Q13356 · PPIL2_HUMAN
- ProteinRING-type E3 ubiquitin-protein ligase PPIL2
- GenePPIL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids520 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation (PubMed:11435423).
May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance (PubMed:15946952).
Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357).
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)
May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance (PubMed:15946952).
Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357).
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | catalytic step 2 spliceosome | |
Cellular Component | cytoplasm | |
Cellular Component | Golgi lumen | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-ubiquitin ligase activity | |
Biological Process | mRNA processing | |
Biological Process | protein folding | |
Biological Process | protein localization to plasma membrane | |
Biological Process | protein polyubiquitination | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRING-type E3 ubiquitin-protein ligase PPIL2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13356
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: May also localize to the cytoplasm and the cell membrane.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 389 | No peptidyl-prolyl cis-trans isomerase activity; enables interaction with cyclosporin A. | ||||
Sequence: Y → H | ||||||
Mutagenesis | 389 | Gain of a peptidyl-prolyl cis-trans isomerase activity; enables interaction with cyclosporin A. | ||||
Sequence: Y → W |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 576 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064171 | 1-520 | RING-type E3 ubiquitin-protein ligase PPIL2 | |||
Sequence: MGKRQHQKDKMYITCAEYTHFYGGKKPDLPQTNFRRLPFDHCSLSLQPFVYPVCTPDGIVFDLLNIVPWLKKYGTNPSNGEKLDGRSLIKLNFSKNSEGKYHCPVLFTVFTNNTHIVAVRTTGNVYAYEAVEQLNIKAKNFRDLLTDEPFSRQDIITLQDPTNLDKFNVSNFYHVKNNMKIIDPDEEKAKQDPSYYLKNTNAETRETLQELYKEFKGDEILAATMKAPEKKKVDKLNAAHYSTGKVSASFTSTAMVPETTHEAAAIDEDVLRYQFVKKKGYVRLHTNKGDLNLELHCDLTPKTCENFIRLCKKHYYDGTIFHRSIRNFVIQGGDPTGTGTGGESYWGKPFKDEFRPNLSHTGRGILSMANSGPNSNRSQFFITFRSCAYLDKKHTIFGRVVGGFDVLTAMENVESDPKTDRPKEEIRIDATTVFVDPYEEADAQIAQERKTQLKVAPETKVKSSQPQAGSQGPQTFRQGVGKYINPAATKRAAEEEPSTSATVPMSKKKPSRGFGDFSSW | ||||||
Cross-link | 216 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 470 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 482 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest expression in thymus, pancreas and testis. Also detected in heart, placenta, lung, liver, skeletal muscle, kidney, spleen, prostate, ovary, small intestine and colon. Poorly detected in brain and leukocytes. Strong protein expression in lymph node (cortical, paracortical and medullar regions), thyroid (follicular epithelial cells), testis (developing spermatozoa), stomach (cells lining the gastric pit), pancreas, kidney (proximal and distal-tubule cells and collecting duct cells but not in glomeruli), endometrium and colon (goblet cells). Moderate protein expression in spleen, prostate (epithelium and squamous cell carcinomas), placenta and adrenal gland. Weak protein expression in liver, heart, breast, ovary, and lung. No protein expression in brain and bladder. High protein expression in most lymphomas and melanomas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the minor spliceosome, which splices U12-type introns. Within this complex, interacts with PRPF8/PRP8, EFTUD2/SNU114 and PLRG1 (PubMed:33509932).
Interacts with isoform 2 of BSG (PubMed:15946952).
Interacts (via the PPIase cyclophilin-type domain) with CRNKL1; they may form a trimeric complex with HSP90
Interacts with isoform 2 of BSG (PubMed:15946952).
