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E3 ubiquitin-protein ligase mib1 (EC 2.3.2.27) (Protein mind bomb) (RING-type E3 ubiquitin transferase mib1)

 MIB1_DANRE              Reviewed;        1030 AA.
Q804S5; Q8JHG3;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
30-AUG-2017, entry version 120.
RecName: Full=E3 ubiquitin-protein ligase mib1;
EC=2.3.2.27;
AltName: Full=Protein mind bomb;
AltName: Full=RING-type E3 ubiquitin transferase mib1 {ECO:0000305};
Name=mib1; Synonyms=mib;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, SUBCELLULAR
LOCATION, INTERACTION WITH DLD, AND MUTAGENESIS OF CYS-1009 AND
MET-1013.
PubMed=12530964; DOI=10.1016/S1534-5807(02)00409-4;
Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D.,
Yeo S.-Y., Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M.,
Lewis J., Chandrasekharappa S.C., Chitnis A.B.;
"Mind bomb is a ubiquitin ligase that is essential for efficient
activation of Notch signaling by Delta.";
Dev. Cell 4:67-82(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-237, FUNCTION, AND
DISRUPTION PHENOTYPE.
TISSUE=Embryo;
PubMed=12006978; DOI=10.1038/ng896;
Golling G., Amsterdam A., Sun Z., Antonelli M., Maldonado E., Chen W.,
Burgess S., Haldi M., Artzt K., Farrington S., Lin S.-Y., Nissen R.M.,
Hopkins N.;
"Insertional mutagenesis in zebrafish rapidly identifies genes
essential for early vertebrate development.";
Nat. Genet. 31:135-140(2002).
[3]
FUNCTION.
PubMed=9806913;
Haddon C., Jiang Y.-J., Smithers L., Lewis J.;
"Delta-Notch signalling and the patterning of sensory cell
differentiation in the zebrafish ear: evidence from the mind bomb
mutant.";
Development 125:4637-4644(1998).
[4]
FUNCTION.
PubMed=10074451; DOI=10.1016/S0960-9822(99)80113-4;
Appel B., Fritz A., Westerfield M., Grunwald D.J., Eisen J.S.,
Riley B.B.;
"Delta-mediated specification of midline cell fates in zebrafish
embryos.";
Curr. Biol. 9:247-256(1999).
[5]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH DLA AND
DLD.
PubMed=15013799; DOI=10.1016/j.ydbio.2003.11.010;
Chen W., Corliss D.C.;
"Three modules of zebrafish Mind bomb work cooperatively to promote
Delta ubiquitination and endocytosis.";
Dev. Biol. 267:361-373(2004).
[6]
FUNCTION.
PubMed=14579383; DOI=10.1002/dvdy.10429;
Bingham S., Chaudhari S., Vanderlaan G., Itoh M., Chitnis A.,
Chandrasekhar A.;
"Neurogenic phenotype of mind bomb mutants leads to severe patterning
defects in the zebrafish hindbrain.";
Dev. Dyn. 228:451-463(2003).
[7]
FUNCTION.
PubMed=15689380; DOI=10.1242/dev.01644;
Crosnier C., Vargesson N., Gschmeissner S., Ariza-McNaughton L.,
Morrison A., Lewis J.;
"Delta-Notch signalling controls commitment to a secretory fate in the
zebrafish intestine.";
Development 132:1093-1104(2005).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of Delta receptors, which act as ligands of Notch proteins.
Positively regulates the Delta-mediated Notch signaling by
ubiquitinating the intracellular domain of Delta, leading to
endocytosis of Delta receptors. It thereby participates in many
processes regulated by the Notch signaling pathway, such as
midline cell fate specification prior to germ layer formation,
patterning of sensory cell differentiation in the ear,
neurogenesis of the hindbrain and commitment to a secretory fate
in the intestine. Essential for early embryonic development.
{ECO:0000269|PubMed:10074451, ECO:0000269|PubMed:12006978,
ECO:0000269|PubMed:12530964, ECO:0000269|PubMed:14579383,
ECO:0000269|PubMed:15013799, ECO:0000269|PubMed:15689380,
ECO:0000269|PubMed:9806913}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with deltaA (dla) and deltaD (dld).
{ECO:0000269|PubMed:12530964, ECO:0000269|PubMed:15013799}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriolar satellite {ECO:0000250}.
Cytoplasm. Cell membrane. Note=Localizes to the plasma membrane.
-!- DOMAIN: The N-terminal domain (1-440) mediates the interaction
with Delta receptors. {ECO:0000269|PubMed:15013799}.
-!- DOMAIN: The ANK repeats are involved in Delta receptor
internalization. {ECO:0000269|PubMed:15013799}.
-!- DOMAIN: The RING fingers mediate the E3 ligase activity. The third
RING finger probably plays a central role in this process. The
role of the other RING fingers remains unclear.
{ECO:0000269|PubMed:15013799}.
-!- DISRUPTION PHENOTYPE: Mutants have a disorganized brain and neural
tube, bent tail and very small or absent otoliths.
{ECO:0000269|PubMed:12006978}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF537301; AAO37830.1; -; mRNA.
EMBL; AF506233; AAM34677.1; -; mRNA.
RefSeq; NP_775393.2; NM_173286.3.
UniGene; Dr.106501; -.
UniGene; Dr.124112; -.
ProteinModelPortal; Q804S5; -.
SMR; Q804S5; -.
BioGrid; 87906; 61.
STRING; 7955.ENSDARP00000109025; -.
PaxDb; Q804S5; -.
PeptideAtlas; Q804S5; -.
PRIDE; Q804S5; -.
Ensembl; ENSDART00000165634; ENSDARP00000139883; ENSDARG00000102184.
GeneID; 352910; -.
KEGG; dre:352910; -.
CTD; 57534; -.
ZFIN; ZDB-GENE-030404-2; mib1.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4582; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00890000139372; -.
HOVERGEN; HBG068386; -.
InParanoid; Q804S5; -.
KO; K10645; -.
OMA; CYNERKT; -.
OrthoDB; EOG091G00Z0; -.
UniPathway; UPA00143; -.
PRO; PR:Q804S5; -.
Proteomes; UP000000437; Chromosome 2.
Bgee; ENSDARG00000102184; -.
ExpressionAtlas; Q804S5; baseline.
GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:ZFIN.
GO; GO:0030139; C:endocytic vesicle; IDA:ZFIN.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IGI:ZFIN.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IPI:ZFIN.
GO; GO:0000151; C:ubiquitin ligase complex; IC:ZFIN.
GO; GO:0042803; F:protein homodimerization activity; IDA:ZFIN.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:ZFIN.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048899; P:anterior lateral line development; IMP:ZFIN.
GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:ZFIN.
GO; GO:0007420; P:brain development; IMP:ZFIN.
GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
GO; GO:0048066; P:developmental pigmentation; IMP:ZFIN.
GO; GO:0021536; P:diencephalon development; IMP:ZFIN.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:ZFIN.
GO; GO:0031076; P:embryonic camera-type eye development; IMP:ZFIN.
GO; GO:0009880; P:embryonic pattern specification; IMP:ZFIN.
GO; GO:0001885; P:endothelial cell development; IMP:ZFIN.
GO; GO:0002064; P:epithelial cell development; IMP:ZFIN.
GO; GO:0021508; P:floor plate formation; IMP:ZFIN.
GO; GO:0048859; P:formation of anatomical boundary; IMP:ZFIN.
GO; GO:0048699; P:generation of neurons; IMP:ZFIN.
GO; GO:0010001; P:glial cell differentiation; IMP:ZFIN.
GO; GO:0021986; P:habenula development; IMP:ZFIN.
GO; GO:0035315; P:hair cell differentiation; IMP:ZFIN.
GO; GO:0007507; P:heart development; IMP:ZFIN.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:ZFIN.
GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
GO; GO:0060113; P:inner ear receptor cell differentiation; IMP:ZFIN.
GO; GO:0048892; P:lateral line nerve development; IMP:ZFIN.
GO; GO:0030318; P:melanocyte differentiation; IMP:ZFIN.
GO; GO:0003407; P:neural retina development; IMP:ZFIN.
GO; GO:0022008; P:neurogenesis; IMP:ZFIN.
GO; GO:0048666; P:neuron development; IMP:ZFIN.
GO; GO:0030182; P:neuron differentiation; IMP:ZFIN.
GO; GO:0048663; P:neuron fate commitment; IMP:ZFIN.
GO; GO:0048665; P:neuron fate specification; IMP:ZFIN.
GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
GO; GO:0060035; P:notochord cell development; IMP:ZFIN.
GO; GO:0030903; P:notochord development; IMP:ZFIN.
GO; GO:0003408; P:optic cup formation involved in camera-type eye development; IMP:ZFIN.
GO; GO:0071599; P:otic vesicle development; IMP:ZFIN.
GO; GO:0050931; P:pigment cell differentiation; IMP:ZFIN.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:ZFIN.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:ZFIN.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IPI:ZFIN.
GO; GO:0048916; P:posterior lateral line development; IMP:ZFIN.
GO; GO:0039022; P:pronephric duct development; IMP:ZFIN.
GO; GO:0048793; P:pronephros development; IMP:ZFIN.
GO; GO:0051865; P:protein autoubiquitination; IDA:ZFIN.
GO; GO:0016567; P:protein ubiquitination; IDA:ZFIN.
GO; GO:0045685; P:regulation of glial cell differentiation; IMP:ZFIN.
GO; GO:0045664; P:regulation of neuron differentiation; IMP:ZFIN.
GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:ZFIN.
GO; GO:0002090; P:regulation of receptor internalization; IDA:ZFIN.
GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IMP:ZFIN.
GO; GO:0021654; P:rhombomere boundary formation; IMP:ZFIN.
GO; GO:0021546; P:rhombomere development; IMP:ZFIN.
GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
GO; GO:0021519; P:spinal cord association neuron specification; IMP:ZFIN.
GO; GO:0021510; P:spinal cord development; IMP:ZFIN.
GO; GO:0021520; P:spinal cord motor neuron cell fate specification; IMP:ZFIN.
GO; GO:0061195; P:taste bud formation; IMP:ZFIN.
GO; GO:0061551; P:trigeminal ganglion development; IMP:ZFIN.
GO; GO:0070086; P:ubiquitin-dependent endocytosis; IPI:ZFIN.
GO; GO:0001570; P:vasculogenesis; IMP:ZFIN.
GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IMP:ZFIN.
GO; GO:0021521; P:ventral spinal cord interneuron specification; IMP:ZFIN.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR010606; Mib_Herc2.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR000433; Znf_ZZ.
Pfam; PF12796; Ank_2; 3.
Pfam; PF06701; MIB_HERC2; 2.
Pfam; PF00569; ZZ; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 8.
SMART; SM00184; RING; 3.
SMART; SM00291; ZnF_ZZ; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 6.
PROSITE; PS51416; MIB_HERC2; 2.
PROSITE; PS50089; ZF_RING_2; 3.
PROSITE; PS01357; ZF_ZZ_1; 1.
PROSITE; PS50135; ZF_ZZ_2; 1.
1: Evidence at protein level;
ANK repeat; Cell membrane; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; Membrane; Metal-binding;
Notch signaling pathway; Reference proteome; Repeat; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1030 E3 ubiquitin-protein ligase mib1.
/FTId=PRO_0000055945.
DOMAIN 6 74 MIB/HERC2 1. {ECO:0000255|PROSITE-
ProRule:PRU00749}.
DOMAIN 143 221 MIB/HERC2 2. {ECO:0000255|PROSITE-
ProRule:PRU00749}.
REPEAT 430 460 ANK 1.
REPEAT 463 492 ANK 2.
REPEAT 496 525 ANK 3.
REPEAT 529 558 ANK 4.
REPEAT 562 591 ANK 5.
REPEAT 595 627 ANK 6.
REPEAT 631 661 ANK 7.
REPEAT 665 694 ANK 8.
REPEAT 698 727 ANK 9.
ZN_FING 79 126 ZZ-type. {ECO:0000255|PROSITE-
ProRule:PRU00228}.
ZN_FING 817 852 RING-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 864 899 RING-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 987 1020 RING-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COILED 957 986 {ECO:0000255}.
MUTAGEN 1009 1009 C->S: In tfi101; induces neurogenic
defects due to reduced notch signaling.
{ECO:0000269|PubMed:12530964}.
MUTAGEN 1013 1013 M->R: In ta52b; induces neurogenic
defects due to reduced notch signaling.
{ECO:0000269|PubMed:12530964}.
CONFLICT 236 237 EQ -> KI (in Ref. 2; AAM34677).
{ECO:0000305}.
SEQUENCE 1030 AA; 112688 MW; DAB541D403215A02 CRC64;
MTTGRNNRVM MEGVGARVIR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
RCSGAYDVRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT TCYHGDKHHL
RHRFYRITTP GSERVLLESR RKSKKITARG IFAGGRVVRG VDWQWEDQDG GNGRRGKVTE
IQDWSAASPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGTFYRDH CPVLGEQNGN
RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
GNRWTFNPAV LTKANVVRSG EVAAGAEGGS SQFMVGDLVQ ICYDIDRIKL LQRGHGEWAE
AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVTKV APAGSAVTNA SGERLSQLLK
KLFETQESGD INEELVKAAA NGDLAKVEDI LKRPDVDVNG QCAGHTAMQA ASQNGHVDVL
KLLLKHSVDL EAEDKDGDRA VHHASFGDEG SVIEVLHRGG ADLNARNKRR QTPLHIAVNK
GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDMLS VLLEAGADVT ITNNNGFNAL
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGNANLD
VQNVNQQTAL HLAVERQHTQ IVRLLVRAEA KLDVQDKDGD TPLHEALRHH TLSQLRQLQD
MQDVSKVEPW EPSKNTLIMG LGTQGAEKKS AASIACFLAA NGADLTIRNK KGQSPLDLCP
DPSLCKALAK CHKEKTSGQV GSRSPSLNSN NETLEECMVC SDMKRDTLFG PCGHIATCSL
CSPRVKKCLI CKEQVQSRTK IEECVVCSDK KAAVLFQPCG HMCACENCAS LMKKCVQCRA
VVERRTPFVL CCGGKGMEDA TDDEDLTGGS NSMAGGSQDL LQPNNLALSW SSGNIPALQR
DKDNTNVNAD VQKLQQQLQD IKEQTMCPVC LDRLKNMIFM CGHGTCQLCG DRMSECPICR
KAIERRILLY


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