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O43447 (PPIH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.9

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRPF4O431722EBI-1055615,EBI-718395

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 177176Peptidyl-prolyl cis-trans isomerase H
PRO_0000064162

Regions

Domain14 – 176163PPIase cyclophilin-type

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Experimental info

Mutagenesis1331W → F: Abolishes inhibition by cyclosporin A. Ref.4

Secondary structure

................................. 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43447 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 566BCE6361E0F339

FASTA17719,208
        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 

« Hide

References

« Hide '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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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.
[9]"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.
RefSeqNP_006338.1. NM_006347.3.
XP_005270419.1. XM_005270362.1.
XP_005270420.1. XM_005270363.1.
XP_005270421.1. XM_005270364.1.
XP_005270422.1. XM_005270365.1.
UniGeneHs.256639.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MZWX-ray2.00A1-177[»]
1QOIX-ray2.00A1-177[»]
ProteinModelPortalO43447.
SMRO43447. Positions 5-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115728. 20 interactions.
IntActO43447. 8 interactions.
MINTMINT-270606.
STRING9606.ENSP00000306614.

Chemistry

DrugBankDB00172. L-Proline.

PTM databases

PhosphoSiteO43447.

Proteomic databases

PaxDbO43447.
PRIDEO43447.

Protocols and materials databases

DNASU10465.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304979; ENSP00000306614; ENSG00000171960.
GeneID10465.
KEGGhsa:10465.
UCSCuc001chq.3. human.

Organism-specific databases

CTD10465.
GeneCardsGC01P043097.
HGNCHGNC:14651. PPIH.
HPAHPA059019.
MIM606095. gene.
neXtProtNX_O43447.
PharmGKBPA33586.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidO43447.
KOK09567.
OMAIISECGE.
OrthoDBEOG79GT7W.
PhylomeDBO43447.
TreeFamTF312958.

Gene expression databases

ArrayExpressO43447.
BgeeO43447.
CleanExHS_PPIH.
GenevestigatorO43447.

Family and domain databases

InterProIPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIH. human.
EvolutionaryTraceO43447.
GeneWikiPPIH.
GenomeRNAi10465.
NextBio39685.
PROO43447.
SOURCESearch...

Entry information

Entry namePPIH_HUMAN
AccessionPrimary (citable) accession number: O43447
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 1998
Last modified: March 19, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM