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Reviewed, UniProtKB/Swiss-Prot O43447 (PPIH_HUMAN)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase H
      Short name=PPIase H
      Short name=Rotamase H
    EC=5.2.1.8
Alternative name(s):
    U-snRNP-associated cyclophilin SnuCyp-20
      Short name=USA-CYP
    Small nuclear ribonucleoprotein particle-specific cyclophilin H
      Short name=CypH
Gene names
Name: PPIH
Synonyms: CYP20, CYPH
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. May act as a chaperone. Ref.2 Ref.4 Ref.8

Catalytic activity

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

Subunit structure

Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. This complex interacts with the U4/U5/U6 tri-snRNP complex. Heterodimer with PRPF18. Ref.2 Ref.4 Ref.1

Subcellular location

Nucleus speckle. Cytoplasm. Note: Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic. Ref.2

Miscellaneous

Inhibited by cyclosporin A.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase H subfamily.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177Peptidyl-prolyl cis-trans isomerase H
PRO_0000064162

Regions

Domain14 – 176163PPIase cyclophilin-type

Amino acid modifications

Modified residue381N6-acetyllysine Ref.6

Experimental info

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O43447-1 [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: 9404889] [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: 9570313] [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: 15489334] [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: 11823439] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-133, INTERACTION WITH PRPF4 AND PRPF18.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, MASS SPECTROMETRY.
[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: 10713041] [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: 12875835] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4, FUNCTION.

Cross-references

Sequence databases

AF016371 mRNA. Translation: AAC51927.1.
AF036331 mRNA. Translation: AAC60793.1.
BC003412 mRNA. Translation: AAH03412.1.
IPIIPI00007346.
RefSeqNP_006338.1.
UniGeneHs.256639

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MZWX-ray2.00A1-177[»]
1QOIX-ray2.00A1-177[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO43447. 1 interaction.
STRINGO43447.

Proteomic databases

PRIDEO43447.

Genome annotation databases

EnsemblENST00000304979; ENSP00000306614; ENSG00000171960; Homo sapiens. [Genome view]
ENST00000372549; ENSP00000361629; ENSG00000171960; Homo sapiens. [Genome view]
ENST00000372550; ENSP00000361630; ENSG00000171960; Homo sapiens. [Genome view]
ENST00000436387; ENSP00000405493; ENSG00000171960; Homo sapiens. [Genome view]
ENST00000440068; ENSP00000402836; ENSG00000171960; Homo sapiens. [Genome view]
ENST00000455203; ENSP00000416361; ENSG00000171960; Homo sapiens. [Genome view]
ENST00000458498; ENSP00000405074; ENSG00000171960; Homo sapiens. [Genome view]
GeneID10465.
KEGGhsa:10465.
UCSCuc001chq.1. human.

Organism-specific databases

CTD10465.
GeneCardsGC01P042897.
H-InvDBHIX0000490.
HIX0056545.
HGNCHGNC:14651. PPIH.
MIM606095. gene.
PharmGKBPA33586.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO43447.
HOVERGENO43447.
OMADGLLIMR.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.

Gene expression databases

ArrayExpressO43447.
BgeeO43447.
CleanExHS_PPIH.
GenevestigatorO43447.
GermOnlineENSG00000171960. Homo sapiens.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00172. L-Proline.
NextBio39685.
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: November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents