Q96AX9 · MIB2_HUMAN
- ProteinE3 ubiquitin-protein ligase MIB2
- GeneMIB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids955 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 91 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 94 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 106 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 109 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 115 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 118 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 124 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | early endosome | |
Cellular Component | plasma membrane | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | actin binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | Notch signaling pathway | |
Biological Process | positive regulation of canonical NF-kappaB signal transduction | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of tumor necrosis factor-mediated signaling pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase MIB2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96AX9
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,438 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | In isoform Q96AX9-8; N-acetylmethionine | ||||
Sequence: M | |||||||
Modified residue | 1 | UniProt | In isoform Q96AX9-10; N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000055947 | 1-955 | UniProt | E3 ubiquitin-protein ligase MIB2 | |||
Sequence: MDPDPQAGVQVGMRVVRGVDWKWGQQDGGEGGVGTVVELGRHGSPSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYDNAQIGVRHPNIICDCCKKHGLRGMRWKCRVCLDYDLCTQCYMHNKHELAHAFDRYETAHSRPVTLSPRQGLPRIPLRGIFQGAKVVRGPDWEWGSQDGGEGKPGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLKCVGEAAGGFYYKDHLPRLGKPAELQRRVSADSQPFQHGDKVKCLLDTDVLREMQEGHGGWNPRMAEFIGQTGTVHRITDRGDVRVQFNHETRWTFHPGALTKHHSFWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAVAGQRWTFSPSCLVAYRPEEDANLDVAERARENKSSLSVALDKLRAQKSDPEHPGRLVVEVALGNAARALDLLRRRPEQVDTKNQGRTALQVAAYLGQVELIRLLLQARAGVDLPDDEGNTALHYAALGNQPEATRVLLSAGCRADAINSTQSTALHVAVQRGFLEVVRALCERGCDVNLPDAHSDTPLHSAISAGTGASGIVEVLTEVPNIDVTATNSQGFTLLHHASLKGHALAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQILIREGRCDVNVRNRKLQSPLHLAVQQAHVGLVPLLVDAGCSVNAEDEEGDTALHVALQRHQLLPLVADGAGGDPGPLQLLSRLQASGLPGSAELTVGAAVACFLALEGADVSYTNHRGRSPLDLAAEGRVLKALQGCAQRFRERQAGGGAAPGPRQTLGTPNTVTNLHVGAAPGPEAAECLVCSELALLVLFSPCQHRTVCEECARRMKKCIRCQVVVSKKLRPDGSEVASAAPAPGPPRQLVEELQSRYRQMEERITCPICIDSHIRLVFQCGHGACAPCGSALSACPICRQPIRDRIQIFV | |||||||
Modified residue | 251 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitinated. Possibly via autoubiquitination (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in skeletal muscle, and to a lesser extent in heart, brain and kidney.
Induction
Down-regulated in many primary skin melanomas. Treatment with a demethylating agent, 5'-aza-2-deoxycytidine, restores expression, suggesting that down-regulation is the result of methylation of the gene.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with actin monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96AX9 | TBK1 Q9UHD2 | 2 | EBI-2130249, EBI-356402 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, zinc finger, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-80 | MIB/HERC2 1 | ||||
Sequence: MDPDPQAGVQVGMRVVRGVDWKWGQQDGGEGGVGTVVELGRHGSPSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYDNA | ||||||
Zinc finger | 86-138 | ZZ-type | ||||
Sequence: HPNIICDCCKKHGLRGMRWKCRVCLDYDLCTQCYMHNKHELAHAFDRYETAHS | ||||||
Domain | 149-227 | MIB/HERC2 2 | ||||
Sequence: LPRIPLRGIFQGAKVVRGPDWEWGSQDGGEGKPGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLKCVGEA | ||||||
Repeat | 464-493 | ANK 1 | ||||
Sequence: QGRTALQVAAYLGQVELIRLLLQARAGVDL | ||||||
Repeat | 497-526 | ANK 2 | ||||
Sequence: EGNTALHYAALGNQPEATRVLLSAGCRADA | ||||||
Repeat | 530-559 | ANK 3 | ||||
Sequence: TQSTALHVAVQRGFLEVVRALCERGCDVNL | ||||||
Repeat | 563-595 | ANK 4 | ||||
Sequence: HSDTPLHSAISAGTGASGIVEVLTEVPNIDVTA | ||||||
Repeat | 599-628 | ANK 5 | ||||
Sequence: QGFTLLHHASLKGHALAVRKILARARQLVD | ||||||
Repeat | 633-663 | ANK 6 | ||||
Sequence: DGFTALHLAALNNHREVAQILIREGRCDVNV | ||||||
Repeat | 667-696 | ANK 7 | ||||
Sequence: KLQSPLHLAVQQAHVGLVPLLVDAGCSVNA | ||||||
Repeat | 700-728 | ANK 8 | ||||
Sequence: EGDTALHVALQRHQLLPLVADGAGGDPGP | ||||||
Repeat | 769-798 | ANK 9 | ||||
Sequence: RGRSPLDLAAEGRVLKALQGCAQRFRERQA | ||||||
Zinc finger | 832-867 | RING-type 1 | ||||
Sequence: CLVCSELALLVLFSPCQHRTVCEECARRMKKCIRCQ | ||||||
Zinc finger | 911-944 | RING-type 2 | ||||
Sequence: CPICIDSHIRLVFQCGHGACAPCGSALSACPICR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 9 isoforms produced by Alternative splicing.
Q96AX9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length955
- Mass (Da)103,658
- Last updated2022-02-23 v4
- Checksum899DCCBC60605F8B
Q96AX9-3
- Name3
- SynonymsGamma
- Differences from canonical
- 289-292: Missing
Q96AX9-4
- Name4
- SynonymsBeta
- Differences from canonical
- 176-240: Missing
Q96AX9-5
- Name5
- Differences from canonical
- 325-359: Missing
Q96AX9-10
- Name10
Q96AX9-7
- Name7
- Differences from canonical
- 1-101: Missing
Q96AX9-8
- Name8
Q96AX9-9
- Name9
- Differences from canonical
- 615-955: Missing
Q96AX9-6
- Name6
- Differences from canonical
- 289-324: Missing
Computationally mapped potential isoform sequences
There are 14 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8C8N694 | A0A8C8N694_HUMAN | MIB2 | 890 | ||
D6RFJ2 | D6RFJ2_HUMAN | MIB2 | 148 | ||
D6RED3 | D6RED3_HUMAN | MIB2 | 395 | ||
D6RE96 | D6RE96_HUMAN | MIB2 | 175 | ||
D6RHY5 | D6RHY5_HUMAN | MIB2 | 128 | ||
D6RAZ0 | D6RAZ0_HUMAN | MIB2 | 816 | ||
D6RDI1 | D6RDI1_HUMAN | MIB2 | 114 | ||
H0YAM8 | H0YAM8_HUMAN | MIB2 | 829 | ||
D6R9Q6 | D6R9Q6_HUMAN | MIB2 | 84 | ||
E9PD12 | E9PD12_HUMAN | MIB2 | 955 | ||
A0A8C8USR6 | A0A8C8USR6_HUMAN | MIB2 | 951 | ||
J3QLE0 | J3QLE0_HUMAN | MIB2 | 57 | ||
J3QR95 | J3QR95_HUMAN | MIB2 | 332 | ||
F2Z2L2 | F2Z2L2_HUMAN | MIB2 | 919 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035508 | 1-101 | in isoform 7 | |||
Sequence: Missing | ||||||
Sequence conflict | 22 | in Ref. 6; AAH16490 | ||||
Sequence: K → N | ||||||
Sequence conflict | 168 | in Ref. 3; BAC77353 | ||||
Sequence: D → F | ||||||
Alternative sequence | VSP_014393 | 176-240 | in isoform 4 and isoform 10 | |||
Sequence: Missing | ||||||
Sequence conflict | 177 | in Ref. 4; BAG63969 | ||||
Sequence: G → R | ||||||
Sequence conflict | 215 | in Ref. 6; AAH37542 | ||||
Sequence: H → Y | ||||||
Alternative sequence | VSP_014395 | 289-292 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_014394 | 289-324 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 317 | in Ref. 4; BAC04646 | ||||
Sequence: F → L | ||||||
Alternative sequence | VSP_014396 | 325-359 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 450 | in Ref. 6; AAH37542 | ||||
Sequence: D → G | ||||||
Sequence conflict | 579 | in Ref. 6; AAH37542 | ||||
Sequence: S → G | ||||||
Alternative sequence | VSP_035510 | 615-955 | in isoform 9 | |||
Sequence: Missing | ||||||
Sequence conflict | 631 | in Ref. 4; BAC04752 | ||||
Sequence: K → E | ||||||
Sequence conflict | 634 | in Ref. 4; BAG53705 | ||||
Sequence: G → D | ||||||
Alternative sequence | VSP_045186 | 795-955 | in isoform 10 | |||
Sequence: ERQAGGGAAPGPRQTLGTPNTVTNLHVGAAPGPEAAECLVCSELALLVLFSPCQHRTVCEECARRMKKCIRCQVVVSKKLRPDGSEVASAAPAPGPPRQLVEELQSRYRQMEERITCPICIDSHIRLVFQCGHGACAPCGSALSACPICRQPIRDRIQIFV → VRAQDEEVHQVPGGRQQETAPRRL | ||||||
Alternative sequence | VSP_035511 | 800-802 | in isoform 8 | |||
Sequence: GGA → RGR | ||||||
Alternative sequence | VSP_035512 | 803-955 | in isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 879 | in Ref. 4; BAC04646 | ||||
Sequence: S → F | ||||||
Sequence conflict | 917 | in Ref. 3; BAC77353 | ||||
Sequence: S → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB074480 EMBL· GenBank· DDBJ | BAB92950.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB064367 EMBL· GenBank· DDBJ | BAB82979.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AB076691 EMBL· GenBank· DDBJ | BAC00992.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB076692 EMBL· GenBank· DDBJ | BAC00993.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB076693 EMBL· GenBank· DDBJ | BAC00994.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB097000 EMBL· GenBank· DDBJ | BAC77353.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK091610 EMBL· GenBank· DDBJ | BAC03707.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK095914 EMBL· GenBank· DDBJ | BAC04646.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK096295 EMBL· GenBank· DDBJ | BAC04752.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK097106 EMBL· GenBank· DDBJ | BAC04952.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK098785 EMBL· GenBank· DDBJ | BAC05413.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122751 EMBL· GenBank· DDBJ | BAG53705.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122863 EMBL· GenBank· DDBJ | BAG53766.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK128167 EMBL· GenBank· DDBJ | BAG54643.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302757 EMBL· GenBank· DDBJ | BAG63969.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL691432 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC016490 EMBL· GenBank· DDBJ | AAH16490.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC037542 EMBL· GenBank· DDBJ | AAH37542.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL834527 EMBL· GenBank· DDBJ | CAD39183.1 EMBL· GenBank· DDBJ | mRNA |