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Protein

Peptidyl-prolyl cis-trans isomerase E

Gene

Ppie

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in pre-mRNA splicing (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase E (EC:5.2.1.8)
Short name:
PPIase E
Alternative name(s):
Cyclophilin E
Cyclophilin-33
Rotamase E
Gene namesi
Name:Ppie
Synonyms:Cyp33
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1917118. Ppie.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Peptidyl-prolyl cis-trans isomerase EPRO_0000064158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei91 – 911PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9QZH3.
MaxQBiQ9QZH3.
PaxDbiQ9QZH3.
PeptideAtlasiQ9QZH3.
PRIDEiQ9QZH3.

2D gel databases

REPRODUCTION-2DPAGEIPI00111343.

PTM databases

iPTMnetiQ9QZH3.
PhosphoSiteiQ9QZH3.

Expressioni

Gene expression databases

BgeeiQ9QZH3.
CleanExiMM_PPIE.
GenevisibleiQ9QZH3. MM.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE.By similarity

Protein-protein interaction databases

BioGridi207784. 1 interaction.
STRINGi10090.ENSMUSP00000030404.

Structurei

3D structure databases

ProteinModelPortaliQ9QZH3.
SMRiQ9QZH3. Positions 1-108, 139-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 8379RRMPROSITE-ProRule annotationAdd
BLAST
Domaini143 – 299157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0111. Eukaryota.
COG0652. LUCA.
COG0724. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiQ9QZH3.
KOiK09564.
OMAiAFIEFEL.
OrthoDBiEOG79GT7W.
PhylomeDBiQ9QZH3.
TreeFamiTF313817.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QZH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA
60 70 80 90 100
FVEFELAEDA AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD
110 120 130 140 150
WLKKFSGKTL EENKEEEGPE PPKAEAQEGE PTAKKARSNP QVYMDIKIGN
160 170 180 190 200
KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK GFGFKGSSFH RIIPQFMCQG
210 220 230 240 250
GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG PNTNGSQFFL
260 270 280 290 300
TCDKTDWLDG KHVVFGEVTE GLDVLRQIEA QGSKDGKPKQ KVMIADCGEY

M
Length:301
Mass (Da):33,449
Last modified:September 26, 2003 - v2
Checksum:i856F7AE7F721B219
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621A → P in AAF01030 (Ref. 3) Curated
Sequence conflicti241 – 2411P → S in AAF01030 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008177 mRNA. Translation: BAB25512.1.
BC045154 mRNA. Translation: AAH45154.1.
AF182825 mRNA. Translation: AAF01030.1.
CCDSiCCDS18610.1.
RefSeqiNP_062362.1. NM_019489.5.
UniGeneiMm.126873.

Genome annotation databases

EnsembliENSMUST00000030404; ENSMUSP00000030404; ENSMUSG00000028651.
GeneIDi56031.
KEGGimmu:56031.
UCSCiuc008uow.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008177 mRNA. Translation: BAB25512.1.
BC045154 mRNA. Translation: AAH45154.1.
AF182825 mRNA. Translation: AAF01030.1.
CCDSiCCDS18610.1.
RefSeqiNP_062362.1. NM_019489.5.
UniGeneiMm.126873.

3D structure databases

ProteinModelPortaliQ9QZH3.
SMRiQ9QZH3. Positions 1-108, 139-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207784. 1 interaction.
STRINGi10090.ENSMUSP00000030404.

PTM databases

iPTMnetiQ9QZH3.
PhosphoSiteiQ9QZH3.

2D gel databases

REPRODUCTION-2DPAGEIPI00111343.

Proteomic databases

EPDiQ9QZH3.
MaxQBiQ9QZH3.
PaxDbiQ9QZH3.
PeptideAtlasiQ9QZH3.
PRIDEiQ9QZH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030404; ENSMUSP00000030404; ENSMUSG00000028651.
GeneIDi56031.
KEGGimmu:56031.
UCSCiuc008uow.1. mouse.

Organism-specific databases

CTDi10450.
MGIiMGI:1917118. Ppie.

Phylogenomic databases

eggNOGiKOG0111. Eukaryota.
COG0652. LUCA.
COG0724. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiQ9QZH3.
KOiK09564.
OMAiAFIEFEL.
OrthoDBiEOG79GT7W.
PhylomeDBiQ9QZH3.
TreeFamiTF313817.

Enzyme and pathway databases

ReactomeiR-MMU-6781823. Formation of TC-NER Pre-Incision Complex.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

PROiQ9QZH3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZH3.
CleanExiMM_PPIE.
GenevisibleiQ9QZH3. MM.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF50891. SSF50891. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Small intestine.
  2. "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].
    Tissue: Eye.
  3. "Cyp33: a new family of cyclophilins."
    Anderson M.S., Diaz M.O.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-301.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPPIE_MOUSE
AccessioniPrimary (citable) accession number: Q9QZH3
Secondary accession number(s): Q9D8C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: September 26, 2003
Last modified: July 6, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.