Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q80SY4 (MIB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase MIB1

EC=6.3.2.-
Alternative name(s):
DAPK-interacting protein 1
Short name=DIP-1
Mind bomb homolog 1
Gene names
Name:Mib1
Synonyms:Dip1, Kiaa1323, Mib
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1006 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation By similarity. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis. Ref.1

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with CEP131 and PCM1 By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity. Cytoplasm. Cell membrane. Note: Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock By similarity. Localizes to the plasma membrane.

Tissue specificity

Detected in all tissues tested. Present in embryo, embryonic stem cells, bladder, skeletal muscle, bladder, uterus, testis, stomach, colon, ileum, trachea, lung, aorta, kidney, spleen, liver and vas deferens (at protein level). Highly expressed in testis. Ref.1 Ref.3

Developmental stage

Highly expressed both in embryos and adult tissues. In E9.5 and E10.5 embryos, it is expressed in the tail bud, limb buds and somites. Expressed in the same pattern than MIB2 in the skin and intestine at postnatal day 1 (P1) and in the hair follicle in the skin in the adult. Ref.3

Post-translational modification

Ubiquitinated; this modification is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock By similarity. Ubiquitinated; possibly via autoubiquitination. Ref.1 Ref.3

Sequence similarities

Contains 9 ANK repeats.

Contains 2 MIB/HERC2 domains.

Contains 3 RING-type zinc fingers.

Contains 1 ZZ-type zinc finger.

Sequence caution

The sequence AAH11287.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH69870.1 differs from that shown. Reason: Chimeric cDNA.

The sequence AAN18022.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC38042.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Ontologies

Keywords
   Biological processNotch signaling pathway
Ubl conjugation pathway
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   DomainANK repeat
Coiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from mutant phenotype PubMed 16000382. Source: MGI

blood vessel development

Inferred from mutant phenotype PubMed 16000382. Source: MGI

heart development

Inferred from mutant phenotype PubMed 16000382. Source: MGI

heart looping

Inferred from mutant phenotype PubMed 16000382. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 16000382. Source: MGI

negative regulation of neuron differentiation

Inferred from mutant phenotype PubMed 16000382. Source: MGI

neural tube formation

Inferred from mutant phenotype PubMed 16000382. Source: MGI

positive regulation of endocytosis

Inferred from direct assay PubMed 16000382. Source: MGI

somitogenesis

Inferred from mutant phenotype PubMed 16000382. Source: MGI

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from direct assay PubMed 16000382. Source: MGI

nuclear membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16857196PubMed 20018188. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CMIPQ8IY222EBI-645227,EBI-7689652From a different organism.
snx5Q6DI324EBI-645227,EBI-8574974From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10061006E3 ubiquitin-protein ligase MIB1
PRO_0000055944

Regions

Domain6 – 7469MIB/HERC2 1
Domain143 – 22179MIB/HERC2 2
Repeat430 – 46031ANK 1
Repeat463 – 49230ANK 2
Repeat496 – 52530ANK 3
Repeat529 – 55830ANK 4
Repeat562 – 59130ANK 5
Repeat595 – 62733ANK 6
Repeat631 – 66131ANK 7
Repeat665 – 69430ANK 8
Repeat698 – 72932ANK 9
Zinc finger79 – 12648ZZ-type
Zinc finger819 – 85436RING-type 1
Zinc finger866 – 90136RING-type 2
Zinc finger963 – 99634RING-type 3
Coiled coil935 – 96228 Potential

Experimental info

Sequence conflict7421L → F in BAC38042. Ref.4
Sequence conflict9071R → K in AAN18022. Ref.3
Sequence conflict9071R → K in AAX84653. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q80SY4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5A8FE2A1BEE638DE

FASTA1,006110,088
        10         20         30         40         50         60 
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY 

        70         80         90        100        110        120 
RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL 

       130        140        150        160        170        180 
RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE 

       190        200        210        220        230        240 
IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN 

       250        260        270        280        290        300 
RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS 

       310        320        330        340        350        360 
GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL LQRGHGEWAE 

       370        380        390        400        410        420 
AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV APAGSAISNA SGERLSQLLK 

       430        440        450        460        470        480 
KLFETQESGD LNEELVKAAA NGDVAKVEDL LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL 

       490        500        510        520        530        540 
KLLLKQNVDV EAEDKDGDRA VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK 

       550        560        570        580        590        600 
GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL 

       610        620        630        640        650        660 
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGNANLD 

       670        680        690        700        710        720 
IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD TPLHEALRHH TLSQLRQLQD 

       730        740        750        760        770        780 
MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK SAASIACFLA ANGADLSIRN KKGQSPLDLC 

       790        800        810        820        830        840 
PDPSLCKALA KCHKEKVSGQ VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC 

       850        860        870        880        890        900 
SLCSPRVKKC LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ASLMKKCVQC 

       910        920        930        940        950        960 
RAVVERRVPF ITCCGGKSSE DPSDEISSGN IPVLQKDKDN TNVNADVQKL QQQLQDIKEQ 

       970        980        990       1000 
TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE RRILLY 

« Hide

References

« Hide 'large scale' references
[1]"A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of DAPK."
Jin Y., Blue E.K., Dixon S., Shao Z., Gallagher P.J.
J. Biol. Chem. 277:46980-46986(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, UBIQUITINATION.
Tissue: Urinary bladder.
[2]"Mind bomb is a ubiquitin ligase that is essential for efficient activation of Notch signaling by Delta."
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.
Dev. Cell 4:67-82(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
[3]"Mind bomb-2 is an E3 ligase for Notch ligand."
Koo B.-K., Yoon K.-J., Yoo K.-W., Lim H.-S., Song R., So J.-H., Kim C.-H., Kong Y.-Y.
J. Biol. Chem. 280:22335-22342(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, UBIQUITINATION.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1006.
Strain: C57BL/6J.
Tissue: Corpora quadrigemina and Head.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1006.
Strain: 129 and FVB/N.
Tissue: Embryo and Mammary tumor.
[6]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 864-1006.
Tissue: Embryonic tail.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY245539 mRNA. Translation: AAO91933.1.
AY149907 mRNA. Translation: AAN75492.1.
AY147848 mRNA. Translation: AAN18022.1. Different initiation.
AY974091 mRNA. Translation: AAX84653.1.
AK053035 mRNA. Translation: BAC35245.1.
AK080847 mRNA. Translation: BAC38042.1. Sequence problems.
BC011287 mRNA. Translation: AAH11287.1. Different initiation.
BC069870 mRNA. Translation: AAH69870.1. Sequence problems.
BC083072 mRNA. Translation: AAH83072.1.
AK129331 mRNA. Translation: BAC98141.1.
CCDSCCDS29058.1.
RefSeqNP_659109.2. NM_144860.2.
XP_006525873.1. XM_006525810.1.
XP_006525874.1. XM_006525811.1.
UniGeneMm.21500.

3D structure databases

ProteinModelPortalQ80SY4.
SMRQ80SY4. Positions 15-70, 154-216, 355-779, 851-908, 953-1003.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230365. 11 interactions.
IntActQ80SY4. 5 interactions.
MINTMINT-1550820.

PTM databases

PhosphoSiteQ80SY4.

Proteomic databases

PaxDbQ80SY4.
PRIDEQ80SY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052838; ENSMUSP00000054428; ENSMUSG00000024294.
ENSMUST00000165555; ENSMUSP00000131712; ENSMUSG00000024294.
GeneID225164.
KEGGmmu:225164.
UCSCuc008ebc.1. mouse.

Organism-specific databases

CTD57534.
MGIMGI:2443157. Mib1.
RougeSearch...

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00660000095288.
HOVERGENHBG068386.
InParanoidQ80SY4.
KOK10645.
OMAHDAISKE.
OrthoDBEOG7WHH8P.
PhylomeDBQ80SY4.
TreeFamTF324147.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ80SY4.
BgeeQ80SY4.
CleanExMM_MIB1.
GenevestigatorQ80SY4.

Family and domain databases

Gene3D1.25.40.20. 3 hits.
3.30.40.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 3 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMIB1. mouse.
NextBio377558.
PROQ80SY4.
SOURCESearch...

Entry information

Entry nameMIB1_MOUSE
AccessionPrimary (citable) accession number: Q80SY4
Secondary accession number(s): Q5XK51 expand/collapse secondary AC list , Q6IS57, Q6YI52, Q6ZPT8, Q8BNR1, Q8C6W2, Q921Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot