NEU1B_MOUSE
ID NEU1B_MOUSE Reviewed; 546 AA.
AC Q0MW30; C9DQJ8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=E3 ubiquitin-protein ligase NEURL1B;
DE EC=2.3.2.27;
DE AltName: Full=Neuralized-2;
DE Short=NEUR2;
DE AltName: Full=Neuralized-like protein 1B;
DE AltName: Full=Neuralized-like protein 2;
DE AltName: Full=Neuralized-like protein 3;
DE AltName: Full=RING-type E3 ubiquitin transferase NEURL1B {ECO:0000305};
GN Name=Neurl1b; Synonyms=Neurl2, Neurl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=17003037; DOI=10.1074/jbc.m606601200;
RA Song R., Koo B.-K., Yoon K.-J., Yoon M.-J., Yoo K.-W., Kim H.-T., Oh H.-J.,
RA Kim Y.-Y., Han J.-K., Kim C.-H., Kong Y.-Y.;
RT "Neuralized-2 regulates a Notch ligand in cooperation with Mind bomb-1.";
RL J. Biol. Chem. 281:36391-36400(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH DLL1 AND DLL4.
RX PubMed=19723503; DOI=10.1016/j.bbrc.2009.08.147;
RA Rullinkov G., Tamme R., Sarapuu A., Lauren J., Sepp M., Palm K.,
RA Timmusk T.;
RT "Neuralized-2: Expression in human and rodents and interaction with Delta-
RT like ligands.";
RL Biochem. Biophys. Res. Commun. 389:420-425(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in regulation of the
CC Notch pathway through influencing the stability and activity of several
CC Notch ligands. {ECO:0000269|PubMed:17003037,
CC ECO:0000269|PubMed:19723503}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DLL1 and DLL4. {ECO:0000269|PubMed:19723503}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19723503}.
CC -!- TISSUE SPECIFICITY: Expressed in the limb buds and dorsal root ganglia.
CC Expressed in brain and kidney and at low levels in the heart.
CC {ECO:0000269|PubMed:17003037}.
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DR EMBL; DQ839448; ABH10575.1; -; mRNA.
DR EMBL; GQ414760; ACV53566.1; -; mRNA.
DR CCDS; CCDS37513.1; -.
DR RefSeq; NP_001075125.1; NM_001081656.2.
DR AlphaFoldDB; Q0MW30; -.
DR SMR; Q0MW30; -.
DR BioGRID; 232152; 1.
DR STRING; 10090.ENSMUSP00000051481; -.
DR iPTMnet; Q0MW30; -.
DR PhosphoSitePlus; Q0MW30; -.
DR PaxDb; Q0MW30; -.
DR PRIDE; Q0MW30; -.
DR ProteomicsDB; 252814; -.
DR Antibodypedia; 49674; 47 antibodies from 10 providers.
DR Ensembl; ENSMUST00000053020; ENSMUSP00000051481; ENSMUSG00000034413.
DR GeneID; 240055; -.
DR KEGG; mmu:240055; -.
DR UCSC; uc008bed.2; mouse.
DR CTD; 54492; -.
DR MGI; MGI:3643092; Neurl1b.
DR VEuPathDB; HostDB:ENSMUSG00000034413; -.
DR eggNOG; KOG4172; Eukaryota.
DR eggNOG; KOG4625; Eukaryota.
DR GeneTree; ENSGT00940000157079; -.
DR HOGENOM; CLU_013230_1_0_1; -.
DR InParanoid; Q0MW30; -.
DR OMA; NKNGECT; -.
DR OrthoDB; 1384219at2759; -.
DR PhylomeDB; Q0MW30; -.
DR TreeFam; TF314368; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 240055; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Neurl1b; mouse.
DR PRO; PR:Q0MW30; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q0MW30; protein.
DR Bgee; ENSMUSG00000034413; Expressed in ureter smooth muscle and 178 other tissues.
DR ExpressionAtlas; Q0MW30; baseline and differential.
DR Genevisible; Q0MW30; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IDA:UniProtKB.
DR Gene3D; 2.60.120.920; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR037962; Neuralized.
DR InterPro; IPR006573; NHR_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12429; PTHR12429; 1.
DR Pfam; PF07177; Neuralized; 2.
DR SMART; SM00588; NEUZ; 2.
DR PROSITE; PS51065; NHR; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Notch signaling pathway; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..546
FT /note="E3 ubiquitin-protein ligase NEURL1B"
FT /id="PRO_0000349383"
FT DOMAIN 38..194
FT /note="NHR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT DOMAIN 270..424
FT /note="NHR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT ZN_FING 494..534
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 429..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A8MQ27"
SQ SEQUENCE 546 AA; 58527 MW; 7201090850E88DD1 CRC64;
MGNTVHRTLP DSSPPARLLA TRPCYGPGPE RRAVLGEAPR FHAQAKGKNV RLDGHSRRAT
RRNSFCNGVT FTQRPIRLYE QVRLRLVAVR PGWSGALRFG FTAHDPSLMS AQDIPKYACP
DLVTRPGYWA KALPENLALR DTVLAYWADR HGRVFYSVND GEPVLFHCGV AVGGPLWALI
DVYGITDEVQ LLESTFADTL TPLRLGQARL SACPPPGSHD AANFDNNELE NNQVVAKLGH
LALGRPDAAV PCVARERPRP ASSPALLDAE LRFHATRGPD VSLSADRRLA CAPRPDGGRT
LVFSERPLRP GESLCVEVGR PGLAAPAAVA FGITSCDPGA LRPSELPADP AALLDRKEYW
VVARAGPVPS GGDALSFTLR PGGDVLLAVN GRPRGRLLCV DTSQALWAFF AVRGGVAGQL
RLLGTLQSSS ETMTPSGSFS GSQDDSDSDM TFGVNQSSSA SESSLVTAPS SPLSPPVSPA
FSAPEPTGSR NGECTVCFDS EVDTVIYTCG HMCLCHGCGL RLRRQARACC PICRRPIKDV
IKIYRP
