617744}. Cytoplasm, Stress granule
{ECO:0000269|PubMed:17617744}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q8K3Y3}. Note=Predominantly cytoplasmic
(PubMed:22118463). In the cytoplasm, localizes to peri-endoplasmic
reticulum regions and detected in the microsomal fraction derived
from rough endoplasmic reticulum (RER) following subcellular
fractionation. May be bound to the cytosolic surface of RER on
which ER-associated mRNAs are translated (By similarity). Shuttle
from the nucleus to the cytoplasm requires RNA-binding
(PubMed:17617744). Nucleolar localization is observed in 10-15% of
the nuclei in differentiated myotubes (By similarity).
{ECO:0000250|UniProtKB:Q8K3Y3, ECO:0000269|PubMed:17617744,
ECO:0000269|PubMed:22118463}.
-!- TISSUE SPECIFICITY: Expressed in embryonic stem cells, placenta
and testis. Tends to be up-regulated in HER2-overexpressing breast
tumors. {ECO:0000269|PubMed:14688391, ECO:0000269|PubMed:15614775,
ECO:0000269|PubMed:15722555, ECO:0000269|PubMed:22118463}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal liver. Expression
decreases during differentiation of ES cells or upon induction of
neuronal differentiation by retinoic acid.
{ECO:0000269|PubMed:14688391, ECO:0000269|PubMed:15614775,
ECO:0000269|PubMed:15722555}.
-!- INDUCTION: Can be negatively regulated by the interaction of
microRNAs miR-125a and miR-125b with at least two miRNA responsive
elements (miREs) in the 3'-UTR of this gene. These interactions
may reduce both translation efficiency and mRNA abundance.
Negatively regulated by retinoic acid.
{ECO:0000269|PubMed:15003116, ECO:0000269|PubMed:16227573}.
-!- DOMAIN: The CSD domain is required for function in muscle
differentiation. {ECO:0000250}.
-!- DOMAIN: The CCHC zinc fingers interact with the GGAG motif at the
3' end of let-7 miRNAs precursors, more generally they bind the
5'-NGNNG-3' consensus motif with micromolar affinity. The CSD
domain recognizes the loop at the 5' end. The flexible linker
allows accommodating variable sequences and lengths among let-7
family members.
-!- MISCELLANEOUS: Overexpressed in primary tumors (overall frequency
approximately 15%), overexpression being linked to repression of
let-7 family miRNAs and derepression of let-7 targets. Facilitates
cellular transformation in vitro, and overexpression is associated
with advanced disease across multiple tumor types.
-!- MISCELLANEOUS: Reactivation of LIN28A expression enhances tissue
repair in some adult tissues by reprogramming cellular
bioenergetics. Improves hair regrowth by promoting anagen in hair
follicle and accelerates regrowth of cartilage, bone and
mesenchyme after ear and digit injuries.
{ECO:0000250|UniProtKB:Q8K3Y3}.
-!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
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EMBL; AF521099; AAM77751.1; -; mRNA.
EMBL; AK022519; BAB14075.1; -; mRNA.
EMBL; AL513365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028566; AAH28566.1; -; mRNA.
CCDS; CCDS280.1; -.
RefSeq; NP_078950.1; NM_024674.5.
RefSeq; XP_011540450.1; XM_011542148.1.
UniGene; Hs.86154; -.
PDB; 2CQF; NMR; -; A=137-186.
PDB; 2LI8; NMR; -; A=124-186.
PDB; 5UDZ; X-ray; 2.00 A; A/B=31-187.
PDBsum; 2CQF; -.
PDBsum; 2LI8; -.
PDBsum; 5UDZ; -.
ProteinModelPortal; Q9H9Z2; -.
SMR; Q9H9Z2; -.
BioGrid; 122842; 89.
IntAct; Q9H9Z2; 2.
STRING; 9606.ENSP00000254231; -.
iPTMnet; Q9H9Z2; -.
PhosphoSitePlus; Q9H9Z2; -.
BioMuta; LIN28A; -.
DMDM; 74752750; -.
EPD; Q9H9Z2; -.
PaxDb; Q9H9Z2; -.
PeptideAtlas; Q9H9Z2; -.
PRIDE; Q9H9Z2; -.
DNASU; 79727; -.
Ensembl; ENST00000254231; ENSP00000254231; ENSG00000131914.
Ensembl; ENST00000326279; ENSP00000363314; ENSG00000131914.
GeneID; 79727; -.
KEGG; hsa:79727; -.
UCSC; uc001bmj.4; human.
CTD; 79727; -.
DisGeNET; 79727; -.
EuPathDB; HostDB:ENSG00000131914.10; -.
GeneCards; LIN28A; -.
HGNC; HGNC:15986; LIN28A.
HPA; CAB020785; -.
MIM; 611043; gene.
neXtProt; NX_Q9H9Z2; -.
OpenTargets; ENSG00000131914; -.
PharmGKB; PA165751523; -.
eggNOG; KOG3070; Eukaryota.
eggNOG; COG1278; LUCA.
GeneTree; ENSGT00880000137959; -.
HOGENOM; HOG000047091; -.
HOVERGEN; HBG081922; -.
InParanoid; Q9H9Z2; -.
KO; K18754; -.
OMA; SGICKWF; -.
OrthoDB; EOG091G0RTY; -.
PhylomeDB; Q9H9Z2; -.
TreeFam; TF316240; -.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
SignaLink; Q9H9Z2; -.
EvolutionaryTrace; Q9H9Z2; -.
GeneWiki; LIN28; -.
GenomeRNAi; 79727; -.
PRO; PR:Q9H9Z2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000131914; -.
CleanEx; HS_LIN28; -.
Genevisible; Q9H9Z2; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:1905538; F:polysome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:BHF-UCL.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
GO; GO:0045686; P:negative regulation of glial cell differentiation; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:1901724; P:positive regulation of cell proliferation involved in kidney development; IEA:Ensembl.
GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISS:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:BHF-UCL.
GO; GO:0032008; P:positive regulation of TOR signaling; ISS:BHF-UCL.
GO; GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0031123; P:RNA 3'-end processing; IMP:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
CDD; cd04458; CSP_CDS; 1.
Gene3D; 4.10.60.10; -; 2.
InterPro; IPR011129; CSD.
InterPro; IPR002059; CSP_DNA-bd.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00313; CSD; 1.
Pfam; PF00098; zf-CCHC; 1.
PRINTS; PR00050; COLDSHOCK.
SMART; SM00357; CSP; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895}.
CHAIN 2 209 Protein lin-28 homolog A.
/FTId=PRO_0000253787.
DOMAIN 39 112 CSD.
ZN_FING 137 154 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 159 176 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 113 136 Flexible linker.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MUTAGEN 46 46 W->A: Does not affect localization to P-
bodies; when associated with A-55 and A-
73. {ECO:0000269|PubMed:17617744}.
MUTAGEN 55 55 F->A: Does not affect localization to P-
bodies; when associated with A-46 and A-
73. {ECO:0000269|PubMed:17617744}.
MUTAGEN 73 73 F->A: Does not affect localization to P-
bodies; when associated with A-46 and A-
55. {ECO:0000269|PubMed:17617744}.
MUTAGEN 147 147 H->A: Abolishes ability to suppress pre-
let-7 biogenesis and localization to P-
bodies without affecting pre-let-7
binding; when associated with A-169.
{ECO:0000269|PubMed:17617744,
ECO:0000269|PubMed:18951094}.
MUTAGEN 169 169 H->A: Abolishes ability to suppress pre-
let-7 biogenesis and localization to P-
bodies without affecting pre-let-7
binding; when associated with A-147.
{ECO:0000269|PubMed:17617744,
ECO:0000269|PubMed:18951094}.
STRAND 36 48 {ECO:0000244|PDB:5UDZ}.
TURN 49 52 {ECO:0000244|PDB:5UDZ}.
STRAND 53 61 {ECO:0000244|PDB:5UDZ}.
STRAND 64 75 {ECO:0000244|PDB:5UDZ}.
HELIX 76 78 {ECO:0000244|PDB:5UDZ}.
STRAND 81 84 {ECO:0000244|PDB:5UDZ}.
STRAND 92 100 {ECO:0000244|PDB:5UDZ}.
STRAND 103 111 {ECO:0000244|PDB:5UDZ}.
HELIX 112 114 {ECO:0000244|PDB:5UDZ}.
TURN 124 126 {ECO:0000244|PDB:5UDZ}.
TURN 140 142 {ECO:0000244|PDB:5UDZ}.
STRAND 145 147 {ECO:0000244|PDB:2CQF}.
HELIX 149 151 {ECO:0000244|PDB:5UDZ}.
TURN 162 164 {ECO:0000244|PDB:5UDZ}.
STRAND 167 169 {ECO:0000244|PDB:2CQF}.
HELIX 171 173 {ECO:0000244|PDB:5UDZ}.
HELIX 175 178 {ECO:0000244|PDB:5UDZ}.
SEQUENCE 209 AA; 22743 MW; FA5EF6DD33FABF54 CRC64;
MGSVSNQQFA GGCAKAAEEA PEEAPEDAAR AADEPQLLHG AGICKWFNVR MGFGFLSMTA
RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS AKGLESIRVT GPGGVFCIGS
ERRPKGKSMQ KRRSKGDRCY NCGGLDHHAK ECKLPPQPKK CHFCQSISHM VASCPLKAQQ
GPSAQGKPTY FREEEEEIHS PTLLPEAQN


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