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Protein

Peptidyl-prolyl cis-trans isomerase G

Gene

Ppig

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. 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: GO_Central
  2. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. protein folding Source: InterPro
  2. protein peptidyl-prolyl isomerization Source: GO_Central
Complete GO annotation...

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: MGI
  2. nuclear matrix Source: UniProtKB-SubCell
  3. nuclear speck Source: UniProtKB-SubCell
  4. nucleus Source: MGI
Complete GO annotation...

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

BgeeiA2AR02.
CleanExiMM_PPIG.
ExpressionAtlasiA2AR02. baseline and differential.
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.
OMAiHNKSKDK.
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

        10         20         30         40         50
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT
60 70 80 90 100
GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF
110 120 130 140 150
AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV
160 170 180 190 200
VREIENQKTD AASKPFAEVR ILSCGELIPK SKVKKEEKKR HKSSSSSSSS
210 220 230 240 250
DSDSSSDSQS SSESSDSESA SEEKSRKRKK KHRKNSRKHK KEKKKRKKSK
260 270 280 290 300
KSPSSESEAE NVDAQPQSTV RPEEIPPIPE NRFLMRKSPP KADDKERKNR
310 320 330 340 350
ERERERECNP PNSQPASYQR RFLVTRSGRK IKGRGPRRYR TPSRSRSRDR
360 370 380 390 400
FRRSETPPHW RQEMQRAQRM RVSSGERWIK GDKSELNEIK ENQRSPVRVK
410 420 430 440 450
EKKITDHRHM SESPNRKVEK EKKAKDHKSE SKERDIRRNS EKDDKYNKNK
460 470 480 490 500
VKKRGKSKSR SKSKERSKSK ERDSKHSRHE DKRVRSRSKE RDHETTKEKE
510 520 530 540 550
KPLDPKGKDQ ERSRSKENSK QVESKSNEHD HSKSKEKDRR AQSRSRERDL
560 570 580 590 600
TKSKHSYNSR TRERSRSRDR SRRVRSRSHD RDRSRSKEYH RYREQEYRRR
610 620 630 640 650
GRSRSRDRRT PGRSRSKDRR RRRRDSRSSE REESQSRNKD KYRSQESKSS
660 670 680 690 700
HRKENSEGEK RTYSKSRDHN SSSNNREKKA DREQSPVSKT KQSSQDNEVK
710 720 730 740 750
SSTLKNQEDE KTRSPVEKEN QKSKGQENDH VHDKNKKCDH ESSPGTDEDK

SG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi230703. 1 interaction.
IntActiA2AR02. 1 interaction.

PTM databases

PhosphoSiteiA2AR02.

Proteomic databases

MaxQBiA2AR02.
PaxDbiA2AR02.
PRIDEiA2AR02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9360.
MGIiMGI:2445173. Ppig.

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiPpig. mouse.
NextBioi378889.
PROiA2AR02.
SOURCEiSearch...

Gene expression databases

BgeeiA2AR02.
CleanExiMM_PPIG.
ExpressionAtlasiA2AR02. baseline and differential.
GenevestigatoriA2AR02.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 69 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.