Search Results

Overview

Uniprot IDQ9Y314
Protein NameNitric oxide synthase-interacting protein
Gene NameNOSIP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
153 PSVGPPSKDKDKVLP
155 VGPPSKDKDKVLPSF
175 TPEAKATKLEKPSRT
19 AVYTYHEKKKDTAAS
20 VYTYHEKKKDTAASG
21 YTYHEKKKDTAASGY
289 GFAGSGVKLQAEKSR
294 GVKLQAEKSRPVMQA
6 **MTRHGKNCTAGAV

Function

E3 ubiquitin-protein ligase that is essential for proper development of the forebrain, the eye, and the face. Catalyzes monoubiquitination of serine/threonine-protein phosphatase 2A (PP2A) catalytic subunit PPP2CA/PPP2CB (By similarity). Negatively regulates nitric oxide production by inducing NOS1 and NOS3 translocation to actin cytoskeleton and inhibiting their enzymatic activity (PubMed:11149895, PubMed:15548660, PubMed:16135813)

Protein Sequence

10 MTRHGKNCTA 20 GAVYTYHEKK 30 KDTAASGYGT 40 QNIRLSRDAV 50 KDFDCCCLSL 60 QPCHDPVVTP 70 DGYLYEREAI 80 LEYILHQKKE 90 IARQMKAYEK 100 QRGTRREEQK 110 ELQRAASQDH 120 VRGFLEKESA 130 IVSRPLNPFT 140 AKALSGTSPD 150 DVQPGPSVGP 160 PSKDKDKVLP 170 SFWIPSLTPE 180 AKATKLEKPS 190 RTVTCPMSGK 200 PLRMSDLTPV 210 HFTPLDSSVD 220 RVGLITRSER 230 YVCAVTRDSL 240 SNATPCAVLR 250 PSGAVVTLEC 260 VEKLIRKDMV 270 DPVTGDKLTD 280 RDIIVLQRGG 290 TGFAGSGVKL 300 QAEKSRPVMQ A

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000139 Golgi membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0140313 molecular sequestering activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0061630 ubiquitin protein ligase activity
Biological Process GO:0043086 negative regulation of catalytic activity
Biological Process GO:0051001 negative regulation of nitric-oxide synthase activity
Biological Process GO:0046209 nitric oxide metabolic process
Biological Process GO:0045428 regulation of nitric oxide biosynthetic process

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] 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.

[5] 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.

[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.