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Q13356 (PPIL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase-like 2

Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Cyclophilin-60
Cyclophilin-like protein Cyp-60
Rotamase PPIL2
Gene names
Name:PPIL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Nucleus.

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.

Sequence similarities

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

Contains 1 PPIase cyclophilin-type domain.

Contains 1 U-box domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZNF830Q96NB32EBI-7705988,EBI-3920997

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
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Peptidyl-prolyl cis-trans isomerase-like 2
PRO_0000064171

Regions

Domain35 – 10874U-box
Domain278 – 433156PPIase cyclophilin-type
Coiled coil197 – 21721 Potential

Amino acid modifications

Modified residue4821N6-acetyllysine Ref.4

Natural variations

Alternative sequence490 – 52031KRAAE…DFSSW → EQQRKSPQPVPLSPCPRRSP VGVLGTSAPGSSRLPDDH in isoform 2.
VSP_005182

Experimental info

Sequence conflict4551V → I in AAH28385. Ref.3

Secondary structure

................................... 520
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3FFA51C3D82F0957

FASTA52058,823
        10         20         30         40         50         60 
MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV 

        70         80         90        100        110        120 
FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR 

       130        140        150        160        170        180 
TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK 

       190        200        210        220        230        240 
IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH 

       250        260        270        280        290        300 
YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT 

       310        320        330        340        350        360 
PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH 

       370        380        390        400        410        420 
TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD 

       430        440        450        460        470        480 
RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV 

       490        500        510        520 
GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW 

« Hide

Isoform 2 [UniParc].

Checksum: 9B494AE6D29EBAC3
Show »

FASTA52759,458

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] [Europe PMC] [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:R84.1-R84.11(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Hippocampus and Kidney.
[4]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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

EMBL
GenBank
DDBJ
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.
PIRS64705.
RefSeqNP_055152.1. NM_014337.3.
NP_680480.1. NM_148175.2.
NP_680481.1. NM_148176.2.
XP_005261504.1. XM_005261447.2.
XP_005261505.1. XM_005261448.2.
UniGeneHs.438587.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZKCX-ray1.65A/B280-457[»]
ProteinModelPortalQ13356.
SMRQ13356. Positions 39-90, 277-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117260. 10 interactions.
IntActQ13356. 2 interactions.
MINTMINT-4654541.
STRING9606.ENSP00000390427.

PTM databases

PhosphoSiteQ13356.

Polymorphism databases

DMDM23813917.

Proteomic databases

PaxDbQ13356.
PeptideAtlasQ13356.
PRIDEQ13356.

Protocols and materials databases

DNASU23759.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335025; ENSP00000334553; ENSG00000100023. [Q13356-1]
ENST00000398831; ENSP00000381812; ENSG00000100023. [Q13356-1]
ENST00000406385; ENSP00000384299; ENSG00000100023. [Q13356-1]
ENST00000412327; ENSP00000390427; ENSG00000100023. [Q13356-2]
ENST00000492445; ENSP00000445312; ENSG00000100023. [Q13356-1]
GeneID23759.
KEGGhsa:23759.
UCSCuc002zvg.4. human. [Q13356-1]
uc002zvh.4. human. [Q13356-2]

Organism-specific databases

CTD23759.
GeneCardsGC22P022006.
HGNCHGNC:9261. PPIL2.
HPAHPA035344.
HPA055637.
MIM607588. gene.
neXtProtNX_Q13356.
PharmGKBPA33588.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000177172.
HOVERGENHBG053655.
InParanoidQ13356.
KOK10598.
OMAVFAWDTV.
OrthoDBEOG769ZKZ.
PhylomeDBQ13356.
TreeFamTF300854.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ13356.
BgeeQ13356.
CleanExHS_PPIL2.
GenevestigatorQ13356.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR026951. PPIL2.
IPR027799. Rtf2_RING-finger.
IPR003613. Ubox_domain.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR11071:SF42. PTHR11071:SF42. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
PF04641. Rtf2. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SMARTSM00504. Ubox. 1 hit.
[Graphical view]
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS51698. U_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIL2. human.
EvolutionaryTraceQ13356.
GeneWikiPPIL2.
GenomeRNAi23759.
NextBio46699.
PROQ13356.
SOURCESearch...

Entry information

Entry namePPIL2_HUMAN
AccessionPrimary (citable) accession number: Q13356
Secondary accession number(s): Q13357, Q8TAH2, Q9BWR8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM