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Reviewed, UniProtKB/Swiss-Prot Q9H2H8 (PPIL3_HUMAN)

Last modified November 3, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase-like 3
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin-like protein PPIL3
    Cyclophilin J
      Short name=CyPJ
Gene names
Name: PPIL3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.

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
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentspliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VP3Q991521EBI-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: dbSNP rs7562391. Ref.5
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).

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 SPICEOSOMAL C COMPLEX.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
NP_570981.1.
NP_572028.1.
UniGeneHs.121076

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XYHX-ray2.60A1-161[»]
2OJUX-ray2.40A/B1-161[»]
2OK3X-ray2.00A1-161[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9H2H8. 2 interactions.
STRINGQ9H2H8.

Proteomic databases

PRIDEQ9H2H8.

Genome annotation databases

EnsemblENST00000234288; ENSP00000234288; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000286175; ENSP00000286175; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000321356; ENSP00000326830; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000334509; ENSP00000334569; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000357369; ENSP00000349935; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000392283; ENSP00000376107; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409264; ENSP00000386893; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409361; ENSP00000386235; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409403; ENSP00000386875; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409449; ENSP00000387012; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000409769; ENSP00000386358; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000415562; ENSP00000400726; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000422134; ENSP00000400192; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000432425; ENSP00000400487; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000434813; ENSP00000394734; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000443398; ENSP00000391082; ENSG00000013441; Homo sapiens. [Genome view]
ENST00000457063; ENSP00000401196; ENSG00000013441; Homo sapiens. [Genome view]
GeneID53938.
KEGGhsa:53938.
UCSCuc002uwh.1. human.
uc002uwi.1. human.

Organism-specific databases

CTD53938.
GeneCardsGC02M201443.
H-InvDBHIX0002729.
HGNCHGNC:9262. PPIL3.
PharmGKBPA33589.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9H2H8.
OMAACENFLA.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.

Gene expression databases

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

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents