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A2AR02

- PPIG_MOUSE

UniProt

A2AR02 - PPIG_MOUSE

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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

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.

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
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: Ensembl
  2. nuclear matrix Source: UniProtKB-SubCell
  3. nuclear speck Source: UniProtKB-SubCell
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 – 2521Phosphoserine By similarity
Modified residuei254 – 2541Phosphoserine By similarity
Modified residuei255 – 2551Phosphoserine By similarity
Modified residuei257 – 2571Phosphoserine By similarity
Modified residuei313 – 3131Phosphoserine By similarity
Modified residuei354 – 3541Phosphoserine By similarity
Modified residuei356 – 3561Phosphothreonine By similarity
Modified residuei395 – 3951Phosphoserine By similarity
Modified residuei411 – 4111Phosphoserine By similarity
Modified residuei413 – 4131Phosphoserine By similarity
Modified residuei685 – 6851Phosphoserine By similarity
Modified residuei688 – 6881Phosphoserine By similarity
Modified residuei694 – 6941Phosphoserine By similarity
Modified residuei746 – 7461Phosphothreonine By similarity
Modified residuei751 – 7511Phosphoserine By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 176166PPIase cyclophilin-typeAdd
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

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

Sequence conflict

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

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

« 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: July 9, 2014
This is version 64 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