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Protein

E3 ubiquitin-protein ligase MIB1

Gene

MIB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis (By similarity). 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 similarity1 Publication

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri79 – 12648ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri819 – 85436RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri866 – 90136RING-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 99634RING-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Notch signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_160089. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SignaLinkiQ86YT6.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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
Zinc finger ZZ type with ankyrin repeat domain protein 2
Gene namesi
Name:MIB1
Synonyms:DIP1, KIAA1323, ZZANK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:21086. MIB1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytoplasmic vesicle Source: Ensembl
  • cytosol Source: Reactome
  • plasma membrane Source: UniProtKB-SubCell
  • postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Left ventricular non-compaction 7 (LVNC7)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies.

See also OMIM:615092
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti943 – 9431V → F in LVNC7. 1 Publication
VAR_069620

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615092. phenotype.
Orphaneti54260. Left ventricular noncompaction.
PharmGKBiPA134862722.

Polymorphism and mutation databases

DMDMi68565512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10061006E3 ubiquitin-protein ligase MIB1PRO_0000055943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei408 – 4081Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated; possibly via autoubiquitination (By similarity). Ubiquitinated; this modification is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock.By similarity2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ86YT6.
PaxDbiQ86YT6.
PRIDEiQ86YT6.

PTM databases

PhosphoSiteiQ86YT6.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed at higher level in spinal cord, ovary, whole brain, and all specific brain regions examined.1 Publication

Gene expression databases

BgeeiQ86YT6.
CleanExiHS_MIB1.
GenevisibleiQ86YT6. HS.

Organism-specific databases

HPAiCAB037044.
HPA019100.

Interactioni

Subunit structurei

Interacts with CEP131 and PCM1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Azi2Q9QYP62EBI-2129148,EBI-6115874From a different organism.
TBK1Q9UHD22EBI-2129148,EBI-356402

Protein-protein interaction databases

BioGridi121593. 35 interactions.
IntActiQ86YT6. 13 interactions.
MINTiMINT-2841371.
STRINGi9606.ENSP00000261537.

Structurei

Secondary structure

1
1006
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 204Combined sources
Turni27 – 304Combined sources
Beta strandi37 – 5216Combined sources
Beta strandi57 – 6610Combined sources
Beta strandi68 – 725Combined sources
Helixi74 – 763Combined sources
Turni86 – 883Combined sources
Beta strandi91 – 10515Combined sources
Helixi110 – 1145Combined sources
Beta strandi124 – 1274Combined sources
Helixi140 – 1423Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi156 – 1594Combined sources
Turni166 – 1694Combined sources
Beta strandi176 – 1827Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi202 – 2087Combined sources
Helixi209 – 2113Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi221 – 2277Combined sources
Helixi228 – 2303Combined sources
Beta strandi251 – 2533Combined sources
Helixi258 – 2647Combined sources
Turni265 – 2695Combined sources
Helixi273 – 2764Combined sources
Helixi277 – 2804Combined sources
Beta strandi283 – 2886Combined sources
Turni290 – 2923Combined sources
Beta strandi294 – 2974Combined sources
Beta strandi303 – 3064Combined sources
Helixi308 – 3103Combined sources
Beta strandi338 – 3414Combined sources
Helixi345 – 35410Combined sources
Helixi360 – 3656Combined sources
Beta strandi369 – 3757Combined sources
Beta strandi381 – 3855Combined sources
Beta strandi388 – 3925Combined sources
Helixi394 – 3963Combined sources
Beta strandi397 – 3993Combined sources
Beta strandi402 – 4054Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TSEX-ray2.06A/B239-409[»]
4XI6X-ray2.04A8-402[»]
4XI7X-ray2.05A8-402[»]
4XIBX-ray2.15A8-402[»]
ProteinModelPortaliQ86YT6.
SMRiQ86YT6. Positions 15-70, 154-216, 382-779, 851-908, 953-1003.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 7469MIB/HERC2 1PROSITE-ProRule annotationAdd
BLAST
Domaini143 – 22179MIB/HERC2 2PROSITE-ProRule annotationAdd
BLAST
Repeati430 – 46031ANK 1Add
BLAST
Repeati463 – 49230ANK 2Add
BLAST
Repeati496 – 52530ANK 3Add
BLAST
Repeati529 – 55830ANK 4Add
BLAST
Repeati562 – 59130ANK 5Add
BLAST
Repeati595 – 62733ANK 6Add
BLAST
Repeati631 – 66131ANK 7Add
BLAST
Repeati665 – 69430ANK 8Add
BLAST
Repeati698 – 72932ANK 9Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili935 – 96228Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 9 ANK repeats.PROSITE-ProRule annotation
Contains 2 MIB/HERC2 domains.PROSITE-ProRule annotation
Contains 3 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri79 – 12648ZZ-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri819 – 85436RING-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri866 – 90136RING-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 99634RING-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00790000122981.
HOVERGENiHBG068386.
InParanoidiQ86YT6.
KOiK10645.
OMAiNNHVEIA.
OrthoDBiEOG7WHH8P.
PhylomeDBiQ86YT6.
TreeFamiTF324147.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 3 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. 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]

Sequencei

Sequence statusi: Complete.

Q86YT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV
60 70 80 90 100
VWDNGTAANY RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC
110 120 130 140 150
AECTNYDLCT VCYHGDKHHL RHRFYRITTP GSERVLLESR RKSKKITARG
160 170 180 190 200
IFAGARVVRG VDWQWEDQDG GNGRRGKVTE IQDWSASSPH SAAYVLWDNG
210 220 230 240 250
AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN RNPGGLQIGD
260 270 280 290 300
LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
310 320 330 340 350
GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL
360 370 380 390 400
LQRGHGEWAE AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV
410 420 430 440 450
ASAGSAISNA SGERLSQLLK KLFETQESGD LNEELVKAAA NGDVAKVEDL
460 470 480 490 500
LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL KLLLKQNVDV EAEDKDGDRA
510 520 530 540 550
VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK GHLQVVKTLL
560 570 580 590 600
DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
610 620 630 640 650
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL
660 670 680 690 700
LVHQGNANLD IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD
710 720 730 740 750
TPLHEALRHH TLSQLRQLQD MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK
760 770 780 790 800
SAASIACFLA ANGADLSIRN KKGQSPLDLC PDPNLCKALA KCHKEKVSGQ
810 820 830 840 850
VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC SLCSPRVKKC
860 870 880 890 900
LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ANLMKKCVQC
910 920 930 940 950
RAVVERRVPF IMCCGGKSSE DATDDISSGN IPVLQKDKDN TNVNADVQKL
960 970 980 990 1000
QQQLQDIKEQ TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE

RRILLY
Length:1,006
Mass (Da):110,136
Last modified:June 1, 2003 - v1
Checksum:i5D7D0D91AF98FF18
GO

Sequence cautioni

The sequence AAH22403.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAN18023.1 differs from that shown. Reason: Frameshift at position 3. Curated
The sequence BAC11439.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti327 – 3271E → K in AAN18023 (Ref. 2) Curated
Sequence conflicti398 – 3981S → F in AAN18023 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741R → H Found in a patient with severe mental retardation, psychomotor delay, no speech, sleep disturbances, feeding problems, abnormal breething, deep-set eyes and short philtrum. 1 Publication
VAR_069385
Natural varianti943 – 9431V → F in LVNC7. 1 Publication
VAR_069620

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY149908 mRNA. Translation: AAN75493.1.
AY147849 mRNA. Translation: AAN18023.1. Frameshift.
EF444995 Genomic DNA. Translation: ACA06016.1.
BC022403 mRNA. Translation: AAH22403.1. Different initiation.
BC110581 mRNA. Translation: AAI10582.1.
BC110582 mRNA. Translation: AAI10583.1.
CR749635 mRNA. Translation: CAH18429.1.
AL713705 mRNA. Translation: CAD28502.1.
AB037744 mRNA. Translation: BAA92561.1.
AK075157 mRNA. Translation: BAC11439.1. Different initiation.
CCDSiCCDS11871.1.
RefSeqiNP_065825.1. NM_020774.3.
UniGeneiHs.140903.

Genome annotation databases

EnsembliENST00000261537; ENSP00000261537; ENSG00000101752.
GeneIDi57534.
KEGGihsa:57534.
UCSCiuc002ktp.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY149908 mRNA. Translation: AAN75493.1.
AY147849 mRNA. Translation: AAN18023.1. Frameshift.
EF444995 Genomic DNA. Translation: ACA06016.1.
BC022403 mRNA. Translation: AAH22403.1. Different initiation.
BC110581 mRNA. Translation: AAI10582.1.
BC110582 mRNA. Translation: AAI10583.1.
CR749635 mRNA. Translation: CAH18429.1.
AL713705 mRNA. Translation: CAD28502.1.
AB037744 mRNA. Translation: BAA92561.1.
AK075157 mRNA. Translation: BAC11439.1. Different initiation.
CCDSiCCDS11871.1.
RefSeqiNP_065825.1. NM_020774.3.
UniGeneiHs.140903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TSEX-ray2.06A/B239-409[»]
4XI6X-ray2.04A8-402[»]
4XI7X-ray2.05A8-402[»]
4XIBX-ray2.15A8-402[»]
ProteinModelPortaliQ86YT6.
SMRiQ86YT6. Positions 15-70, 154-216, 382-779, 851-908, 953-1003.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121593. 35 interactions.
IntActiQ86YT6. 13 interactions.
MINTiMINT-2841371.
STRINGi9606.ENSP00000261537.

PTM databases

PhosphoSiteiQ86YT6.

Polymorphism and mutation databases

DMDMi68565512.

Proteomic databases

MaxQBiQ86YT6.
PaxDbiQ86YT6.
PRIDEiQ86YT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261537; ENSP00000261537; ENSG00000101752.
GeneIDi57534.
KEGGihsa:57534.
UCSCiuc002ktp.3. human.

Organism-specific databases

CTDi57534.
GeneCardsiGC18P019284.
HGNCiHGNC:21086. MIB1.
HPAiCAB037044.
HPA019100.
MIMi608677. gene.
615092. phenotype.
neXtProtiNX_Q86YT6.
Orphaneti54260. Left ventricular noncompaction.
PharmGKBiPA134862722.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00790000122981.
HOVERGENiHBG068386.
InParanoidiQ86YT6.
KOiK10645.
OMAiNNHVEIA.
OrthoDBiEOG7WHH8P.
PhylomeDBiQ86YT6.
TreeFamiTF324147.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_160089. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SignaLinkiQ86YT6.

Miscellaneous databases

ChiTaRSiMIB1. human.
GeneWikiiMIB1_(gene).
GenomeRNAii57534.
NextBioi63948.
PROiQ86YT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ86YT6.
CleanExiHS_MIB1.
GenevisibleiQ86YT6. HS.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 3 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. Yoo K.-W., Chitnis A., Kim C.-H.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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].
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-1006.
    Tissue: Amygdala and Endometrial tumor.
  6. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 611-1006, TISSUE SPECIFICITY.
    Tissue: Brain.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 627-1006.
    Tissue: Placenta.
  8. "Death-associated protein kinase expression in human temporal lobe epilepsy."
    Henshall D.C., Schindler C.K., So N.K., Lan J.-Q., Meller R., Simon R.P.
    Ann. Neurol. 55:485-494(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE SUBCELLULAR LOCATION.
  9. "Mapping a dynamic innate immunity protein interaction network regulating type I interferon production."
    Li S., Wang L., Berman M., Kong Y.Y., Dorf M.E.
    Immunity 35:426-440(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION OF TBK1.
  10. "A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis."
    Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B., Merdes A., Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N., Bekker-Jensen S.
    EMBO J. 32:3029-3040(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF CEP131 AND PCM1, FUNCTION IN CILIOGENESIS, UBIQUITINATION, INTERACTION WITH CEP131 AND PCM1, SUBCELLULAR LOCATION.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: VARIANT HIS-174.
  13. Cited for: VARIANT LVNC7 PHE-943.

Entry informationi

Entry nameiMIB1_HUMAN
AccessioniPrimary (citable) accession number: Q86YT6
Secondary accession number(s): B0YJ38
, Q2TB37, Q68D01, Q6YI51, Q8NBY0, Q8TCB5, Q8TCL7, Q9P2M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In epilepsy brain tissue, levels of expression are increased in the cytoplasm and microsomal fractions (endoplasmic reticulum).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.