Interacts (via the PPIase cyclophilin-type domain) with CRNKL1; they may form a trimeric complex with HSP90
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13356 | DCAF10 Q5QP82 | 3 | EBI-7705988, EBI-723230 | |
BINARY | Q13356 | TRIM23 P36406 | 3 | EBI-7705988, EBI-740098 | |
BINARY | Q13356 | ZNF830 Q96NB3 | 3 | EBI-7705988, EBI-3920997 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-108 | U-box | ||||
Sequence: RRLPFDHCSLSLQPFVYPVCTPDGIVFDLLNIVPWLKKYGTNPSNGEKLDGRSLIKLNFSKNSEGKYHCPVLFT | ||||||
Coiled coil | 197-217 | |||||
Sequence: LKNTNAETRETLQELYKEFKG | ||||||
Domain | 278-433 | PPIase cyclophilin-type | ||||
Sequence: KKGYVRLHTNKGDLNLELHCDLTPKTCENFIRLCKKHYYDGTIFHRSIRNFVIQGGDPTGTGTGGESYWGKPFKDEFRPNLSHTGRGILSMANSGPNSNRSQFFITFRSCAYLDKKHTIFGRVVGGFDVLTAMENVESDPKTDRPKEEIRIDATTV | ||||||
Region | 456-520 | Disordered | ||||
Sequence: APETKVKSSQPQAGSQGPQTFRQGVGKYINPAATKRAAEEEPSTSATVPMSKKKPSRGFGDFSSW | ||||||
Compositional bias | 457-478 | Polar residues | ||||
Sequence: PETKVKSSQPQAGSQGPQTFRQ |
Sequence similarities
Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q13356-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length520
- Mass (Da)58,823
- Last updated1996-11-01 v1
- Checksum3FFA51C3D82F0957
Q13356-2
- Name2
- Differences from canonical
- 490-520: KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW → EQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WC56 | F8WC56_HUMAN | PPIL2 | 41 | ||
A0A7P0T8E8 | A0A7P0T8E8_HUMAN | PPIL2 | 573 | ||
A0A7P0T8P6 | A0A7P0T8P6_HUMAN | PPIL2 | 101 | ||
A0A7P0T9A5 | A0A7P0T9A5_HUMAN | PPIL2 | 43 | ||
A0A7P0T843 | A0A7P0T843_HUMAN | PPIL2 | 510 | ||
A0A7P0T839 | A0A7P0T839_HUMAN | PPIL2 | 305 | ||
A0A7P0T896 | A0A7P0T896_HUMAN | PPIL2 | 250 | ||
C9JDF0 | C9JDF0_HUMAN | PPIL2 | 160 | ||
A0A7P0TBL3 | A0A7P0TBL3_HUMAN | PPIL2 | 415 | ||
A0A7P0TAH4 | A0A7P0TAH4_HUMAN | PPIL2 | 342 | ||
A0A7P0TB19 | A0A7P0TB19_HUMAN | PPIL2 | 614 | ||
A0A7P0TA15 | A0A7P0TA15_HUMAN | PPIL2 | 549 | ||
A0A7P0Z4K4 | A0A7P0Z4K4_HUMAN | PPIL2 | 499 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 455 | in Ref. 3; AAH28385 | ||||
Sequence: V → I | ||||||
Compositional bias | 457-478 | Polar residues | ||||
Sequence: PETKVKSSQPQAGSQGPQTFRQ | ||||||
Alternative sequence | VSP_005182 | 490-520 | in isoform 2 | |||
Sequence: KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW → EQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U37219 EMBL· GenBank· DDBJ | AAC50376.1 EMBL· GenBank· DDBJ | mRNA | ||
U37220 EMBL· GenBank· DDBJ | AAC50377.1 EMBL· GenBank· DDBJ | mRNA | ||
U37221 EMBL· GenBank· DDBJ | AAC50378.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456548 EMBL· GenBank· DDBJ | CAG30434.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028385 EMBL· GenBank· DDBJ | AAH28385.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000022 EMBL· GenBank· DDBJ | AAH00022.1 EMBL· GenBank· DDBJ | mRNA |