O43447 (PPIH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Rotamase H
Small nuclear ribonucleoprotein particle-specific cyclophilin H
Short name=CypH
U-snRNP-associated cyclophilin SnuCyp-20
Short name=USA-CYP

Gene names

Name:	PPIH
Synonyms:	CYP20, CYPH

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	177 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. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. Ref.2 Ref.4 Ref.8
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by cyclosporin A.
Subunit structure	Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Heterodimer with PRPF18. Ref.1 Ref.2 Ref.4 Ref.5
Subcellular location	Nucleus speckle. Cytoplasm. Note: Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic. Ref.2
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase H subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Molecular function	Chaperone Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Inferred by curator Ref.2. Source: BHF-UCL positive regulation of viral genome replication Inferred from mutant phenotype PubMed 19932913. Source: UniProtKB protein complex assembly Traceable author statement Ref.2. Source: ProtInc protein folding Traceable author statement Ref.2. Source: ProtInc
Cellular_component	U4/U6 snRNP Inferred from direct assay Ref.2. Source: BHF-UCL U4/U6 x U5 tri-snRNP complex Inferred from direct assay Ref.2. Source: BHF-UCL cytoplasm Inferred from direct assay Ref.2. Source: BHF-UCL nuclear speck Inferred from direct assay Ref.2. Source: BHF-UCL spliceosomal complex Inferred by curator Ref.2. Source: BHF-UCL
Molecular_function	cyclosporin A binding Traceable author statement Ref.2. Source: ProtInc peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.2. Source: BHF-UCL ribonucleoprotein complex binding Inferred from direct assay Ref.2. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 177

177

Peptidyl-prolyl cis-trans isomerase H

PRO_0000064162

Regions

Domain

14 – 176

163

PPIase cyclophilin-type

Experimental info

Mutagenesis

133

1

W → F: Abolishes inhibition by cyclosporin A. Ref.4

Secondary structure

1

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177

Helix Strand Turn

Details...

Beta strand

12 – 19

8

Beta strand

22 – 31

10

Turn

33 – 35

3

Helix

37 – 48

12

Beta strand

67 – 69

3

Turn

70 – 72

3

Beta strand

73 – 76

4

Turn

79 – 81

3

Beta strand

82 – 84

3

Beta strand

109 – 112

4

Beta strand

124 – 129

6

Helix

132 – 134

3

Turn

135 – 137

3

Beta strand

140 – 146

7

Helix

148 – 155

8

Helix

161 – 163

3

Beta strand

165 – 167

3

Beta strand

169 – 176

8

Sequences

	Sequence		Length	Mass (Da)
	O43447 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 566BCE6361E0F339	FASTA	177	19,208
	10 20 30 40 50 60 MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY 70 80 90 100 110 120 KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN 130 140 150 160 170 GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs." Horowitz D.S., Kobayashi R., Krainer A.R. RNA 3:1374-1387(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164, INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS. Tissue: Liver.
[2]	"The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins." Teigelkamp S., Achsel T., Mundt C., Goethel S.-F., Cronshagen U., Lane W.S., Marahiel M., Luehrmann R. RNA 4:127-141(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-67; 71-81 AND 153-164, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE U4/U5/U6 TRI-SNRNP COMPLEX. Tissue: Liver.
[3]	"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: Placenta.
[4]	"A cyclophilin functions in pre-mRNA splicing." Horowitz D.S., Lee E.J., Mabon S.A., Misteli T. EMBO J. 21:470-480(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TRP-133, INTERACTION WITH PRPF4 AND PRPF18.
[5]	"The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP." Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R. RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[6]	"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].
[7]	"Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin." Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R., Ficner R. J. Biol. Chem. 275:7439-7442(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177.
[8]	"Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide." Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R., Ficner R. J. Mol. Biol. 331:45-56(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF016371 mRNA. Translation: AAC51927.1.
AF036331 mRNA. Translation: AAC60793.1.
BC003412 mRNA. Translation: AAH03412.1.

IPI

IPI00007346.

RefSeq

NP_006338.1. NM_006347.3.

UniGene

Hs.256639.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MZW	X-ray	2.00	A	1-177	[»]
1QOI	X-ray	2.00	A	1-177	[»]

ProteinModelPortal

O43447.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43447. 6 interactions.

MINT

MINT-270606.

STRING

9606.ENSP00000306614.

PTM databases

PhosphoSite

O43447.

Proteomic databases

PaxDb

O43447.

PRIDE

O43447.

Protocols and materials databases

DNASU

10465.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000304979; ENSP00000306614; ENSG00000171960.

GeneID

10465.

KEGG

hsa:10465.

UCSC

uc001chq.3. human.

Organism-specific databases

CTD

10465.

GeneCards

GC01P043097.

HGNC

HGNC:14651. PPIH.

MIM

606095. gene.

neXtProt

NX_O43447.

PharmGKB

PA33586.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0652.

HOGENOM

HOG000065981.

HOVERGEN

HBG001065.

InParanoid

O43447.

KO

K09567.

OMA

GYKGASF.

OrthoDB

EOG4ZS946.

PhylomeDB

O43447.

Gene expression databases

ArrayExpress

O43447.

Bgee

O43447.

CleanEx

HS_PPIH.

Genevestigator

O43447.

GermOnline

ENSG00000171960. Homo sapiens.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

PPIH. human.

DrugBank

DB00172. L-Proline.

EvolutionaryTrace

O43447.

GenomeRNAi

10465.

NextBio

39685.

SOURCE

Search...

Entry information

Entry name

PPIH_HUMAN

Accession

Primary (citable) accession number: O43447

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 117 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.