PPIL2

Protein-coding gene in the species Homo sapiens
PPIL2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1ZKC

Identifiers
AliasesPPIL2, CYC4, CYP60, Cyp-60, UBOX7, hCyP-60, peptidylprolyl isomerase like 2
External IDsOMIM: 607588; MGI: 2447857; HomoloGene: 8643; GeneCards: PPIL2; OMA:PPIL2 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for PPIL2
Genomic location for PPIL2
Band22q11.21-q11.22Start21,666,000 bp[1]
End21,700,015 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for PPIL2
Genomic location for PPIL2
Band16|16 A3Start16,904,419 bp[2]
End16,929,121 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • granulocyte

  • body of pancreas

  • gastric mucosa

  • minor salivary glands

  • apex of heart

  • body of stomach

  • nipple

  • anterior pituitary
Top expressed in
  • spermatocyte

  • spermatid

  • genital tubercle

  • tail of embryo

  • ventricular zone

  • thymus

  • neural layer of retina

  • neural tube

  • right kidney

  • granulocyte
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • ubiquitin-ubiquitin ligase activity
  • protein binding
  • isomerase activity
  • ubiquitin protein ligase activity
  • ubiquitin-protein transferase activity
  • transferase activity
  • peptidyl-prolyl cis-trans isomerase activity
  • cyclosporin A binding
Cellular component
  • cytoplasm
  • Golgi lumen
  • plasma membrane
  • nucleus
  • nucleoplasm
Biological process
  • protein polyubiquitination
  • protein localization to plasma membrane
  • protein folding
  • protein ubiquitination
  • leukocyte migration
  • protein peptidyl-prolyl isomerization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23759

66053

Ensembl

ENSG00000100023

ENSMUSG00000022771

UniProt

Q13356

Q9D787

RefSeq (mRNA)

NM_014337
NM_148175
NM_148176
NM_001317996

NM_001252444
NM_001252445
NM_144954
NM_001356386

RefSeq (protein)

NP_001304925
NP_055152
NP_680480
NP_680481

NP_001239373
NP_001239374
NP_659203
NP_001343315

Location (UCSC)Chr 22: 21.67 – 21.7 MbChr 16: 16.9 – 16.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene.[5][6]

This gene is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. This protein interacts with the proteinase inhibitor eglin c and is localized in the nucleus. Multiple transcript variants encoding different isoforms have been found for this gene.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100023 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022771 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al. (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
  6. ^ a b "Entrez Gene: PPIL2 peptidylprolyl isomerase (cyclophilin)-like 2".

Further reading

  • Wang BB, Hayenga KJ, Payan DG, Fisher JM (1996). "Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c". Biochem. J. 314 (1): 313–9. doi:10.1042/bj3140313. PMC 1217042. PMID 8660300.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Pushkarsky T, Yurchenko V, Vanpouille C, et al. (2005). "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60". J. Biol. Chem. 280 (30): 27866–71. doi:10.1074/jbc.M503770200. PMID 15946952.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Davis TL, Walker JR, Campagna-Slater V, et al. (2010). "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. 8 (7): e1000439. doi:10.1371/journal.pbio.1000439. PMC 2911226. PMID 20676357.
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  • 1zkc: Crystal Structure of the cyclophiln_RING domain of human peptidylprolyl isomerase (cyclophilin)-like 2 isoform b
    1zkc: Crystal Structure of the cyclophiln_RING domain of human peptidylprolyl isomerase (cyclophilin)-like 2 isoform b


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