Q9UNP9 (PPIE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase E
Short name=PPIase E
EC=5.2.1.8

Alternative name(s):
Cyclophilin E
Cyclophilin-33
Rotamase E

Gene names

Name:	PPIE
Synonyms:	CYP33

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Identified in the spliceosome C complex. Ref.9
Subcellular location	Nucleus.
Tissue specificity	Found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase E subfamily. Contains 1 PPIase cyclophilin-type domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Isomerase Rotamase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.9. Source: UniProtKB positive regulation of viral genome replication Inferred from mutant phenotype PubMed 19932913. Source: UniProtKB protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 11313484. Source: UniProtKB
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement PubMed 11313484. Source: UniProtKB cyclosporin A binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro peptidyl-prolyl cis-trans isomerase activity Traceable author statement PubMed 11313484. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLL	Q03164	5	EBI-591818,EBI-591370

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q9UNP9-1)

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 B (identifier: Q9UNP9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     280-301: AQGSKDGKPKQKVIIADCGEYV → KQEESAITSQPRSWKLT

Isoform 3 (identifier: Q9UNP9-3)

Also known as: Cyclophilin-33B;

The sequence of this isoform differs from the canonical sequence as follows:
     280-301: AQGSKDGKPKQKVIIADCGEYV → VAPDTKASKARGSRKNKDGQERNWGKSQKVESHTI

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 301

301

Peptidyl-prolyl cis-trans isomerase E

PRO_0000064157

Regions

Domain

6 – 84

79

RRM

Domain

143 – 299

157

PPIase cyclophilin-type

Compositional bias

60 – 63

4

Poly-Ala

Natural variations

Alternative sequence

280 – 301

22

AQGSK…CGEYV → VAPDTKASKARGSRKNKDGQ ERNWGKSQKVESHTI in isoform 3.

VSP_046370

Alternative sequence

280 – 301

22

AQGSK…CGEYV → KQEESAITSQPRSWKLT in isoform B.

