Q13427 (PPIG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Traceable author statement Ref.2. Source: ProtInc protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement Ref.2. Source: ProtInc
Molecular_function	cyclosporin A binding Traceable author statement Ref.2. Source: ProtInc peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 754

754

Peptidyl-prolyl cis-trans isomerase G

PRO_0000064150

Regions

Domain

11 – 176

166

PPIase cyclophilin-type

Compositional bias

180 – 192

13

Arg/Lys-rich (basic)

Compositional bias

193 – 225

33

Asp/Glu/Ser-rich

Compositional bias

193 – 208

16

Poly-Ser

Compositional bias

226 – 253

28

Arg/Lys-rich (basic)

Compositional bias

540 – 639

100

Arg/Ser-rich (RS domain)

Compositional bias

621 – 626

6

Poly-Arg

Amino acid modifications

Modified residue

195

1

Phosphoserine By similarity

Modified residue

200

1

Phosphoserine By similarity

Modified residue

202

1

Phosphoserine By similarity

Modified residue

206

1

Phosphoserine By similarity

Modified residue

254

1

Phosphoserine Ref.9

Modified residue

256

1

Phosphoserine Ref.9

Modified residue

257

1

Phosphoserine Ref.9

Modified residue

259

1

Phosphoserine Ref.9

Modified residue

315

1

Phosphoserine Ref.8

Modified residue

345

1

Phosphoserine By similarity

Modified residue

347

1

Phosphoserine By similarity

Modified residue

356

1

Phosphoserine Ref.7 Ref.12

Modified residue

358

1

Phosphothreonine Ref.7 Ref.12

Modified residue

397

1

Phosphoserine Ref.9

Modified residue

413

1

Phosphoserine Ref.11

Modified residue

415

1

Phosphoserine Ref.11

Modified residue

687

1

Phosphoserine Ref.7 Ref.9 Ref.11 Ref.12

Modified residue

690

1

Phosphoserine Ref.11 Ref.12

Modified residue

696

1

Phosphoserine Ref.8 Ref.11

Modified residue

744

1

Phosphoserine By similarity

Modified residue

745

1

Phosphoserine By similarity

Modified residue

748

1

Phosphothreonine Ref.11 Ref.12

Modified residue

753

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

340 – 357

18

RYRTP…FRRSE → VGDSFPRDLHNIAFVFLK in isoform 2.

VSP_009662

Alternative sequence

358 – 754

397

Missing in isoform 2.

VSP_009663

Natural variant

445

1

D → E.
Corresponds to variant rs1050354 [ dbSNP | Ensembl ].

VAR_055084

Natural variant

699

1

N → D. Ref.1 Ref.2 Ref.8 Ref.11
Corresponds to variant rs8207 [ dbSNP | Ensembl ].

VAR_055085

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

754

Helix Strand Turn

Details...

Beta strand

9 – 16

8

Beta strand

19 – 28

10

Turn

30 – 32

3

Helix

34 – 45

12

Turn

46 – 48

3

Turn

52 – 54

3

Beta strand

56 – 58

3

Beta strand

64 – 69

6

Turn

70 – 72

3

Beta strand

73 – 76

4

Turn

79 – 81

3

Beta strand

82 – 85

4

Beta strand

109 – 112

4

Beta strand

114 – 116

3

Beta strand

124 – 129

6

Helix

132 – 134

3

Turn

135 – 137

3

Beta strand

140 – 146

7

Helix

148 – 155

8

Beta strand

165 – 167

3

Beta strand

169 – 176

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: D4884808D8060CD6	FASTA	754	88,617
	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
	Isoform 2 [UniParc]. Checksum: 506BC6E24E1ADD4B	FASTA	357	40,299
	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 NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRV GDSFPRDLHN IAFVFLK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.

IPI

IPI00006298.
IPI00409624.

PIR

JC5314.

RefSeq

NP_004783.2. NM_004792.2.

UniGene

Hs.727580.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GW2	X-ray	1.80	A	1-179	[»]
2WFI	X-ray	0.75	A	1-177	[»]
2WFJ	X-ray	0.75	A	1-177	[»]

ProteinModelPortal

Q13427.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13427. 8 interactions.

MINT

MINT-1684213.

STRING

9606.ENSP00000260970.

PTM databases

PhosphoSite

Q13427.

Polymorphism databases

DMDM

229462749.

Proteomic databases

PaxDb

Q13427.

PRIDE

Q13427.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260970; ENSP00000260970; ENSG00000138398.
ENST00000448752; ENSP00000407083; ENSG00000138398.
ENST00000462903; ENSP00000435987; ENSG00000138398.

GeneID

9360.

KEGG

hsa:9360.

UCSC

uc002uez.3. human.
uc002ufa.3. human.

Organism-specific databases

CTD

9360.

GeneCards

GC02P170404.

H-InvDB

HIX0029914.

HGNC

HGNC:14650. PPIG.

HPA

HPA021788.

MIM

606093. gene.

neXtProt

NX_Q13427.

PharmGKB

PA33585.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0652.

HOVERGEN

HBG048162.

InParanoid

Q13427.

KO

K09566.

OMA

NKKFDHE.

OrthoDB

EOG43FGWT.

PhylomeDB

Q13427.

Gene expression databases

ArrayExpress

Q13427.

Bgee

Q13427.

CleanEx

HS_PPIG.

Genevestigator

Q13427.

GermOnline

ENSG00000138398. Homo sapiens.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PPIG. human.

DrugBank

DB00172. L-Proline.

EvolutionaryTrace

Q13427.

GenomeRNAi

9360.

NextBio

35051.

SOURCE

Search...

Entry information

Entry name

PPIG_HUMAN

Accession

Primary (citable) accession number: Q13427
Secondary accession number(s): D3DPC5 , D3DPC6, O00706, Q53R40, Q53SN4, Q96DG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.