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 27-MAR-2024, entry version 200. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-6864; -. DR SMR; Q13427; -. DR BioGRID; 114761; 151. DR IntAct; Q13427; 52. DR MINT; Q13427; -. DR STRING; 9606.ENSP00000260970; -. DR BindingDB; Q13427; -. DR ChEMBL; CHEMBL3707467; -. DR DrugBank; DB00172; Proline. DR GlyGen; Q13427; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000260970; -. DR PeptideAtlas; Q13427; -. DR ProteomicsDB; 59415; -. [Q13427-1] DR ProteomicsDB; 59416; -. [Q13427-2] DR Pumba; Q13427; -. DR Antibodypedia; 19292; 329 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 AGR; HGNC:14650; -. 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; NQNQFNR; -. DR OrthoDB; 5324361at2759; -. DR PhylomeDB; Q13427; -. DR TreeFam; TF318563; -. DR BRENDA; 5.2.1.8; 2681. DR PathwayCommons; Q13427; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR SignaLink; Q13427; -. DR BioGRID-ORCS; 9360; 14 hits in 1163 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 220 other cell types or tissues. DR ExpressionAtlas; Q13427; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:Reactome. 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; Cyclophilin-like; 1. DR InterPro; IPR029000; Cyclophilin-like_dom_sf. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; Cyclophilin-like; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. DR Genevisible; Q13427; HS. 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 //