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Q13444

- ADA15_HUMAN

UniProt

Q13444 - ADA15_HUMAN

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Protein

Disintegrin and metalloproteinase domain-containing protein 15

Gene

ADAM15

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

Functioni

Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.7 Publications

Cofactori

Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by hydroxamate-type metalloproteinase inhibitors such as marimastat. Inhibited by metalloproteinase inhibitor 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not significantly inhibited by TIMP-1 at concentrations of up to 100 nM. Not activated by PMA or ionomycin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi179 – 1791Zinc; in inhibited formBy similarity
Metal bindingi348 – 3481Zinc; catalyticBy similarity
Active sitei349 – 3491PROSITE-ProRule annotation
Metal bindingi352 – 3521Zinc; catalyticBy similarity
Metal bindingi358 – 3581Zinc; catalyticBy similarity

GO - Molecular functioni

  1. integrin binding Source: UniProtKB
  2. metalloendopeptidase activity Source: InterPro
  3. metallopeptidase activity Source: BHF-UCL
  4. SH3 domain binding Source: BHF-UCL
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cardiac epithelial to mesenchymal transition Source: Ensembl
  3. cell-matrix adhesion Source: ProtInc
  4. collagen catabolic process Source: UniProtKB-KW
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. innate immune response Source: UniProtKB
  8. integrin-mediated signaling pathway Source: UniProtKB
  9. negative regulation of cell growth Source: UniProtKB
  10. negative regulation of cell-matrix adhesion Source: UniProtKB
  11. negative regulation of cell migration Source: UniProtKB
  12. negative regulation of receptor binding Source: UniProtKB
  13. protein kinase C signaling Source: UniProtKB
  14. tissue regeneration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Cell adhesion, Collagen degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM12.215.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 15 (EC:3.4.24.-)
Short name:
ADAM 15
Alternative name(s):
Metalloprotease RGD disintegrin protein
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
Short name:
MDC-15
Metargidin
Gene namesi
Name:ADAM15
Synonyms:MDC15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:193. ADAM15.

Subcellular locationi

Endomembrane system 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junctionadherens junction 1 Publication. Cell projectionciliumflagellum By similarity. Cytoplasmic vesiclesecretory vesicleacrosome By similarity
Note: The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed By similarity.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cell surface Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. extracellular vesicular exosome Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi484 – 4852RG → SV: Reduces ADAM15-mediated T-cell aggregation. 1 Publication

Organism-specific databases

PharmGKBiPA24510.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 206189By similarityPRO_0000029082Add
BLAST
Chaini207 – 863657Disintegrin and metalloproteinase domain-containing protein 15PRO_0000029083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi323 ↔ 409By similarity
Disulfide bondi365 ↔ 393By similarity
Disulfide bondi367 ↔ 376By similarity
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi480 ↔ 500By similarity
Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi611 – 6111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi657 ↔ 667By similarity
Disulfide bondi661 ↔ 673By similarity
Disulfide bondi675 ↔ 684By similarity
Modified residuei715 – 7151Phosphotyrosine; by HCK and LCK1 Publication
Modified residuei735 – 7351Phosphotyrosine; by HCK and LCK1 Publication

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Phosphorylation increases association with PTKs.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiQ13444.
PaxDbiQ13444.
PRIDEiQ13444.

PTM databases

PhosphoSiteiQ13444.

Expressioni

Tissue specificityi

Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells.4 Publications

Gene expression databases

BgeeiQ13444.
CleanExiHS_ADAM15.
ExpressionAtlasiQ13444. baseline and differential.
GenevestigatoriQ13444.

Organism-specific databases

HPAiHPA011633.

Interactioni

Subunit structurei

Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi. Interacts with ITAG9-ITGB1 By similarity. Interacts specifically with Src family protein-tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FYNP062412EBI-77818,EBI-515315
GRB2P629933EBI-77818,EBI-401755
HCKP086313EBI-77818,EBI-346340
LCKP062393EBI-77818,EBI-1348
NPHP1O152592EBI-77818,EBI-953828
PACSIN3Q9UKS63EBI-77818,EBI-77926
SH3GL2Q999622EBI-77818,EBI-77938
SH3PXD2AQ5TCZ12EBI-77818,EBI-2483234
SNX33Q8WV412EBI-77818,EBI-2481535
SNX9Q9Y5X12EBI-77818,EBI-77848
SRCP129313EBI-77818,EBI-621482

Protein-protein interaction databases

BioGridi114287. 27 interactions.
IntActiQ13444. 27 interactions.
MINTiMINT-108799.
STRINGi9606.ENSP00000349436.

