P0CP90 · PPIL2_CRYNJ

Function

function

May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins.

Catalytic activity

Pathway

Protein modification; protein ubiquitination.

GO annotations

AspectTerm
Cellular Componentcatalytic step 2 spliceosome
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionubiquitin protein ligase activity
Biological Processprotein folding
Biological Processprotein peptidyl-prolyl isomerization
Biological Processprotein polyubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase-like 2
  • EC number
  • Short names
    PPIase
  • Alternative names
    • Cyclophilin-60
    • Cyclophilin-like protein Cyp-60
    • RING-type E3 ubiquitin transferase isomerase-like 2
    • Rotamase

Gene names

    • Name
      CYP8
    • Ordered locus names
      CNJ00200

Organism names

Accessions

  • Primary accession
    P0CP90
  • Secondary accessions
    • Q55KK3
    • Q5KAW8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002329841-573Peptidyl-prolyl cis-trans isomerase-like 2

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain37-119U-box
Region223-247Disordered
Domain312-469PPIase cyclophilin-type
Region489-515Disordered
Compositional bias490-515Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    573
  • Mass (Da)
    63,562
  • Last updated
    2011-06-28 v1
  • Checksum
    2921176BE24684D0
MGHNSDKLYVTHSEHAAGSHTASSFGKRQETGKSEFQRLPFDCCALSLQPFKNPVAVISETKAGEAPRADVFDLLNIVPYIRKFKSNPVTGKPLETSQLIKLNFSRNAEGNLHDPITYKVFSPHIHIVFLKNTGNVFDMASLQLLAIKPKTWRDLVNDEPFKRKDIITIQDPENLAARDLREYDYVKKDLKVSEDELAGDPLRGINVDAAGGASKVLKMIAEKNKSGQSPAPTPSKIDDGKGQEKKEGVVAKRKVEQMAYNASNYSSGRAAASLTSTSLMPETKSERAMFDEEEYMFEELSRPTKDKERQKSKAYATITTNFGPLNVELHGDRAPKTVYNFVQLAKAGKYDNVVFHRLIPGFMVQGGDPTGTGRGGESYWGEPFRDEHGEKGAYKHDSRGVLSMANSGPRTNGSQFFFTFRPTPHLDGKHTVFGKLVGGEETLDKIERVNVRPGGDRPVRDIVIQGVTVLQDPFEAYQARLQARLARQDQSDAALKRRAEAQKEREKDRTTWLGTKLGEKGAVGKRRMEEDVGVGKYLKVGGEAGQRTTLDVVDYGVEKKKKKAGGFGDFSGW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias490-515Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017350
EMBL· GenBank· DDBJ
AAW45760.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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