Search Results

Overview

Uniprot ID	Q13033
Protein Name	Striatin-3
Gene Name	STRN3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
363	KKERKGKKGVKRANR
366	RKGKKGVKRANRTKL
517	QKTVPAKKSASLDVE

Function

Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:30622739, PubMed:33633399). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable)

Protein Sequence

10 MDELAGGGGG 20 GPGMAAPPRQ 30 QQGPGGNLGL 40 SPGGNGAAGG 50 GGPPASEGAG 60 PAAGPELSRP 70 QQYTIPGILH 80 YIQHEWARFE 90 MERAHWEVER 100 AELQARIAFL 110 QGERKGQENL 120 KKDLVRRIKM 130 LEYALKQERA 140 KYHKLKYGTE 150 LNQGDLKMPT 160 FESEETKDTE 170 APTAPQNSQL 180 TWKQGRQLLR 190 QYLQEVGYTD 200 TILDVRSQRV 210 RSLLGLSNSE 220 PNGSVETKNL 230 EQILNGGESP 240 KQKGQEIKRS 250 SGDVLETFNF 260 LENADDSDED 270 EENDMIEGIP 280 EGKDKHRMNK 290 HKIGNEGLAA 300 DLTDDPDTEE 310 ALKEFDFLVT 320 AEDGEGAGEA 330 RSSGDGTEWD 340 KDDLSPTAEV 350 WDVDQGLISK 360 LKEQYKKERK 370 GKKGVKRANR 380 TKLYDMIADL 390 GDDELPHIPS 400 GIINQSRSAS 410 TRMTDHEGAR 420 AEEAEPITFP 430 SGGGKSFIMG 440 SDDVLLSVLG 450 LGDLADLTVT 460 NDADYSYDLP 470 ANKDAFRKTW 480 NPKYTLRSHF 490 DGVRALAFHP 500 VEPVLVTASE 510 DHTLKLWNLQ 520 KTVPAKKSAS 530 LDVEPIYTFR 540 AHIGPVLSLA 550 ISSNGEQCFS 560 GGIDATIQWW 570 NMPSPSVDPY 580 DTYEPNVLAG 590 TLVGHTDAVW 600 GLAYSGIKNQ 610 LLSCSADGTV 620 RLWNPQEKLP 630 CICTYNGDKK 640 HGIPTSVDFI 650 GCDPAHMVTS 660 FNTGSAVIYD 670 LETSQSLVIL 680 SSQVDSGLQS 690 NNHINRVVSH 700 PTLPVTITAH 710 EDRHIKFFDN 720 KTGKMIHSMV 730 AHLDAVTSLA 740 VDPNGIYLMS 750 GSHDCSIRLW 760 NLDSKTCVQE 770 ITAHRKKLDE 780 SIYDVAFHSS 790 KAYIASAGAD ALAKVFV

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0030425	dendrite
Cellular Component	GO:0090443	FAR/SIN/STRIPAK complex
Cellular Component	GO:0005794	Golgi apparatus
Cellular Component	GO:0043025	neuronal cell body
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0098794	postsynapse
Cellular Component	GO:0032991	protein-containing complex
Molecular Function	GO:0070016	armadillo repeat domain binding
Molecular Function	GO:0005516	calmodulin binding
Molecular Function	GO:0019901	protein kinase binding
Molecular Function	GO:0051721	protein phosphatase 2A binding
Molecular Function	GO:0044877	protein-containing complex binding
Molecular Function	GO:0030674	protein-macromolecule adaptor activity
Molecular Function	GO:0031267	small GTPase binding
Biological Process	GO:0045892	negative regulation of DNA-templated transcription
Biological Process	GO:0035331	negative regulation of hippo signaling
Biological Process	GO:0033147	negative regulation of intracellular estrogen receptor signaling pathway
Biological Process	GO:0000122	negative regulation of transcription by RNA polymerase II
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:0035330	regulation of hippo signaling
Biological Process	GO:0032355	response to estradiol

Reference

[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[2] 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.

[3] 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.