B2AXJ0 · B2AXJ0_PODAN

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

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
  • Alternative names
    • Cyclophilin-60
    • Cyclophilin-like protein Cyp-60
    • RING-type E3 ubiquitin transferase isomerase-like 2

Gene names

    • ORF names
      PODANS_7_10730

Organism names

Accessions

  • Primary accession
    B2AXJ0

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain43-116U-box
Region245-284Disordered
Compositional bias248-284Polar residues
Domain338-494PPIase cyclophilin-type
Compositional bias501-536Basic and acidic residues
Region501-587Disordered
Compositional bias547-574Basic and acidic residues

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    587
  • Mass (Da)
    64,495
  • Last updated
    2008-05-20 v1
  • Checksum
    5F437DA853E076FF
MGKGTDKLYITHSEWSSADAYGASVGANAGSRAQRTGAHASFKRLPFNFCAASLQPFKNPVCTADGTIFDIEVISAWLEKKGTNPVDGKPLSAKDLIKLNFARNADTNNSNDRNGIPTDGKGDFIDPVTFKVFTDNTHIVAIRHGNYANVFAWETVERMNIKPKMWRDLVDDAEFGRKDIITLQDPQNAASRDLSQFKHIQDGEEAALTPEQAETRKESGINIDALGRIGDKVLRAKEAVARAREARQSASDINQSASSKTLTKSSSSTTTPRQSLIQEKQKPSNSAIYTTGAAAASFTSTGLTPSTSGSLALLSEEEYLLKPRRLSNSKHPAYVRISTTLGDLTLELFPEFAPKAVWNFLRLSQKGYYNNTLFHRNIKNFMIQGGDPTGTGRGGTSIWKKTFNDELEGPLKHDKRGVVSMANKGKNTNSSQFFITYREASHLDRKHTVFGRVVDSEGTLAKMEGGEGGGGGIVRPFGRRSRSKEVVVLLDCFEEFLREKGEKEREEEKKKEVERKGGTEDDRTTWTGKRLRGEDGGGGKGGVGKYLKEVKGQRQEGEGEGETDTWEEPVKKKTRVGGGGFGNFDGW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias248-284Polar residues
Compositional bias501-536Basic and acidic residues
Compositional bias547-574Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU633900
EMBL· GenBank· DDBJ
CAP69114.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp