PPIG_HUMAN
ID PPIG_HUMAN Reviewed; 754 AA.
AC Q13427; D3DPC5; D3DPC6; O00706; Q53R40; Q53SN4; Q96DG9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase G;
DE Short=PPIase G;
DE Short=Peptidyl-prolyl isomerase G;
DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
DE AltName: Full=CASP10;
DE AltName: Full=Clk-associating RS-cyclophilin;
DE Short=CARS-Cyp;
DE Short=CARS-cyclophilin;
DE Short=SR-cyclophilin;
DE Short=SR-cyp;
DE Short=SRcyp;
DE AltName: Full=Cyclophilin G;
DE AltName: Full=Rotamase G;
GN Name=PPIG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP ASP-699.
RC TISSUE=T-cell;
RX PubMed=8973360; DOI=10.1016/s0378-1119(96)00436-2;
RA Nestel F.P., Colwill K., Harper S., Pawson T., Anderson S.K.;
RT "RS cyclophilins: identification of an NK-TR1-related cyclophilin.";
RL Gene 180:151-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLK1 AND RNA
RP POLYMERASE II, DOMAIN, AND VARIANT ASP-699.
RC TISSUE=B-cell;
RX PubMed=9153302; DOI=10.1093/nar/25.11.2055;
RA Bourquin J.-P., Stagljar I., Meier P., Moosmann P., Silke J., Baechi T.,
RA Georgiev O., Schaffner W.;
RT "A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-
RT terminal domain of RNA polymerase II.";
RL Nucleic Acids Res. 25:2055-2061(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH PNN, AND SUBCELLULAR LOCATION.
RX PubMed=15358154; DOI=10.1016/j.bbrc.2004.07.013;
RA Lin C.L., Leu S., Lu M.C., Ouyang P.;
RT "Over-expression of SR-cyclophilin, an interaction partner of nuclear
RT pinin, releases SR family splicing factors from nuclear speckles.";
RL Biochem. Biophys. Res. Commun. 321:638-647(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-696, VARIANT
RP [LARGE SCALE ANALYSIS] ASP-699, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-256; SER-257;
RP SER-259; SER-397 AND SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-415; SER-687;
RP SER-690; SER-696; THR-748 AND SER-753, VARIANT [LARGE SCALE ANALYSIS]
RP ASP-699, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358; SER-687;
RP SER-690 AND THR-748, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358; SER-386;
RP SER-397; SER-687; SER-745 AND THR-748, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-744; SER-745 AND
RP THR-748, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-392 AND LYS-693, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16] {ECO:0007744|PDB:2GW2}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-179, FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding (PubMed:20676357). May be implicated in the folding, transport,
CC and assembly of proteins. May play an important role in the regulation
CC of pre-mRNA splicing. {ECO:0000269|PubMed:20676357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000305|PubMed:20676357}.
CC -!- SUBUNIT: Interacts with CLK1, PNN and with the phosphorylated C-
CC terminal domain of RNA polymerase II. {ECO:0000269|PubMed:15358154,
CC ECO:0000269|PubMed:9153302}.
CC -!- INTERACTION:
CC Q13427; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-396072, EBI-10181188;
CC Q13427; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-396072, EBI-739624;
CC Q13427; O75553: DAB1; NbExp=3; IntAct=EBI-396072, EBI-7875264;
CC Q13427; Q9UI36-2: DACH1; NbExp=3; IntAct=EBI-396072, EBI-10186082;
CC Q13427; Q96C98: FHL3; NbExp=3; IntAct=EBI-396072, EBI-10229248;
CC Q13427; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-396072, EBI-2511344;
CC Q13427; P17931: LGALS3; NbExp=3; IntAct=EBI-396072, EBI-1170392;
CC Q13427; Q6NVH9: LGALS3; NbExp=3; IntAct=EBI-396072, EBI-10187804;
CC Q13427; Q15365: PCBP1; NbExp=2; IntAct=EBI-396072, EBI-946095;
CC Q13427; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-396072, EBI-302355;
CC Q13427; Q96CD2: PPCDC; NbExp=3; IntAct=EBI-396072, EBI-724333;
CC Q13427; Q14498: RBM39; NbExp=3; IntAct=EBI-396072, EBI-395290;
CC Q13427; Q16637: SMN2; NbExp=4; IntAct=EBI-396072, EBI-395421;
CC Q13427; Q12800: TFCP2; NbExp=3; IntAct=EBI-396072, EBI-717422;
CC Q13427; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-396072, EBI-741515;
CC Q13427; PRO_0000037309 [P0C6X7]: rep; Xeno; NbExp=4; IntAct=EBI-396072, EBI-25475797;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:15358154}.
CC Nucleus speckle {ECO:0000269|PubMed:15358154}. Note=Colocalizes with
CC RNA splicing factors at nuclear speckles.
CC {ECO:0000269|PubMed:15358154}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13427-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13427-2; Sequence=VSP_009662, VSP_009663;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8973360}.
CC -!- DOMAIN: The RS domain is required for the interaction with the
CC phosphorylated C-terminal domain of RNA polymerase II.
CC {ECO:0000269|PubMed:9153302}.
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DR EMBL; U40763; AAB40347.1; -; mRNA.
DR EMBL; X99717; CAA68053.1; -; mRNA.
DR EMBL; AC093899; AAY24119.1; -; Genomic_DNA.
DR EMBL; AC016772; AAY24233.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11267.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11268.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11269.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11270.1; -; Genomic_DNA.
DR EMBL; BC001555; AAH01555.1; -; mRNA.
DR CCDS; CCDS2235.1; -. [Q13427-1]
DR PIR; JC5314; JC5314.
DR RefSeq; NP_004783.2; NM_004792.2. [Q13427-1]
DR RefSeq; XP_005247023.1; XM_005246966.1. [Q13427-1]
DR RefSeq; XP_005247024.1; XM_005246967.1. [Q13427-1]
DR PDB; 2GW2; X-ray; 1.80 A; A=1-179.
DR PDB; 2WFI; X-ray; 0.75 A; A=1-177.
DR PDB; 2WFJ; X-ray; 0.75 A; A=1-177.
DR PDB; 5YZG; EM; 4.10 A; 3=1-754.
DR PDBsum; 2GW2; -.
DR PDBsum; 2WFI; -.
DR PDBsum; 2WFJ; -.
DR PDBsum; 5YZG; -.
DR AlphaFoldDB; Q13427; -.
DR SMR; Q13427; -.
DR BioGRID; 114761; 128.
DR IntAct; Q13427; 51.
DR MINT; Q13427; -.
DR STRING; 9606.ENSP00000260970; -.
DR BindingDB; Q13427; -.
DR ChEMBL; CHEMBL3707467; -.
DR DrugBank; DB00172; Proline.
DR GlyGen; Q13427; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13427; -.
DR PhosphoSitePlus; Q13427; -.
DR BioMuta; PPIG; -.
DR DMDM; 229462749; -.
DR EPD; Q13427; -.
DR jPOST; Q13427; -.
DR MassIVE; Q13427; -.
DR MaxQB; Q13427; -.
DR PaxDb; Q13427; -.
DR PeptideAtlas; Q13427; -.
DR PRIDE; Q13427; -.
DR ProteomicsDB; 59415; -. [Q13427-1]
DR ProteomicsDB; 59416; -. [Q13427-2]
DR Antibodypedia; 19292; 284 antibodies from 34 providers.
DR DNASU; 9360; -.
DR Ensembl; ENST00000260970.8; ENSP00000260970.3; ENSG00000138398.17. [Q13427-1]
DR Ensembl; ENST00000414307.6; ENSP00000402222.2; ENSG00000138398.17. [Q13427-2]
DR Ensembl; ENST00000433207.6; ENSP00000408683.2; ENSG00000138398.17. [Q13427-1]
DR Ensembl; ENST00000448752.7; ENSP00000407083.2; ENSG00000138398.17. [Q13427-1]
DR Ensembl; ENST00000462903.6; ENSP00000435987.1; ENSG00000138398.17. [Q13427-2]
DR Ensembl; ENST00000676756.1; ENSP00000503525.1; ENSG00000138398.17. [Q13427-1]
DR Ensembl; ENST00000678499.1; ENSP00000503136.1; ENSG00000138398.17. [Q13427-1]
DR Ensembl; ENST00000679107.1; ENSP00000502997.1; ENSG00000138398.17. [Q13427-1]
DR GeneID; 9360; -.
DR KEGG; hsa:9360; -.
DR MANE-Select; ENST00000260970.8; ENSP00000260970.3; NM_004792.3; NP_004783.2.
DR UCSC; uc002uez.4; human. [Q13427-1]
DR CTD; 9360; -.
DR DisGeNET; 9360; -.
DR GeneCards; PPIG; -.
DR HGNC; HGNC:14650; PPIG.
DR HPA; ENSG00000138398; Low tissue specificity.
DR MIM; 606093; gene.
DR neXtProt; NX_Q13427; -.
DR OpenTargets; ENSG00000138398; -.
DR PharmGKB; PA33585; -.
DR VEuPathDB; HostDB:ENSG00000138398; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000157954; -.
DR HOGENOM; CLU_012062_33_6_1; -.
DR InParanoid; Q13427; -.
DR OMA; YDHYERS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q13427; -.
DR TreeFam; TF318563; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; Q13427; -.
DR SignaLink; Q13427; -.
DR BioGRID-ORCS; 9360; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; PPIG; human.
DR EvolutionaryTrace; Q13427; -.
DR GeneWiki; PPIG_(gene); -.
DR GenomeRNAi; 9360; -.
DR Pharos; Q13427; Tchem.
DR PRO; PR:Q13427; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13427; protein.
DR Bgee; ENSG00000138398; Expressed in sural nerve and 218 other tissues.
DR ExpressionAtlas; Q13427; baseline and differential.
DR Genevisible; Q13427; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isomerase; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Rotamase; Ubl conjugation.
FT CHAIN 1..754
FT /note="Peptidyl-prolyl cis-trans isomerase G"
FT /id="PRO_0000064150"
FT DOMAIN 11..176
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 182..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..349
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 748
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 693
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 340..357
FT /note="RYRTPSRSRSRDRFRRSE -> VGDSFPRDLHNIAFVFLK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009662"
FT VAR_SEQ 358..754
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009663"
FT VARIANT 445
FT /note="D -> E (in dbSNP:rs1050354)"
FT /id="VAR_055084"
FT VARIANT 699
FT /note="N -> D (in dbSNP:rs8207)"
FT /evidence="ECO:0000269|PubMed:8973360,
FT ECO:0000269|PubMed:9153302, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT /id="VAR_055085"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:2WFI"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2WFI"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:2WFI"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2WFJ"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2WFI"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2WFI"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2WFJ"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2WFI"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2WFI"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:2WFI"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2WFI"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2WFI"
SQ SEQUENCE 754 AA; 88617 MW; D4884808D8060CD6 CRC64;
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK
SKVKKEEKKR HKSSSSSSSS SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK
HKKEKKKRKK SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR DRFRRSETPP
HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR VKERKITDHR NVSESPNRKN
EKEKKVKDHK SNSKERDIRR NSEKDDKYKN KVKKRAKSKS RSKSKEKSKS KERDSKHNRN
EEKRMRSRSK GRDHENVKEK EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR
RAQSRSRECD ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK SSHRKENSES
EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE LKSSMLKNKE DEKIRSSVEK
ENQKSKGQEN DHVHEKNKKF DHESSPGTDE DKSG