Structurei

3D structure databases

ProteinModelPortaliQ13444.
SMRiQ13444. Positions 213-646.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini207 – 696490ExtracellularSequence AnalysisAdd
BLAST
Topological domaini718 – 863146CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei697 – 71721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini213 – 414202Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini421 – 50888DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini657 – 68529EGF-likePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi177 – 1848Cysteine switchBy similarity
Motifi484 – 4863Cell attachment sitePROSITE-ProRule annotation
Motifi815 – 8217SH3-bindingSequence Analysis
Motifi850 – 8567SH3-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi509 – 656148Cys-richAdd
BLAST

Domaini

The cytoplasmic domain is required for SH3GL2- and SNX9-binding.
Disintegrin domain binds to integrin alphaV-beta3.
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

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

EGF-like domain, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG294463.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230884.
HOVERGENiHBG006978.
InParanoidiQ13444.
KOiK06836.
OMAiHGVCDSN.
OrthoDBiEOG7F7W89.
PhylomeDBiQ13444.
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.
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.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (13)i

Sequence statusi: Complete.

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

This entry describes 13 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13444-1) [UniParc]FASTAAdd to Basket

Also known as: 6b

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
MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ
60 70 80 90 100
DDLPISLKKV LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY
110 120 130 140 150
QPDGTRVVSE GHTLENCCYQ GRVRGYAGSW VSICTCSGLR GLVVLTPERS
160 170 180 190 200
YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA LSWRESVHTQ KPPEHPLGQR
210 220 230 240 250
HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL EVALLLDTFF
260 270 280 290 300
RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS
310 320 330 340 350
AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL
360 370 380 390 400
GHSLGLDHDL PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK
410 420 430 440 450
ALLDGMGSCL FERLPSLPPM AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS
460 470 480 490 500
LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC RPTRGDCDLP EFCPGDSSQC
510 520 530 540 550
PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ PAAPLCLQTA
560 570 580 590 600
NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW
610 620 630 640 650
ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD
660 670 680 690 700
LLGAQECRSK CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL
710 720 730 740 750
SLLVLLVLVM LGASYWYRAR LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ
760 770 780 790 800
RALLARGTKQ ASALSFPAPP SRPLPPDPVS KRLQAELADR PNPPTRPLPA
810 820 830 840 850
DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA GIPPLVVPSR
860
PAPPPPTVSS LYL
Length:863
Mass (Da):92,959
Last modified:July 13, 2010 - v4
Checksum:i004936E9182629CA
GO
Isoform 2 (identifier: Q13444-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     760-808: Missing.

Show »
Length:814
Mass (Da):87,744
Checksum:iC6A297D51BED277E
GO
Isoform 3 (identifier: Q13444-3) [UniParc]FASTAAdd to Basket

Also known as: 6a

The sequence of this isoform differs from the canonical sequence as follows:
     760-760: Missing.

Show »
Length:862
Mass (Da):92,831
Checksum:iC39147754DD6B63C
GO
Isoform 4 (identifier: Q13444-4) [UniParc]FASTAAdd to Basket

Also known as: 4a

The sequence of this isoform differs from the canonical sequence as follows:
     785-808: Missing.

Show »
Length:839
Mass (Da):90,383
Checksum:i3B5F7590EFE0EBC1
GO
Isoform 5 (identifier: Q13444-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     760-784: Missing.

