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Protein Overview: lin-28

General Information:
Name(s) found: lin-28 / CE24880 [WormBase]
Description(s) found:
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  • WBGene00003014 locus:lin-28 Protein lin-28 status:Confirmed UniProt:P92186 protein_id:CAB61009.1 [WormBase]
  • gi|71983225|ref|NP_492281.2| abnormal cell LINeage family member (lin-28) [Caenorhabditis elegans] [NCBI NR]
  • gi|6434276|emb|CAB61009.1| C. elegans protein F02E9.2b, confirmed by transcript evidence [Caenorhabditis elegans] [NCBI NR]
  • [wormpep67.fasta]
  • CE24880 WBGene00003014 locus:lin-28 cold shock domain status:Confirmed TR:Q9U3K6 protein_id:CAB61009.1 [wormpep150.fasta]
  • 24880 WBGene00003014 locus:lin-28 cold shock domain status:Confirmed TR:Q9U3K6 protein_id:CAB61009.1 [wormpep130-phg-ecoli-orf-rand.fasta]
  • Hypothetical protein F02E9.2b [Caenorhabditis elegans] [nrdb_11152004_Chlamydomonas]
  • locus:lin-28 cold shock domain status:Confirmed TR:Q9U3K6 protein_id:CAB61009.1 [wormpep115.fasta.reversed]
  • CE24880 locus:lin-28 cold shock domain status:Confirmed TR:Q9U3K6 protein_id:CAB61009.1 [wormpep80.hongbin]
  • CE24880 WBGene00003014 locus:lin-28 cold shock domain status:Confirmed UniProt:P92186 protein_id:CAB61009.1 [WormBase_C-elegans_193_07-31-2008_con_reversed.fasta]
  • CE24880 WBGene00003014 locus:lin-28 cold shock domain status:Confirmed UniProt:P92186 protein_id:CAB61009.1| [wormORF-contam.fasta]
  • abnormal cell LINeage family member (lin-28) [Caenorhabditis elegans] [nr-271106-contam.fasta]
  • CE24880 WBGene00003014 locus:lin-28 cold shock domain status:Confirmed SW:P92186 protein_id:CAB61009.1 [WormBase_C-elegans_wp180_08-19-2007_reversed.fasta]
  • [wormpep210-phg-orf-LaDeana-ecoli-contam.fasta.nr]
  • CE24880 WBGene00003014 locus:lin-28 status:Confirmed UniProt:P92186 protein_id:CAB61009.1 Protein lin-28 [wormpep246-ecoli-contam.fasta]
  • Isoform of P92186, Isoform b of Protein lin-28 OS=Caenorhabditis elegans GN=lin-28 [CAEEL.fasta.20160308]
    • Organism: Caenorhabditis elegans
    Length: 196 amino acids

    Gene Ontology:
    Cellular Component: soluble fraction [IDALink to PubMed article]
    cytoplasm [IEALink to PubMed article]
    Biological Process: regulation of development, heterochronic [IMPLink to PubMed article]
    regulation of transcription, DNA-dependent [IEALink to PubMed article]
    oviposition [IMPLink to PubMed article]
    response to stress [IEALink to PubMed article]
    Molecular Function: nucleic acid binding [IEALink to PubMed article]
    DNA binding [IEALink to PubMed article]
    zinc ion binding [IEALink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MIEAALENPV PIKSQLSPTP RYFGSCKWFN VSKGYGFVID DITGEDLFVH QSNLNMQGFR  60
   61 SLDEGERVSY YIQERSNGKG REAYAVSGEV EGQGLKGSRI HPLGRKKAVS LRCFRCGKFA 120
  121 THKAKSCPNV KTDAKVCYTC GSEEHVSSIC PERRRKHRPE QVAAEEAEAA RMAAEKSSPT 180
  181 TSDDDIREKN SNSSDE

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..91] PSI-BLAST 20.221849 CRYSTAL STRUCTURE OF CSPA, THE MAJOR COLD SHOCK PROTEIN OF ESCHERICHIA COLI
    2 View Details [92..196] PSI-BLAST 8.154902 NUCLEOCAPSID ZINC FINGERS DETECTED IN RETROVIRUSES: EXAFS STUDIES ON INTACT VIRUSES AND THE SOLUTION-STATE STRUCTURE OF THE NUCLEOCAPSID PROTEIN FROM HIV-1


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.99

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle