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Q9H9Z2

- LN28A_HUMAN

UniProt

Q9H9Z2 - LN28A_HUMAN

Protein

Protein lin-28 homolog A

Gene

LIN28A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing 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 stabilizing the mRNAs. 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 By similarity. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells. In contrast, LIN28A down-regulation in neural stem cells by miR-125, allows the processing of pre-let-7. Specifically recognizes the 5'-GGAG-3' motif in the terminal loop of pre-let-7. Also recognizes and binds non pre-let-7 pre-miRNAs that contain the 5'-GGAG-3' motif in the terminal loop, leading to their terminal uridylation and subsequent degradation.By similarity2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri137 – 15418CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri159 – 17618CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. miRNA binding Source: Ensembl
    3. mRNA binding Source: Ensembl
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. germ cell development Source: Ensembl
    2. miRNA catabolic process Source: UniProtKB
    3. negative regulation of glial cell differentiation Source: Ensembl
    4. positive regulation of neuron differentiation Source: Ensembl
    5. positive regulation of translation Source: Ensembl
    6. pre-miRNA processing Source: UniProtKB
    7. regulation of gene silencing by miRNA Source: Ensembl
    8. regulation of transcription, DNA-templated Source: InterPro
    9. RNA 3'-end processing Source: UniProtKB
    10. stem cell maintenance Source: UniProtKB

    Keywords - Biological processi

    RNA-mediated gene silencing

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinkiQ9H9Z2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein lin-28 homolog A
    Short name:
    Lin-28A
    Alternative name(s):
    Zinc finger CCHC domain-containing protein 1
    Gene namesi
    Name:LIN28A
    Synonyms:CSDD1, LIN28, ZCCHC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:15986. LIN28A.

    Subcellular locationi

    Cytoplasm. Nucleusnucleolus
    Note: Nucleolar localization observed in 10-15% of the nuclei in differentiated myotubes By similarity. Shuttles between the cytoplasm and the nucleus. Localizes to cytoplasmic processing bodies and stress granules.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytoplasmic mRNA processing body Source: UniProtKB
    3. cytoplasmic stress granule Source: UniProtKB
    4. nucleolus Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461W → A: Does not affect localization to cytoplasmic processing bodies; when associated with A-55 and A-73. 1 Publication
    Mutagenesisi55 – 551F → A: Does not affect localization to cytoplasmic processing bodies; when associated with A-46 and A-73. 1 Publication
    Mutagenesisi73 – 731F → A: Does not affect localization to cytoplasmic processing bodies; when associated with A-46 and A-55. 1 Publication
    Mutagenesisi147 – 1471H → A: Abolishes ability to suppress pre-let-7 biogenesis and localization to cytoplasmic processing bodies without affecting pre-let-7 binding; when associated with A-169. 2 Publications
    Mutagenesisi169 – 1691H → A: Abolishes ability to suppress pre-let-7 biogenesis and localization to cytoplasmic processing bodies without affecting pre-let-7 binding; when associated with A-147. 2 Publications

    Organism-specific databases

    PharmGKBiPA165751523.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 209208Protein lin-28 homolog APRO_0000253787Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine2 Publications
    Modified residuei3 – 31Phosphoserine1 Publication
    Modified residuei120 – 1201Phosphoserine1 Publication
    Modified residuei200 – 2001Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9H9Z2.
    PRIDEiQ9H9Z2.

    PTM databases

    PhosphoSiteiQ9H9Z2.

    Expressioni

    Tissue specificityi

    Expressed in embryonic stem cells (ES cells), placenta and testis.3 Publications

    Developmental stagei

    Expressed in fetal liver. Expression decreases during differentiation of ES cells or upon induction of neuronal differentiation by retinoic acid.3 Publications

    Inductioni

    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.2 Publications

    Gene expression databases

    BgeeiQ9H9Z2.
    CleanExiHS_LIN28.
    GenevestigatoriQ9H9Z2.

    Organism-specific databases

    HPAiCAB020785.

    Interactioni

    Subunit structurei

    Monomer. During skeletal muscle differentiation, associated with translation initiation complexes in the polysomal compartment. Directly interacts with EIF3S2. Interaction with NCL is RNA-dependent By similarity. Interacts with ZCCHC11/TUT4.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi122842. 84 interactions.
    IntActiQ9H9Z2. 2 interactions.
    STRINGi9606.ENSP00000254231.

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi140 – 1423
    Beta strandi145 – 1473
    Turni149 – 1513
    Turni162 – 1643
    Beta strandi167 – 1693
    Turni171 – 1733
    Helixi176 – 1783

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQFNMR-A137-186[»]
    2LI8NMR-A124-186[»]
    ProteinModelPortaliQ9H9Z2.
    SMRiQ9H9Z2. Positions 34-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H9Z2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 11274CSDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni113 – 13624Flexible linkerAdd
    BLAST

    Domaini

    The CSD domain is required for function in muscle differentiation.By similarity
    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.

    Sequence similaritiesi

    Belongs to the lin-28 family.Curated
    Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 CSD (cold-shock) domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri137 – 15418CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri159 – 17618CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244191.
    HOGENOMiHOG000047091.
    HOVERGENiHBG081922.
    InParanoidiQ9H9Z2.
    OMAiSGICKWF.
    OrthoDBiEOG72JWJ8.
    PhylomeDBiQ9H9Z2.
    TreeFamiTF316240.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    4.10.60.10. 1 hit.
    InterProiIPR011129. Cold_shock_prot.
    IPR002059. CSP_DNA-bd.
    IPR012340. NA-bd_OB-fold.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00313. CSD. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    PRINTSiPR00050. COLDSHOCK.
    SMARTiSM00357. CSP. 1 hit.
    SM00343. ZnF_C2HC. 2 hits.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9H9Z2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSVSNQQFA GGCAKAAEEA PEEAPEDAAR AADEPQLLHG AGICKWFNVR    50
    MGFGFLSMTA RAGVALDPPV DVFVHQSKLH MEGFRSLKEG EAVEFTFKKS 100
    AKGLESIRVT GPGGVFCIGS ERRPKGKSMQ KRRSKGDRCY NCGGLDHHAK 150
    ECKLPPQPKK CHFCQSISHM VASCPLKAQQ GPSAQGKPTY FREEEEEIHS 200
    PTLLPEAQN 209
    Length:209
    Mass (Da):22,743
    Last modified:March 1, 2001 - v1
    Checksum:iFA5EF6DD33FABF54
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF521099 mRNA. Translation: AAM77751.1.
    AK022519 mRNA. Translation: BAB14075.1.
    AL513365 Genomic DNA. Translation: CAI21500.1.
    BC028566 mRNA. Translation: AAH28566.1.
    CCDSiCCDS280.1.
    RefSeqiNP_078950.1. NM_024674.4.
    XP_006710962.1. XM_006710899.1.
    XP_006710963.1. XM_006710900.1.
    UniGeneiHs.86154.

    Genome annotation databases

    EnsembliENST00000254231; ENSP00000254231; ENSG00000131914.
    ENST00000326279; ENSP00000363314; ENSG00000131914.
    GeneIDi79727.
    KEGGihsa:79727.
    UCSCiuc001bmj.3. human.

    Polymorphism databases

    DMDMi74752750.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF521099 mRNA. Translation: AAM77751.1 .
    AK022519 mRNA. Translation: BAB14075.1 .
    AL513365 Genomic DNA. Translation: CAI21500.1 .
    BC028566 mRNA. Translation: AAH28566.1 .
    CCDSi CCDS280.1.
    RefSeqi NP_078950.1. NM_024674.4.
    XP_006710962.1. XM_006710899.1.
    XP_006710963.1. XM_006710900.1.
    UniGenei Hs.86154.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQF NMR - A 137-186 [» ]
    2LI8 NMR - A 124-186 [» ]
    ProteinModelPortali Q9H9Z2.
    SMRi Q9H9Z2. Positions 34-186.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122842. 84 interactions.
    IntActi Q9H9Z2. 2 interactions.
    STRINGi 9606.ENSP00000254231.

    PTM databases

    PhosphoSitei Q9H9Z2.

    Polymorphism databases

    DMDMi 74752750.

    Proteomic databases

    PaxDbi Q9H9Z2.
    PRIDEi Q9H9Z2.

    Protocols and materials databases

    DNASUi 79727.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254231 ; ENSP00000254231 ; ENSG00000131914 .
    ENST00000326279 ; ENSP00000363314 ; ENSG00000131914 .
    GeneIDi 79727.
    KEGGi hsa:79727.
    UCSCi uc001bmj.3. human.

    Organism-specific databases

    CTDi 79727.
    GeneCardsi GC01P026737.
    HGNCi HGNC:15986. LIN28A.
    HPAi CAB020785.
    MIMi 611043. gene.
    neXtProti NX_Q9H9Z2.
    PharmGKBi PA165751523.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244191.
    HOGENOMi HOG000047091.
    HOVERGENi HBG081922.
    InParanoidi Q9H9Z2.
    OMAi SGICKWF.
    OrthoDBi EOG72JWJ8.
    PhylomeDBi Q9H9Z2.
    TreeFami TF316240.

    Enzyme and pathway databases

    Reactomei REACT_200812. Transcriptional regulation of pluripotent stem cells.
    SignaLinki Q9H9Z2.

    Miscellaneous databases

    EvolutionaryTracei Q9H9Z2.
    GeneWikii LIN28.
    GenomeRNAii 79727.
    NextBioi 69098.
    PROi Q9H9Z2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H9Z2.
    CleanExi HS_LIN28.
    Genevestigatori Q9H9Z2.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    4.10.60.10. 1 hit.
    InterProi IPR011129. Cold_shock_prot.
    IPR002059. CSP_DNA-bd.
    IPR012340. NA-bd_OB-fold.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00313. CSD. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    PRINTSi PR00050. COLDSHOCK.
    SMARTi SM00357. CSP. 1 hit.
    SM00343. ZnF_C2HC. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation of the heterochronic regulator Lin-28, its developmental expression and microRNA complementary sites."
      Moss E.G., Tang L.
      Dev. Biol. 258:432-442(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Erratum
      Moss E.G., Tang L.
      Dev. Biol. 262:361-361(2003)
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Teratocarcinoma.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    6. "Expression profiling of mammalian microRNAs uncovers a subset of brain-expressed microRNAs with possible roles in murine and human neuronal differentiation."
      Sempere L.F., Freemantle S., Pitha-Rowe I., Moss E.G., Dmitrovsky E., Ambros V.
      Genome Biol. 5:R13.1-R13.11(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "The transcriptome profile of human embryonic stem cells as defined by SAGE."
      Richards M., Tan S.-P., Tan J.-H., Chan W.-K., Bongso A.
      Stem Cells 22:51-64(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    8. "Vascular gene expression and phenotypic correlation during differentiation of human embryonic stem cells."
      Gerecht-Nir S., Dazard J.-E., Golan-Mashiach M., Osenberg S., Botvinnik A., Amariglio N., Domany E., Rechavi G., Givol D., Itskovitz-Eldor J.
      Dev. Dyn. 232:487-497(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    9. "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."
      Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.
      J. Biol. Chem. 280:16635-16641(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    10. "Micro-RNA regulation of the mammalian lin-28 gene during neuronal differentiation of embryonal carcinoma cells."
      Wu L., Belasco J.G.
      Mol. Cell. Biol. 25:9198-9208(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Localization of the developmental timing regulator Lin28 to mRNP complexes, P-bodies and stress granules."
      Balzer E., Moss E.G.
      RNA Biol. 4:16-25(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-46; PHE-55; PHE-73; HIS-147 AND HIS-169.
    12. "Lin28 mediates the terminal uridylation of let-7 precursor MicroRNA."
      Heo I., Joo C., Cho J., Ha M., Han J., Kim V.N.
      Mol. Cell 32:276-284(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, MUTAGENESIS OF HIS-147 AND HIS-169.
    13. "TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-microRNA uridylation."
      Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J., Kim V.N.
      Cell 138:696-708(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH ZCCHC11.
    14. Cited for: POSSIBLE INVOLVEMENT IN CANCERS.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-120 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Solution structure of the zinc-finger domain in LIN-28."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 134-186.
    18. "Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28."
      Loughlin F.E., Gebert L.F., Towbin H., Brunschweiger A., Hall J., Allain F.H.
      Nat. Struct. Mol. Biol. 19:84-89(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 124-186 IN COMPLEX WITH SHORT RNA, CONSENSUS MOTIF.

    Entry informationi

    Entry nameiLN28A_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9Z2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3