VSP_005181

Experimental info

Sequence conflict

151

1

K → R in AAZ93379. Ref.3

Sequence conflict

207

1

N → D in AAZ93379. Ref.3

Sequence conflict

287

1

K → N in AAC00006. Ref.2

Secondary structure

1

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301

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

19 – 26

8

Helix

27 – 29

3

Beta strand

32 – 36

5

Turn

41 – 43

3

Beta strand

48 – 56

9

Helix

57 – 67

11

Beta strand

70 – 72

3

Beta strand

78 – 81

4

Beta strand

141 – 148

8

Beta strand

151 – 160

10

Turn

162 – 164

3

Helix

166 – 177

12

Turn

178 – 180

3

Beta strand

188 – 193

6

Turn

194 – 196

3

Beta strand

197 – 200

4

Turn

203 – 205

3

Beta strand

206 – 209

4

Beta strand

214 – 217

4

Beta strand

230 – 236

7

Beta strand

248 – 253

6

Helix

256 – 258

3

Turn

259 – 261

3

Beta strand

264 – 270

7

Helix

272 – 279

8

Beta strand

292 – 299

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F3226149A790BA42	FASTA	301	33,431
	10 20 30 40 50 60 MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA 70 80 90 100 110 120 AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGSE 130 140 150 160 170 180 PPKAETQEGE PIAKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK 190 200 210 220 230 240 GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG 250 260 270 280 290 300 PNTNGSQFFL TCDKTDWLDG KHVVFGEVTE GLDVLRQIEA QGSKDGKPKQ KVIIADCGEY V
	Isoform B [UniParc]. Checksum: B70A7F239825B54D	FASTA	296	33,085
	10 20 30 40 50 60 MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA 70 80 90 100 110 120 AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGSE 130 140 150 160 170 180 PPKAETQEGE PIAKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK 190 200 210 220 230 240 GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG 250 260 270 280 290 PNTNGSQFFL TCDKTDWLDG KHVVFGEVTE GLDVLRQIEK QEESAITSQP RSWKLT
	Isoform 3 (Cyclophilin-33B) [UniParc]. Checksum: C5D0CFB2673046D7	FASTA	314	34,991
	10 20 30 40 50 60 MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA 70 80 90 100 110 120 AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGSE 130 140 150 160 170 180 PPKAETQEGE PIAKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK 190 200 210 220 230 240 GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG 250 260 270 280 290 300 PNTNGSQFFL TCDKTDWLDG KHVVFGEVTE GLDVLRQIEV APDTKASKAR GSRKNKDGQE 310 RNWGKSQKVE SHTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Co-amplification of a novel cyclophilin-like gene (PPIE) with L-myc in small cell lung cancer cell lines." Kim J.-O., Nau M.M., Allikian K.A., Makela T.P., Alitalo K., Johnson B.E., Kelley M.J. Oncogene 17:1019-1026(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
[2]	Slater C., Thill G., Obar R. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
[3]	Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Tang Z., Huang B., Lin L., Yang S. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	"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. , 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 A). Tissue: Brain.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 A). Tissue: Bone marrow, Colon and Lung.
[8]	"A nuclear RNA-binding cyclophilin in human T cells." Mi H., Kops O., Zimmermann E., Jaeschke A., Tropschug M. FEBS Lett. 398:201-205(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"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.
[10]	"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].
[11]	"Solution structure of the RNA recognition motif in peptidyl-prolyl cis-trans isomerase E." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-89.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF104012 mRNA. Translation: AAD19906.1.
AF104013 mRNA. Translation: AAD19907.1.
AF042385 mRNA. Translation: AAC00006.1.
AF042386 mRNA. Translation: AAC00007.1.
DQ160195 mRNA. Translation: AAZ93379.1.
AK313666 mRNA. Translation: BAG36418.1.
AL049824, AL033527, AL035404 Genomic DNA. Translation: CAI19347.1.
AL049824, AL033527, AL035404 Genomic DNA. Translation: CAI19348.1.
AL049824, AL035404 Genomic DNA. Translation: CAI19350.1.
AL033527, AL035404, AL049824 Genomic DNA. Translation: CAI19409.1.
AL033527, AL035404, AL049824 Genomic DNA. Translation: CAI19410.1.
AL035404, AL033527, AL049824 Genomic DNA. Translation: CAI19576.1.
AL035404, AL033527, AL049824 Genomic DNA. Translation: CAI19577.1.
AL035404, AL049824 Genomic DNA. Translation: CAI19579.1.
CH471059 Genomic DNA. Translation: EAX07255.1.
BC004898 mRNA. Translation: AAH04898.1.
BC008451 mRNA. Translation: AAH08451.1.
BC107736 mRNA. Translation: AAI07737.1.

IPI

IPI00009316.
IPI00220188.
IPI00514173.

PIR

S66681.

RefSeq

NP_006103.1. NM_006112.3.
NP_982281.1. NM_203456.2.

UniGene

Hs.524690.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZMF	X-ray	1.88	A	137-301	[»]
2CQB	NMR	-	A	1-89	[»]
2KU7	NMR	-	A	2-82	[»]
2KYX	NMR	-	A	3-83	[»]
2R99	X-ray	1.61	A	131-301	[»]
3LPY	X-ray	2.00	A/B	5-82	[»]
3MDF	X-ray	1.85	A/B	1-83	[»]
3UCH	X-ray	2.50	A	129-301	[»]

ProteinModelPortal

Q9UNP9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UNP9. 8 interactions.

STRING

9606.ENSP00000312769.

PTM databases

PhosphoSite

Q9UNP9.

Polymorphism databases

DMDM

13124097.

Proteomic databases

PaxDb

Q9UNP9.

PRIDE

Q9UNP9.

Protocols and materials databases

DNASU

10450.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324379; ENSP00000312769; ENSG00000084072.
ENST00000356511; ENSP00000348904; ENSG00000084072.
ENST00000372830; ENSP00000361918; ENSG00000084072.

GeneID

10450.

KEGG

hsa:10450.

UCSC

uc001cds.2. human.
uc001cdv.3. human.

Organism-specific databases

CTD

10450.

GeneCards

GC01P040157.

HGNC

HGNC:9258. PPIE.

HPA

HPA020131.

MIM

602435. gene.

neXtProt

NX_Q9UNP9.

PharmGKB

PA33583.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0724.

HOVERGEN

HBG001065.

KO

K09564.

OrthoDB

EOG4STS55.

PhylomeDB

Q9UNP9.

Gene expression databases

ArrayExpress

Q9UNP9.

Bgee

Q9UNP9.

CleanEx

HS_PPIE.

Genevestigator

Q9UNP9.

GermOnline

ENSG00000084072. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR016304. Cyclophilin-type_PPIase_E.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001475. PPI_cyclophilin_E. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SMART

SM00360. RRM. 1 hit.
[Graphical view]

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PPIE. human.

EvolutionaryTrace

Q9UNP9.

GenomeRNAi

10450.

NextBio

39609.

SOURCE

Search...

Entry information

Entry name

PPIE_HUMAN

Accession

Primary (citable) accession number: Q9UNP9
Secondary accession number(s): B2R971 , O43634, O43635, Q32Q72, Q3S611, Q5TGA0, Q5TGA2, Q5TGA3, Q9UIZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.