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A2AR02 (PPIG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase G
Short name=PPIase G
Short name=Peptidyl-prolyl isomerase G
EC=5.2.1.8
Alternative name(s):
Cyclophilin G
Rotamase G
Gene names
Name:Ppig
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

Cyclosporin A (CsA)-sensitive By similarity.

Subunit structure

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

Subcellular location

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

Domain

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

Sequence similarities

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionIsomerase
Rotamase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Compara

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752Peptidyl-prolyl cis-trans isomerase G
PRO_0000282597

Regions

Domain11 – 176166PPIase cyclophilin-type
Compositional bias180 – 19213Arg/Lys-rich (basic)
Compositional bias193 – 22331Asp/Glu/Ser-rich
Compositional bias193 – 20614Poly-Ser
Compositional bias224 – 25128Arg/Lys-rich (basic)
Compositional bias539 – 63799Arg/Ser-rich (RS domain)
Compositional bias619 – 6246Poly-Arg

Amino acid modifications

Modified residue1931Phosphoserine By similarity
Modified residue1981Phosphoserine By similarity
Modified residue2001Phosphoserine By similarity
Modified residue2041Phosphoserine By similarity
Modified residue2521Phosphoserine By similarity
Modified residue2541Phosphoserine By similarity
Modified residue2551Phosphoserine By similarity
Modified residue2571Phosphoserine By similarity
Modified residue3131Phosphoserine By similarity
Modified residue3431Phosphoserine Ref.4
Modified residue3451Phosphoserine Ref.4
Modified residue3541Phosphoserine By similarity
Modified residue3561Phosphothreonine By similarity
Modified residue3951Phosphoserine By similarity
Modified residue4111Phosphoserine By similarity
Modified residue4131Phosphoserine By similarity
Modified residue6851Phosphoserine By similarity
Modified residue6881Phosphoserine By similarity
Modified residue6941Phosphoserine By similarity
Modified residue7421Phosphoserine Ref.4
Modified residue7431Phosphoserine Ref.4
Modified residue7461Phosphothreonine Ref.4
Modified residue7511Phosphoserine By similarity

Experimental info

Sequence conflict211Missing in AAC05726. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2AR02 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: A78CA4EEB0E0871B

FASTA75288,325
        10         20         30         40         50         60 
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY 

        70         80         90        100        110        120 
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN 

       130        140        150        160        170        180 
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK 

       190        200        210        220        230        240 
SKVKKEEKKR HKSSSSSSSS DSDSSSDSQS SSESSDSESA SEEKSRKRKK KHRKNSRKHK 

       250        260        270        280        290        300 
KEKKKRKKSK KSPSSESEAE NVDAQPQSTV RPEEIPPIPE NRFLMRKSPP KADDKERKNR 

       310        320        330        340        350        360 
ERERERECNP PNSQPASYQR RFLVTRSGRK IKGRGPRRYR TPSRSRSRDR FRRSETPPHW 

       370        380        390        400        410        420 
RQEMQRAQRM RVSSGERWIK GDKSELNEIK ENQRSPVRVK EKKITDHRHM SESPNRKVEK 

       430        440        450        460        470        480 
EKKAKDHKSE SKERDIRRNS EKDDKYNKNK VKKRGKSKSR SKSKERSKSK ERDSKHSRHE 

       490        500        510        520        530        540 
DKRVRSRSKE RDHETTKEKE KPLDPKGKDQ ERSRSKENSK QVESKSNEHD HSKSKEKDRR 

       550        560        570        580        590        600 
AQSRSRERDL TKSKHSYNSR TRERSRSRDR SRRVRSRSHD RDRSRSKEYH RYREQEYRRR 

       610        620        630        640        650        660 
GRSRSRDRRT PGRSRSKDRR RRRRDSRSSE REESQSRNKD KYRSQESKSS HRKENSEGEK 

       670        680        690        700        710        720 
RTYSKSRDHN SSSNNREKKA DREQSPVSKT KQSSQDNEVK SSTLKNQEDE KTRSPVEKEN 

       730        740        750 
QKSKGQENDH VHDKNKKCDH ESSPGTDEDK SG

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. 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] OF 287-495 AND 549-752.
Strain: C57BL/6J.
Tissue: Stomach.
[4]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-345; SER-742; SER-743 AND THR-746, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL845261 Genomic DNA. Translation: CAM16370.1.
U91923 mRNA. Translation: AAC05726.1.
AK135713 mRNA. Translation: BAE22623.1.
AK164670 mRNA. Translation: BAE37869.1.
IPIIPI00349306.
RefSeqNP_001074555.1. NM_001081086.1.
UniGeneMm.11815.
Mm.474951.
Mm.488936.

3D structure databases

ProteinModelPortalA2AR02.
SMRA2AR02. Positions 6-177.
ModBaseSearch...

PTM databases

PhosphoSiteA2AR02.

Proteomic databases

PaxDbA2AR02.
PRIDEA2AR02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040915; ENSMUSP00000045945; ENSMUSG00000042133.
ENSMUST00000090858; ENSMUSP00000088370; ENSMUSG00000042133.
GeneID228005.
KEGGmmu:228005.
UCSCuc008jyl.1. mouse.

Organism-specific databases

CTD9360.
MGIMGI:2445173. Ppig.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00550000074595.
HOGENOMHOG000115659.
HOVERGENHBG048162.
InParanoidA2AR02.
KOK09566.
OMANKKFDHE.
OrthoDBEOG43FGWT.

Gene expression databases

ArrayExpressA2AR02.
BgeeA2AR02.
CleanExMM_PPIG.
GenevestigatorA2AR02.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378889.
SOURCESearch...

Entry information

Entry namePPIG_MOUSE
AccessionPrimary (citable) accession number: A2AR02
Secondary accession number(s): O70134, Q3TP68, Q3UXE0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 20, 2007
Last modified: April 3, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents