Reviewed,
UniProtKB/Swiss-Prot Q13356 (PPIL2_HUMAN)
Last modified
November 25, 2008.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peptidyl-prolyl cis-trans isomerase-like 2 Short name=PPIase Short name=Rotamase EC=5.2.1.8 Alternative name(s): Cyclophilin-60 Cyclophilin-like protein Cyp-60 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 520 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). |
| Subcellular location | |
| 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 leucocytes. 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 carcinoma), 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. |
| Sequence similarities | Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily. Contains 1 PPIase cyclophilin-type domain. Contains 1 U-box domain. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil |
| Molecular function | Isomerase Rotamase |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein polyubiquitinationInferred from direct assay. Source: MGI |
| Cellular component | Golgi lumen Inferred from Experiment. Source: Reactome nucleus Ref.1Traceable author statement. Source: UniProtKB ubiquitin ligase complexInferred from electronic annotation. Source: InterPro |
| Molecular function | peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activityInferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: 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. | ||||||
| Isoform 2 (identifier: Q13356-2) The sequence of this isoform differs from the canonical sequence as follows: 490-520: KRAAEEEPSTSATVPMSKKKPSRGFGDFSSW → EQQRKSPQPVPLSPCPRRSPVGVLGTSAPGSSRLPDDH | ||||||
| Notes: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 520 | 520 | Peptidyl-prolyl cis-trans isomerase-like 2 | PRO_0000064171 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Domain | 42 – 101 | 60 | U-box | ||||||||||||||||||||||||||||||||||||||||
| Domain | 278 – 433 | 156 | PPIase cyclophilin-type | ||||||||||||||||||||||||||||||||||||||||
| Coiled coil | 197 – 217 | 21 | Potential | ||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 490 – 520 | 31 | KRAAE…DFSSW → EQQRKSPQPVPLSPCPRRSP VGVLGTSAPGSSRLPDDH in isoform 2. | VSP_005182 | |||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 455 | 1 | V → I in AAH28385. Ref.3 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 280 – 286 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 289 – 295 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 297 – 299 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 301 – 312 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 313 – 318 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 323 – 325 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 326 – 328 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 329 – 332 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 337 – 340 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 365 – 368 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 380 – 385 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 388 – 390 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 391 – 393 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 396 – 402 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 404 – 412 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 417 – 419 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 422 – 424 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 427 – 435 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 439 – 455 | 17 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c." Wang B.B., Hayenga K.J., Payan D.G., Fisher J.M. Biochem. J. 314:313-319(1996) [PubMed: 8660300] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Lymphocyte. |
| [2] | "A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Hippocampus and Kidney. |
| [4] | "Crystal structure of the human peptidylprolyl isomerase-like 2 isoform B." Structural genomics consortium (SGC) Submitted (JAN-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 280-457. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U37219 mRNA. Translation: AAC50376.1. U37220 mRNA. Translation: AAC50377.1. U37221 mRNA. Translation: AAC50378.1. CR456548 mRNA. Translation: CAG30434.1. BC028385 mRNA. Translation: AAH28385.1. BC000022 mRNA. Translation: AAH00022.1. | |||||||||||||
| PIR | S64705. | ||||||||||||
| RefSeq | NP_055152.1. NP_680480.1. NP_680481.1. | ||||||||||||
| UniGene | Hs.438587 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q13356. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | Q13356. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000100023. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 23759. | ||||||||||||
| KEGG | hsa:23759. | ||||||||||||
| NMPDR | fig|9606.3.peg.21326. | ||||||||||||
Organism-specific databases | |||||||||||||
| H-InvDB | HIX0016279. | ||||||||||||
| HGNC | HGNC:9261. PPIL2. | ||||||||||||
| MIM | 607588. gene. | ||||||||||||
| PharmGKB | PA33588. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
| GeneCards | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | Q13356. | ||||||||||||
| HOVERGEN | Q13356. | ||||||||||||
Gene expression databases | |||||||||||||
| CleanEx | HS_PPIL2. | ||||||||||||
| GermOnline | ENSG00000100023. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002130. PPIase_cyclophilin. IPR003613. Ubox. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. | ||||||||||||
| PANTHER | PTHR11071. PPIase_cyclophilin. 1 hit. | ||||||||||||
| Pfam | PF00160. Pro_isomerase. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00153. CSAPPISMRASE. | ||||||||||||
| SMART | SM00504. Ubox. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 46699. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | PPIL2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q13356 Secondary accession number(s): Q13357, Q8TAH2, Q9BWR8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 22 Human chromosome 22: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


