Search Results

Overview

Uniprot IDQ13427
Protein NamePeptidyl-prolyl cis-trans isomerase G
Gene NamePPIG
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
180 SCGELIPKSKVKKEE
182 GELIPKSKVKKEEKK
553 SRECDITKGKHSYNS
693 QSPFSKIKQSSQDNE
707 ELKSSMLKNKEDEKI

Function

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing

Protein Sequence

10 MGIKVQRPRC 20 FFDIAINNQP 30 AGRVVFELFS 40 DVCPKTCENF 50 RCLCTGEKGT 60 GKSTQKPLHY 70 KSCLFHRVVK 80 DFMVQGGDFS 90 EGNGRGGESI 100 YGGFFEDESF 110 AVKHNKEFLL 120 SMANRGKDTN 130 GSQFFITTKP 140 TPHLDGHHVV 150 FGQVISGQEV 160 VREIENQKTD 170 AASKPFAEVR 180 ILSCGELIPK 190 SKVKKEEKKR 200 HKSSSSSSSS 210 SSDSDSSSDS 220 QSSSDSSDSE 230 SATEEKSKKR 240 KKKHRKNSRK 250 HKKEKKKRKK 260 SKKSASSESE 270 AENLEAQPQS 280 TVRPEEIPPI 290 PENRFLMRKS 300 PPKADEKERK 310 NREREREREC 320 NPPNSQPASY 330 QRRLLVTRSG 340 RKIKGRGPRR 350 YRTPSRSRSR 360 DRFRRSETPP 370 HWRQEMQRAQ 380 RMRVSSGERW 390 IKGDKSELNE 400 IKENQRSPVR 410 VKERKITDHR 420 NVSESPNRKN 430 EKEKKVKDHK 440 SNSKERDIRR 450 NSEKDDKYKN 460 KVKKRAKSKS 470 RSKSKEKSKS 480 KERDSKHNRN 490 EEKRMRSRSK 500 GRDHENVKEK 510 EKQSDSKGKD 520 QERSRSKEKS 530 KQLESKSNEH 540 DHSKSKEKDR 550 RAQSRSRECD 560 ITKGKHSYNS 570 RTRERSRSRD 580 RSRRVRSRTH 590 DRDRSRSKEY 600 HRYREQEYRR 610 RGRSRSRERR 620 TPPGRSRSKD 630 RRRRRRDSRS 640 SEREESQSRN 650 KDKYRNQESK 660 SSHRKENSES 670 EKRMYSKSRD 680 HNSSNNSREK 690 KADRDQSPFS 700 KIKQSSQDNE 710 LKSSMLKNKE 720 DEKIRSSVEK 730 ENQKSKGQEN 740 DHVHEKNKKF 750 DHESSPGTDE DKSG

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0016018 cyclosporin A binding
Molecular Function GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006457 protein folding
Biological Process GO:0008380 RNA splicing

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.