Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D868 (PPIH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Gene names
Name:Ppih
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Enzyme regulation

Inhibited by cyclosporin A By similarity.

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. Heterodimer with PRPF18 By similarity.

Subcellular location

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

Sequence similarities

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

Contains 1 PPIase cyclophilin-type domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D868-1)

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.
Isoform 2 (identifier: Q9D868-2)

The sequence of this isoform differs from the canonical sequence as follows:
     156-188: FQAPLGKRVQAWTHSLTCPALTGILALILMPTE → NVPTGPNNKPKLPVVISQCGEM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 188187Peptidyl-prolyl cis-trans isomerase H
PRO_0000064163

Regions

Domain14 – 176163PPIase cyclophilin-type

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence156 – 18833FQAPL…LMPTE → NVPTGPNNKPKLPVVISQCG EM in isoform 2.
VSP_008325

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E11D29067BA98101

FASTA18820,464
        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        180 
GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIEFQAPL GKRVQAWTHS LTCPALTGIL 


ALILMPTE 

« Hide

Isoform 2 [UniParc].

Checksum: 566BCE6361E0F339
Show »

FASTA17719,208

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Cerebellum, Embryo, Head and Small intestine.
[2]"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] (ISOFORM 2).
Tissue: Mammary cancer and Pancreas.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003179 mRNA. Translation: BAB22623.1.
AK008394 mRNA. Translation: BAB25645.1.
AK005202 mRNA. Translation: BAB23880.1.
AK014665 mRNA. Translation: BAB29493.1.
BC016565 mRNA. No translation available.
BC050116 mRNA. Translation: AAH50116.1.
CCDSCCDS18580.1. [Q9D868-2]
CCDS51288.1. [Q9D868-1]
RefSeqNP_001103599.1. NM_001110129.1. [Q9D868-2]
NP_001103600.1. NM_001110130.1. [Q9D868-1]
NP_082953.1. NM_028677.4. [Q9D868-2]
UniGeneMm.304080.
Mm.371613.
Mm.380651.

3D structure databases

ProteinModelPortalQ9D868.
SMRQ9D868. Positions 5-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D868. 1 interaction.
MINTMINT-4108453.

PTM databases

PhosphoSiteQ9D868.

Proteomic databases

MaxQBQ9D868.
PaxDbQ9D868.
PRIDEQ9D868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056458; ENSMUSP00000051221; ENSMUSG00000060288. [Q9D868-2]
ENSMUST00000106317; ENSMUSP00000101924; ENSMUSG00000060288. [Q9D868-1]
ENSMUST00000106318; ENSMUSP00000101925; ENSMUSG00000060288. [Q9D868-2]
ENSMUST00000106321; ENSMUSP00000101928; ENSMUSG00000060288. [Q9D868-2]
GeneID66101.
KEGGmmu:66101.
UCSCuc008ulz.2. mouse. [Q9D868-1]

Organism-specific databases

CTD10465.
MGIMGI:106499. Ppih.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00750000117331.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidQ9D868.
KOK09567.
OMAISQCGQM.
OrthoDBEOG79GT7W.
PhylomeDBQ9D868.
TreeFamTF312958.

Gene expression databases

ArrayExpressQ9D868.
BgeeQ9D868.
CleanExMM_PPIH.
GenevestigatorQ9D868.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. 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.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320626.
PROQ9D868.
SOURCESearch...

Entry information

Entry namePPIH_MOUSE
AccessionPrimary (citable) accession number: Q9D868
Secondary accession number(s): Q9CQU7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot