Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01341
Entry Name
UniProt Accession
Theoretical PI
8.8
Molecular Weight
61777.85
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
E3 ubiquitin-protein ligase NEURL1
Protein Synonyms/Alias
6.3.2.-; Neuralized-like protein 1A; m-neu1; m-neuralized 1; Neuralized1;
Gene Name
Neurl1
Gene Synonyms/Alias
Neurl; Neurl1a;
Created Date
15-MAR-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNNFSSVS
[1][2]
N-Myristoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Benetka W, Mehlmer N, Maurer-Stroh S, Sammer M, Koranda M, Neumüller R,Betschinger J, Knoblich JA, Teige M, Eisenhaber F. Experimental testing ofpredicted myristoylation targets involved in asymmetric cell division andcalcium-dependent signalling. Cell Cycle. 2008 Dec;7(23):3709-19. Epub 2008 Dec13. Erratum in: Cell Cycle. 2009 Feb 1;8(3):508-9.[PMID:19029837]
[2] Koutelou E, Sato S, Tomomori-Sato C, Florens L, Swanson SK, Washburn MP,Kokkinaki M, Conaway RC, Conaway JW, Moschonas NK. Neuralized-like 1 (Neurl1)targeted to the plasma membrane by N-myristoylation regulates the Notch ligandJagged1. J Biol Chem. 2008 Feb 15;283(7):3846-53. Epub 2007 Dec 12.[PMID:18077452]
Functional Description
Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element- binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway.
Sequence Annotation
Domain: 61 217 NHR 1.
Domain: 292 447 NHR 2.
Protein Length
574 AA.
Protein Sequence
(Canonical)
MGNNFSSVSS LQRGNPSRAS RGHPQNLKDS IGGSFPVPSH RCHHKQKHCP PTLSGGGLPA  60
TPLLFHPHTK GSQILMDLSH KAVKRQASFC NAITFSNRPV LIYEQVRLKI TKKQCCWSGA  120
LRLGFTSKDP SRIHPDSLPK YACPDLVSQS GFWAKALPEE FANEGNIIAF WVDKKGRVFY  180
RINESAAMLF FSGVRTVDPL WALVDVYGLT RGVQLLDSEL VLPDCLRPRS FTALRRPSLR  240
CEADEARLSV SLCDLNVPGA DGDDGAPPAG CPIPQNSLNS QHSRALPAQL DGDLRFHALR  300
AGAHVRILDE QTVARLEHGR DERALVFTSR PVRVAETIFI KVTRSGGGRA GALSFGVTTC  360
DPGTLRPADL PFSPEALVDR KEFWAVCRVP GPLHSGDILG LVVNADGELH LSHNGAAAGM  420
QLCVDASQPL WMLFSLHGAI TQVRILGSTI MTERGGPSLP CSPASTPTSP SALGIRLSDP  480
LLSTCGSGPL GGSAGGTAPN SPVSLPESPV TPGLGQWSDE CTICYEHAVD TVIYTCGHMC  540
LCYSCGLRLK KALHACCPIC RRPIKDIIKT YRSS                              574
FASTA
(Canonical)
>LipidDB-10090-01341|Q923S6
MGNNFSSVSSLQRGNPSRASRGHPQNLKDSIGGSFPVPSHRCHHKQKHCPPTLSGGGLPA
TPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGA
LRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFY
RINESAAMLFFSGVRTVDPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLR
CEADEARLSVSLCDLNVPGADGDDGAPPAGCPIPQNSLNSQHSRALPAQLDGDLRFHALR
AGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTC
DPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAGM
QLCVDASQPLWMLFSLHGAITQVRILGSTIMTERGGPSLPCSPASTPTSPSALGIRLSDP
LLSTCGSGPLGGSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMC
LCYSCGLRLKKALHACCPICRRPIKDIIKTYRSS
Gene Ontology
GO:0097440; C:apical dendrite; IDA:UniProtKB
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005737; C:cytoplasm; IDA:MGI
GO:0043197; C:dendritic spine; IDA:UniProtKB
GO:0043204; C:perikaryon; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:MGI
GO:0014069; C:postsynaptic density; IDA:UniProtKB
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW
GO:0016874; F:ligase activity; IEA:UniProtKB-KW
GO:0045183; F:translation factor activity, non-nucleic acid binding; IDA:UniProtKB
GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0007420; P:brain development; IEA:Ensembl
GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB
GO:0007595; P:lactation; IMP:MGI
GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB
GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB
GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW
GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB
GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB
GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IMP:MGI
GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB
GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IDA:UniProtKB
GO:0090129; P:positive regulation of synapse maturation; IDA:UniProtKB
GO:0006513; P:protein monoubiquitination; IDA:UniProtKB
GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl
GO:0007288; P:sperm axoneme assembly; IMP:MGI
GO:0030317; P:sperm motility; IMP:MGI
Interpro
InterPro; IPR006573; NeuZ_dom
InterPro; IPR001841; Znf_RING
InterPro; IPR013083; Znf_RING/FYVE/PHD
Pfam
Pfam; PF07177; Neuralized;
SMART
SMART; SM00588; NEUZ;
SMART; SM00184; RING;
PROSITE
PROSITE; PS51065; NHR;
PROSITE; PS50089; ZF_RING_2;
PRINTS