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Protein

Disintegrin and metalloproteinase domain-containing protein 15

Gene

ADAM15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Zn2+By similarityNote: 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)DescriptionActionsGraphical viewLength
Metal bindingi179Zinc; in inhibited formBy similarity1
Metal bindingi348Zinc; catalyticBy similarity1
Active sitei349PROSITE-ProRule annotation1
Metal bindingi352Zinc; catalyticBy similarity1
Metal bindingi358Zinc; catalyticBy similarity1

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: Reactome
  • metallopeptidase activity Source: BHF-UCL
  • SH3 domain binding Source: BHF-UCL

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cardiac epithelial to mesenchymal transition Source: Ensembl
  • cell-matrix adhesion Source: ProtInc
  • collagen catabolic process Source: UniProtKB-KW
  • extracellular matrix disassembly Source: Reactome
  • innate immune response Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • male gonad development Source: Ensembl
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of cell-matrix adhesion Source: UniProtKB
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of receptor binding Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000143537-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
SIGNORiQ13444.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:193. ADAM15.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini207 – 696ExtracellularSequence analysisAdd BLAST490
Transmembranei697 – 717HelicalSequence analysisAdd BLAST21
Topological domaini718 – 863CytoplasmicSequence analysisAdd BLAST146

GO - Cellular componenti

  • acrosomal vesicle Source: UniProtKB-SubCell
  • adherens junction Source: UniProtKB-SubCell
  • cell projection Source: UniProtKB-KW
  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi484 – 485RG → SV: Reduces ADAM15-mediated T-cell aggregation. 1 Publication2

Organism-specific databases

DisGeNETi8751.
OpenTargetsiENSG00000143537.
PharmGKBiPA24510.

Chemistry databases

ChEMBLiCHEMBL2331050.

Polymorphism and mutation databases

BioMutaiADAM15.
DMDMi300669614.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002908218 – 206By similarityAdd BLAST189
ChainiPRO_0000029083207 – 863Disintegrin and metalloproteinase domain-containing protein 15Add BLAST657

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi237N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi323 ↔ 409By similarity
Disulfide bondi365 ↔ 393By similarity
Disulfide bondi367 ↔ 376By similarity
Glycosylationi389N-linked (GlcNAc...)Sequence analysis1
Glycosylationi392N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi480 ↔ 500By similarity
Glycosylationi606N-linked (GlcNAc...)Sequence analysis1
Glycosylationi611N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi657 ↔ 667By similarity
Disulfide bondi661 ↔ 673By similarity
Disulfide bondi675 ↔ 684By similarity
Modified residuei715Phosphotyrosine; by HCK and LCK1 Publication1
Modified residuei735Phosphotyrosine; by HCK and LCK1 Publication1

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

EPDiQ13444.
MaxQBiQ13444.
PaxDbiQ13444.
PeptideAtlasiQ13444.
PRIDEiQ13444.

PTM databases

iPTMnetiQ13444.
PhosphoSitePlusiQ13444.

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

BgeeiENSG00000143537.
CleanExiHS_ADAM15.
GenevisibleiQ13444. HS.

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
BANPQ8N9N53EBI-77818,EBI-744695
FHL3Q136433EBI-77818,EBI-741101
FYNP062412EBI-77818,EBI-515315
GRB2P629933EBI-77818,EBI-401755
HCKP086313EBI-77818,EBI-346340
LCKP062393EBI-77818,EBI-1348
NPHP1O152592EBI-77818,EBI-953828
NUP62P371983EBI-77818,EBI-347978
PACSIN3Q9UKS63EBI-77818,EBI-77926
RBPMSQ930623EBI-77818,EBI-740322
SH3GL2Q999622EBI-77818,EBI-77938
SH3PXD2AQ5TCZ12EBI-77818,EBI-2483234
SNX33Q8WV412EBI-77818,EBI-2481535
SNX9Q9Y5X12EBI-77818,EBI-77848
SP4Q024463EBI-77818,EBI-10198587
SRCP129313EBI-77818,EBI-621482

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • SH3 domain binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114287. 32 interactors.
IntActiQ13444. 33 interactors.
MINTiMINT-108799.
STRINGi9606.ENSP00000349436.

Structurei

3D structure databases

ProteinModelPortaliQ13444.
SMRiQ13444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini213 – 414Peptidase M12BPROSITE-ProRule annotationAdd BLAST202
Domaini421 – 508DisintegrinPROSITE-ProRule annotationAdd BLAST88
Domaini657 – 685EGF-likePROSITE-ProRule annotationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi177 – 184Cysteine switchBy similarity8
Motifi484 – 486Cell attachment sitePROSITE-ProRule annotation3
Motifi815 – 821SH3-bindingSequence analysis7
Motifi850 – 856SH3-bindingSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi509 – 656Cys-richAdd BLAST148

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

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230884.
HOVERGENiHBG006978.
InParanoidiQ13444.
KOiK06836.
OMAiHGVCDSN.
OrthoDBiEOG091G01NX.
PhylomeDBiQ13444.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR033605. ADAM15.
IPR006586. ADAM_Cys-rich.
IPR001762. Disintegrin_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PANTHERiPTHR11905:SF130. PTHR11905:SF130. 2 hits.
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.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti81I → V in BAG52157 (PubMed:16303743).Curated1
Sequence conflicti104G → C in BAG59890 (PubMed:14702039).Curated1
Sequence conflicti191K → T in BAG59890 (PubMed:14702039).Curated1
Sequence conflicti286H → Y in BAG59477 (PubMed:14702039).Curated1
Sequence conflicti649V → A in BAG52157 (PubMed:16303743).Curated1
Sequence conflicti714S → G in AAC50404 (PubMed:9039960).Curated1
Sequence conflicti840A → P in AAC51112 (PubMed:8617717).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060315191K → T.7 PublicationsCorresponds to variant rs6427128dbSNPEnsembl.1
Natural variantiVAR_068970216E → K.1 PublicationCorresponds to variant rs115753757dbSNPEnsembl.1
Natural variantiVAR_060316294P → H.Corresponds to variant rs2306122dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04469526I → IVLSWGVLGPA in isoform 12. 1 Publication1
Alternative sequenceiVSP_05514327 – 87GGTEE…ELLQN → VSACNVEAPQVALRSSRQSQ RRPRGSPWSPRSFRTISQLA SKRCF in isoform 13. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_03952494 – 387Missing in isoform 11. 1 PublicationAdd BLAST294
Alternative sequenceiVSP_055144641 – 649CIDHRCQRV → SSLGGQDQV in isoform 13. 1 Publication9
Alternative sequenceiVSP_055145650 – 863Missing in isoform 13. 1 PublicationAdd BLAST214
Alternative sequenceiVSP_039525736 – 772RAAQS…APPSR → SLRGQPSPHPQGSHCLPTPR AGAHRVTCPAQGLESRP in isoform 10. 3 PublicationsAdd BLAST37
Alternative sequenceiVSP_039526737 – 796AAQSG…NPPTR → LVLSASRPPLPGRCRLTLCP RDSSLRGQPSPHPQGSHCLP TPRAGAHRVTCPAQGLESRP in isoform 9. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_039527760 – 808Missing in isoform 2, isoform 11 and isoform 12. 8 PublicationsAdd BLAST49
Alternative sequenceiVSP_039528760 – 784Missing in isoform 5 and isoform 8. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_039529760Missing in isoform 3 and isoform 7. 1 Publication1
Alternative sequenceiVSP_039530773 – 863Missing in isoform 10. 3 PublicationsAdd BLAST91
Alternative sequenceiVSP_039531785 – 808Missing in isoform 4. 2 PublicationsAdd BLAST24
Alternative sequenceiVSP_039532797 – 863Missing in isoform 9. 1 PublicationAdd BLAST67
Alternative sequenceiVSP_039533809 – 863SQGPA…SSLYL → VTVGGEKGTASPPT in isoform 6, isoform 7 and isoform 8. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human. [Q13444-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ13444.
SMRiQ13444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114287. 32 interactors.
IntActiQ13444. 33 interactors.
MINTiMINT-108799.
STRINGi9606.ENSP00000349436.

Chemistry databases

ChEMBLiCHEMBL2331050.

Protein family/group databases

MEROPSiM12.215.

PTM databases

iPTMnetiQ13444.
PhosphoSitePlusiQ13444.

Polymorphism and mutation databases

BioMutaiADAM15.
DMDMi300669614.

Proteomic databases

EPDiQ13444.
MaxQBiQ13444.
PaxDbiQ13444.
PeptideAtlasiQ13444.
PRIDEiQ13444.

Protocols and materials databases

DNASUi8751.
Structural Biology KnowledgebaseSearch...

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.3. human. [Q13444-1]

Organism-specific databases

CTDi8751.
DisGeNETi8751.
GeneCardsiADAM15.
HGNCiHGNC:193. ADAM15.
HPAiHPA011633.
MIMi605548. gene.
neXtProtiNX_Q13444.
OpenTargetsiENSG00000143537.
PharmGKBiPA24510.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230884.
HOVERGENiHBG006978.
InParanoidiQ13444.
KOiK06836.
OMAiHGVCDSN.
OrthoDBiEOG091G01NX.
PhylomeDBiQ13444.
TreeFamiTF314733.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143537-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
SIGNORiQ13444.

Miscellaneous databases

GeneWikiiADAM15.
GenomeRNAii8751.
PROiQ13444.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143537.
CleanExiHS_ADAM15.
GenevisibleiQ13444. HS.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR033605. ADAM15.
IPR006586. ADAM_Cys-rich.
IPR001762. Disintegrin_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PANTHERiPTHR11905:SF130. PTHR11905:SF130. 2 hits.
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.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.