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Q13443

- ADAM9_HUMAN

UniProt

Q13443 - ADAM9_HUMAN

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Protein

Disintegrin and metalloproteinase domain-containing protein 9

Gene

ADAM9

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

Functioni

Probable zinc protease. May mediate cell-cell or cell-matrix interactions. Isoform 2 displays alpha-secretase activity for APP.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi347 – 3471Zinc; catalyticBy similarity
Active sitei348 – 3481PROSITE-ProRule annotation
Metal bindingi351 – 3511Zinc; catalyticBy similarity
Metal bindingi357 – 3571Zinc; catalyticBy similarity

GO - Molecular functioni

  1. collagen binding Source: BHF-UCL
  2. integrin binding Source: BHF-UCL
  3. laminin binding Source: BHF-UCL
  4. metalloendopeptidase activity Source: BHF-UCL
  5. metallopeptidase activity Source: BHF-UCL
  6. protein kinase C binding Source: BHF-UCL
  7. SH3 domain binding Source: BHF-UCL
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of MAPKK activity Source: BHF-UCL
  2. cell adhesion Source: BHF-UCL
  3. cell adhesion mediated by integrin Source: BHF-UCL
  4. cell-cell adhesion mediated by integrin Source: BHF-UCL
  5. cell-matrix adhesion Source: BHF-UCL
  6. cellular response to lipopolysaccharide Source: BHF-UCL
  7. collagen catabolic process Source: Reactome
  8. extracellular matrix disassembly Source: Reactome
  9. extracellular matrix organization Source: Reactome
  10. integrin-mediated signaling pathway Source: BHF-UCL
  11. keratinocyte differentiation Source: BHF-UCL
  12. membrane protein ectodomain proteolysis Source: BHF-UCL
  13. monocyte activation Source: BHF-UCL
  14. PMA-inducible membrane protein ectodomain proteolysis Source: BHF-UCL
  15. positive regulation of cell adhesion mediated by integrin Source: BHF-UCL
  16. positive regulation of keratinocyte migration Source: BHF-UCL
  17. positive regulation of macrophage fusion Source: BHF-UCL
  18. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  19. positive regulation of protein secretion Source: BHF-UCL
  20. response to calcium ion Source: BHF-UCL
  21. response to glucocorticoid Source: BHF-UCL
  22. response to hydrogen peroxide Source: BHF-UCL
  23. response to laminar fluid shear stress Source: Ensembl
  24. response to manganese ion Source: BHF-UCL
  25. response to tumor necrosis factor Source: BHF-UCL
  26. transforming growth factor beta receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM12.209.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:216. ADAM9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 697669ExtracellularSequence AnalysisAdd
BLAST
Transmembranei698 – 71821HelicalSequence AnalysisAdd
BLAST
Topological domaini719 – 819101CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. cell surface Source: BHF-UCL
  3. cytoplasm Source: Ensembl
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. integral component of membrane Source: UniProtKB-KW
  8. intrinsic component of external side of plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Cone-rod dystrophy 9 (CORD9) [MIM:612775]: An 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Cone-rod dystrophy

Organism-specific databases

MIMi612775. phenotype.
Orphaneti1872. Cone rod dystrophy.
PharmGKBiPA24534.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 819791Disintegrin and metalloproteinase domain-containing protein 9PRO_0000029062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi322 ↔ 401By similarity
Disulfide bondi363 ↔ 385By similarity
Disulfide bondi365 ↔ 370By similarity
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi473 ↔ 493By similarity
Glycosylationi487 – 4871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi644 ↔ 656By similarity
Disulfide bondi650 ↔ 662By similarity
Disulfide bondi664 ↔ 673By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ13443.
PaxDbiQ13443.
PRIDEiQ13443.

PTM databases

PhosphoSiteiQ13443.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ13443.
CleanExiHS_ADAM9.
ExpressionAtlasiQ13443. baseline and differential.
GenevestigatoriQ13443.

Organism-specific databases

HPAiHPA004000.

Interactioni

Subunit structurei

Interacts with SH3GL2 and SNX9 through its cytoplasmic tail.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAD2L2Q9UI953EBI-77903,EBI-77889
PACSIN3Q9UKS62EBI-77903,EBI-77926
SH3GL2Q999622EBI-77903,EBI-77938

Protein-protein interaction databases

BioGridi114290. 13 interactions.
IntActiQ13443. 3 interactions.
MINTiMINT-108373.
STRINGi9606.ENSP00000305538.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M1Vmodel-A208-404[»]
ProteinModelPortaliQ13443.
SMRiQ13443. Positions 212-638.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini212 – 406195Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini414 – 50188DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini644 – 69855EGF-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi505 – 634130Cys-richAdd
BLAST
Compositional biasi790 – 7956Poly-Pro

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG294463.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ13443.
KOiK06834.
OMAiFCQPDVF.
OrthoDBiEOG7F7W89.
PhylomeDBiQ13443.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. 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.
[Graphical view]

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

Isoform 1 (identifier: Q13443-1) [UniParc]FASTAAdd 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]FASTAAdd to Basket

