A0A7I2V3W3 · A0A7I2V3W3_HUMAN

  • Protein
    ADAM metallopeptidase domain 9
  • Gene
    ADAM9
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site, active site.

1754100200300400500600700
Type
IDPosition(s)Description
Binding site347Zn2+ (UniProtKB | ChEBI); catalytic
Active site348
Binding site351Zn2+ (UniProtKB | ChEBI); catalytic
Binding site357Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processproteolysis

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • ADAM metallopeptidase domain 9

Gene names

    • Name
      ADAM9

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A0A7I2V3W3

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Single-pass type I membrane protein

Keywords

  • Cellular component

Disease & Variants

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue (large scale data).

Type
IDPosition(s)Source
Description
Signal1-28UniProt
ChainPRO_502961344329-754UniProt
Disulfide bond365↔370UniProt
Disulfide bond473↔493UniProt
Modified residue (large scale data)670PRIDEPhosphothreonine
Modified residue (large scale data)671PRIDEPhosphotyrosine
Modified residue (large scale data)687PRIDEPhosphoserine
Modified residue (large scale data)693PRIDEPhosphoserine
Modified residue (large scale data)696PRIDEPhosphothreonine
Modified residue (large scale data)704PRIDEPhosphotyrosine
Modified residue (large scale data)713PRIDEPhosphotyrosine
Modified residue (large scale data)733PRIDEPhosphoserine
Modified residue (large scale data)734PRIDEPhosphoserine
Modified residue (large scale data)750PRIDEPhosphotyrosine
Modified residue (large scale data)754PRIDEPhosphothreonine

Keywords

Proteomic databases

Expression

Gene expression databases

    • ENSG00000168615Expressed in stromal cell of endometrium and 143 other cell types or tissues

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain212-406Peptidase M12B
Domain414-501Disintegrin
Region669-698Disordered
Compositional bias673-689Polar residues
Region714-754Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    754
  • Mass (Da)
    83,431
  • Last updated
    2021-04-07 v1
  • Checksum
    40B7C39728D2282B
MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT

Computationally mapped potential isoform sequences

There are 18 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q13443ADAM9_HUMANADAM9819
C9J6H5C9J6H5_HUMANADAM9128
A0AVL1A0AVL1_HUMANADAM9712
F8WC54F8WC54_HUMANADAM9628
C9JPM3C9JPM3_HUMANADAM9147
A0A0J9YY58A0A0J9YY58_HUMANADAM953
A0A7I2YQ97A0A7I2YQ97_HUMANADAM9707
A0A7I2V2E1A0A7I2V2E1_HUMANADAM9566
A0A7I2V303A0A7I2V303_HUMANADAM9446
A0A7I2V2Z6A0A7I2V2Z6_HUMANADAM9780
A0A7I2V3B5A0A7I2V3B5_HUMANADAM9575
A0A7I2V3C1A0A7I2V3C1_HUMANADAM9533
A0A7I2V3I3A0A7I2V3I3_HUMANADAM969
A0A7I2V4B3A0A7I2V4B3_HUMANADAM9850
A0A7I2V4T8A0A7I2V4T8_HUMANADAM9131
A0A7I2V5C0A0A7I2V5C0_HUMANADAM9214
A0A7I2V5N8A0A7I2V5N8_HUMANADAM9752
A0A7I2V5Q0A0A7I2V5Q0_HUMANADAM9485

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias673-689Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC105091
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC108863
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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