Q13444 (ADA15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disintegrin and metalloproteinase domain-containing protein 15
Short name=ADAM 15
EC=3.4.24.-

Alternative name(s):
Metalloprotease RGD disintegrin protein
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
Short name=MDC-15
Metargidin

Gene names

Name:	ADAM15
Synonyms:	MDC15

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	863 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Cofactor	Binds 1 zinc ion per subunit By similarity.
Enzyme regulation	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. Ref.23
Subunit structure	Interacts with ITAGV-ITGB3 (vitronectin receptor), PACSIN3 and SNX9. PACSIN3 and SNX9 preferentially bind the precursor but not the processed form of ADAM15, suggesting that the interaction occurs in a secretory pathway compartment prior to the medial Golgi By similarity. 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. Ref.5 Ref.12 Ref.13 Ref.15 Ref.17 Ref.24
Subcellular location	Endomembrane system; Single-pass type I membrane protein. Cell junction › adherens junction. Cell projection › cilium › flagellum By similarity. Cytoplasmic vesicle › secretory vesicle › acrosome 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. Ref.14
Tissue specificity	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. Ref.3 Ref.11 Ref.16 Ref.19
Domain	The cytoplasmic domain interacts with endophilin I and sorting nexin 9 By similarity. 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.
Post-translational modification	The precursor is cleaved by a furin endopeptidase By similarity. Phosphorylation increases association with PTKs.
Sequence similarities	Contains 1 disintegrin domain. Contains 1 EGF-like domain. Contains 1 peptidase M12B domain.

Ontologies

Keywords
Biological process	Angiogenesis Cell adhesion Collagen degradation
Cellular component	Cell junction Cell projection Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain SH3-binding Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell-matrix adhesion Traceable author statement. Source: ProtInc collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	acrosomal vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell flagellum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	SH3 domain binding Inferred from physical interaction. Source: BHF-UCL metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PACSIN3	Q9UKS6	2	EBI-77818,EBI-77926
SH3GL2	Q99962	2	EBI-77818,EBI-77938

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13444-1)

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.

Isoform 2 (identifier: Q13444-2)

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

Isoform 3 (identifier: Q13444-3)

Also known as: 6a;

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

Isoform 4 (identifier: Q13444-4)

Also known as: 4a;

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

Isoform 5 (identifier: Q13444-5)

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

Isoform 6 (identifier: Q13444-6)

Also known as: 7b;

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

Isoform 7 (identifier: Q13444-7)

Also known as: 7a;

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

Isoform 8 (identifier: Q13444-8)

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

Isoform 9 (identifier: Q13444-9)

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.

Isoform 10 (identifier: Q13444-10)

Also known as: 1;

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

Isoform 11 (identifier: Q13444-11)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – 206	189	By similarity		PRO_0000029082
	Chain	207 – 863	657	Disintegrin and metalloproteinase domain-containing protein 15		PRO_0000029083
Regions
	Topological domain	207 – 696	490	Extracellular Potential
	Transmembrane	697 – 717	21	Helical; Potential
	Topological domain	718 – 863	146	Cytoplasmic Potential
	Domain	213 – 414	202	Peptidase M12B
	Domain	421 – 508	88	Disintegrin
	Domain	657 – 685	29	EGF-like
	Motif	177 – 184	8	Cysteine switch By similarity
	Motif	484 – 486	3	Cell attachment site Potential
	Motif	815 – 821	7	SH3-binding Potential
	Motif	850 – 856	7	SH3-binding Potential
	Compositional bias	509 – 656	148	Cys-rich
Sites
	Active site	349	1	By similarity
	Metal binding	179	1	Zinc; in inhibited form By similarity
	Metal binding	348	1	Zinc; catalytic By similarity
	Metal binding	352	1	Zinc; catalytic By similarity
	Metal binding	358	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	715	1	Phosphotyrosine; by HCK and LCK Ref.15
	Modified residue	735	1	Phosphotyrosine; by HCK and LCK Ref.15
	Glycosylation	237	1	N-linked (GlcNAc...) Potential
	Glycosylation	389	1	N-linked (GlcNAc...) Potential
	Glycosylation	392	1	N-linked (GlcNAc...) Potential
	Glycosylation	606	1	N-linked (GlcNAc...) Potential
	Glycosylation	611	1	N-linked (GlcNAc...) Potential
	Disulfide bond	323 ↔ 409		By similarity
	Disulfide bond	365 ↔ 393		By similarity
	Disulfide bond	367 ↔ 376		By similarity
	Disulfide bond	480 ↔ 500		By similarity
	Disulfide bond	657 ↔ 667		By similarity
	Disulfide bond	661 ↔ 673		By similarity
	Disulfide bond	675 ↔ 684		By similarity
Natural variations
	Alternative sequence	94 – 387	294	Missing in isoform 11.		VSP_039524
	Alternative sequence	736 – 772	37	RAAQS…APPSR → SLRGQPSPHPQGSHCLPTPR AGAHRVTCPAQGLESRP in isoform 10.		VSP_039525
	Alternative sequence	737 – 796	60	AAQSG…NPPTR → LVLSASRPPLPGRCRLTLCP RDSSLRGQPSPHPQGSHCLP TPRAGAHRVTCPAQGLESRP in isoform 9.		VSP_039526
	Alternative sequence	760 – 808	49	Missing in isoform 2 and isoform 11.		VSP_039527
	Alternative sequence	760 – 784	25	Missing in isoform 5 and isoform 8.		VSP_039528
	Alternative sequence	760	1	Missing in isoform 3 and isoform 7.		VSP_039529
	Alternative sequence	773 – 863	91	Missing in isoform 10.		VSP_039530
	Alternative sequence	785 – 808	24	Missing in isoform 4.		VSP_039531
	Alternative sequence	797 – 863	67	Missing in isoform 9.		VSP_039532
	Alternative sequence	809 – 863	55	SQGPA…SSLYL → VTVGGEKGTASPPT in isoform 6, isoform 7 and isoform 8.		VSP_039533
	Natural variant	191	1	K → T. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Ref.10 Corresponds to variant rs6427128 [ dbSNP | Ensembl ].		VAR_060315
	Natural variant	294	1	P → H. Corresponds to variant rs2306122 [ dbSNP | Ensembl ].		VAR_060316
	Natural variant	502	1	P → Q. Corresponds to variant rs17093828 [ dbSNP | Ensembl ].		VAR_054339
Experimental info
	Mutagenesis	484 – 485	2	RG → SV: Reduces ADAM15-mediated T-cell aggregation. Ref.20
	Sequence conflict	81	1	I → V in BAG52157. Ref.8
	Sequence conflict	649	1	V → A in BAG52157. Ref.8
	Sequence conflict	714	1	S → G in AAC50404. Ref.2
	Sequence conflict	840	1	A → P in AAC51112. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (6b) [UniParc]. Last modified July 13, 2010. Version 4. Checksum: 004936E9182629CA	FASTA	863	92,959
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS 790 800 810 820 830 840 KRLQAELADR PNPPTRPLPA DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA 850 860 GIPPLVVPSR PAPPPPTVSS LYL
	Isoform 2 [UniParc]. Checksum: C6A297D51BED277E	FASTA	814	87,744
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKS QGPAKPPPPR KPLPADPQGR 790 800 810 CPSGDLPGPG AGIPPLVVPS RPAPPPPTVS SLYL
	Isoform 3 (6a) [UniParc]. Checksum: C39147754DD6B63C	FASTA	862	92,831
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKA SALSFPAPPS RPLPPDPVSK 790 800 810 820 830 840 RLQAELADRP NPPTRPLPAD PVVRSPKSQG PAKPPPPRKP LPADPQGRCP SGDLPGPGAG 850 860 IPPLVVPSRP APPPPTVSSL YL
	Isoform 4 (4a) [UniParc]. Checksum: 3B5F7590EFE0EBC1	FASTA	839	90,383
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS 790 800 810 820 830 KRLQSQGPAK PPPPRKPLPA DPQGRCPSGD LPGPGAGIPP LVVPSRPAPP PPTVSSLYL