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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 118118Missing no nucleotide entry (PubMed:8809033)CuratedAdd
BLAST
Sequence conflicti117 – 1171R → Q in BAA03499. (PubMed:7584026)Curated
Sequence conflicti119 – 13517YVEGV…SDCFG → MWREFIIHPLLLATVLD no nucleotide entry (PubMed:8809033)CuratedAdd
BLAST
Sequence conflicti154 – 1541N → M no nucleotide entry (PubMed:8809033)Curated
Sequence conflicti566 – 5661G → GLSLKFHAPFLSTMLQEAVR QTGTYLGGSVCCMKSDCRIV TLVK no nucleotide entry (PubMed:8809033)Curated
Sequence conflicti713 – 73523AIFIF…KRSQT → DYFYLHQEGSTVEKLLQKEE ITN no nucleotide entry (PubMed:8809033)CuratedAdd
BLAST
Sequence conflicti736 – 81984Missing no nucleotide entry (PubMed:8809033)CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei655 – 6551V → K in isoform 2. 2 PublicationsVSP_011057
Alternative sequencei656 – 819164Missing in isoform 2. 2 PublicationsVSP_011058Add
BLAST

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.
CCDSiCCDS6112.1. [Q13443-1]
PIRiJC7850.
S71949.
RefSeqiNP_003807.1. NM_003816.2. [Q13443-1]
UniGeneiHs.591852.

Genome annotation databases

EnsembliENST00000379917; ENSP00000369249; ENSG00000168615. [Q13443-2]
ENST00000487273; ENSP00000419446; ENSG00000168615. [Q13443-1]
GeneIDi8754.
KEGGihsa:8754.
UCSCiuc003xmr.3. human. [Q13443-1]

Polymorphism databases

DMDMi24211441.

Keywords - Coding sequence diversityi

Alternative splicing

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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M1V model - A 208-404 [» ]
ProteinModelPortali Q13443.
SMRi Q13443. Positions 212-638.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114290. 13 interactions.
IntActi Q13443. 3 interactions.
MINTi MINT-108373.
STRINGi 9606.ENSP00000305538.

Chemistry

BindingDBi Q13443.
ChEMBLi CHEMBL5982.

Protein family/group databases

MEROPSi M12.209.

PTM databases

PhosphoSitei Q13443.

Polymorphism databases

DMDMi 24211441.

Proteomic databases

MaxQBi Q13443.
PaxDbi Q13443.
PRIDEi Q13443.

Protocols and materials databases

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.3. human. [Q13443-1 ]

Organism-specific databases

CTDi 8754.
GeneCardsi GC08P038871.
HGNCi HGNC:216. ADAM9.
HPAi HPA004000.
MIMi 602713. gene.
612775. phenotype.
neXtProti NX_Q13443.
Orphaneti 1872. Cone rod dystrophy.
PharmGKBi PA24534.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG294463.
GeneTreei ENSGT00760000118888.
HOGENOMi HOG000230883.
HOVERGENi HBG006978.
InParanoidi Q13443.
KOi K06834.
OMAi FCQPDVF.
OrthoDBi EOG7F7W89.
PhylomeDBi Q13443.
TreeFami TF314733.

Enzyme and pathway databases

Reactomei REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi ADAM9. human.
GeneWikii ADAM9.
GenomeRNAii 8754.
NextBioi 32845.
PROi Q13443.
SOURCEi Search...

Gene expression databases

Bgeei Q13443.
CleanExi HS_ADAM9.
ExpressionAtlasi Q13443. baseline and differential.
Genevestigatori Q13443.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProi IPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view ]
Pfami PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view ]
SMARTi SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF57552. SSF57552. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains."
    Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P.
    J. Cell Biol. 132:717-726(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Mammary carcinoma.
  2. "Cloning of a novel membrane-linked metalloproteinase from human myeloma cells."
    McKie N., Dallas D.J., Edwards T., Apperley J.F., Russell R.G.G., Croucher P.I.
    Biochem. J. 318:459-462(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "A secreted form of human ADAM9 has an alpha-secretase activity for APP."
    Hotoda N., Koike H., Sasagawa N., Ishiura S.
    Biochem. Biophys. Res. Commun. 293:800-805(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Bone marrow.
  5. Ohara O., Nagase T., Kikuno R., Nomura N.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 2).
    Tissue: Lung.
  8. "Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes."
    McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R., Russell G., Croucher P.I.
    Biochem. Biophys. Res. Commun. 230:335-339(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
    Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
    J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3GL2 AND SNX9.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: INVOLVEMENT IN CORD9.
  12. "Exploring the substrate affinities of MMP-3, ADAM-9 and ADAM-10 using molecular modelling and dynamics simulations."
    Manzetti S., McCulloch D.R., Herington A.C.
    Submitted (JUN-2002) to the PDB data bank
    Cited for: 3D-STRUCTURE MODELING OF 208-404.

Entry informationi

Entry nameiADAM9_HUMAN
AccessioniPrimary (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 26, 2014
This is version 155 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3