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Protein

Peptidyl-prolyl cis-trans isomerase G

Gene

PPIG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.

Catalytic activityi

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

Enzyme regulationi

Cyclosporin A (CsA)-sensitive.

GO - Molecular functioni

  • cyclosporin A binding Source: ProtInc
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • protein folding Source: InterPro
  • RNA splicing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BioCyciZFISH:HS06500-MONOMER.
BRENDAi5.2.1.8. 2681.

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):
CASP10
Clk-associating RS-cyclophilin
Short name:
CARS-Cyp
Short name:
CARS-cyclophilin
Short name:
SR-cyclophilin
Short name:
SR-cyp
Short name:
SRcyp
Cyclophilin G
Rotamase G
Gene namesi
Name:PPIG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:14650. PPIG.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nuclear matrix Source: UniProtKB-SubCell
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi9360.
OpenTargetsiENSG00000138398.
PharmGKBiPA33585.

Chemistry databases

DrugBankiDB00172. L-Proline.

Polymorphism and mutation databases

BioMutaiPPIG.
DMDMi229462749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641501 – 754Peptidyl-prolyl cis-trans isomerase GAdd BLAST754

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei254PhosphoserineCombined sources1
Modified residuei256PhosphoserineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei315PhosphoserineCombined sources1
Modified residuei356PhosphoserineCombined sources1
Modified residuei358PhosphothreonineCombined sources1
Modified residuei386PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Modified residuei413PhosphoserineCombined sources1
Modified residuei415PhosphoserineCombined sources1
Modified residuei687PhosphoserineCombined sources1
Modified residuei690PhosphoserineCombined sources1
Modified residuei696PhosphoserineCombined sources1
Modified residuei744PhosphoserineCombined sources1
Modified residuei745PhosphoserineCombined sources1
Modified residuei748PhosphothreonineCombined sources1
Modified residuei753PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13427.
MaxQBiQ13427.
PaxDbiQ13427.
PeptideAtlasiQ13427.
PRIDEiQ13427.

PTM databases

iPTMnetiQ13427.
PhosphoSitePlusiQ13427.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000138398.
CleanExiHS_PPIG.
ExpressionAtlasiQ13427. baseline and differential.
GenevisibleiQ13427. HS.

Organism-specific databases

HPAiHPA021788.
HPA057469.

Interactioni

Subunit structurei

Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BEND7Q8N7W2-23EBI-396072,EBI-10181188
CEP70Q8NHQ13EBI-396072,EBI-739624
DAB1O755533EBI-396072,EBI-7875264
DACH1Q9UI36-23EBI-396072,EBI-10186082
FHL3Q96C983EBI-396072,EBI-10229248
KCTD6Q8NC693EBI-396072,EBI-2511344
LGALS3P179313EBI-396072,EBI-1170392
LGALS3Q6NVH93EBI-396072,EBI-10187804
PCBP1Q153652EBI-396072,EBI-946095
PNMA2Q9UL423EBI-396072,EBI-302355
PPCDCQ96CD23EBI-396072,EBI-724333
RBM39Q144983EBI-396072,EBI-395290
SMN2Q166374EBI-396072,EBI-395421
TFCP2Q128003EBI-396072,EBI-717422
THAP1Q9NVV93EBI-396072,EBI-741515

Protein-protein interaction databases

BioGridi114761. 45 interactors.
IntActiQ13427. 32 interactors.
MINTiMINT-1684213.
STRINGi9606.ENSP00000260970.

Chemistry databases

BindingDBiQ13427.