Show »
Length:838
Mass (Da):90,320
Checksum:i22637515284E16E8
GO
Isoform 6 (identifier: Q13444-6) [UniParc]FASTAAdd to Basket

Also known as: 7b

The sequence of this isoform differs from the canonical sequence as follows:
     809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT

Show »
Length:822
Mass (Da):88,779
Checksum:i2C01760368BEAF58
GO
Isoform 7 (identifier: Q13444-7) [UniParc]FASTAAdd to Basket

Also known as: 7a

The sequence of this isoform differs from the canonical sequence as follows:
     760-760: Missing.
     809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT

Show »
Length:821
Mass (Da):88,651
Checksum:i574AC60AD10ACFCE
GO
Isoform 8 (identifier: Q13444-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     760-784: Missing.
     809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT

Show »
Length:797
Mass (Da):86,140
Checksum:i402644A60C8BB7A3
GO
Isoform 9 (identifier: Q13444-9) [UniParc]FASTAAdd to Basket

Also known as: 3a

The sequence of this isoform differs from the canonical sequence as follows:
     737-796: AAQSGPSERP...LADRPNPPTR → LVLSASRPPL...CPAQGLESRP
     797-863: Missing.

Show »
Length:796
Mass (Da):86,311
Checksum:i7C808DCF0D1C296A
GO
Isoform 10 (identifier: Q13444-10) [UniParc]FASTAAdd to Basket

Also known as: 1

The sequence of this isoform differs from the canonical sequence as follows:
     736-772: RAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSR → SLRGQPSPHPQGSHCLPTPRAGAHRVTCPAQGLESRP
     773-863: Missing.

Show »
Length:772
Mass (Da):83,664
Checksum:i3EE4998C8EDCF958
GO
Isoform 11 (identifier: Q13444-11) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     94-387: Missing.
     760-808: Missing.

Show »
Length:520
Mass (Da):55,446
Checksum:i601F3874454899A0
GO
Isoform 12 (identifier: Q13444-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-26: I → IVLSWGVLGPA
     760-808: Missing.

Note: No experimental confirmation available.

Show »
Length:824
Mass (Da):88,724
Checksum:i84B3BF611CBF9E9D
GO
Isoform 13 (identifier: Q13444-13) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-87: GGTEEQQAES...DSHILELLQN → VSACNVEAPQ...ISQLASKRCF
     641-649: CIDHRCQRV → SSLGGQDQV
     650-863: Missing.

Note: No experimental confirmation available.

Show »
Length:633
Mass (Da):68,256
Checksum:i6C412A20B4E83369
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811I → V in BAG52157. (PubMed:16303743)Curated
Sequence conflicti104 – 1041G → C in BAG59890. (PubMed:14702039)Curated
Sequence conflicti191 – 1911K → T in BAG59890. (PubMed:14702039)Curated
Sequence conflicti286 – 2861H → Y in BAG59477. (PubMed:14702039)Curated
Sequence conflicti649 – 6491V → A in BAG52157. (PubMed:16303743)Curated
Sequence conflicti714 – 7141S → G in AAC50404. (PubMed:9039960)Curated
Sequence conflicti840 – 8401A → P in AAC51112. (PubMed:8617717)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911K → T.7 Publications
Corresponds to variant rs6427128 [ dbSNP | Ensembl ].
VAR_060315
Natural varianti216 – 2161E → K.1 Publication
Corresponds to variant rs115753757 [ dbSNP | Ensembl ].
VAR_068970
Natural varianti294 – 2941P → H.
Corresponds to variant rs2306122 [ dbSNP | Ensembl ].
VAR_060316
Natural varianti502 – 5021P → Q.
Corresponds to variant rs17093828 [ dbSNP | Ensembl ].
VAR_054339

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 261I → IVLSWGVLGPA in isoform 12. 1 PublicationVSP_044695
Alternative sequencei27 – 8761GGTEE…ELLQN → VSACNVEAPQVALRSSRQSQ RRPRGSPWSPRSFRTISQLA SKRCF in isoform 13. 1 PublicationVSP_055143Add
BLAST
Alternative sequencei94 – 387294Missing in isoform 11. 1 PublicationVSP_039524Add
BLAST
Alternative sequencei641 – 6499CIDHRCQRV → SSLGGQDQV in isoform 13. 1 PublicationVSP_055144
Alternative sequencei650 – 863214Missing in isoform 13. 1 PublicationVSP_055145Add
BLAST
Alternative sequencei736 – 77237RAAQS…APPSR → SLRGQPSPHPQGSHCLPTPR AGAHRVTCPAQGLESRP in isoform 10. 3 PublicationsVSP_039525Add
BLAST
Alternative sequencei737 – 79660AAQSG…NPPTR → LVLSASRPPLPGRCRLTLCP RDSSLRGQPSPHPQGSHCLP TPRAGAHRVTCPAQGLESRP in isoform 9. 1 PublicationVSP_039526Add
BLAST
Alternative sequencei760 – 80849Missing in isoform 2, isoform 11 and isoform 12. 8 PublicationsVSP_039527Add
BLAST
Alternative sequencei760 – 78425Missing in isoform 5 and isoform 8. 1 PublicationVSP_039528Add
BLAST
Alternative sequencei760 – 7601Missing in isoform 3 and isoform 7. 1 PublicationVSP_039529
Alternative sequencei773 – 86391Missing in isoform 10. 3 PublicationsVSP_039530Add
BLAST
Alternative sequencei785 – 80824Missing in isoform 4. 2 PublicationsVSP_039531Add
BLAST
Alternative sequencei797 – 86367Missing in isoform 9. 1 PublicationVSP_039532Add
BLAST
Alternative sequencei809 – 86355SQGPA…SSLYL → VTVGGEKGTASPPT in isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_039533Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U41767 mRNA. Translation: AAC50404.1.
U46005 mRNA. Translation: AAC51112.1.
AY518542 mRNA. Translation: AAR99331.1.
AF314227 Genomic DNA. Translation: AAM44189.1.
AF314227 Genomic DNA. Translation: AAS48590.1.
AF314227 Genomic DNA. Translation: AAS48591.1.
AF314227 Genomic DNA. Translation: AAS48592.1.
AF314227 Genomic DNA. Translation: AAS48593.1.
AF314227 Genomic DNA. Translation: AAS48594.1.
AF314227 Genomic DNA. Translation: AAS48595.1.
AF314227 Genomic DNA. Translation: AAS48596.1.
AF314227 Genomic DNA. Translation: AAS48597.1.
AF314227 Genomic DNA. Translation: AAS72298.1.
AY560593 mRNA. Translation: AAS72991.1.
AY560594 mRNA. Translation: AAS72992.1.
AY560595 mRNA. Translation: AAS72993.1.
AY560596 mRNA. Translation: AAS72994.1.
AY560597 mRNA. Translation: AAS72995.1.
AY560598 mRNA. Translation: AAS72996.1.
AY560599 mRNA. Translation: AAS72997.1.
AY560600 mRNA. Translation: AAS72998.1.
AY560601 mRNA. Translation: AAS72999.1.
AY576417 mRNA. Translation: AAS73000.1.
BT009764 mRNA. Translation: AAP88766.1.
AK296925 mRNA. Translation: BAG59477.1.
AK297468 mRNA. Translation: BAG59890.1.
AK075498 mRNA. Translation: BAG52157.1.
AL451085, AL691442 Genomic DNA. Translation: CAI13273.1.
AL451085, AL691442 Genomic DNA. Translation: CAI13274.1.
AL691442, AL451085 Genomic DNA. Translation: CAI15327.1.
AL691442, AL451085 Genomic DNA. Translation: CAI15328.1.
BC014566 mRNA. Translation: AAH14566.1.
CCDSiCCDS1084.1. [Q13444-2]
CCDS1085.1. [Q13444-4]
CCDS1086.1. [Q13444-5]
CCDS1087.1. [Q13444-1]
CCDS1088.1. [Q13444-10]
CCDS44236.1. [Q13444-3]
CCDS58031.1. [Q13444-12]
CCDS58032.1. [Q13444-9]
CCDS60282.1. [Q13444-13]
PIRiG02390.
RefSeqiNP_001248393.1. NM_001261464.1. [Q13444-12]
NP_001248394.1. NM_001261465.1. [Q13444-9]
NP_001248395.1. NM_001261466.1. [Q13444-13]
NP_003806.3. NM_003815.4. [Q13444-2]
NP_997074.1. NM_207191.2. [Q13444-10]
NP_997077.1. NM_207194.2. [Q13444-4]
NP_997078.1. NM_207195.2. [Q13444-5]
NP_997079.1. NM_207196.2. [Q13444-3]
NP_997080.1. NM_207197.2. [Q13444-1]
UniGeneiHs.312098.

Genome annotation databases

EnsembliENST00000271836; ENSP00000271836; ENSG00000143537. [Q13444-2]
ENST00000355956; ENSP00000348227; ENSG00000143537. [Q13444-4]
ENST00000356955; ENSP00000349436; ENSG00000143537. [Q13444-1]
ENST00000359280; ENSP00000352226; ENSG00000143537. [Q13444-5]
ENST00000360674; ENSP00000353892; ENSG00000143537. [Q13444-10]
ENST00000368412; ENSP00000357397; ENSG00000143537. [Q13444-9]
ENST00000368413; ENSP00000357398; ENSG00000143537. [Q13444-11]
ENST00000447332; ENSP00000476000; ENSG00000143537. [Q13444-13]
ENST00000449910; ENSP00000403843; ENSG00000143537. [Q13444-3]
ENST00000526491; ENSP00000432347; ENSG00000143537. [Q13444-6]
ENST00000529473; ENSP00000434227; ENSG00000143537. [Q13444-8]
ENST00000531455; ENSP00000432927; ENSG00000143537. [Q13444-12]
GeneIDi8751.
KEGGihsa:8751.
UCSCiuc001fgr.2. human. [Q13444-1]
uc001fgs.2. human. [Q13444-9]
uc001fgt.2. human. [Q13444-3]
uc001fgu.2. human. [Q13444-5]
uc001fgv.2. human. [Q13444-4]
uc001fgw.2. human. [Q13444-2]
uc001fgx.2. human. [Q13444-10]

Polymorphism databases

DMDMi300669614.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U41767 mRNA. Translation: AAC50404.1 .
U46005 mRNA. Translation: AAC51112.1 .
AY518542 mRNA. Translation: AAR99331.1 .
AF314227 Genomic DNA. Translation: AAM44189.1 .
AF314227 Genomic DNA. Translation: AAS48590.1 .
AF314227 Genomic DNA. Translation: AAS48591.1 .
AF314227 Genomic DNA. Translation: AAS48592.1 .
AF314227 Genomic DNA. Translation: AAS48593.1 .
AF314227 Genomic DNA. Translation: AAS48594.1 .
AF314227 Genomic DNA. Translation: AAS48595.1 .
AF314227 Genomic DNA. Translation: AAS48596.1 .
AF314227 Genomic DNA. Translation: AAS48597.1 .
AF314227 Genomic DNA. Translation: AAS72298.1 .
AY560593 mRNA. Translation: AAS72991.1 .
AY560594 mRNA. Translation: AAS72992.1 .
AY560595 mRNA. Translation: AAS72993.1 .
AY560596 mRNA. Translation: AAS72994.1 .
AY560597 mRNA. Translation: AAS72995.1 .
AY560598 mRNA. Translation: AAS72996.1 .
AY560599 mRNA. Translation: AAS72997.1 .
AY560600 mRNA. Translation: AAS72998.1 .
AY560601 mRNA. Translation: AAS72999.1 .
AY576417 mRNA. Translation: AAS73000.1 .
BT009764 mRNA. Translation: AAP88766.1 .
AK296925 mRNA. Translation: BAG59477.1 .
AK297468 mRNA. Translation: BAG59890.1 .
AK075498 mRNA. Translation: BAG52157.1 .
AL451085 , AL691442 Genomic DNA. Translation: CAI13273.1 .
AL451085 , AL691442 Genomic DNA. Translation: CAI13274.1 .
AL691442 , AL451085 Genomic DNA. Translation: CAI15327.1 .
AL691442 , AL451085 Genomic DNA. Translation: CAI15328.1 .
BC014566 mRNA. Translation: AAH14566.1 .
CCDSi CCDS1084.1. [Q13444-2 ]
CCDS1085.1. [Q13444-4 ]
CCDS1086.1. [Q13444-5 ]
CCDS1087.1. [Q13444-1 ]
CCDS1088.1. [Q13444-10 ]
CCDS44236.1. [Q13444-3 ]
CCDS58031.1. [Q13444-12 ]
CCDS58032.1. [Q13444-9 ]
CCDS60282.1. [Q13444-13 ]
PIRi G02390.
RefSeqi NP_001248393.1. NM_001261464.1. [Q13444-12 ]
NP_001248394.1. NM_001261465.1. [Q13444-9 ]
NP_001248395.1. NM_001261466.1. [Q13444-13 ]
NP_003806.3. NM_003815.4. [Q13444-2 ]
NP_997074.1. NM_207191.2. [Q13444-10 ]
NP_997077.1. NM_207194.2. [Q13444-4 ]
NP_997078.1. NM_207195.2. [Q13444-5 ]
NP_997079.1. NM_207196.2. [Q13444-3 ]
NP_997080.1. NM_207197.2. [Q13444-1 ]
UniGenei Hs.312098.

3D structure databases

ProteinModelPortali Q13444.
SMRi Q13444. Positions 213-646.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114287. 27 interactions.
IntActi Q13444. 27 interactions.
MINTi MINT-108799.
STRINGi 9606.ENSP00000349436.

Chemistry

ChEMBLi CHEMBL2331050.

Protein family/group databases

MEROPSi M12.215.

PTM databases

PhosphoSitei Q13444.

Polymorphism databases

DMDMi 300669614.

Proteomic databases

MaxQBi Q13444.
PaxDbi Q13444.
PRIDEi Q13444.

Protocols and materials databases

DNASUi 8751.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000271836 ; ENSP00000271836 ; ENSG00000143537 . [Q13444-2 ]
ENST00000355956 ; ENSP00000348227 ; ENSG00000143537 . [Q13444-4 ]
ENST00000356955 ; ENSP00000349436 ; ENSG00000143537 . [Q13444-1 ]
ENST00000359280 ; ENSP00000352226 ; ENSG00000143537 . [Q13444-5 ]
ENST00000360674 ; ENSP00000353892 ; ENSG00000143537 . [Q13444-10 ]
ENST00000368412 ; ENSP00000357397 ; ENSG00000143537 . [Q13444-9 ]
ENST00000368413 ; ENSP00000357398 ; ENSG00000143537 . [Q13444-11 ]
ENST00000447332 ; ENSP00000476000 ; ENSG00000143537 . [Q13444-13 ]
ENST00000449910 ; ENSP00000403843 ; ENSG00000143537 . [Q13444-3 ]
ENST00000526491 ; ENSP00000432347 ; ENSG00000143537 . [Q13444-6 ]
ENST00000529473 ; ENSP00000434227 ; ENSG00000143537 . [Q13444-8 ]
ENST00000531455 ; ENSP00000432927 ; ENSG00000143537 . [Q13444-12 ]
GeneIDi 8751.
KEGGi hsa:8751.
UCSCi uc001fgr.2. human. [Q13444-1 ]
uc001fgs.2. human. [Q13444-9 ]
uc001fgt.2. human. [Q13444-3 ]
uc001fgu.2. human. [Q13444-5 ]
uc001fgv.2. human. [Q13444-4 ]
uc001fgw.2. human. [Q13444-2 ]
uc001fgx.2. human. [Q13444-10 ]

Organism-specific databases

CTDi 8751.
GeneCardsi GC01P155023.
HGNCi HGNC:193. ADAM15.
HPAi HPA011633.
MIMi 605548. gene.
neXtProti NX_Q13444.
PharmGKBi PA24510.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG294463.
GeneTreei ENSGT00760000118888.
HOGENOMi HOG000230884.
HOVERGENi HBG006978.
InParanoidi Q13444.
KOi K06836.
OMAi HGVCDSN.
OrthoDBi EOG7F7W89.
PhylomeDBi Q13444.
TreeFami TF314733.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.

Miscellaneous databases

GeneWikii ADAM15.
GenomeRNAii 8751.
NextBioi 32829.
PROi Q13444.
SOURCEi Search...

Gene expression databases

Bgeei Q13444.
CleanExi HS_ADAM15.
ExpressionAtlasi Q13444. baseline and differential.
Genevestigatori Q13444.

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.
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.
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. "Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence."
    Kraetzschmar J., Lum L., Blobel C.P.
    J. Biol. Chem. 271:4593-4596(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-191.
    Tissue: Mammary carcinoma.
  2. "Expression of a disintegrin-like protein in cultured human vascular cells and in vivo."
    Herren B., Raines E.W., Ross R.
    FASEB J. 11:173-180(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-191.
    Tissue: Umbilical vein.
  3. "ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers."
    Charrier L., Yan Y., Driss A., Laboisse C.L., Sitaraman S.V., Merlin D.
    Am. J. Physiol. 288:G346-G353(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORM 2).
  4. "ADAM15 gene structure and differential alternative exon use in human tissues."
    Kleino I., Ortiz R.M., Huovila A.P.
    BMC Mol. Biol. 8:90-90(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10), VARIANT THR-191.
  5. "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
    Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
    Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 10), ALTERNATIVE SPLICING, INTERACTION WITH GRB2; MAPK1; MAPK3; NCK1; PTK6; SH3PXD2A AND SRC.
  6. "Characterization of human ADAM15 gene and promoter, and evidence for alternative exon use."
    Karkkainen I., Ortiz R.M., Huovila A.-P.J.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9), VARIANT THR-191.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-191.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 12 AND 13), VARIANTS THR-191 AND LYS-216.
    Tissue: Tongue.
  9. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
    Tissue: Embryo.
  10. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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), VARIANT THR-191.
    Tissue: Kidney.
  12. "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.
  13. "Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3."
    Zhang X.P., Kamata T., Yokoyama K., Puzon-McLaughlin W., Takada Y.
    J. Biol. Chem. 273:7345-7350(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3.
  14. "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.
  15. "Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells."
    Nath D., Slocombe P.M., Stephens P.E., Warn A., Hutchinson G.R., Yamada K.M., Docherty A.J., Murphy G.
    J. Cell Sci. 112:579-587(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND INTEGRIN ALPHA5-BETA1.
  16. "ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin."
    Ham C., Levkau B., Raines E.W., Herren B.
    Exp. Cell Res. 279:239-247(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases."
    Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R.
    J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-715 AND TYR-735, INTERACTION WITH GRB2; LCK AND HCK.
  18. "The role of ADAM 15 in glomerular mesangial cell migration."
    Martin J., Eynstone L.V., Davies M., Williams J.D., Steadman R.
    J. Biol. Chem. 277:33683-33689(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  19. "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
    Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
    J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3PXD2A.
  20. "Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling."
    Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., Burkhardt H.
    Arthritis Rheum. 52:1100-1109(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Inhibition of airway smooth muscle adhesion and migration by the disintegrin domain of ADAM-15."
    Lu D., Xie S., Sukkar M.B., Lu X., Scully M.F., Chung K.F.
    Am. J. Respir. Cell Mol. Biol. 37:494-500(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  22. "ADAM-15/metargidin mediates homotypic aggregation of human T lymphocytes and heterotypic interactions of T lymphocytes with intestinal epithelial cells."
    Charrier L., Yan Y., Nguyen H.T., Dalmasso G., Laboisse C.L., Gewirtz A.T., Sitaraman S.V., Merlin D.
    J. Biol. Chem. 282:16948-16958(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 484-ARG-GLY-485.
  23. "ADAM15 suppresses cell motility by driving integrin alpha5beta1 cell surface expression via Erk inactivation."
    Chen Q., Meng L.H., Zhu C.H., Lin L.P., Lu H., Ding J.
    Int. J. Biochem. Cell Biol. 40:2164-2173(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation."
    Najy A.J., Day K.C., Day M.L.
    J. Biol. Chem. 283:18393-18401(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays."
    Maretzky T., Yang G., Ouerfelli O., Overall C.M., Worpenberg S., Hassiepen U., Eder J., Blobel C.P.
    Biochem. J. 420:105-113(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  26. "Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
    Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
    J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCK; ITSN1; ITSN2; LYN; NCF1; NEPHROCYSTIN; SH3PXD2A; SNX33; SNX9 AND SRC.

Entry informationi

Entry nameiADA15_HUMAN
AccessioniPrimary (citable) accession number: Q13444
Secondary accession number(s): B3KQU5
, B4DLB5, B4DMH8, E9PN65, Q13493, Q53XQ0, Q5SR68, Q5SR69, Q6R267, Q71S61, Q71S62, Q71S63, Q71S64, Q71S65, Q71S66, Q71S67, Q71S68, Q71S69, Q96C78, U3KQL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 13, 2010
Last modified: October 29, 2014
This is version 160 of the entry and version 4 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3