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Q9H2H8 (PPIL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. 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

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.6

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
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA 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

Initiator methionine11Removed Ref.7
Chain2 – 161160Peptidyl-prolyl cis-trans isomerase-like 3
PRO_0000064166

Regions

Domain2 – 154153PPIase cyclophilin-type

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.9

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

................................... 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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] [Europe PMC] [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.
CCDSCCDS2332.1. [Q9H2H8-2]
CCDS2333.1. [Q9H2H8-1]
RefSeqNP_115861.1. NM_032472.3. [Q9H2H8-2]
NP_570981.1. NM_130906.2. [Q9H2H8-1]
XP_005246708.1. XM_005246651.2. [Q9H2H8-2]
XP_005246709.1. XM_005246652.2. [Q9H2H8-1]
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...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119820. 19 interactions.
IntActQ9H2H8. 3 interactions.
MINTMINT-3063495.
STRING9606.ENSP00000286175.

PTM databases

PhosphoSiteQ9H2H8.

Polymorphism databases

DMDM73921766.

Proteomic databases

MaxQBQ9H2H8.
PaxDbQ9H2H8.
PRIDEQ9H2H8.

Protocols and materials databases

DNASU53938.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286175; ENSP00000286175; ENSG00000240344. [Q9H2H8-2]
ENST00000392283; ENSP00000376107; ENSG00000240344. [Q9H2H8-1]
ENST00000409449; ENSP00000387012; ENSG00000240344. [Q9H2H8-2]
GeneID53938.
KEGGhsa:53938.
UCSCuc002uwh.3. human. [Q9H2H8-1]
uc002uwi.3. human. [Q9H2H8-2]

Organism-specific databases

CTD53938.
GeneCardsGC02M201737.
HGNCHGNC:9262. PPIL3.
HPAHPA040765.
neXtProtNX_Q9H2H8.
PharmGKBPA33589.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
KOK12734.
OMACEMESRC.
OrthoDBEOG769ZKZ.
PhylomeDBQ9H2H8.
TreeFamTF352224.

Enzyme and pathway databases

BRENDA5.2.1.8. 2681.

Gene expression databases

ArrayExpressQ9H2H8.
BgeeQ9H2H8.
CleanExHS_PPIL3.
GenevestigatorQ9H2H8.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIL3. human.
EvolutionaryTraceQ9H2H8.
GeneWikiPPIL3.
GenomeRNAi53938.
NextBio56240.
PROQ9H2H8.

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: July 9, 2014
This is version 111 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

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