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Overview

Uniprot IDQ12972
Protein NameNuclear inhibitor of protein phosphatase 1
Gene NamePPP1R8
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
193 NLDIQRPKRKRKNSR
234 QTAVVPVKKKRVEGP
235 TAVVPVKKKRVEGPG
236 AVVPVKKKRVEGPGS

Function

Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation

Protein Sequence

10 MAAAANSGSS 20 LPLFDCPTWA 30 GKPPPGLHLD 40 VVKGDKLIEK 50 LIIDEKKYYL 60 FGRNPDLCDF 70 TIDHQSCSRV 80 HAALVYHKHL 90 KRVFLIDLNS 100 THGTFLGHIR 110 LEPHKPQQIP 120 IDSTVSFGAS 130 TRAYTLREKP 140 QTLPSAVKGD 150 EKMGGEDDEL 160 KGLLGLPEEE 170 TELDNLTEFN 180 TAHNKRISTL 190 TIEEGNLDIQ 200 RPKRKRKNSR 210 VTFSEDDEII 220 NPEDVDPSVG 230 RFRNMVQTAV 240 VPVKKKRVEG 250 PGSLGLEESG 260 SRRMQNFAFS 270 GGLYGGLPPT 280 HSEAGSQPHG 290 IHGTALIGGL 300 PMPYPNLAPD 310 VDLTPVVPSA 320 VNMNPAPNPA 330 VYNPEAVNEP 340 KKKKYAKEAW 350 PGKKPTPSLL I

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140678 molecular function inhibitor activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0004865 protein serine/threonine phosphatase inhibitor activity
Molecular Function GO:0008995 ribonuclease E activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0004521 RNA endonuclease activity
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006397 mRNA processing
Biological Process GO:0006401 RNA catabolic process
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] 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.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.