	Isoform 5 [UniParc]. Checksum: 22637515284E16E8	FASTA	838	90,320
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKA ELADRPNPPT RPLPADPVVR 790 800 810 820 830 SPKSQGPAKP PPPRKPLPAD PQGRCPSGDL PGPGAGIPPL VVPSRPAPPP PTVSSLYL
	Isoform 6 (7b) [UniParc]. Checksum: 2C01760368BEAF58	FASTA	822	88,779
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS 790 800 810 820 KRLQAELADR PNPPTRPLPA DPVVRSPKVT VGGEKGTASP PT
	Isoform 7 (7a) [UniParc]. Checksum: 574AC60AD10ACFCE	FASTA	821	88,651
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKA SALSFPAPPS RPLPPDPVSK 790 800 810 820 RLQAELADRP NPPTRPLPAD PVVRSPKVTV GGEKGTASPP T
	Isoform 8 [UniParc]. Checksum: 402644A60C8BB7A3	FASTA	797	86,140
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKA ELADRPNPPT RPLPADPVVR 790 SPKVTVGGEK GTASPPT
	Isoform 9 (3a) [UniParc]. Checksum: 7C808DCF0D1C296A	FASTA	796	86,311
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 780 LHQRLCQLKG PTCQYRLVLS ASRPPLPGRC RLTLCPRDSS LRGQPSPHPQ GSHCLPTPRA 790 GAHRVTCPAQ GLESRP
	Isoform 10 (1) [UniParc]. Checksum: 3EE4998C8EDCF958	FASTA	772	83,664
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 130 140 150 160 170 180 GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 190 200 210 220 230 240 LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 250 260 270 280 290 300 EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 310 320 330 340 350 360 AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 370 380 390 400 410 420 PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 430 440 450 460 470 480 AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 490 500 510 520 530 540 RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 550 560 570 580 590 600 PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 610 620 630 640 650 660 ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 670 680 690 700 710 720 CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 730 740 750 760 770 LHQRLCQLKG PTCQYSLRGQ PSPHPQGSHC LPTPRAGAHR VTCPAQGLES RP
	Isoform 11 [UniParc]. Checksum: 601F3874454899A0	FASTA	520	55,446
	10 20 30 40 50 60 MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 70 80 90 100 110 120 LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGLNFSNCS RRALEKALLD GMGSCLFERL 130 140 150 160 170 180 PSLPPMAAFC GNMFVEPGEQ CDCGFLDDCV DPCCDSLTCQ LRPGAQCASD GPCCQNCQLR 190 200 210 220 230 240 PSGWQCRPTR GDCDLPEFCP GDSSQCPPDV SLGDGEPCAG GQAVCMHGRC ASYAQQCQSL 250 260 270 280 290 300 WGPGAQPAAP LCLQTANTRG NAFGSCGRNP SGSYVSCTPR DAICGQLQCQ TGRTQPLLGS 310 320 330 340 350 360 IRDLLWETID VNGTELNCSW VHLDLGSDVA QPLLTLPGTA CGPGLVCIDH RCQRVDLLGA 370 380 390 400 410 420 QECRSKCHGH GVCDSNRHCY CEEGWAPPDC TTQLKATSSL TTGLLLSLLV LLVLVMLGAS 430 440 450 460 470 480 YWYRARLHQR LCQLKGPTCQ YRAAQSGPSE RPGPPQRALL ARGTKSQGPA KPPPPRKPLP 490 500 510 520 ADPQGRCPSG DLPGPGAGIP PLVVPSRPAP PPPTVSSLYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8617717] [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: 9039960] [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: 15358598] [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: 17937806] [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: 18296648] [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]	"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: 16303743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11). Tissue: Embryo.
[9]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-191. Tissue: Kidney.
[11]	"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: 9016778] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"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: 9516430] [Abstract] Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3.
[13]	"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: 9914169] [Abstract] Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND INTEGRIN ALPHA5-BETA1.
[14]	"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: 12243749] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"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: 11741929] [Abstract] Cited for: PHOSPHORYLATION AT TYR-715 AND TYR-735, INTERACTION WITH GRB2; LCK AND HCK.
[16]	"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: 12091380] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[17]	"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: 12615925] [Abstract] Cited for: INTERACTION WITH SH3PXD2A.
[18]	"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: 15818704] [Abstract] Cited for: FUNCTION.
[19]	"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: 17575078] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[20]	"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: 17416588] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 484-ARG-GLY-485.
[21]	"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: 18387333] [Abstract] Cited for: FUNCTION.
[22]	"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: 18434311] [Abstract] Cited for: FUNCTION.
[23]	"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: 19207106] [Abstract] Cited for: ENZYME REGULATION.
[24]	"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: 19718658] [Abstract] Cited for: INTERACTION WITH HCK; ITSN1; ITSN2; LYN; NCF1; NEPHROCYSTIN; SH3PXD2A; SNX33; SNX9 AND SRC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. 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.
IPI	IPI00013302. IPI00420067. IPI00420068. IPI00420069. IPI00420070. IPI00513871. IPI00742904. IPI00843806. IPI00969092. IPI00969132. IPI00969145.
PIR	G02390.
RefSeq	NP_003806.3. NM_003815.3. NP_997074.1. NM_207191.1. NP_997077.1. NM_207194.1. NP_997078.1. NM_207195.1. NP_997079.1. NM_207196.1. NP_997080.1. NM_207197.1.
UniGene	Hs.312098.
3D structure databases
ProteinModelPortal	Q13444.
SMR	Q13444. Positions 207-691.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13444. 8 interactions.
MINT	MINT-1445912.
STRING	Q13444.
Protein family/group databases
MEROPS	M12.215.
PTM databases
PhosphoSite	Q13444.
Polymorphism databases
DMDM	300669614.
Proteomic databases
PRIDE	Q13444.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000271836; ENSP00000271836; ENSG00000143537. ENST00000355956; ENSP00000348227; ENSG00000143537. ENST00000356955; ENSP00000349436; ENSG00000143537. ENST00000359280; ENSP00000352226; ENSG00000143537. ENST00000360674; ENSP00000353892; ENSG00000143537. ENST00000368412; ENSP00000357397; ENSG00000143537. ENST00000368413; ENSP00000357398; ENSG00000143537. ENST00000449910; ENSP00000403843; ENSG00000143537.
GeneID	8751.
KEGG	hsa:8751.
Organism-specific databases
CTD	8751.
GeneCards	GC01P155023.
H-InvDB	HIX0001025.
HGNC	HGNC:193. ADAM15.
HPA	HPA011633.
MIM	605548. gene.
neXtProt	NX_Q13444.
PharmGKB	PA24510.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04319.
GeneTree	ENSGT00590000082827.
HOVERGEN	HBG006978.
OMA	IMEASTD.
OrthoDB	EOG479F6Q.
PhylomeDB	Q13444.
Gene expression databases
ArrayExpress	Q13444.
Bgee	Q13444.
CleanEx	HS_ADAM15.
Genevestigator	Q13444.
GermOnline	ENSG00000143537. Homo sapiens.
Family and domain databases
InterPro	IPR006586. ADAM_Cys-rich. IPR001762. Blood-coag_inhib_Disintegrin. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. IPR002870. Peptidase_M12B_N. [Graphical view]
Gene3D	G3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit. G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KO	K06836.
Pfam	PF08516. ADAM_CR. 1 hit. PF00200. Disintegrin. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. [Graphical view]
SMART	SM00608. ACR. 1 hit. SM00050. DISIN. 1 hit. SM00181. EGF. 1 hit. [Graphical view]
SUPFAM	SSF57552. Disintegrin. 1 hit.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00546. CYSTEINE_SWITCH. False negative. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. 1 hit. PS00022. EGF_1. False negative. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	32829.
SOURCE	Search...

Entry information

Entry name

ADA15_HUMAN

Accession

Primary (citable) accession number: Q13444
Secondary accession number(s): B3KQU5 , Q13493, Q53XQ0, Q5SR68, Q5SR69, Q6R267, Q71S61, Q71S62, Q71S63, Q71S64, Q71S65, Q71S66, Q71S67, Q71S68, Q71S69, Q96C78

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	July 13, 2010
Last modified:	January 25, 2012
This is version 129 of the entry and version 4 of the sequence. [Complete history]

Entry status

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.