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Q9H2H8 (PPIL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
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 3
Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Cyclophilin J
Short name=CyPJ
Cyclophilin-like protein PPIL3
Rotamase PPIL3
Gene names
Name:PPIL3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length161 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. May be involved in pre-mRNA splicing.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subunit structure

Identified in the spliceosome C complex.

Tissue specificity

Ubiquitous. Detected at low levels. Ref.1

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentSpliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processnuclear mRNA splicing, via spliceosome

Inferred by curator Ref.6. Source: UniProtKB

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 18474220. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VP3Q991523EBI-751051,EBI-1776808From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H2H8-1)

Also known as: PPIL3b;

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: Q9H2H8-2)

Also known as: PPIL3a;

The sequence of this isoform differs from the canonical sequence as follows:
     27-58: NFLALCASNYYNGCIFHRNIKGFMVQTGDPTG → MESRCVPQAGVQWRDLGSLQPPPPGFKQVFCLSLPR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Peptidyl-prolyl cis-trans isomerase-like 3
PRO_0000064166

Regions

Domain1 – 154154PPIase cyclophilin-type

Natural variations

Alternative sequence27 – 5832NFLAL…GDPTG → MESRCVPQAGVQWRDLGSLQ PPPPGFKQVFCLSLPR in isoform 2.
VSP_015468
Natural variant1461D → E. Ref.5
Corresponds to variant rs7562391 [ dbSNP | Ensembl ].
VAR_023417

Experimental info

Sequence conflict61 – 622RG → KR in AAO64723. Ref.2
Sequence conflict651S → V in AAO64723. Ref.2
Sequence conflict781Y → I in AAO64723. Ref.2

Secondary structure

1 ................................... 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PPIL3b) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5FE190D7858B07D4

FASTA16118,155
        10         20         30         40         50         60 
MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC IFHRNIKGFM VQTGDPTGTG 

        70         80         90        100        110        120 
RGGNSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK 

       130        140        150        160 
VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA Q

« Hide

Isoform 2 (PPIL3a) [UniParc].

Checksum: A533E5F757C18934
Show »

FASTA16518,627

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain."
Zhou Z., Ying K., Dai J., Tang R., Wang W., Huang Y., Zhao W., Xie Y., Mao Y.
Cytogenet. Cell Genet. 92:231-236(2001) [PubMed: 11435694] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]Ding J.B., Yu L., Zhao S.Y.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryo.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1), VARIANT GLU-146.
Tissue: Placenta.
[6]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed: 11991638] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[7]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family."
Huang L.-L., Zhao X.-M., Huang C.-Q., Yu L., Xia Z.-X.
Acta Crystallogr. D 61:316-321(2005) [PubMed: 15735342] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF251049 mRNA. Translation: AAK34939.1.
AF271652 mRNA. Translation: AAG44766.1.
AF146799 mRNA. Translation: AAO64723.1.
AK027315 mRNA. Translation: BAB55036.1.
AC005037 Genomic DNA. Translation: AAY14723.1.
BC007693 mRNA. Translation: AAH07693.1.
IPIIPI00032473.
IPI00300952.
RefSeqNP_115861.1. NM_032472.3.
NP_570981.1. NM_130906.2.
UniGeneHs.121076.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XYHX-ray2.60A1-161[»]
2OJUX-ray2.40A/B1-161[»]
2OK3X-ray2.00A1-161[»]
ProteinModelPortalQ9H2H8.
SMRQ9H2H8. Positions 1-160.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9H2H8. 2 interactions.
STRINGQ9H2H8.

Polymorphism databases

DMDM73921766.

Proteomic databases

PRIDEQ9H2H8.

Protocols and materials databases

DNASU53938.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234288; ENSP00000234288; ENSG00000240344.
ENST00000392283; ENSP00000376107; ENSG00000240344.
GeneID53938.
KEGGhsa:53938.
UCSCuc002uwh.3. human.
uc002uwi.3. human.

Organism-specific databases

CTD53938.
GeneCardsGC02M201737.
HGNCHGNC:9262. PPIL3.
neXtProtNX_Q9H2H8.
PharmGKBPA33589.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00640000091305.
HOGENOMHOG000065981.
HOVERGENHBG001065.
KOK12734.
OrthoDBEOG43XV4M.

Enzyme and pathway databases

BRENDA5.2.1.8. 2681.

Gene expression databases

ArrayExpressQ9H2H8.
BgeeQ9H2H8.
CleanExHS_PPIL3.
GenevestigatorQ9H2H8.
GermOnlineENSG00000115934. Homo sapiens.

Family and domain databases

Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H2H8.
NextBio56240.

Entry information

Entry namePPIL3_HUMAN
AccessionPrimary (citable) accession number: Q9H2H8
Secondary accession number(s): Q86WF9, Q96IA9, Q9BXZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: May 16, 2012
This is version 91 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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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