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A2AR02

- PPIG_MOUSE

UniProt

A2AR02 - PPIG_MOUSE

Protein

Peptidyl-prolyl cis-trans isomerase G

Gene

Ppig

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (20 Feb 2007)
      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. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Cyclosporin A (CsA)-sensitive.By similarity

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase G (EC:5.2.1.8)
    Short name:
    PPIase G
    Short name:
    Peptidyl-prolyl isomerase G
    Alternative name(s):
    Cyclophilin G
    Rotamase G
    Gene namesi
    Name:Ppig
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2445173. Ppig.

    Subcellular locationi

    Nucleus matrix. Nucleus speckle
    Note: Colocalizes with splicing factors at nuclear speckles.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nuclear matrix Source: UniProtKB-SubCell
    3. nuclear speck Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 752752Peptidyl-prolyl cis-trans isomerase GPRO_0000282597Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei252 – 2521PhosphoserineBy similarity
    Modified residuei254 – 2541PhosphoserineBy similarity
    Modified residuei255 – 2551PhosphoserineBy similarity
    Modified residuei257 – 2571PhosphoserineBy similarity
    Modified residuei313 – 3131PhosphoserineBy similarity
    Modified residuei354 – 3541PhosphoserineBy similarity
    Modified residuei356 – 3561PhosphothreonineBy similarity
    Modified residuei395 – 3951PhosphoserineBy similarity
    Modified residuei411 – 4111PhosphoserineBy similarity
    Modified residuei413 – 4131PhosphoserineBy similarity
    Modified residuei685 – 6851PhosphoserineBy similarity
    Modified residuei688 – 6881PhosphoserineBy similarity
    Modified residuei694 – 6941PhosphoserineBy similarity
    Modified residuei746 – 7461PhosphothreonineBy similarity
    Modified residuei751 – 7511PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiA2AR02.
    PaxDbiA2AR02.
    PRIDEiA2AR02.

    PTM databases

    PhosphoSiteiA2AR02.

    Expressioni

    Gene expression databases

    ArrayExpressiA2AR02.
    BgeeiA2AR02.
    CleanExiMM_PPIG.
    GenevestigatoriA2AR02.

    Interactioni

    Subunit structurei

    Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II.By similarity

    Protein-protein interaction databases

    BioGridi230703. 1 interaction.
    IntActiA2AR02. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliA2AR02.
    SMRiA2AR02. Positions 6-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 176166PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi180 – 19213Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi193 – 22331Asp/Glu/Ser-richAdd
    BLAST
    Compositional biasi193 – 20614Poly-SerAdd
    BLAST
    Compositional biasi224 – 25128Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi539 – 63799Arg/Ser-rich (RS domain)Add
    BLAST
    Compositional biasi619 – 6246Poly-Arg

    Domaini

    The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0652.
    GeneTreeiENSGT00550000074595.
    HOGENOMiHOG000115659.
    HOVERGENiHBG048162.
    InParanoidiA2AR02.
    KOiK09566.
    OMAiHDKNKKF.
    OrthoDBiEOG79GT7W.
    PhylomeDBiA2AR02.
    TreeFamiTF318563.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    A2AR02-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT    50
    GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF 100
    AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV 150
    VREIENQKTD AASKPFAEVR ILSCGELIPK SKVKKEEKKR HKSSSSSSSS 200
    DSDSSSDSQS SSESSDSESA SEEKSRKRKK KHRKNSRKHK KEKKKRKKSK 250
    KSPSSESEAE NVDAQPQSTV RPEEIPPIPE NRFLMRKSPP KADDKERKNR 300
    ERERERECNP PNSQPASYQR RFLVTRSGRK IKGRGPRRYR TPSRSRSRDR 350
    FRRSETPPHW RQEMQRAQRM RVSSGERWIK GDKSELNEIK ENQRSPVRVK 400
    EKKITDHRHM SESPNRKVEK EKKAKDHKSE SKERDIRRNS EKDDKYNKNK 450
    VKKRGKSKSR SKSKERSKSK ERDSKHSRHE DKRVRSRSKE RDHETTKEKE 500
    KPLDPKGKDQ ERSRSKENSK QVESKSNEHD HSKSKEKDRR AQSRSRERDL 550
    TKSKHSYNSR TRERSRSRDR SRRVRSRSHD RDRSRSKEYH RYREQEYRRR 600
    GRSRSRDRRT PGRSRSKDRR RRRRDSRSSE REESQSRNKD KYRSQESKSS 650
    HRKENSEGEK RTYSKSRDHN SSSNNREKKA DREQSPVSKT KQSSQDNEVK 700
    SSTLKNQEDE KTRSPVEKEN QKSKGQENDH VHDKNKKCDH ESSPGTDEDK 750
    SG 752
    Length:752
    Mass (Da):88,325
    Last modified:February 20, 2007 - v1
    Checksum:iA78CA4EEB0E0871B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211Missing in AAC05726. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL845261 Genomic DNA. Translation: CAM16370.1.
    U91923 mRNA. Translation: AAC05726.1.
    AK135713 mRNA. Translation: BAE22623.1.
    AK164670 mRNA. Translation: BAE37869.1.
    CCDSiCCDS38137.1.
    RefSeqiNP_001074555.1. NM_001081086.1.
    XP_006499247.1. XM_006499184.1.
    XP_006499248.1. XM_006499185.1.
    XP_006499249.1. XM_006499186.1.
    XP_006499250.1. XM_006499187.1.
    UniGeneiMm.11815.
    Mm.474951.
    Mm.488936.

    Genome annotation databases

    EnsembliENSMUST00000040915; ENSMUSP00000045945; ENSMUSG00000042133.
    ENSMUST00000090858; ENSMUSP00000088370; ENSMUSG00000042133.
    GeneIDi228005.
    KEGGimmu:228005.
    UCSCiuc008jyl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL845261 Genomic DNA. Translation: CAM16370.1 .
    U91923 mRNA. Translation: AAC05726.1 .
    AK135713 mRNA. Translation: BAE22623.1 .
    AK164670 mRNA. Translation: BAE37869.1 .
    CCDSi CCDS38137.1.
    RefSeqi NP_001074555.1. NM_001081086.1.
    XP_006499247.1. XM_006499184.1.
    XP_006499248.1. XM_006499185.1.
    XP_006499249.1. XM_006499186.1.
    XP_006499250.1. XM_006499187.1.
    UniGenei Mm.11815.
    Mm.474951.
    Mm.488936.

    3D structure databases

    ProteinModelPortali A2AR02.
    SMRi A2AR02. Positions 6-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230703. 1 interaction.
    IntActi A2AR02. 1 interaction.

    PTM databases

    PhosphoSitei A2AR02.

    Proteomic databases

    MaxQBi A2AR02.
    PaxDbi A2AR02.
    PRIDEi A2AR02.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040915 ; ENSMUSP00000045945 ; ENSMUSG00000042133 .
    ENSMUST00000090858 ; ENSMUSP00000088370 ; ENSMUSG00000042133 .
    GeneIDi 228005.
    KEGGi mmu:228005.
    UCSCi uc008jyl.1. mouse.

    Organism-specific databases

    CTDi 9360.
    MGIi MGI:2445173. Ppig.

    Phylogenomic databases

    eggNOGi COG0652.
    GeneTreei ENSGT00550000074595.
    HOGENOMi HOG000115659.
    HOVERGENi HBG048162.
    InParanoidi A2AR02.
    KOi K09566.
    OMAi HDKNKKF.
    OrthoDBi EOG79GT7W.
    PhylomeDBi A2AR02.
    TreeFami TF318563.

    Miscellaneous databases

    NextBioi 378889.
    PROi A2AR02.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi A2AR02.
    Bgeei A2AR02.
    CleanExi MM_PPIG.
    Genevestigatori A2AR02.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. Lee C.G., Hurwitz J.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-74.
      Strain: 129/Sv.
    3. "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] OF 287-495 AND 549-752.
      Strain: C57BL/6J.
      Tissue: Stomach.

    Entry informationi

    Entry nameiPPIG_MOUSE
    AccessioniPrimary (citable) accession number: A2AR02
    Secondary accession number(s): O70134, Q3TP68, Q3UXE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 65 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