Genular: Defining Cellular Identity and Function

Details for: Adam10

Gene ID: 11487

Symbol: Adam10

Ensembl ID: ENSMUSG00000054693

Description: a disintegrin and metallopeptidase domain 10

Associated with

Degradation of the extracellular matrix
(R-MMU-1474228)
Extracellular matrix organization
(R-MMU-1474244)
Immune system
(R-MMU-168256)
Innate immune system
(R-MMU-168249)
Metabolism of proteins
(R-MMU-392499)
Neutrophil degranulation
(R-MMU-6798695)
Notch3 activation and transmission of signal to the nucleus
(R-MMU-9013507)
Post-translational protein modification
(R-MMU-597592)
Post-translational protein phosphorylation
(R-MMU-8957275)
Regulation of insulin-like growth factor (igf) transport and uptake by insulin-like growth factor binding proteins (igfbps)
(R-MMU-381426)
Signaling by notch
(R-MMU-157118)
Signaling by notch3
(R-MMU-9012852)
Signal transduction
(R-MMU-162582)
Adherens junction organization
(GO:0034332)
Amyloid-beta formation
(GO:0034205)
Amyloid precursor protein catabolic process
(GO:0042987)
Anchoring junction
(GO:0070161)
Cell projection
(GO:0042995)
Cell surface
(GO:0009986)
Cochlea development
(GO:0090102)
Collagen-containing extracellular matrix
(GO:0062023)
Constitutive protein ectodomain proteolysis
(GO:0051089)
Cytoplasm
(GO:0005737)
Cytoplasmic vesicle
(GO:0031410)
Dendrite
(GO:0030425)
Dendritic spine
(GO:0043197)
Endopeptidase activity
(GO:0004175)
Epidermal growth factor receptor ligand maturation
(GO:0038004)
Glutamatergic synapse
(GO:0098978)
Golgi-associated vesicle
(GO:0005798)
Golgi apparatus
(GO:0005794)
Hydrolase activity
(GO:0016787)
Intracellular membrane-bounded organelle
(GO:0043231)
In utero embryonic development
(GO:0001701)
Membrane
(GO:0016020)
Membrane protein ectodomain proteolysis
(GO:0006509)
Metal ion binding
(GO:0046872)
Metallodipeptidase activity
(GO:0070573)
Metalloendopeptidase activity
(GO:0004222)
Metalloendopeptidase activity involved in amyloid precursor protein catabolic process
(GO:1902945)
Metallopeptidase activity
(GO:0008237)
Molecular adaptor activity
(GO:0060090)
Monocyte activation
(GO:0042117)
Negative regulation of cell adhesion
(GO:0007162)
Negative regulation of gene expression
(GO:0010629)
Neuronal cell body
(GO:0043025)
Notch receptor processing
(GO:0007220)
Notch signaling pathway
(GO:0007219)
Nucleocytoplasmic transport
(GO:0006913)
Nucleus
(GO:0005634)
Peptidase activity
(GO:0008233)
Perinuclear endoplasmic reticulum
(GO:0097038)
Plasma membrane
(GO:0005886)
Pore complex
(GO:0046930)
Pore complex assembly
(GO:0046931)
Positive regulation of apoptotic process
(GO:0043065)
Positive regulation of cell growth
(GO:0030307)
Positive regulation of cell migration
(GO:0030335)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of t cell chemotaxis
(GO:0010820)
Postsynapse
(GO:0098794)
Postsynapse organization
(GO:0099173)
Postsynaptic density
(GO:0014069)
Postsynaptic membrane
(GO:0045211)
Protein binding
(GO:0005515)
Protein catabolic process at postsynapse
(GO:0140249)
Protein homodimerization activity
(GO:0042803)
Protein kinase binding
(GO:0019901)
Protein phosphorylation
(GO:0006468)
Protein processing
(GO:0016485)
Proteolysis
(GO:0006508)
Regulation of dendritic spine morphogenesis
(GO:0061001)
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
(GO:0098696)
Regulation of notch signaling pathway
(GO:0008593)
Regulation of postsynapse organization
(GO:0099175)
Regulation of vasculature development
(GO:1901342)
Response to tumor necrosis factor
(GO:0034612)
Sh2 domain binding
(GO:0042169)
Sh3 domain binding
(GO:0017124)
Signaling receptor ligand precursor processing
(GO:0140448)
Synaptic membrane
(GO:0097060)
Synaptic vesicle
(GO:0008021)
Tetraspanin-enriched microdomain
(GO:0097197)
Toxin transport
(GO:1901998)
Trans-golgi network
(GO:0005802)

Other Information

Proteins

Disintegrin and metalloproteinase domain-containing protein 10
Q6NZC0_MOUSE

Genular Protein ID: 508909538

Symbol: ADA10_MOUSE

Name: Disintegrin and metalloproteinase domain-containing protein 10

UniProtKB Accession Codes:

O35598 B8JJJ0

Database IDs:

Citations:

PubMed ID: 9244301

Title: Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis.

PubMed ID: 9244301

DOI: 10.1016/s0092-8674(00)80335-9

PubMed ID: 19468303

Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.

PubMed ID: 19468303

DOI: 10.1371/journal.pbio.1000112

PubMed ID: 16141072

Title: The transcriptional landscape of the mammalian genome.

PubMed ID: 16141072

DOI: 10.1126/science.1112014

PubMed ID: 10958785

Title: Regulated cleavage of a contact-mediated axon repellent.

PubMed ID: 10958785

DOI: 10.1126/science.289.5483.1360

PubMed ID: 17245433

Title: Metalloproteases regulate T-cell proliferation and effector function via LAG-3.

PubMed ID: 17245433

DOI: 10.1038/sj.emboj.7601520

PubMed ID: 19349973

Title: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.

PubMed ID: 19349973

DOI: 10.1038/nbt.1532

PubMed ID: 21183079

Title: A tissue-specific atlas of mouse protein phosphorylation and expression.

PubMed ID: 21183079

DOI: 10.1016/j.cell.2010.12.001

PubMed ID: 23035126

Title: The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression.

PubMed ID: 23035126

DOI: 10.1074/jbc.m112.416503

PubMed ID: 23676497

Title: Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease.

PubMed ID: 23676497

DOI: 10.1172/jci65401

PubMed ID: 26876177

Title: Proteolytic Cleavage Governs Interleukin-11 Trans-signaling.

PubMed ID: 26876177

DOI: 10.1016/j.celrep.2016.01.053

PubMed ID: 26668317

Title: TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: evidence for distinct binding mechanisms for different TspanC8 proteins.

PubMed ID: 26668317

DOI: 10.1074/jbc.m115.703058

PubMed ID: 29397483

Title: Glomerular endothelial cell maturation depends on ADAM10, a key regulator of Notch signaling.

PubMed ID: 29397483

DOI: 10.1007/s10456-018-9599-4

PubMed ID: 30463011

Title: A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to Promote alpha-Toxin Cytotoxicity.

PubMed ID: 30463011

DOI: 10.1016/j.celrep.2018.10.088

PubMed ID: 29430990

Title: The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation.

PubMed ID: 29430990

DOI: 10.1096/fj.201700823rr

PubMed ID: 29325091

Title: alpha-secretase ADAM10 physically interacts with beta-secretase BACE1 in neurons and regulates CHL1 proteolysis.

PubMed ID: 29325091

DOI: 10.1093/jmcb/mjy001

PubMed ID: 30446855

Title: ADAM10 controls the differentiation of the coronary arterial endothelium.

PubMed ID: 30446855

DOI: 10.1007/s10456-018-9653-2

PubMed ID: 30639848

Title: EphA4-ADAM10 Interplay Patterns the Cochlear Sensory Epithelium through Local Disruption of Adherens Junctions.

PubMed ID: 30639848

DOI: 10.1016/j.isci.2018.12.017

Sequence Information:

Length: 749
Mass: 83968
Checksum: 6AA2230B2251ABDA
Sequence:

MVLPTVLILL LSWAAGLGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK RAVSHEDQFL 
LLDFHAHGRQ FNLRMKRDTS LFSDEFKVET SNKVLDYDTS HIYTGHIYGE EGSFSHGSVI 
DGRFEGFIKT RGGTFYIEPA ERYIKDRILP FHSVIYHEDD INYPHKYGPQ GGCADHSVFE 
RMRKYQMTGV EEGARAHPEK HAASSGPELL RKKRTTLAER NTCQLYIQTD HLFFKYYGTR 
EAVIAQISSH VKAIDTIYQT TDFSGIRNIS FMVKRIRINT TSDEKDPTNP FRFPNIGVEK 
FLELNSEQNH DDYCLAYVFT DRDFDDGVLG LAWVGAPSGS SGGICEKSKL YSDGKKKSLN 
TGIITVQNYG SHVPPKVSHI TFAHEVGHNF GSPHDSGTEC TPGESKNLGQ KENGNYIMYA 
RATSGDKLNN NKFSLCSIRN ISQVLEKKRN NCFVESGQPI CGNGMVEQGE ECDCGYSDQC 
KDDCCFDANQ PEGKKCKLKP GKQCSPSQGP CCTAQCAFKS KSEKCRDDSD CAKEGICNGF 
TALCPASDPK PNFTDCNRHT QVCINGQCAG SICEKYDLEE CTCASSDGKD DKELCHVCCM 
KKMAPSTCAS TGSLQWSKQF SGRTITLQPG SPCNDFRGYC DVFMRCRLVD ADGPLARLKK 
AIFSPQLYEN IAEWIVAHWW AVLLMGIALI MLMAGFIKIC SVHTPSSNPK LPPPKPLPGT 
LKRRRPPQPI QQPPRQRPRE SYQMGHMRR

Genular Protein ID: 505564773

Symbol: Q6NZC0_MOUSE

Name: N/A

UniProtKB Accession Codes:

Q6NZC0

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

Sequence Information:

Length: 381
Mass: 43514
Checksum: 99DD307012DB0DB4
Sequence:

MVLPTVLILL LSWAAGLGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK RAVSHEDQFL 
LLDFHAHGRQ FNLRMKRDTS LFSDEFKVET SNKVPDYDTS HIYTGHIYGE EGSFSHGSVI 
DGRFEGFIKT RGGTFYIEPA ERYIKDRILP FHSVIYHEDD INYPHKYGPQ GGCADHSVFE 
RMRKYQMTGV EEGARAHPEK HAASSGPELL RKKRTTLAER NICQLYIQTD HLFFKYYGTR 
EAVIARISSH VKAIDTIYQT TDFSGIRNIS FMVKRIRINT TSDEKDPTNP FRFPNIGVEK 
FLELNSEQNH DDYCLAYVLT DRDFNDGVLG LAWVGAPSGS SGGICEKSKL YSDGKKKSLN 
TGIITVQNYG SHVQKKKKKK K

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Adam10

Associated with

Other Information

Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. PubMed ID: 9244301

Lineage-specific biology revealed by a finished genome assembly of the mouse. PubMed ID: 19468303

The transcriptional landscape of the mammalian genome. PubMed ID: 16141072

Regulated cleavage of a contact-mediated axon repellent. PubMed ID: 10958785

Metalloproteases regulate T-cell proliferation and effector function via LAG-3. PubMed ID: 17245433

Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. PubMed ID: 19349973

A tissue-specific atlas of mouse protein phosphorylation and expression. PubMed ID: 21183079

The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression. PubMed ID: 23035126

Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease. PubMed ID: 23676497

Proteolytic Cleavage Governs Interleukin-11 Trans-signaling. PubMed ID: 26876177

TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: evidence for distinct binding mechanisms for different TspanC8 proteins. PubMed ID: 26668317

Glomerular endothelial cell maturation depends on ADAM10, a key regulator of Notch signaling. PubMed ID: 29397483

A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to Promote alpha-Toxin Cytotoxicity. PubMed ID: 30463011

The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation. PubMed ID: 29430990

alpha-secretase ADAM10 physically interacts with beta-secretase BACE1 in neurons and regulates CHL1 proteolysis. PubMed ID: 29325091

ADAM10 controls the differentiation of the coronary arterial endothelium. PubMed ID: 30446855

EphA4-ADAM10 Interplay Patterns the Cochlear Sensory Epithelium through Local Disruption of Adherens Junctions. PubMed ID: 30639848

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334