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Protein

Peptidyl-prolyl cis-trans isomerase H

Gene

Ppih

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Enzyme regulationi

Inhibited by cyclosporin A.By similarity

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: MGI
  2. ribonucleoprotein complex binding Source: MGI

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. positive regulation of viral genome replication Source: MGI
  3. protein folding Source: InterPro
  4. protein peptidyl-prolyl isomerization Source: GO_Central
  5. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase H (EC:5.2.1.8)
Short name:
PPIase H
Alternative name(s):
Rotamase H
Gene namesi
Name:Ppih
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:106499. Ppih.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nuclear speck Source: MGI
  3. spliceosomal complex Source: UniProtKB-KW
  4. U4/U6 snRNP Source: MGI
  5. U4/U6 x U5 tri-snRNP complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 188187Peptidyl-prolyl cis-trans isomerase HPRO_0000064163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D868.
PaxDbiQ9D868.
PRIDEiQ9D868.

PTM databases

PhosphoSiteiQ9D868.

Expressioni

Gene expression databases

BgeeiQ9D868.
CleanExiMM_PPIH.
ExpressionAtlasiQ9D868. baseline and differential.
GenevestigatoriQ9D868.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ9D868. 1 interaction.
MINTiMINT-4108453.

Structurei

3D structure databases

ProteinModelPortaliQ9D868.
SMRiQ9D868. Positions 5-155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 176163PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiQ9D868.
KOiK09567.
OMAiGTGVMSI.
OrthoDBiEOG79GT7W.
PhylomeDBiQ9D868.
TreeFamiTF312958.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9D868-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE
60 70 80 90 100
FRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF
110 120 130 140 150
KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV
160 170 180
MRKIEFQAPL GKRVQAWTHS LTCPALTGIL ALILMPTE
Length:188
Mass (Da):20,464
Last modified:June 1, 2001 - v1
Checksum:iE11D29067BA98101
GO
Isoform 2 (identifier: Q9D868-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:177
Mass (Da):19,208
Checksum:i566BCE6361E0F339
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei156 – 18833FQAPL…LMPTE → NVPTGPNNKPKLPVVISQCG EM in isoform 2. 2 PublicationsVSP_008325Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18580.1. [Q9D868-2]
CCDS51288.1. [Q9D868-1]
RefSeqiNP_001103599.1. NM_001110129.1. [Q9D868-2]
NP_001103600.1. NM_001110130.1. [Q9D868-1]
NP_082953.1. NM_028677.4. [Q9D868-2]
UniGeneiMm.304080.
Mm.371613.
Mm.380651.

Genome annotation databases

EnsembliENSMUST00000056458; ENSMUSP00000051221; ENSMUSG00000060288. [Q9D868-2]
ENSMUST00000106317; ENSMUSP00000101924; ENSMUSG00000060288. [Q9D868-1]
ENSMUST00000106318; ENSMUSP00000101925; ENSMUSG00000060288. [Q9D868-2]
ENSMUST00000106321; ENSMUSP00000101928; ENSMUSG00000060288. [Q9D868-2]
GeneIDi66101.
KEGGimmu:66101.
UCSCiuc008ulz.2. mouse. [Q9D868-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18580.1. [Q9D868-2]
CCDS51288.1. [Q9D868-1]
RefSeqiNP_001103599.1. NM_001110129.1. [Q9D868-2]
NP_001103600.1. NM_001110130.1. [Q9D868-1]
NP_082953.1. NM_028677.4. [Q9D868-2]
UniGeneiMm.304080.
Mm.371613.
Mm.380651.

3D structure databases

ProteinModelPortaliQ9D868.
SMRiQ9D868. Positions 5-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D868. 1 interaction.
MINTiMINT-4108453.

Chemistry

BindingDBiQ9D868.

PTM databases

PhosphoSiteiQ9D868.

Proteomic databases

MaxQBiQ9D868.
PaxDbiQ9D868.
PRIDEiQ9D868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056458; ENSMUSP00000051221; ENSMUSG00000060288. [Q9D868-2]
ENSMUST00000106317; ENSMUSP00000101924; ENSMUSG00000060288. [Q9D868-1]
ENSMUST00000106318; ENSMUSP00000101925; ENSMUSG00000060288. [Q9D868-2]
ENSMUST00000106321; ENSMUSP00000101928; ENSMUSG00000060288. [Q9D868-2]
GeneIDi66101.
KEGGimmu:66101.
UCSCiuc008ulz.2. mouse. [Q9D868-1]

Organism-specific databases

CTDi10465.
MGIiMGI:106499. Ppih.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiQ9D868.
KOiK09567.
OMAiGTGVMSI.
OrthoDBiEOG79GT7W.
PhylomeDBiQ9D868.
TreeFamiTF312958.

Miscellaneous databases

NextBioi320626.
PROiQ9D868.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D868.
CleanExiMM_PPIH.
ExpressionAtlasiQ9D868. baseline and differential.
GenevestigatoriQ9D868.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiPPIH_MOUSE
AccessioniPrimary (citable) accession number: Q9D868
Secondary accession number(s): Q9CQU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.