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UniProtKB/Swiss-Prot entry Q9H2H8

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PPIL3_HUMAN
Primary accession number Q9H2H8
Secondary accession numbers Q86WF9 Q96IA9 Q9BXZ1
Integrated into Swiss-Prot on August 30, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 52)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase-like 3
Synonyms PPIase
Rotamase
EC 5.2.1.8
Cyclophilin-like protein PPIL3
Cyclophilin J
CyPJ
Gene name
Name: PPIL3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11435694 [NCBI, ExPASy, EBI, Israel, Japan]
Zhou Z., Ying K., Dai J., Tang R., Wang W., Huang Y., Zhao W., Xie Y., Mao Y.;
"Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain.";
Cytogenet. Cell Genet. 92:231-236(2001).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ding J.B., Yu L., Zhao S.Y.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryo;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-146.
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
 IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.";
RNA 8:426-439(2002).
[7]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1107/S0907444904033189; PubMed=15735342 [NCBI, ExPASy, EBI, Israel, Japan]
Huang L.-L., Zhao X.-M., Huang C.-Q., Yu L., Xia Z.-X.;
"Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family.";
Acta Crystallogr. D 61:316-321(2005).
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: 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.
  • INTERACTION:
    Q99152:VP3 (xeno); NbExp=1; IntAct=EBI-751051, EBI-1776808;
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsPPIL3b
    Isoform IDQ9H2H8-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsPPIL3a
    Isoform IDQ9H2H8-2
    Features which should be applied to build the isoform sequence: VSP_015468.
  • TISSUE SPECIFICITY: Ubiquitous. Detected at low levels.
  • SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily.
  • SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF251049; AAK34939.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF271652; AAG44766.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146799; AAO64723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027315; BAB55036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005037; AAY14723.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007693; AAH07693.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_115861.1; -.
NP_570981.1; -.
NP_572028.1; -.
UniGene Hs.121076
3D structure databases
PDB
1XYH; X-ray; 2.60 A; A=1-161.[ExPASy / RCSB / EBI]
2OJU; X-ray; 2.40 A; A/B=1-161.[ExPASy / RCSB / EBI]
2OK3; X-ray; 2.00 A; A=1-161.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XYH; -.
2OJU; -.
2OK3; -.
ModBase Q9H2H8.
Protein-protein interaction databases
IntAct Q9H2H8; -.
PTM databases
PhosphoSite Q9H2H8; -.
Organism-specific databases
H-InvDB HIX0002729; -.
HGNC HGNC:9262; PPIL3.
GenAtlas PPIL3.
PharmGKB PA33589; -.
GeneCards Q9H2H8.
Gene expression databases
ArrayExpress Q9H2H8; -.
CleanEx HS_PPIL3; -.
GermOnline ENSG00000115934; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR002130; PPIase_cyclophilin.
Graphical view of domain structure.
Gene3D G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
PANTHER PTHR11071; PPIase_cyclophilin; 1.
Pfam PF00160; Pro_isomerase; 1.
Pfam graphical view of domain structure.
PRINTS PR00153; CSAPPISMRASE.
PROSITE PS00170; CSA_PPIASE_1; 1.
PS50072; CSA_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9H2H8.
Genome annotation databases
Ensembl ENSG00000115934; Homo sapiens. [Contig view]
GeneID 53938; -.
KEGG hsa:53938; -.
Phylogenomic databases
HOVERGEN Q9H2H8; -.
Other
ProtoNet Q9H2H8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Isomerase; mRNA processing; mRNA splicing; Polymorphism; Rotamase; Spliceosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   161  161     Peptidyl-prolyl cis-trans isomerase-like 3. PRO_0000064166
DOMAIN   1   154  154     PPIase cyclophilin-type. 
VAR_SEQ   27    58        NFLALCASNYYNGCIFHRNIKGFMVQTGDPTG -> MESRCVPQAGVQWRDLGSLQPPPPGFKQVFCLSLPR (in isoform 2). VSP_015468
VARIANT   146   146  1     D -> E (in dbSNP:rs7562391 [NCBI]). VAR_023417 [3D]
CONFLICT   61    62        RG -> KR (in Ref. 2; AAO64723). 
CONFLICT   65    65        S -> V (in Ref. 2; AAO64723). 
CONFLICT   78    78        Y -> I (in Ref. 2; AAO64723). 
STRAND   2     7  6      
STRAND   10    16  7      
TURN   18    20  3      
HELIX   22    33  12      
TURN   34    39  6      
STRAND   44    46  3      
TURN   47    49  3      
STRAND   50    53  4      
STRAND   58    61  4      
STRAND   86    89  4      
STRAND   92    95  4      
STRAND   101   106  6      
HELIX   109   111  3      
TURN   112   114  3      
STRAND   117   123  7      
HELIX   125   132  8      
TURN   138   140  3      
STRAND   143   145  3      
STRAND   148   155  8      
Sequence information
Length: 161 AA [This is the length of the unprocessed precursor] Molecular weight: 18155 Da [This is the MW of the unprocessed precursor] CRC64: 5FE190D7858B07D4 [This is a checksum on the sequence] 
        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
Q9H2H8 in FASTA format

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