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Overview

Uniprot IDQ9H307
Protein NamePinin
Gene NamePNN
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
157 MGTLQKFKQESTVAT
528 GHLLPERKDFPVESV
553 LTVHPESKSKTKTRS
555 VHPESKSKTKTRSRS
75 SGGGPPAKQRDLEGA

Function

Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Component of the PSAP complex which binds RNA in a sequence-independent manner and is proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma

Protein Sequence

10 MAVAVRTLQE 20 QLEKAKESLK 30 NVDENIRKLT 40 GRDPNDVRPI 50 QARLLALSGP 60 GGGRGRGSLL 70 LRRGFSDSGG 80 GPPAKQRDLE 90 GAVSRLGGER 100 RTRRESRQES 110 DPEDDDVKKP 120 ALQSSVVATS 130 KERTRRDLIQ 140 DQNMDEKGKQ 150 RNRRIFGLLM 160 GTLQKFKQES 170 TVATERQKRR 180 QEIEQKLEVQ 190 AEEERKQVEN 200 ERRELFEERR 210 AKQTELRLLE 220 QKVELAQLQE 230 EWNEHNAKII 240 KYIRTKTKPH 250 LFYIPGRMCP 260 ATQKLIEESQ 270 RKMNALFEGR 280 RIEFAEQINK 290 MEARPRRQSM 300 KEKEHQVVRN 310 EEQKAEQEEG 320 KVAQREEELE 330 ETGNQHNDVE 340 IEEAGEEEEK 350 EIAIVHSDAE 360 KEQEEEEQKQ 370 EMEVKMEEET 380 EVRESEKQQD 390 SQPEEVMDVL 400 EMVENVKHVI 410 ADQEVMETNR 420 VESVEPSENE 430 ASKELEPEME 440 FEIEPDKECK 450 TLSPGKENVS 460 ALDMEKESEE 470 KEEKESEPQP 480 EPVAQPQPQS 490 QPQLQLQSQS 500 QPVLQSQPPS 510 QPEDLSLAVL 520 QPTPQVTQEQ 530 GHLLPERKDF 540 PVESVKLTEV 550 PVEPVLTVHP 560 ESKSKTKTRS 570 RSRGRARNKT 580 SKSRSRSSSS 590 SSSSSSSTSS 600 SSGSSSSSGS 610 SSSRSSSSSS 620 SSTSGSSSRD 630 SSSSTSSSSE 640 SRSRSRGRGH 650 NRDRKHRRSV 660 DRKRRDTSGL 670 ERSHKSSKGG 680 SSRDTKGSKD 690 KNSRSDRKRS 700 ISESSRSGKR 710 SSRSERDRKS DRKDKRR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0005911 cell-cell junction
Cellular Component GO:0030057 desmosome
Cellular Component GO:0005882 intermediate filament
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0005198 structural molecule activity
Biological Process GO:0007155 cell adhesion
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0048255 mRNA stabilization
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0050684 regulation of mRNA processing

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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] 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.