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Q9D868

- PPIH_MOUSE

UniProt

Q9D868 - PPIH_MOUSE

Protein

Peptidyl-prolyl cis-trans isomerase H

Gene

Ppih

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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: UniProtKB-KW
    2. ribonucleoprotein complex binding Source: Ensembl

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. positive regulation of viral genome replication Source: Ensembl
    3. protein folding Source: UniProtKB-KW
    4. RNA splicing Source: UniProtKB-KW

    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: UniProtKB-SubCell
    2. nuclear speck Source: UniProtKB-SubCell
    3. spliceosomal complex Source: UniProtKB-KW
    4. U4/U6 snRNP Source: Ensembl
    5. U4/U6 x U5 tri-snRNP complex Source: Ensembl

    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

    ArrayExpressiQ9D868.
    BgeeiQ9D868.
    CleanExiMM_PPIH.
    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.
    GeneTreeiENSGT00750000117331.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiQ9D868.
    KOiK09567.
    OMAiISQCGQM.
    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

    MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE    50
    FRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF 100
    KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV 150
    MRKIEFQAPL GKRVQAWTHS LTCPALTGIL ALILMPTE 188
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS18580.1. [Q9D868-2 ]
    CCDS51288.1. [Q9D868-1 ]
    RefSeqi NP_001103599.1. NM_001110129.1. [Q9D868-2 ]
    NP_001103600.1. NM_001110130.1. [Q9D868-1 ]
    NP_082953.1. NM_028677.4. [Q9D868-2 ]
    UniGenei Mm.304080.
    Mm.371613.
    Mm.380651.

    3D structure databases

    ProteinModelPortali Q9D868.
    SMRi Q9D868. Positions 5-155.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D868. 1 interaction.
    MINTi MINT-4108453.

    PTM databases

    PhosphoSitei Q9D868.

    Proteomic databases

    MaxQBi Q9D868.
    PaxDbi Q9D868.
    PRIDEi Q9D868.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056458 ; ENSMUSP00000051221 ; ENSMUSG00000060288 . [Q9D868-2 ]
    ENSMUST00000106317 ; ENSMUSP00000101924 ; ENSMUSG00000060288 . [Q9D868-1 ]
    ENSMUST00000106318 ; ENSMUSP00000101925 ; ENSMUSG00000060288 . [Q9D868-2 ]
    ENSMUST00000106321 ; ENSMUSP00000101928 ; ENSMUSG00000060288 . [Q9D868-2 ]
    GeneIDi 66101.
    KEGGi mmu:66101.
    UCSCi uc008ulz.2. mouse. [Q9D868-1 ]

    Organism-specific databases

    CTDi 10465.
    MGIi MGI:106499. Ppih.

    Phylogenomic databases

    eggNOGi COG0652.
    GeneTreei ENSGT00750000117331.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    InParanoidi Q9D868.
    KOi K09567.
    OMAi ISQCGQM.
    OrthoDBi EOG79GT7W.
    PhylomeDBi Q9D868.
    TreeFami TF312958.

    Miscellaneous databases

    NextBioi 320626.
    PROi Q9D868.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D868.
    Bgeei Q9D868.
    CleanExi MM_PPIH.
    Genevestigatori Q9D868.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 109 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