ADAM9

Functionⁱ

Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins.By similarity

Isoform 2: May act as alpha-secretase for amyloid precursor protein (APP).1 Publication

Caution

Has sometimes been referred to as ADAM-12.Curated

Cofactorⁱ

Zn²⁺CuratedNote: Binds 1 zinc ion per subunit.Curated

Activity regulationⁱ

Synthesized as an inactive form which is proteolytically cleaved to generate an active enzyme. Processing at the upstream site is particularly important for activation of the proenzyme, whereas processing at the boundary between the pro-domain and the catalytic domain does not appear to be essential. Inhibited by hydroxamic acid-based inhibitors.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	347	Zinc; catalyticBy similarity	1
Active siteⁱ	348	PROSITE-ProRule annotation	1
Metal bindingⁱ	351	Zinc; catalyticBy similarity	1
Metal bindingⁱ	357	Zinc; catalyticBy similarity	1

GO - Molecular functionⁱ

collagen binding
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15361064
integrin binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 15361064
laminin binding
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15361064
metal ion binding Source: UniProtKB-KW
metalloendopeptidase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 9920899
metallopeptidase activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 12535668
protein kinase C binding
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 8647900
SH3 domain binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 10531379

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of MAPKK activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 17704059
cell adhesion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11162558
- 17704059
cell adhesion mediated by integrin
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17704059
cell-cell adhesion mediated by integrin
Source: BHF-UCL
Inferred from expression patternⁱ
- 17704059
cell-matrix adhesion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15361064
cell migration Source: UniProtKB
cellular response to lipopolysaccharide
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 22480688
integrin-mediated signaling pathway
Source: BHF-UCL
Inferred by curatorⁱ
- 11162558
keratinocyte differentiation
Source: BHF-UCL
Inferred from expression patternⁱ
- 17704059
membrane protein ectodomain proteolysis
Source: BHF-UCL
Inferred from direct assayⁱ
- 9920899
monocyte activation
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11831872
PMA-inducible membrane protein ectodomain proteolysis
Source: BHF-UCL
Inferred from direct assayⁱ
- 12054541
positive regulation of cell adhesion mediated by integrin
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11162558
positive regulation of keratinocyte migration
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17704059
positive regulation of macrophage fusion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11831872
positive regulation of membrane protein ectodomain proteolysis
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 8647900
positive regulation of protein secretion
Source: BHF-UCL
Inferred from direct assayⁱ
- 17704059
response to antineoplastic agent Source: Ensembl
response to calcium ion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11162558
response to glucocorticoid
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 8647900
response to hydrogen peroxide
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17018608
response to laminar fluid shear stress Source: Ensembl
response to manganese ion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11162558
response to tumor necrosis factor
Source: BHF-UCL
Inferred from direct assayⁱ
- 11831872
transforming growth factor beta receptor signaling pathway
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11955914

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Metalloprotease, Protease
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	3.4.24.B9 2681
Reactomeⁱ	R-HSA-1442490 Collagen degradation

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	M12.209

MEROPSⁱ

M12.209

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Disintegrin and metalloproteinase domain-containing protein 9 (EC:3.4.24.-) Short name: ADAM 9 Alternative name(s): Cellular disintegrin-related protein Meltrin-gamma Metalloprotease/disintegrin/cysteine-rich protein 9 Myeloma cell metalloproteinase
Gene namesⁱ	Name:ADAM9 Synonyms:KIAA0021, MCMP, MDC9, MLTNG
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 8

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000168615.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:216 ADAM9
MIMⁱ	602713 gene
neXtProtⁱ	NX_Q13443

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	29 – 697	ExtracellularSequence analysisAdd BLAST	669
Transmembraneⁱ	698 – 718	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	719 – 819	CytoplasmicSequence analysisAdd BLAST	101

Keywords - Cellular componentⁱ

Cell membrane, Membrane, Secreted

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Cone-rod dystrophy 9 (CORD9)1 Publication

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

Disease descriptionAn inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors.

Keywords - Diseaseⁱ

Cone-rod dystrophy

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8754
MalaCards human disease database More...MalaCardsⁱ	ADAM9
MIMⁱ	612775 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000168615
Orphanetⁱ	1872 Cone rod dystrophy
PharmGKBⁱ	PA24534

Chemistry databases

ChEMBLⁱ	CHEMBL5982
Drug and drug target database More...DrugBankⁱ	DB05033 INCB7839
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1657

Polymorphism and mutation databases

BioMutaⁱ	ADAM9
DMDMⁱ	24211441

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 28	Sequence analysisAdd BLAST		28
ChainⁱPRO_0000029062	29 – 819	Disintegrin and metalloproteinase domain-containing protein 9Add BLAST		791

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	125	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	144	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	154	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	231	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	322 ↔ 401	By similarity
Disulfide bondⁱ	363 ↔ 385	By similarity
Disulfide bondⁱ	365 ↔ 370	By similarity
Glycosylationⁱ	381	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	473 ↔ 493	By similarity
Glycosylationⁱ	487	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	644 ↔ 656	By similarity
Disulfide bondⁱ	650 ↔ 662	By similarity
Disulfide bondⁱ	664 ↔ 673	By similarity
Modified residueⁱ	758	PhosphoserineCombined sources	1
Modified residueⁱ	761	PhosphothreonineCombined sources	1

Post-translational modificationⁱ

Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9.By similarity

Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA).By similarity

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	56 – 57	CleavageBy similarity		2
Siteⁱ	205 – 206	Cleavage; by furin-like proteaseBy similarity		2

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDⁱ	Q13443
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q13443
PaxDbⁱ	Q13443
PeptideAtlas More...PeptideAtlasⁱ	Q13443
PRIDEⁱ	Q13443
ProteomicsDBⁱ	59440 59441 [Q13443-2]

PTM databases

GlyConnectⁱ	1181
iPTMnetⁱ	Q13443
PhosphoSitePlusⁱ	Q13443

Expressionⁱ

Tissue specificityⁱ

Widely expressed. Expressed in chondrocytes. Isoform 2 is highly expressed in liver and heart.4 Publications

Gene expression databases

Bgeeⁱ	ENSG00000168615 Expressed in 233 organ(s), highest expression level in amniotic fluid
CleanExⁱ	HS_ADAM9
ExpressionAtlasⁱ	Q13443 baseline and differential
Genevisibleⁱ	Q13443 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA004000

HPAⁱ

HPA004000

Interactionⁱ

Subunit structureⁱ

Interacts with SH3GL2 and SNX9 through its cytoplasmic tail (PubMed:10531379). Interacts with ITGA6.By similarity1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
MAD2L2	Q9UI95	3	EBI-77903,EBI-77889
PACSIN3	Q9UKS6	2	EBI-77903,EBI-77926
SH3GL2	Q99962	2	EBI-77903,EBI-77938

GO - Molecular functionⁱ

integrin binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 15361064
laminin binding
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 15361064
protein kinase C binding
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 8647900
SH3 domain binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 10531379

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	114290, 28 interactors
CORUMⁱ	Q13443
IntActⁱ	Q13443, 12 interactors
Molecular INTeraction database More...MINTⁱ	Q13443
STRINGⁱ	9606.ENSP00000419446

Chemistry databases

BindingDBⁱ

Q13443

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q13443
SMRⁱ	Q13443
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	212 – 406	Peptidase M12BPROSITE-ProRule annotationAdd BLAST	195
Domainⁱ	414 – 501	DisintegrinPROSITE-ProRule annotationAdd BLAST	88
Domainⁱ	644 – 698	EGF-likePROSITE-ProRule annotationAdd BLAST	55

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	505 – 634	Cys-richAdd BLAST		130
Compositional biasⁱ	790 – 795	Poly-Pro		6

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3607 Eukaryota ENOG410XX2M LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144019
HOGENOMⁱ	HOG000230883
HOVERGENⁱ	HBG006978
InParanoidⁱ	Q13443
KEGG Orthology (KO) More...KOⁱ	K06834
OMAⁱ	FYRMDDV
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G01NX
PhylomeDBⁱ	Q13443
TreeFamⁱ	TF314733

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd04269 ZnMc_adamalysin_II_like, 1 hit
Gene3Dⁱ	3.40.390.10, 1 hit 4.10.70.10, 1 hit
InterProⁱ	View protein in InterPro IPR006586 ADAM_Cys-rich IPR018358 Disintegrin_CS IPR001762 Disintegrin_dom IPR036436 Disintegrin_dom_sf IPR013032 EGF-like_CS IPR000742 EGF-like_dom IPR024079 MetalloPept_cat_dom_sf IPR001590 Peptidase_M12B IPR002870 Peptidase_M12B_N IPR034027 Reprolysin_adamalysin
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08516 ADAM_CR, 1 hit PF00200 Disintegrin, 1 hit PF01562 Pep_M12B_propep, 1 hit PF01421 Reprolysin, 1 hit
SMARTⁱ	View protein in SMART SM00608 ACR, 1 hit SM00050 DISIN, 1 hit
SUPFAMⁱ	SSF57552 SSF57552, 1 hit
PROSITEⁱ	View protein in PROSITE PS50215 ADAM_MEPRO, 1 hit PS00427 DISINTEGRIN_1, 1 hit PS50214 DISINTEGRIN_2, 1 hit PS01186 EGF_2, 1 hit PS50026 EGF_3, 1 hit PS00142 ZINC_PROTEASE, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q13443-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR 
        60         70         80         90        100
LTRERREAPR PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE 
       110        120        130        140        150
GTLITDHPNI QNHCHYRGYV EGVHNSSIAL SDCFGLRGLL HLENASYGIE 
       160        170        180        190        200
PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK DIEKETAKDE EEEPPSMTQL 
       210        220        230        240        250
LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI LLANYLDSMY 
       260        270        280        290        300
IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS 
       310        320        330        340        350
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG 
       360        370        380        390        400
HNLGMNHDDG RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN 
       410        420        430        440        450
CLLNIPKPDE AYSAPSCGNK LVDAGEECDC GTPKECELDP CCEGSTCKLK 
       460        470        480        490        500
SFAECAYGDC CKDCRFLPGG TLCRGKTSEC DVPEYCNGSS QFCQPDVFIQ 
       510        520        530        540        550
NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF IEVNSKGDRF 
       560        570        580        590        600
GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC 
       610        620        630        640        650
WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC 
       660        670        680        690        700
HGHGVCNSNK NCHCENGWAP PNCETKGYGG SVDSGPTYNE MNTALRDGLL 
       710        720        730        740        750
VFFFLIVPLI VCAIFIFIKR DQLWRSYFRK KRSQTYESDG KNQANPSRQP 
       760        770        780        790        800
GSVPRHVSPV TPPREVPIYA NRFAVPTYAA KQPQQFPSRP PPPQPKVSSQ 
       810 
GNLIPARPAP APPLYSSLT

Length:819

Mass (Da):90,556

Last modified:November 1, 1996 - v1

Checksum:ⁱBC186641833137FF

GO

Isoform 2 (identifier: Q13443-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
655-655: V → K
656-819: Missing.

« Hide

        10         20         30         40         50
MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR 
        60         70         80         90        100
LTRERREAPR PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE 
       110        120        130        140        150
GTLITDHPNI QNHCHYRGYV EGVHNSSIAL SDCFGLRGLL HLENASYGIE 
       160        170        180        190        200
PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK DIEKETAKDE EEEPPSMTQL 
       210        220        230        240        250
LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI LLANYLDSMY 
       260        270        280        290        300
IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS 
       310        320        330        340        350
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG 
       360        370        380        390        400
HNLGMNHDDG RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN 
       410        420        430        440        450
CLLNIPKPDE AYSAPSCGNK LVDAGEECDC GTPKECELDP CCEGSTCKLK 
       460        470        480        490        500
SFAECAYGDC CKDCRFLPGG TLCRGKTSEC DVPEYCNGSS QFCQPDVFIQ 
       510        520        530        540        550
NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF IEVNSKGDRF 
       560        570        580        590        600
GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC 
       610        620        630        640        650
WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC 

HGHGK

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »

Length:655

Mass (Da):72,359

Checksum:ⁱ1E99DD3A056B90B7

GO

Computationally mapped potential isoform sequencesⁱ

There are 5 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0AVL1	A0AVL1_HUMAN	ADAM9 protein ADAM9 protein (Disintegrin and metalloproteinase domain-containing protein 9)	ADAM9	712	Annotation score:
F8WC54	F8WC54_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 9	ADAM9	628	Annotation score:
C9JPM3	C9JPM3_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 9	ADAM9	147	Annotation score:
C9J6H5	C9J6H5_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 9	ADAM9	128	Annotation score:
A0A0J9YY58	A0A0J9YY58_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 9	ADAM9	53	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	1 – 118	Missing no nucleotide entry (PubMed:8809033).CuratedAdd BLAST	118
Sequence conflictⁱ	117	R → Q in BAA03499 (PubMed:7584026).Curated	1
Sequence conflictⁱ	119 – 135	YVEGV…SDCFG → MWREFIIHPLLLATVLD no nucleotide entry (PubMed:8809033).CuratedAdd BLAST	17
Sequence conflictⁱ	154	N → M no nucleotide entry (PubMed:8809033).Curated	1
Sequence conflictⁱ	566	G → GLSLKFHAPFLSTMLQEAVR QTGTYLGGSVCCMKSDCRIV TLVK no nucleotide entry (PubMed:8809033).Curated	1
Sequence conflictⁱ	713 – 735	AIFIF…KRSQT → DYFYLHQEGSTVEKLLQKEE ITN no nucleotide entry (PubMed:8809033).CuratedAdd BLAST	23
Sequence conflictⁱ	736 – 819	Missing no nucleotide entry (PubMed:8809033).CuratedAdd BLAST	84

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_011057	655	V → K in isoform 2. 2 Publications		1
Alternative sequenceⁱVSP_011058	656 – 819	Missing in isoform 2. 2 PublicationsAdd BLAST		164

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U41766 mRNA Translation: AAC50403.1 AF495383 mRNA Translation: AAM49575.1 D14665 mRNA Translation: BAA03499.2 CH471080 Genomic DNA Translation: EAW63284.1 BC143923 mRNA Translation: AAI43924.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6112.1 [Q13443-1]
PIRⁱ	JC7850 S71949
NCBI Reference Sequences More...RefSeqⁱ	NP_003807.1, NM_003816.2 [Q13443-1]
UniGeneⁱ	Hs.591852

Genome annotation databases

Ensemblⁱ	ENST00000379917; ENSP00000369249; ENSG00000168615 [Q13443-2] ENST00000487273; ENSP00000419446; ENSG00000168615 [Q13443-1]
GeneIDⁱ	8754
KEGGⁱ	hsa:8754
UCSC genome browser More...UCSCⁱ	uc003xmr.4 human [Q13443-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q13443	Uncharacterized protein		MACMU		821	UniRef90_Q13443
Uncharacterized protein		MACFA		821
Uncharacterized protein		AOTNA		820
ADAM metallopeptidase domain 9		CALJA		819
ADAM metallopeptidase domain 9		PANTR		819
+45
Q13443-2	ADAM metallopeptidase domain 9		MUSPF		785	UniRef90_Q13443-2
ADAM9 isoform 1		PONAB		655
ADAM9 isoform 1		PANTR		655
Disintegrin and metalloproteinase domain-containing protein 9		HUMAN		628
UPI00094003C6		great roundleaf bat		667
+6

Protein	Similar proteins		Species	Score	Length	Source
Q13443	Disintegrin and metalloproteinase domain-containing protein 9		MOUSE		845	UniRef50_Q13443
Uncharacterized protein		MACMU		821
Uncharacterized protein		MACFA		821
Uncharacterized protein		AOTNA		820
Uncharacterized protein		RHIBE		819
+180
Q13443-2	ADAM metallopeptidase domain 9		MUSPF		785	UniRef50_Q13443-2
ADAM9 isoform 1		PONAB		655
ADAM9 isoform 1		PANTR		655
Disintegrin and metalloproteinase domain-containing protein 9		HUMAN		628
Disintegrin and metalloproteinase domain-containing protein 9		HETGA		941
+26

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U41766 mRNA Translation: AAC50403.1 AF495383 mRNA Translation: AAM49575.1 D14665 mRNA Translation: BAA03499.2 CH471080 Genomic DNA Translation: EAW63284.1 BC143923 mRNA Translation: AAI43924.1
CCDSⁱ	CCDS6112.1 [Q13443-1]
PIRⁱ	JC7850 S71949
RefSeqⁱ	NP_003807.1, NM_003816.2 [Q13443-1]
UniGeneⁱ	Hs.591852

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1M1V	model	-	A	208-404	[»]
ProteinModelPortalⁱ	Q13443
SMRⁱ	Q13443
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114290, 28 interactors
CORUMⁱ	Q13443
IntActⁱ	Q13443, 12 interactors
MINTⁱ	Q13443
STRINGⁱ	9606.ENSP00000419446

Chemistry databases

BindingDBⁱ	Q13443
ChEMBLⁱ	CHEMBL5982
DrugBankⁱ	DB05033 INCB7839
GuidetoPHARMACOLOGYⁱ	1657

Protein family/group databases

MEROPSⁱ	M12.209

MEROPSⁱ

M12.209

PTM databases

GlyConnectⁱ	1181
iPTMnetⁱ	Q13443
PhosphoSitePlusⁱ	Q13443

Polymorphism and mutation databases

BioMutaⁱ	ADAM9
DMDMⁱ	24211441

Proteomic databases

EPDⁱ	Q13443
MaxQBⁱ	Q13443
PaxDbⁱ	Q13443
PeptideAtlasⁱ	Q13443
PRIDEⁱ	Q13443
ProteomicsDBⁱ	59440 59441 [Q13443-2]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000379917; ENSP00000369249; ENSG00000168615 [Q13443-2] ENST00000487273; ENSP00000419446; ENSG00000168615 [Q13443-1]
GeneIDⁱ	8754
KEGGⁱ	hsa:8754
UCSCⁱ	uc003xmr.4 human [Q13443-1]

Organism-specific databases

CTDⁱ	8754
DisGeNETⁱ	8754
EuPathDBⁱ	HostDB:ENSG00000168615.11
GeneCardsⁱ	ADAM9
HGNCⁱ	HGNC:216 ADAM9
HPAⁱ	HPA004000
MalaCardsⁱ	ADAM9
MIMⁱ	602713 gene 612775 phenotype
neXtProtⁱ	NX_Q13443
OpenTargetsⁱ	ENSG00000168615
Orphanetⁱ	1872 Cone rod dystrophy
PharmGKBⁱ	PA24534
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3607 Eukaryota ENOG410XX2M LUCA
GeneTreeⁱ	ENSGT00910000144019
HOGENOMⁱ	HOG000230883
HOVERGENⁱ	HBG006978
InParanoidⁱ	Q13443
KOⁱ	K06834
OMAⁱ	FYRMDDV
OrthoDBⁱ	EOG091G01NX
PhylomeDBⁱ	Q13443
TreeFamⁱ	TF314733

Enzyme and pathway databases

BRENDAⁱ	3.4.24.B9 2681
Reactomeⁱ	R-HSA-1442490 Collagen degradation

Miscellaneous databases

ChiTaRSⁱ	ADAM9 human
GeneWikiⁱ	ADAM9
GenomeRNAiⁱ	8754
Protein Ontology More...PROⁱ	PR:Q13443
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000168615 Expressed in 233 organ(s), highest expression level in amniotic fluid
CleanExⁱ	HS_ADAM9
ExpressionAtlasⁱ	Q13443 baseline and differential
Genevisibleⁱ	Q13443 HS

Family and domain databases

CDDⁱ	cd04269 ZnMc_adamalysin_II_like, 1 hit
Gene3Dⁱ	3.40.390.10, 1 hit 4.10.70.10, 1 hit
InterProⁱ	View protein in InterPro IPR006586 ADAM_Cys-rich IPR018358 Disintegrin_CS IPR001762 Disintegrin_dom IPR036436 Disintegrin_dom_sf IPR013032 EGF-like_CS IPR000742 EGF-like_dom IPR024079 MetalloPept_cat_dom_sf IPR001590 Peptidase_M12B IPR002870 Peptidase_M12B_N IPR034027 Reprolysin_adamalysin
Pfamⁱ	View protein in Pfam PF08516 ADAM_CR, 1 hit PF00200 Disintegrin, 1 hit PF01562 Pep_M12B_propep, 1 hit PF01421 Reprolysin, 1 hit
SMARTⁱ	View protein in SMART SM00608 ACR, 1 hit SM00050 DISIN, 1 hit
SUPFAMⁱ	SSF57552 SSF57552, 1 hit
PROSITEⁱ	View protein in PROSITE PS50215 ADAM_MEPRO, 1 hit PS00427 DISINTEGRIN_1, 1 hit PS50214 DISINTEGRIN_2, 1 hit PS01186 EGF_2, 1 hit PS50026 EGF_3, 1 hit PS00142 ZINC_PROTEASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ADAM9_HUMAN
Accessionⁱ	Q13443Primary (citable) accession number: Q13443 Secondary accession number(s): B7ZLN7, Q10718, Q8NFM6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
	Last sequence update:	November 1, 1996
	Last modified:	November 7, 2018
	This is version 190 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q13443 (ADAM9_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Disintegrin and metalloproteinase domain-containing protein 9

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Extracellular region or secreted

Extracellular region or secreted

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Compositional bias

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