Search Results

Overview

Uniprot ID	Q86TM6
Protein Name	E3 ubiquitin-protein ligase synoviolin
Gene Name	SYVN1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
610	LRRRRLQKLESPVAH

Function

E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:27827840, PubMed:26471130, PubMed:28827405). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130, PubMed:28842558). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation (PubMed:17141218). Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (By similarity)

Protein Sequence

10 MFRTAVMMAA 20 SLALTGAVVA 30 HAYYLKHQFY 40 PTVVYLTKSS 50 PSMAVLYIQA 60 FVLVFLLGKV 70 MGKVFFGQLR 80 AAEMEHLLER 90 SWYAVTETCL 100 AFTVFRDDFS 110 PRFVALFTLL 120 LFLKCFHWLA 130 EDRVDFMERS 140 PNISWLFHCR 150 IVSLMFLLGI 160 LDFLFVSHAY 170 HSILTRGASV 180 QLVFGFEYAI 190 LMTMVLTIFI 200 KYVLHSVDLQ 210 SENPWDNKAV 220 YMLYTELFTG 230 FIKVLLYMAF 240 MTIMIKVHTF 250 PLFAIRPMYL 260 AMRQFKKAVT 270 DAIMSRRAIR 280 NMNTLYPDAT 290 PEELQAMDNV 300 CIICREEMVT 310 GAKRLPCNHI 320 FHTSCLRSWF 330 QRQQTCPTCR 340 MDVLRASLPA 350 QSPPPPEPAD 360 QGPPPAPHPP 370 PLLPQPPNFP 380 QGLLPPFPPG 390 MFPLWPPMGP 400 FPPVPPPPSS 410 GEAVAPPSTS 420 AAALSRPSGA 430 ATTTAAGTSA 440 TAASATASGP 450 GSGSAPEAGP 460 APGFPFPPPW 470 MGMPLPPPFA 480 FPPMPVPPAG 490 FAGLTPEELR 500 ALEGHERQHL 510 EARLQSLRNI 520 HTLLDAAMLQ 530 INQYLTVLAS 540 LGPPRPATSV 550 NSTEETATTV 560 VAAASSTSIP 570 SSEATTPTPG 580 ASPPAPEMER 590 PPAPESVGTE 600 EMPEDGEPDA 610 AELRRRRLQK LESPVAH

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0036513	Derlin-1 retrotranslocation complex
Cellular Component	GO:0012505	endomembrane system
Cellular Component	GO:0005783	endoplasmic reticulum
Cellular Component	GO:0005789	endoplasmic reticulum membrane
Cellular Component	GO:0044322	endoplasmic reticulum quality control compartment
Cellular Component	GO:0000836	Hrd1p ubiquitin ligase complex
Cellular Component	GO:0000839	Hrd1p ubiquitin ligase ERAD-L complex
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0005790	smooth endoplasmic reticulum
Molecular Function	GO:0051117	ATPase binding
Molecular Function	GO:0140297	DNA-binding transcription factor binding
Molecular Function	GO:0051087	protein-folding chaperone binding
Molecular Function	GO:0061630	ubiquitin protein ligase activity
Molecular Function	GO:1990381	ubiquitin-specific protease binding
Molecular Function	GO:0051082	unfolded protein binding
Molecular Function	GO:0008270	zinc ion binding
Biological Process	GO:1904380	endoplasmic reticulum mannose trimming
Biological Process	GO:0036503	ERAD pathway
Biological Process	GO:0002327	immature B cell differentiation
Biological Process	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
Biological Process	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process	GO:0070936	protein K48-linked ubiquitination
Biological Process	GO:0050821	protein stabilization
Biological Process	GO:0016567	protein ubiquitination
Biological Process	GO:0030970	retrograde protein transport, ER to cytosol
Biological Process	GO:0006511	ubiquitin-dependent protein catabolic process

Reference

[1] 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.

[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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.