Structurei

Secondary structure

1754
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 16Combined sources8
Beta strandi19 – 28Combined sources10
Turni30 – 32Combined sources3
Helixi34 – 45Combined sources12
Turni46 – 48Combined sources3
Turni52 – 54Combined sources3
Beta strandi56 – 58Combined sources3
Beta strandi64 – 69Combined sources6
Turni70 – 72Combined sources3
Beta strandi73 – 76Combined sources4
Turni79 – 81Combined sources3
Beta strandi82 – 85Combined sources4
Beta strandi109 – 112Combined sources4
Beta strandi114 – 116Combined sources3
Beta strandi124 – 129Combined sources6
Helixi132 – 134Combined sources3
Turni135 – 137Combined sources3
Beta strandi140 – 146Combined sources7
Helixi148 – 155Combined sources8
Beta strandi165 – 167Combined sources3
Beta strandi169 – 176Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GW2X-ray1.80A1-179[»]
2WFIX-ray0.75A1-177[»]
2WFJX-ray0.75A1-177[»]
ProteinModelPortaliQ13427.
SMRiQ13427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13427.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 176PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST166

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi180 – 192Arg/Lys-rich (basic)Add BLAST13
Compositional biasi193 – 225Asp/Glu/Ser-richAdd BLAST33
Compositional biasi193 – 208Poly-SerAdd BLAST16
Compositional biasi226 – 253Arg/Lys-rich (basic)Add BLAST28
Compositional biasi540 – 639Arg/Ser-rich (RS domain)Add BLAST100
Compositional biasi621 – 626Poly-Arg6

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00550000074595.
HOVERGENiHBG048162.
InParanoidiQ13427.
KOiK09566.
OMAiKERDHET.
OrthoDBiEOG091G0BGL.
PhylomeDBiQ13427.
TreeFamiTF318563.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13427-1) [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

        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
SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK HKKEKKKRKK
260 270 280 290 300
SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK
310 320 330 340 350
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR
360 370 380 390 400
DRFRRSETPP HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR
410 420 430 440 450
VKERKITDHR NVSESPNRKN EKEKKVKDHK SNSKERDIRR NSEKDDKYKN
460 470 480 490 500
KVKKRAKSKS RSKSKEKSKS KERDSKHNRN EEKRMRSRSK GRDHENVKEK
510 520 530 540 550
EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR RAQSRSRECD
560 570 580 590 600
ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR
610 620 630 640 650
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK
660 670 680 690 700
SSHRKENSES EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE
710 720 730 740 750
LKSSMLKNKE DEKIRSSVEK ENQKSKGQEN DHVHEKNKKF DHESSPGTDE

DKSG
Length:754
Mass (Da):88,617
Last modified:May 5, 2009 - v2
Checksum:iD4884808D8060CD6
GO
Isoform 2 (identifier: Q13427-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-357: RYRTPSRSRSRDRFRRSE → VGDSFPRDLHNIAFVFLK
     358-754: Missing.

Show »
Length:357
Mass (Da):40,299
Checksum:i506BC6E24E1ADD4B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_055084445D → E.Corresponds to variant rs1050354dbSNPEnsembl.1
Natural variantiVAR_055085699N → D.Combined sources2 PublicationsCorresponds to variant rs8207dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009662340 – 357RYRTP…FRRSE → VGDSFPRDLHNIAFVFLK in isoform 2. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_009663358 – 754Missing in isoform 2. 1 PublicationAdd BLAST397

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40763 mRNA. Translation: AAB40347.1.
X99717 mRNA. Translation: CAA68053.1.
AC093899 Genomic DNA. Translation: AAY24119.1.
AC016772 Genomic DNA. Translation: AAY24233.1.
CH471058 Genomic DNA. Translation: EAX11267.1.
CH471058 Genomic DNA. Translation: EAX11268.1.
CH471058 Genomic DNA. Translation: EAX11269.1.
CH471058 Genomic DNA. Translation: EAX11270.1.
BC001555 mRNA. Translation: AAH01555.1.
CCDSiCCDS2235.1. [Q13427-1]
PIRiJC5314.
RefSeqiNP_004783.2. NM_004792.2. [Q13427-1]
XP_005247023.1. XM_005246966.1. [Q13427-1]
XP_005247024.1. XM_005246967.1. [Q13427-1]
UniGeneiHs.470544.
Hs.593163.

Genome annotation databases

EnsembliENST00000260970; ENSP00000260970; ENSG00000138398. [Q13427-1]
ENST00000448752; ENSP00000407083; ENSG00000138398. [Q13427-1]
ENST00000462903; ENSP00000435987; ENSG00000138398. [Q13427-2]
GeneIDi9360.
KEGGihsa:9360.
UCSCiuc002uez.4. human. [Q13427-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40763 mRNA. Translation: AAB40347.1.
X99717 mRNA. Translation: CAA68053.1.
AC093899 Genomic DNA. Translation: AAY24119.1.
AC016772 Genomic DNA. Translation: AAY24233.1.
CH471058 Genomic DNA. Translation: EAX11267.1.
CH471058 Genomic DNA. Translation: EAX11268.1.
CH471058 Genomic DNA. Translation: EAX11269.1.
CH471058 Genomic DNA. Translation: EAX11270.1.
BC001555 mRNA. Translation: AAH01555.1.
CCDSiCCDS2235.1. [Q13427-1]
PIRiJC5314.
RefSeqiNP_004783.2. NM_004792.2. [Q13427-1]
XP_005247023.1. XM_005246966.1. [Q13427-1]
XP_005247024.1. XM_005246967.1. [Q13427-1]
UniGeneiHs.470544.
Hs.593163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GW2X-ray1.80A1-179[»]
2WFIX-ray0.75A1-177[»]
2WFJX-ray0.75A1-177[»]
ProteinModelPortaliQ13427.
SMRiQ13427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114761. 45 interactors.
IntActiQ13427. 32 interactors.
MINTiMINT-1684213.
STRINGi9606.ENSP00000260970.

Chemistry databases

BindingDBiQ13427.
DrugBankiDB00172. L-Proline.

PTM databases

iPTMnetiQ13427.
PhosphoSitePlusiQ13427.

Polymorphism and mutation databases

BioMutaiPPIG.
DMDMi229462749.

Proteomic databases

EPDiQ13427.
MaxQBiQ13427.
PaxDbiQ13427.
PeptideAtlasiQ13427.
PRIDEiQ13427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260970; ENSP00000260970; ENSG00000138398. [Q13427-1]
ENST00000448752; ENSP00000407083; ENSG00000138398. [Q13427-1]
ENST00000462903; ENSP00000435987; ENSG00000138398. [Q13427-2]
GeneIDi9360.
KEGGihsa:9360.
UCSCiuc002uez.4. human. [Q13427-1]

Organism-specific databases

CTDi9360.
DisGeNETi9360.
GeneCardsiPPIG.
H-InvDBHIX0029914.
HGNCiHGNC:14650. PPIG.
HPAiHPA021788.
HPA057469.
MIMi606093. gene.
neXtProtiNX_Q13427.
OpenTargetsiENSG00000138398.
PharmGKBiPA33585.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00550000074595.
HOVERGENiHBG048162.
InParanoidiQ13427.
KOiK09566.
OMAiKERDHET.
OrthoDBiEOG091G0BGL.
PhylomeDBiQ13427.
TreeFamiTF318563.

Enzyme and pathway databases

BioCyciZFISH:HS06500-MONOMER.
BRENDAi5.2.1.8. 2681.

Miscellaneous databases

ChiTaRSiPPIG. human.
EvolutionaryTraceiQ13427.
GeneWikiiPPIG_(gene).
GenomeRNAii9360.
PROiQ13427.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138398.
CleanExiHS_PPIG.
ExpressionAtlasiQ13427. baseline and differential.
GenevisibleiQ13427. HS.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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...

Entry informationi

Entry nameiPPIG_HUMAN
AccessioniPrimary (citable) accession number: Q13427
Secondary accession number(s): D3DPC5
, D3DPC6, O00706, Q53R40, Q53SN4, Q96DG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 5, 2009
Last modified: November 2, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.