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Q13427 (PPIG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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):
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 names
Name:PPIG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length754 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.

Catalytic activity

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

Enzyme regulation

Cyclosporin A (CsA)-sensitive.

Subunit structure

Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II. Ref.2 Ref.6

Subcellular location

Nucleus matrix. Nucleus speckle. Note: Colocalizes with RNA splicing factors at nuclear speckles. Ref.6

Tissue specificity

Ubiquitous.

Domain

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

Sequence similarities

Contains 1 PPIase cyclophilin-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PCBP1Q153652EBI-396072,EBI-946095

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13427-1)

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.
Isoform 2 (identifier: Q13427-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 754754Peptidyl-prolyl cis-trans isomerase G
PRO_0000064150

Regions

Domain11 – 176166PPIase cyclophilin-type
Compositional bias180 – 19213Arg/Lys-rich (basic)
Compositional bias193 – 22533Asp/Glu/Ser-rich
Compositional bias193 – 20816Poly-Ser
Compositional bias226 – 25328Arg/Lys-rich (basic)
Compositional bias540 – 639100Arg/Ser-rich (RS domain)
Compositional bias621 – 6266Poly-Arg

Amino acid modifications

Modified residue2541Phosphoserine Ref.9
Modified residue2561Phosphoserine Ref.9
Modified residue2571Phosphoserine Ref.9
Modified residue2591Phosphoserine Ref.9
Modified residue3151Phosphoserine Ref.8
Modified residue3561Phosphoserine Ref.7 Ref.12
Modified residue3581Phosphothreonine Ref.7 Ref.12
Modified residue3971Phosphoserine Ref.9
Modified residue4131Phosphoserine Ref.11
Modified residue4151Phosphoserine Ref.11
Modified residue6871Phosphoserine Ref.7 Ref.9 Ref.11 Ref.12
Modified residue6901Phosphoserine Ref.11 Ref.12
Modified residue6961Phosphoserine Ref.8 Ref.11
Modified residue7481Phosphothreonine Ref.11 Ref.12
Modified residue7531Phosphoserine Ref.11

Natural variations

Alternative sequence340 – 35718RYRTP…FRRSE → VGDSFPRDLHNIAFVFLK in isoform 2.
VSP_009662
Alternative sequence358 – 754397Missing in isoform 2.
VSP_009663
Natural variant4451D → E.
Corresponds to variant rs1050354 [ dbSNP | Ensembl ].
VAR_055084
Natural variant6991N → D. Ref.1 Ref.2 Ref.8 Ref.11
Corresponds to variant rs8207 [ dbSNP | Ensembl ].
VAR_055085

Secondary structure

...................................... 754
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: D4884808D8060CD6

FASTA75488,617
        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 SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK 

       250        260        270        280        290        300 
HKKEKKKRKK SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK 

       310        320        330        340        350        360 
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR DRFRRSETPP 

       370        380        390        400        410        420 
HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR VKERKITDHR NVSESPNRKN 

       430        440        450        460        470        480 
EKEKKVKDHK SNSKERDIRR NSEKDDKYKN KVKKRAKSKS RSKSKEKSKS KERDSKHNRN 

       490        500        510        520        530        540 
EEKRMRSRSK GRDHENVKEK EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR 

       550        560        570        580        590        600 
RAQSRSRECD ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR 

       610        620        630        640        650        660 
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK SSHRKENSES 

       670        680        690        700        710        720 
EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE LKSSMLKNKE DEKIRSSVEK 

       730        740        750 
ENQKSKGQEN DHVHEKNKKF DHESSPGTDE DKSG 

« Hide

Isoform 2 [UniParc].

Checksum: 506BC6E24E1ADD4B
Show »

FASTA35740,299

References

« Hide 'large scale' references
[1]"RS cyclophilins: identification of an NK-TR1-related cyclophilin."
Nestel F.P., Colwill K., Harper S., Pawson T., Anderson S.K.
Gene 180:151-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-699.
Tissue: T-cell.
[2]"A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II."
Bourquin J.-P., Stagljar I., Meier P., Moosmann P., Silke J., Baechi T., Georgiev O., Schaffner W.
Nucleic Acids Res. 25:2055-2061(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLK1 AND RNA POLYMERASE II, VARIANT ASP-699.
Tissue: B-cell.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles."
Lin C.L., Leu S., Lu M.C., Ouyang P.
Biochem. Biophys. Res. Commun. 321:638-647(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PNN, SUBCELLULAR LOCATION.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-696, VARIANT [LARGE SCALE ANALYSIS] ASP-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-256; SER-257; SER-259; SER-397 AND SER-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-415; SER-687; SER-690; SER-696; THR-748 AND SER-753, VARIANT [LARGE SCALE ANALYSIS] ASP-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358; SER-687; SER-690 AND THR-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5314.
RefSeqNP_004783.2. NM_004792.2.
XP_005247023.1. XM_005246966.1.
XP_005247024.1. XM_005246967.1.
UniGeneHs.470544.
Hs.593163.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GW2X-ray1.80A1-179[»]
2WFIX-ray0.75A1-177[»]
2WFJX-ray0.75A1-177[»]
ProteinModelPortalQ13427.
SMRQ13427. Positions 6-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114761. 14 interactions.
IntActQ13427. 16 interactions.
MINTMINT-1684213.
STRING9606.ENSP00000260970.

Chemistry

DrugBankDB00172. L-Proline.

PTM databases

PhosphoSiteQ13427.

Polymorphism databases

DMDM229462749.

Proteomic databases

PaxDbQ13427.
PRIDEQ13427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260970; ENSP00000260970; ENSG00000138398. [Q13427-1]
ENST00000448752; ENSP00000407083; ENSG00000138398. [Q13427-1]
ENST00000462903; ENSP00000435987; ENSG00000138398. [Q13427-2]
GeneID9360.
KEGGhsa:9360.
UCSCuc002uez.3. human. [Q13427-1]
uc002ufa.3. human. [Q13427-2]

Organism-specific databases

CTD9360.
GeneCardsGC02P170404.
H-InvDBHIX0029914.
HGNCHGNC:14650. PPIG.
HPAHPA021788.
MIM606093. gene.
neXtProtNX_Q13427.
PharmGKBPA33585.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOVERGENHBG048162.
InParanoidQ13427.
KOK09566.
OMANKKFDHE.
OrthoDBEOG79GT7W.
PhylomeDBQ13427.
TreeFamTF318563.

Gene expression databases

ArrayExpressQ13427.
BgeeQ13427.
CleanExHS_PPIG.
GenevestigatorQ13427.

Family and domain databases

InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIG. human.
EvolutionaryTraceQ13427.
GeneWikiPPIG_(gene).
GenomeRNAi9360.
NextBio35051.
PROQ13427.
SOURCESearch...

Entry information

Entry namePPIG_HUMAN
AccessionPrimary (citable) accession number: Q13427
Secondary accession number(s): D3DPC5 expand/collapse secondary AC list , D3DPC6, O00706, Q53R40, Q53SN4, Q96DG9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM