Reviewed, UniProtKB/Swiss-Prot O43447 (PPIH_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Molecular function	Chaperone Isomerase Rotamase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Ref.2 Traceable author statement. Source: ProtInc protein folding Ref.2 Traceable author statement. Source: ProtInc snRNP protein import into nucleus Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Ref.2 Traceable author statement. Source: ProtInc
Molecular function	cyclosporin A binding Ref.2 Traceable author statement. Source: ProtInc peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
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

Amino acid modifications

Modified residue

38

1

N6-acetyllysine Ref.6

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)
	O43447-1 [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: 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

EMBLGenBankDDBJ

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

IPI

IPI00007346.

RefSeq

NP_006338.1.

UniGene

Hs.256639

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

O43447. 1 interaction.

STRING

O43447.

Proteomic databases

PRIDE

O43447.

Genome annotation databases

Ensembl

ENST00000304979; 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]

GeneID

10465.

KEGG

hsa:10465.

UCSC

uc001chq.1. human.

Organism-specific databases

CTD

10465.

GeneCards

GC01P042897.

H-InvDB

HIX0000490.
HIX0056545.

HGNC

HGNC:14651. PPIH.

MIM

606095. gene.

PharmGKB

PA33586.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O43447.

HOVERGEN

O43447.

OMA

DGLLIMR.

Enzyme and pathway databases

BRENDA

5.2.1.8. 247.

Gene expression databases

ArrayExpress

O43447.

Bgee

O43447.

CleanEx

HS_PPIH.

Genevestigator

O43447.

GermOnline

ENSG00000171960. Homo sapiens.

Family and domain databases

InterPro

IPR002130. PPIase_cyclophilin.
[Graphical view]

Gene3D

G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

PROSITE

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

ProtoNet

Search...

Other Resources

DrugBank

DB00172. L-Proline.

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:	November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.