Ppil2 peptidylprolyl isomerase (cyclophilin)-like 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ppil2provided by MGI
Official Full Name: peptidylprolyl isomerase (cyclophilin)-like 2provided by MGI
Primary source: MGI:MGI:2447857
See related: Ensembl:ENSMUSG00000022771 AllianceGenome:MGI:2447857
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: CYC4; 0610009L05Rik; 1700016N17Rik; 4921520K19Rik; 4930511F14Rik; C130078A06Rik
Summary: Predicted to enable ubiquitin-ubiquitin ligase activity. Predicted to be involved in protein folding; protein localization to plasma membrane; and protein polyubiquitination. Predicted to be located in cytoplasm; nucleoplasm; and plasma membrane. Predicted to be part of catalytic step 2 spliceosome. Orthologous to human PPIL2 (peptidylprolyl isomerase like 2). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in thymus adult (RPKM 36.1), mammary gland adult (RPKM 30.8) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 16 A3; 16 10.59 cM

Exon count:: 21

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	16	NC_000082.7 (16904419..16929126, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	16	NC_000082.6 (17086555..17111263, complement)

Chromosome 16 - NC_000082.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cpsf2,Ppil2, and SNAP-25 are the most promising targets for the NSm protein of the virus during an infection.
Title: The Rift Valley Fever virus protein NSm and putative cellular protein interactions.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables peptidyl-prolyl cis-trans isomerase activity	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ubiquitin protein ligase activity	ISO Inferred from Sequence Orthology more info
enables ubiquitin-protein transferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables ubiquitin-ubiquitin ligase activity	ISO Inferred from Sequence Orthology more info
enables ubiquitin-ubiquitin ligase activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in RNA splicing	IEA Inferred from Electronic Annotation more info
involved_in mRNA processing	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein localization to plasma membrane	ISO Inferred from Sequence Orthology more info
involved_in protein localization to plasma membrane	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within protein polyubiquitination	ISO Inferred from Sequence Orthology more info
involved_in protein polyubiquitination	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
part_of catalytic step 2 spliceosome	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISS Inferred from Sequence or Structural Similarity more info
part_of spliceosomal complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: RING-type E3 ubiquitin-protein ligase PPIL2

Names: PPIase; RING-type E3 ubiquitin transferase isomerase-like 2; cyclophilin-60; cyclophilin-like protein Cyp-60; peptidyl-prolyl cis-trans isomerase-like 2; probable inactive peptidyl-prolyl cis-trans isomerase-like 2; rotamase PPIL2

NP_001239373.1

EC 2.3.2.27

NP_001239374.1

EC 2.3.2.27

NP_001343315.1

EC 2.3.2.27

NP_659203.1

EC 2.3.2.27

XP_006522506.1

EC 2.3.2.27

XP_006522508.1

EC 2.3.2.27

XP_006522509.1

EC 2.3.2.27

XP_006522510.1

EC 2.3.2.27

XP_030105088.1

EC 2.3.2.27

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001252444.1 → NP_001239373.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform 1

See identical proteins and their annotated locations for NP_001239373.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longest transcript. Variants 1, 2 and 3 encode the same protein.

Source sequence(s)

AI837084, AK012472, BY033661, BY145175

Consensus CDS

CCDS27993.1

UniProtKB/Swiss-Prot

Q542A2, Q9CZL1, Q9D787

UniProtKB/TrEMBL

Q8BUY4

Related

ENSMUSP00000023455.6, ENSMUST00000023455.14

Conserved Domains (2) summary

smart00504
Location:42 → 96

Ubox; Modified RING finger domain

cd01923
Location:281 → 440

cyclophilin_RING; cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal ...
NM_001252445.1 → NP_001239374.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform 1

See identical proteins and their annotated locations for NP_001239374.1

Status: VALIDATED

Description

Transcript Variant: This variant (3) differs in the 3' UTR compared to variant 1. Variants 1, 2 and 3 encode the same protein.

Source sequence(s)

AC154667, AK161596, BY033661

Consensus CDS

CCDS27993.1

UniProtKB/Swiss-Prot

Q542A2, Q9CZL1, Q9D787

UniProtKB/TrEMBL

Q8BUY4

Related

ENSMUSP00000155861.2, ENSMUST00000231712.2

Conserved Domains (2) summary

smart00504
Location:42 → 96

Ubox; Modified RING finger domain

cd01923
Location:281 → 440

cyclophilin_RING; cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal ...
NM_001356386.1 → NP_001343315.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform 2

Status: VALIDATED

Source sequence(s)

AC154667

Conserved Domains (1) summary

cd01923
Location:103 → 262

cyclophilin_RING; cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human ...
NM_144954.3 → NP_659203.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform 1

See identical proteins and their annotated locations for NP_659203.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate splice site in the 3' UTR compared to variant 1. Variants 1, 2 and 3 encode the same protein.

Source sequence(s)

AC154667

Consensus CDS

CCDS27993.1

UniProtKB/Swiss-Prot

Q542A2, Q9CZL1, Q9D787

UniProtKB/TrEMBL

Q8BUY4

Related

ENSMUSP00000131422.3, ENSMUST00000164458.10

Conserved Domains (2) summary

smart00504
Location:42 → 96

Ubox; Modified RING finger domain

cd01923
Location:281 → 440

cyclophilin_RING; cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000082.7 Reference GRCm39 C57BL/6J

Range

16904419..16929126 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006522447.5 → XP_006522510.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform X3

Conserved Domains (4) summary

cd01923
Location:281 → 440

cyclophilin_RING; cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human ...

cd00162
Location:103 → 146

RING_Ubox; U-box domain, a modified RING finger [structural motif]

cd16663
Location:38 → 110

RING-Ubox_PPIL2; U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins

cl17238
Location:100 → 159

RING_Ubox; The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain
XM_006522443.5 → XP_006522506.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform X1

Conserved Domains (4) summary

cd00162
Location:103 → 146

RING_Ubox; U-box domain, a modified RING finger [structural motif]

cd16663
Location:38 → 110

RING-Ubox_PPIL2; U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins

cl00197
Location:281 → 410

cyclophilin; cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug ...

cl17238
Location:100 → 159

RING_Ubox; The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain
XM_006522445.5 → XP_006522508.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform X2

See identical proteins and their annotated locations for XP_006522508.1

Conserved Domains (1) summary

cd01923
Location:103 → 262

cyclophilin_RING; cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human ...
XM_030249228.1 → XP_030105088.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform X2

Conserved Domains (1) summary

cd01923
Location:103 → 262

cyclophilin_RING; cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human ...
XM_006522446.5 → XP_006522509.1 RING-type E3 ubiquitin-protein ligase PPIL2 isoform X2

See identical proteins and their annotated locations for XP_006522509.1

Conserved Domains (1) summary

cd01923
Location:103 → 262

cyclophilin_RING; cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human ...