PPIE

Functionⁱ

Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346). Combines RNA-binding and PPIase activities (PubMed:8977107, PubMed:18258190, PubMed:20677832, PubMed:20460131). Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules (PubMed:8977107, PubMed:18258190, PubMed:20460131). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins (PubMed:8977107, PubMed:18258190, PubMed:20677832, PubMed:20541251). Inhibits KMT2A activity; this requires proline isomerase activity (PubMed:20677832, PubMed:20541251, PubMed:20460131).7 Publications

Catalytic activityⁱ

[protein]-peptidylproline (ω=180)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
[protein]-peptidylproline (ω=0)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
6 Publications
Manual assertion based on experiment inⁱ
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
- Ref.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, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
- Ref.10
  "Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33."
  Wang Y., Han R., Zhang W., Yuan Y., Zhang X., Long Y., Mi H.
  FEBS Lett. 582:835-839(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, ACTIVITY REGULATION.
- Ref.18
  "The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression."
  Park S., Osmers U., Raman G., Schwantes R.H., Diaz M.O., Bushweller J.H.
  Biochemistry 49:6576-6586(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY NMR OF 3-83, CATALYTIC ACTIVITY, INTERACTION WITH KMT2A AND RNA, FUNCTION, DOMAIN, MUTAGENESIS OF LEU-39; LYS-45; ARG-47; PHE-49; PHE-51; ARG-191 AND PHE-196.
- Ref.19
  "Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression."
  Wang Z., Song J., Milne T.A., Wang G.G., Li H., Allis C.D., Patel D.J.
  Cell 141:1183-1194(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY NMR OF 2-82 IN COMPLEX WITH KMT2A, CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH KMT2A, MUTAGENESIS OF PHE-51 AND 196-PHE-MET-197.
- Ref.21
  "Cryo-EM structure of a human spliceosome activated for step 2 of splicing."
  Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K., Urlaub H., Kastner B., Stark H., Luhrmann R.
  Nature 542:318-323(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
EC:5.2.1.8
6 Publications
Manual assertion based on experiment inⁱ
- Ref.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: FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, SUBCELLULAR LOCATION, ACTIVITY REGULATION.
- Ref.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, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
- Ref.10
  "Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33."
  Wang Y., Han R., Zhang W., Yuan Y., Zhang X., Long Y., Mi H.
  FEBS Lett. 582:835-839(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, ACTIVITY REGULATION.
- Ref.18
  "The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression."
  Park S., Osmers U., Raman G., Schwantes R.H., Diaz M.O., Bushweller J.H.
  Biochemistry 49:6576-6586(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY NMR OF 3-83, CATALYTIC ACTIVITY, INTERACTION WITH KMT2A AND RNA, FUNCTION, DOMAIN, MUTAGENESIS OF LEU-39; LYS-45; ARG-47; PHE-49; PHE-51; ARG-191 AND PHE-196.
- Ref.19
  "Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression."
  Wang Z., Song J., Milne T.A., Wang G.G., Li H., Allis C.D., Patel D.J.
  Cell 141:1183-1194(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY NMR OF 2-82 IN COMPLEX WITH KMT2A, CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH KMT2A, MUTAGENESIS OF PHE-51 AND 196-PHE-MET-197.
- Ref.21
  "Cryo-EM structure of a human spliceosome activated for step 2 of splicing."
  Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K., Urlaub H., Kastner B., Stark H., Luhrmann R.
  Nature 542:318-323(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
[protein]-peptidylproline (ω=180)
peptidylproline (ω=180) residue
zoom
=
[protein]-peptidylproline (ω=0)
peptidylproline (ω=0) residue
zoom

Activity regulationⁱ

GO - Molecular functionⁱ

cyclosporin A binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20676357
mRNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 18258190
peptidyl-prolyl cis-trans isomerase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 18258190
- 20676357
poly(A) binding
Source: UniProtKB
Inferred from direct assayⁱ
- 18258190
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674
unfolded protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

mRNA splicing, via spliceosome
Source: UniProtKB
Inferred from direct assayⁱ
- 28076346
neutrophil degranulation Source: Reactome
positive regulation of viral genome replication
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19932913
protein peptidyl-prolyl isomerization
Source: UniProtKB
Inferred from direct assayⁱ
- 20676357
protein refolding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 11313484
transcription-coupled nucleotide-excision repair Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase, RNA-binding, Rotamase
Biological process	mRNA processing, mRNA splicing

Enzyme and pathway databases

BRENDAⁱ	5.2.1.8 2681
Reactomeⁱ	R-HSA-6781823 Formation of TC-NER Pre-Incision Complex R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER) R-HSA-6782135 Dual incision in TC-NER R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-6798695 Neutrophil degranulation R-HSA-72163 mRNA Splicing - Major Pathway

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Peptidyl-prolyl cis-trans isomerase E (EC:5.2.1.84 Publications) Short name: PPIase E Alternative name(s): Cyclophilin E Cyclophilin-331 Publication Rotamase E
Gene namesⁱ	Name:PPIE Synonyms:CYP331 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000084072.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9258 PPIE
MIMⁱ	602435 gene
neXtProtⁱ	NX_Q9UNP9

Keywords - Cellular componentⁱ

Nucleus, Spliceosome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	9	Y → A: Decreased affinity for RNA. 1 Publication	1
Mutagenesisⁱ	39	L → A: Decreased affinity for KMT2A. 2 Publications	1
Mutagenesisⁱ	40 – 45	Missing : Abolishes interaction with KMT2A. 1 Publication	6
Mutagenesisⁱ	42	E → A: Slightly decreased affinity for KMT2A. 1 Publication	1
Mutagenesisⁱ	45	K → A: No effect on interaction with KMT2A. 1 Publication	1
Mutagenesisⁱ	47	R → A: No effect on interaction with KMT2A. 2 Publications	1
Mutagenesisⁱ	49	F → A: Strongly decreased affinity for KMT2A. Decreased affinity for RNA. 2 Publications	1
Mutagenesisⁱ	51	F → A: Impairs protein folding. 2 Publications	1
Mutagenesisⁱ	51	F → D: Abolishes interaction with KMT2A. Abolishes inhibition of KMT2A activity. 1 Publication	1
Mutagenesisⁱ	191	R → A: Expected to disrupt proline isomerase activity. Abolishes inhibition of KMT2A activity; when associated with A-196. 1 Publication	1
Mutagenesisⁱ	196 – 197	FM → EE: Expected to disrupt peptidylproline binding. Decreases interaction with KMT2A. Abolishes inhibition of KMT2A activity. 1 Publication	2
Mutagenesisⁱ	196	F → A: Expected to disrupt proline isomerase activity. Abolishes inhibition of KMT2A activity; when associated with A-191. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10450
Open Targets More...OpenTargetsⁱ	ENSG00000084072
PharmGKBⁱ	PA33583

Polymorphism and mutation databases

BioMutaⁱ	PPIE
DMDMⁱ	13124097

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000064157	1 – 301	Peptidyl-prolyl cis-trans isomerase EAdd BLAST		301

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	91	PhosphoserineCombined sources	1
Modified residueⁱ	97	PhosphoserineCombined sources	1
Modified residueⁱ	119	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q9UNP9
jPOSTⁱ	Q9UNP9
PeptideAtlas More...PeptideAtlasⁱ	Q9UNP9
PRIDEⁱ	Q9UNP9
ProteomicsDBⁱ	85321 85322 [Q9UNP9-2]
TopDownProteomicsⁱ	Q9UNP9-1 [Q9UNP9-1] Q9UNP9-2 [Q9UNP9-2]

PTM databases

iPTMnetⁱ	Q9UNP9
PhosphoSitePlusⁱ	Q9UNP9

Expressionⁱ

Tissue specificityⁱ

Found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

Bgeeⁱ	ENSG00000084072 Expressed in 227 organ(s), highest expression level in right testis
ExpressionAtlasⁱ	Q9UNP9 baseline and differential
Genevisibleⁱ	Q9UNP9 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA019357 HPA020131

HPAⁱ

HPA019357
HPA020131

Interactionⁱ

Subunit structureⁱ

Identified in the spliceosome C complex (PubMed:11991638, PubMed:28076346). Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE (PubMed:17981804). Identified in a pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome as a preassembled complex (PubMed:25599396). The IB complex does not contain PRPF19 (PubMed:25599396). Interacts (via RNA-binding domain) with KMT2A (via the third PHD-type zinc-finger) (PubMed:20677832, PubMed:20541251, PubMed:20460131).7 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
AQR	O60306	8	EBI-591818,EBI-2512328
KMT2A	Q03164	4	EBI-591818,EBI-591370
XAB2	Q9HCS7	10	EBI-591818,EBI-295232

GO - Molecular functionⁱ

unfolded protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	115714, 222 interactors
CORUMⁱ	Q9UNP9
Database of interacting proteins More...DIPⁱ	DIP-34757N
IntActⁱ	Q9UNP9, 18 interactors
Molecular INTeraction database More...MINTⁱ	Q9UNP9

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 11	Combined sources	7
Helixⁱ	19 – 26	Combined sources	8
Helixⁱ	27 – 29	Combined sources	3
Beta strandⁱ	32 – 36	Combined sources	5
Turnⁱ	41 – 43	Combined sources	3
Beta strandⁱ	48 – 56	Combined sources	9
Helixⁱ	57 – 67	Combined sources	11
Beta strandⁱ	70 – 72	Combined sources	3
Beta strandⁱ	78 – 81	Combined sources	4
Beta strandⁱ	141 – 148	Combined sources	8
Beta strandⁱ	151 – 160	Combined sources	10
Turnⁱ	162 – 164	Combined sources	3
Helixⁱ	166 – 177	Combined sources	12
Turnⁱ	178 – 180	Combined sources	3
Beta strandⁱ	188 – 193	Combined sources	6
Turnⁱ	194 – 196	Combined sources	3
Beta strandⁱ	197 – 200	Combined sources	4
Turnⁱ	203 – 205	Combined sources	3
Beta strandⁱ	206 – 209	Combined sources	4
Beta strandⁱ	214 – 217	Combined sources	4
Beta strandⁱ	230 – 236	Combined sources	7
Beta strandⁱ	248 – 253	Combined sources	6
Helixⁱ	256 – 258	Combined sources	3
Turnⁱ	259 – 261	Combined sources	3
Beta strandⁱ	264 – 270	Combined sources	7
Helixⁱ	272 – 279	Combined sources	8
Beta strandⁱ	292 – 299	Combined sources	8

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	5MQF	electron microscopy	5.90	o	1-301	[»]
	5YZG	electron microscopy	4.10	1	1-301	[»]
	5Z56	electron microscopy	5.10	y	1-301	[»]
	5Z57	electron microscopy	6.50	y	1-301	[»]
ProteinModelPortalⁱ	Q9UNP9
SMRⁱ	Q9UNP9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9UNP9

EvolutionaryTraceⁱ

Q9UNP9

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	6 – 84	RRMPROSITE-ProRule annotationAdd BLAST		79
Domainⁱ	143 – 299	PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST		157

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	60 – 63	Poly-Ala		4

Domainⁱ

The RRM domain mediates both interaction with RNA and with KMT2A (via the third PHD-type zinc-finger), but has much higher affinity for the KMT2A PHD-type zinc-finger.2 Publications

Sequence similaritiesⁱ

Belongs to the cyclophilin-type PPIase family. PPIase E subfamily.Curated

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158790
HOGENOMⁱ	HOG000065981
HOVERGENⁱ	HBG001065
InParanoidⁱ	Q9UNP9
KEGG Orthology (KO) More...KOⁱ	K09564
OMAⁱ	FNLKHNS
Database of Orthologous Groups More...OrthoDBⁱ	1484092at2759
PhylomeDBⁱ	Q9UNP9
TreeFamⁱ	TF313817

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd12347 RRM_PPIE, 1 hit
Gene3Dⁱ	2.40.100.10, 1 hit 3.30.70.330, 1 hit
InterProⁱ	View protein in InterPro IPR029000 Cyclophilin-like_dom_sf IPR024936 Cyclophilin-type_PPIase IPR020892 Cyclophilin-type_PPIase_CS IPR002130 Cyclophilin-type_PPIase_dom IPR012677 Nucleotide-bd_a/b_plait_sf IPR016304 PPIE IPR034168 PPIE_RRM IPR035979 RBD_domain_sf IPR000504 RRM_dom
PANTHERⁱ	PTHR11071 PTHR11071, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00160 Pro_isomerase, 1 hit PF00076 RRM_1, 1 hit
PIRSFⁱ	PIRSF001475 PPI_cyclophilin_E, 1 hit
PRINTSⁱ	PR00153 CSAPPISMRASE
SMARTⁱ	View protein in SMART SM00360 RRM, 1 hit
SUPFAMⁱ	SSF50891 SSF50891, 1 hit SSF54928 SSF54928, 1 hit
PROSITEⁱ	View protein in PROSITE PS00170 CSA_PPIASE_1, 1 hit PS50072 CSA_PPIASE_2, 1 hit PS50102 RRM, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show all Align All

Isoform A (identifier: Q9UNP9-1) [UniParc]FASTA Add to basket

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.

« 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 EENKEEEGSE PPKAETQEGE PIAKKARSNP 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 KVIIADCGEY 

V

Length:301

Mass (Da):33,431

Last modified:May 1, 2000 - v1

Checksum:ⁱF3226149A790BA42

GO

Isoform B (identifier: Q9UNP9-2) [UniParc]FASTA Add to basket

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

« 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 EENKEEEGSE PPKAETQEGE PIAKKARSNP 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 
TCDKTDWLDG KHVVFGEVTE GLDVLRQIEK QEESAITSQP RSWKLT

Show »

Length:296

Mass (Da):33,085

Checksum:ⁱB70A7F239825B54D

GO

Isoform 3 (identifier: Q9UNP9-3) [UniParc]FASTA Add to basket

Also known as: Cyclophilin-33B

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

« 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 EENKEEEGSE PPKAETQEGE PIAKKARSNP 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 GLDVLRQIEV APDTKASKAR GSRKNKDGQE 
       310 
RNWGKSQKVE SHTI

Show »

Length:314

Mass (Da):34,991

Checksum:ⁱC5D0CFB2673046D7

GO

Computationally mapped potential isoform sequencesⁱ

There are 7 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E9PEQ6	E9PEQ6_HUMAN	Peptidyl-prolyl cis-trans isomerase Peptidyl-prolyl cis-trans isomerase, PPIase, EC 5.2.1.8	PPIE	250	Annotation score:
E9PKY5	E9PKY5_HUMAN	Peptidyl-prolyl cis-trans isomerase Peptidyl-prolyl cis-trans isomerase, PPIase, EC 5.2.1.8	PPIE	213	Annotation score:
E9PK21	E9PK21_HUMAN	Peptidyl-prolyl cis-trans isomerase... Peptidyl-prolyl cis-trans isomerase E	PPIE	208	Annotation score:
E9PIB0	E9PIB0_HUMAN	Peptidyl-prolyl cis-trans isomerase... Peptidyl-prolyl cis-trans isomerase E	PPIE	71	Annotation score:
H0YE31	H0YE31_HUMAN	Peptidyl-prolyl cis-trans isomerase... Peptidyl-prolyl cis-trans isomerase E	PPIE	36	Annotation score:
H0YCV4	H0YCV4_HUMAN	Peptidyl-prolyl cis-trans isomerase... Peptidyl-prolyl cis-trans isomerase E	PPIE	37	Annotation score:
E9PMH0	E9PMH0_HUMAN	Peptidyl-prolyl cis-trans isomerase... Peptidyl-prolyl cis-trans isomerase E	PPIE	38	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	151	K → R in AAZ93379 (Ref. 3) Curated	1
Sequence conflictⁱ	207	N → D in AAZ93379 (Ref. 3) Curated	1
Sequence conflictⁱ	287	K → N in AAC00006 (Ref. 2) Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_046370	280 – 301	AQGSK…CGEYV → VAPDTKASKARGSRKNKDGQ ERNWGKSQKVESHTI in isoform 3. 1 PublicationAdd BLAST		22
Alternative sequenceⁱVSP_005181	280 – 301	AQGSK…CGEYV → KQEESAITSQPRSWKLT in isoform B. 2 PublicationsAdd BLAST		22

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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 Genomic DNA No translation available. AL033527 Genomic DNA No translation available. AL035404 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX07255.1 BC004898 mRNA Translation: AAH04898.1 BC008451 mRNA Translation: AAH08451.1 BC107736 mRNA Translation: AAI07737.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS442.1 [Q9UNP9-2] CCDS443.1 [Q9UNP9-1] CCDS53299.1 [Q9UNP9-3]
PIRⁱ	S66681
NCBI Reference Sequences More...RefSeqⁱ	NP_001181936.1, NM_001195007.1 [Q9UNP9-3] NP_006103.1, NM_006112.3 [Q9UNP9-1] NP_982281.1, NM_203456.2 [Q9UNP9-2] XP_016855540.1, XM_017000051.1 [Q9UNP9-3]
UniGeneⁱ	Hs.524690

Genome annotation databases

Ensemblⁱ	ENST00000324379; ENSP00000312769; ENSG00000084072 [Q9UNP9-1] ENST00000356511; ENSP00000348904; ENSG00000084072 [Q9UNP9-2] ENST00000372830; ENSP00000361918; ENSG00000084072 [Q9UNP9-3]
GeneIDⁱ	10450
KEGGⁱ	hsa:10450
UCSC genome browser More...UCSCⁱ	uc001cds.3 human [Q9UNP9-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UNP9	Peptidyl-prolyl cis-trans isomerase E		PANTR		301	UniRef100_Q9UNP9
Peptidyl-prolyl cis-trans isomerase E		PANPA		301
Peptidyl-prolyl cis-trans isomerase E		GORGO		301
Peptidyl-prolyl cis-trans isomerase		HUMAN		217
UPI000017304D		PANPA		235
Q9UNP9-2	Peptidyl-prolyl cis-trans isomerase E		PANPA		296	UniRef100_Q9UNP9-2
UPI000D0C9291		HUMAN		212

Protein	Similar proteins		Species	Score	Length	Source
Q9UNP9	Peptidyl-prolyl cis-trans isomerase E		PANTR		301	UniRef90_Q9UNP9
Peptidyl-prolyl cis-trans isomerase E		PANPA		301
Peptidyl-prolyl cis-trans isomerase E		GORGO		301
Peptidyl-prolyl cis-trans isomerase		HUMAN		217
Peptidylprolyl isomerase E		PAPAN		343
+226

Protein	Similar proteins		Species	Score	Length	Source
Q9UNP9	Peptidyl-prolyl cis-trans isomerase E		PANTR		301	UniRef50_Q9UNP9
Peptidyl-prolyl cis-trans isomerase E		PANPA		301
Peptidyl-prolyl cis-trans isomerase E		GORGO		301
Peptidyl-prolyl cis-trans isomerase		HUMAN		217
Peptidylprolyl isomerase E		PAPAN		343
+750

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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 Genomic DNA No translation available. AL033527 Genomic DNA No translation available. AL035404 Genomic DNA No translation available. CH471059 Genomic DNA Translation: EAX07255.1 BC004898 mRNA Translation: AAH04898.1 BC008451 mRNA Translation: AAH08451.1 BC107736 mRNA Translation: AAI07737.1
CCDSⁱ	CCDS442.1 [Q9UNP9-2] CCDS443.1 [Q9UNP9-1] CCDS53299.1 [Q9UNP9-3]
PIRⁱ	S66681
RefSeqⁱ	NP_001181936.1, NM_001195007.1 [Q9UNP9-3] NP_006103.1, NM_006112.3 [Q9UNP9-1] NP_982281.1, NM_203456.2 [Q9UNP9-2] XP_016855540.1, XM_017000051.1 [Q9UNP9-3]
UniGeneⁱ	Hs.524690

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB 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	[»]
	5MQF	electron microscopy	5.90	o	1-301	[»]
	5YZG	electron microscopy	4.10	1	1-301	[»]
	5Z56	electron microscopy	5.10	y	1-301	[»]
	5Z57	electron microscopy	6.50	y	1-301	[»]
ProteinModelPortalⁱ	Q9UNP9
SMRⁱ	Q9UNP9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115714, 222 interactors
CORUMⁱ	Q9UNP9
DIPⁱ	DIP-34757N
IntActⁱ	Q9UNP9, 18 interactors
MINTⁱ	Q9UNP9

PTM databases

iPTMnetⁱ	Q9UNP9
PhosphoSitePlusⁱ	Q9UNP9

Polymorphism and mutation databases

BioMutaⁱ	PPIE
DMDMⁱ	13124097

Proteomic databases

EPDⁱ	Q9UNP9
jPOSTⁱ	Q9UNP9
PeptideAtlasⁱ	Q9UNP9
PRIDEⁱ	Q9UNP9
ProteomicsDBⁱ	85321 85322 [Q9UNP9-2]
TopDownProteomicsⁱ	Q9UNP9-1 [Q9UNP9-1] Q9UNP9-2 [Q9UNP9-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	10450
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000324379; ENSP00000312769; ENSG00000084072 [Q9UNP9-1] ENST00000356511; ENSP00000348904; ENSG00000084072 [Q9UNP9-2] ENST00000372830; ENSP00000361918; ENSG00000084072 [Q9UNP9-3]
GeneIDⁱ	10450
KEGGⁱ	hsa:10450
UCSCⁱ	uc001cds.3 human [Q9UNP9-1]

Organism-specific databases

CTDⁱ	10450
DisGeNETⁱ	10450
EuPathDBⁱ	HostDB:ENSG00000084072.16
GeneCardsⁱ	PPIE
HGNCⁱ	HGNC:9258 PPIE
HPAⁱ	HPA019357 HPA020131
MIMⁱ	602435 gene
neXtProtⁱ	NX_Q9UNP9
OpenTargetsⁱ	ENSG00000084072
PharmGKBⁱ	PA33583
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

GeneTreeⁱ	ENSGT00940000158790
HOGENOMⁱ	HOG000065981
HOVERGENⁱ	HBG001065
InParanoidⁱ	Q9UNP9
KOⁱ	K09564
OMAⁱ	FNLKHNS
OrthoDBⁱ	1484092at2759
PhylomeDBⁱ	Q9UNP9
TreeFamⁱ	TF313817

Enzyme and pathway databases

BRENDAⁱ	5.2.1.8 2681
Reactomeⁱ	R-HSA-6781823 Formation of TC-NER Pre-Incision Complex R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER) R-HSA-6782135 Dual incision in TC-NER R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-6798695 Neutrophil degranulation R-HSA-72163 mRNA Splicing - Major Pathway

Miscellaneous databases

ChiTaRSⁱ	PPIE human
EvolutionaryTraceⁱ	Q9UNP9
GeneWikiⁱ	PPIE_(gene)
GenomeRNAiⁱ	10450
Protein Ontology More...PROⁱ	PR:Q9UNP9
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000084072 Expressed in 227 organ(s), highest expression level in right testis
ExpressionAtlasⁱ	Q9UNP9 baseline and differential
Genevisibleⁱ	Q9UNP9 HS

Family and domain databases

CDDⁱ	cd12347 RRM_PPIE, 1 hit
Gene3Dⁱ	2.40.100.10, 1 hit 3.30.70.330, 1 hit
InterProⁱ	View protein in InterPro IPR029000 Cyclophilin-like_dom_sf IPR024936 Cyclophilin-type_PPIase IPR020892 Cyclophilin-type_PPIase_CS IPR002130 Cyclophilin-type_PPIase_dom IPR012677 Nucleotide-bd_a/b_plait_sf IPR016304 PPIE IPR034168 PPIE_RRM IPR035979 RBD_domain_sf IPR000504 RRM_dom
PANTHERⁱ	PTHR11071 PTHR11071, 1 hit
Pfamⁱ	View protein in Pfam PF00160 Pro_isomerase, 1 hit PF00076 RRM_1, 1 hit
PIRSFⁱ	PIRSF001475 PPI_cyclophilin_E, 1 hit
PRINTSⁱ	PR00153 CSAPPISMRASE
SMARTⁱ	View protein in SMART SM00360 RRM, 1 hit
SUPFAMⁱ	SSF50891 SSF50891, 1 hit SSF54928 SSF54928, 1 hit
PROSITEⁱ	View protein in PROSITE PS00170 CSA_PPIASE_1, 1 hit PS50072 CSA_PPIASE_2, 1 hit PS50102 RRM, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PPIE_HUMAN
Accessionⁱ	Q9UNP9Primary (citable) accession number: Q9UNP9 Secondary accession number(s): B2R971 Q9UIZ5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
	Last sequence update:	May 1, 2000
	Last modified:	February 13, 2019
	This is version 187 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - Q9UNP9 (PPIE_HUMAN)

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Peptidyl-prolyl cis-trans isomerase E

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

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Miscellaneous databases

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