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Protein

Disintegrin and metalloproteinase domain-containing protein 33

Gene

ADAM33

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

Functioni

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Zinc; in inhibited formBy similarity
Metal bindingi345 – 3451Zinc; catalytic
Active sitei346 – 3461PROSITE-ProRule annotation
Metal bindingi349 – 3491Zinc; catalytic
Metal bindingi355 – 3551Zinc; catalytic

GO - Molecular functioni

  1. metalloendopeptidase activity Source: UniProtKB
  2. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.244.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 33 (EC:3.4.24.-)
Short name:
ADAM 33
Gene namesi
Name:ADAM33
Synonyms:C20orf153
ORF Names:UNQ873/PRO1891
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15478. ADAM33.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 701672ExtracellularSequence AnalysisAdd
BLAST
Transmembranei702 – 72221HelicalSequence AnalysisAdd
BLAST
Topological domaini723 – 81391CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Asthma3 Publications

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionThe most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi.

See also OMIM:600807

Keywords - Diseasei

Asthma

Organism-specific databases

MIMi600807. phenotype.
PharmGKBiPA24526.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Propeptidei30 – 203174By similarityPRO_0000029142Add
BLAST
Chaini204 – 813610Disintegrin and metalloproteinase domain-containing protein 33PRO_0000029143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi231 – 2311N-linked (GlcNAc...)
Glycosylationi276 – 2761N-linked (GlcNAc...)
Disulfide bondi320 ↔ 404
Disulfide bondi360 ↔ 388
Disulfide bondi361 ↔ 371
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi475 ↔ 495By similarity
Disulfide bondi653 ↔ 663By similarity
Disulfide bondi657 ↔ 669By similarity
Disulfide bondi671 ↔ 680By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9BZ11.
PRIDEiQ9BZ11.

PTM databases

PhosphoSiteiQ9BZ11.

Expressioni

Tissue specificityi

Expressed in all tissues, except liver, with high expression in placenta, lung, spleen and veins.1 Publication

Gene expression databases

BgeeiQ9BZ11.
CleanExiHS_ADAM33.
ExpressionAtlasiQ9BZ11. baseline and differential.
GenevestigatoriQ9BZ11.

Interactioni

Protein-protein interaction databases

BioGridi123243. 4 interactions.
IntActiQ9BZ11. 2 interactions.
MINTiMINT-2876745.
STRINGi9606.ENSP00000348912.

Structurei

Secondary structure

1
813
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2189Combined sources
Helixi220 – 2256Combined sources
Turni226 – 2283Combined sources
Helixi230 – 24819Combined sources
Helixi249 – 2513Combined sources
Beta strandi253 – 26210Combined sources
Beta strandi264 – 2663Combined sources
Helixi275 – 29218Combined sources
Beta strandi296 – 3038Combined sources
Helixi307 – 3093Combined sources
Turni322 – 3243Combined sources
Beta strandi326 – 3305Combined sources
Beta strandi333 – 3353Combined sources
Helixi336 – 35015Combined sources
Helixi366 – 3683Combined sources
Helixi387 – 39812Combined sources
Turni399 – 4024Combined sources
Helixi403 – 4064Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R54X-ray1.85A204-409[»]
1R55X-ray1.58A204-409[»]
ProteinModelPortaliQ9BZ11.
SMRiQ9BZ11. Positions 204-681.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZ11.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini210 – 409200Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini417 – 50387DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini649 – 68133EGF-likePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 1388Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi503 – 648146Cys-richAdd
BLAST

Domaini

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, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG294463.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9BZ11.
KOiK08616.
OMAiHFLPCAG.
OrthoDBiEOG7F7W89.
PhylomeDBiQ9BZ11.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZ11-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGWRPRRARG TPLLLLLLLL LLWPVPGAGV LQGHIPGQPV TPHWVLDGQP
60 70 80 90 100
WRTVSLEEPV SKPDMGLVAL EAEGQELLLE LEKNHRLLAP GYIETHYGPD
110 120 130 140 150
GQPVVLAPNH TDHCHYQGRV RGFPDSWVVL CTCSGMSGLI TLSRNASYYL
160 170 180 190 200
RPWPPRGSKD FSTHEIFRME QLLTWKGTCG HRDPGNKAGM TSLPGGPQSR
210 220 230 240 250
GRREARRTRK YLELYIVADH TLFLTRHRNL NHTKQRLLEV ANYVDQLLRT
260 270 280 290 300
LDIQVALTGL EVWTERDRSR VTQDANATLW AFLQWRRGLW AQRPHDSAQL
310 320 330 340 350
LTGRAFQGAT VGLAPVEGMC RAESSGGVST DHSELPIGAA ATMAHEIGHS
360 370 380 390 400
LGLSHDPDGC CVEAAAESGG CVMAAATGHP FPRVFSACSR RQLRAFFRKG
410 420 430 440 450
GGACLSNAPD PGLPVPPALC GNGFVEAGEE CDCGPGQECR DLCCFAHNCS
460 470 480 490 500
LRPGAQCAHG DCCVRCLLKP AGALCRQAMG DCDLPEFCTG TSSHCPPDVY
510 520 530 540 550
LLDGSPCARG SGYCWDGACP TLEQQCQQLW GPGSHPAPEA CFQVVNSAGD
560 570 580 590 600
AHGNCGQDSE GHFLPCAGRD ALCGKLQCQG GKPSLLAPHM VPVDSTVHLD
610 620 630 640 650
GQEVTCRGAL ALPSAQLDLL GLGLVEPGTQ CGPRMVCQSR RCRKNAFQEL
660 670 680 690 700
QRCLTACHSH GVCNSNHNCH CAPGWAPPFC DKPGFGGSMD SGPVQAENHD
710 720 730 740 750
TFLLAMLLSV LLPLLPGAGL AWCCYRLPGA HLQRCSWGCR RDPACSGPKD
760 770 780 790 800
GPHRDHPLGG VHPMELGPTA TGQPWPLDPE NSHEPSSHPE KPLPAVSPDP
810
QADQVQMPRS CLW
Length:813
Mass (Da):87,739
Last modified:March 27, 2002 - v2
Checksum:i90713A99668D5569
GO
Isoform 2 (identifier: Q9BZ11-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     636-661: Missing.

Show »
Length:787
Mass (Da):84,724
Checksum:iCBAF1B08B263A890
GO
Isoform 3 (identifier: Q9BZ11-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-478: Missing.
     636-661: Missing.

Note: No experimental confirmation available. By similarity with mouse isoform.

Show »
Length:309
Mass (Da):32,554
Checksum:iA60AC04E056CF264
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti802 – 8021Missing in AAM80482 (PubMed:12110844).Curated
Sequence conflicti802 – 8021Missing in AAM80483 (PubMed:12110844).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091N → S.1 Publication
Corresponds to variant rs41467948 [ dbSNP | Ensembl ].
VAR_030512
Natural varianti178 – 1781T → A.1 Publication
Corresponds to variant rs3918392 [ dbSNP | Ensembl ].
VAR_029143
Natural varianti272 – 2721T → M.1 Publication
Corresponds to variant rs41534847 [ dbSNP | Ensembl ].
VAR_030513
Natural varianti305 – 3051A → V in a cutaneous metastatic melanoma sample; somatic mutation. 1 Publication
VAR_066337
Natural varianti316 – 3161V → I.1 Publication
Corresponds to variant rs41459049 [ dbSNP | Ensembl ].
VAR_030514
Natural varianti336 – 3361P → S.1 Publication
Corresponds to variant rs41483049 [ dbSNP | Ensembl ].
VAR_030515
Natural varianti365 – 3651A → S.1 Publication
Corresponds to variant rs41419248 [ dbSNP | Ensembl ].
VAR_030516
Natural varianti441 – 4411D → E.1 Publication
Corresponds to variant rs41382144 [ dbSNP | Ensembl ].
VAR_030517
Natural varianti515 – 5151W → R.1 Publication
Corresponds to variant rs615436 [ dbSNP | Ensembl ].
VAR_030518
Natural varianti612 – 6121L → H.1 Publication
Corresponds to variant rs41453444 [ dbSNP | Ensembl ].
VAR_030519
Natural varianti710 – 7101V → I.1 Publication
Corresponds to variant rs3918396 [ dbSNP | Ensembl ].
VAR_030520
Natural varianti739 – 7391C → G.1 Publication
Corresponds to variant rs41434648 [ dbSNP | Ensembl ].
VAR_030521
Natural varianti742 – 7421D → Y.1 Publication
Corresponds to variant rs41462450 [ dbSNP | Ensembl ].
VAR_030522
Natural varianti764 – 7641M → T.1 Publication
Corresponds to variant rs2280091 [ dbSNP | Ensembl ].
VAR_021847
Natural varianti774 – 7741P → S.1 Publication
Corresponds to variant rs2280090 [ dbSNP | Ensembl ].
VAR_029144

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 478478Missing in isoform 3. CuratedVSP_015421Add
BLAST
Alternative sequencei636 – 66126Missing in isoform 2 and isoform 3. 1 PublicationVSP_005495Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055891 mRNA. Translation: BAB83092.1.
AF466287 mRNA. Translation: AAM80482.1.
AF466288 Genomic DNA. Translation: AAM80483.1.
AY358314 mRNA. Translation: AAQ88680.1.
DQ995342 Genomic DNA. Translation: ABI97387.1.
AL109804, AL356755 Genomic DNA. Translation: CAI18840.1.
CCDSiCCDS13058.1. [Q9BZ11-1]
RefSeqiNP_001269376.1. NM_001282447.1.
NP_079496.1. NM_025220.3. [Q9BZ11-1]
NP_694882.1. NM_153202.2. [Q9BZ11-2]
UniGeneiHs.173716.

Genome annotation databases

EnsembliENST00000350009; ENSP00000322550; ENSG00000149451. [Q9BZ11-2]
ENST00000356518; ENSP00000348912; ENSG00000149451. [Q9BZ11-1]
GeneIDi80332.
KEGGihsa:80332.
UCSCiuc002wis.3. human. [Q9BZ11-3]
uc002wit.3. human. [Q9BZ11-1]
uc002wiu.3. human. [Q9BZ11-2]

Polymorphism databases

DMDMi20137458.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB055891 mRNA. Translation: BAB83092.1.
AF466287 mRNA. Translation: AAM80482.1.
AF466288 Genomic DNA. Translation: AAM80483.1.
AY358314 mRNA. Translation: AAQ88680.1.
DQ995342 Genomic DNA. Translation: ABI97387.1.
AL109804, AL356755 Genomic DNA. Translation: CAI18840.1.
CCDSiCCDS13058.1. [Q9BZ11-1]
RefSeqiNP_001269376.1. NM_001282447.1.
NP_079496.1. NM_025220.3. [Q9BZ11-1]
NP_694882.1. NM_153202.2. [Q9BZ11-2]
UniGeneiHs.173716.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R54X-ray1.85A204-409[»]
1R55X-ray1.58A204-409[»]
ProteinModelPortaliQ9BZ11.
SMRiQ9BZ11. Positions 204-681.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123243. 4 interactions.
IntActiQ9BZ11. 2 interactions.
MINTiMINT-2876745.
STRINGi9606.ENSP00000348912.

Chemistry

BindingDBiQ9BZ11.
ChEMBLiCHEMBL6121.

Protein family/group databases

MEROPSiM12.244.

PTM databases

PhosphoSiteiQ9BZ11.

Polymorphism databases

DMDMi20137458.

Proteomic databases

PaxDbiQ9BZ11.
PRIDEiQ9BZ11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350009; ENSP00000322550; ENSG00000149451. [Q9BZ11-2]
ENST00000356518; ENSP00000348912; ENSG00000149451. [Q9BZ11-1]
GeneIDi80332.
KEGGihsa:80332.
UCSCiuc002wis.3. human. [Q9BZ11-3]
uc002wit.3. human. [Q9BZ11-1]
uc002wiu.3. human. [Q9BZ11-2]

Organism-specific databases

CTDi80332.
GeneCardsiGC20M003596.
HGNCiHGNC:15478. ADAM33.
MIMi600807. phenotype.
607114. gene.
neXtProtiNX_Q9BZ11.
PharmGKBiPA24526.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG294463.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9BZ11.
KOiK08616.
OMAiHFLPCAG.
OrthoDBiEOG7F7W89.
PhylomeDBiQ9BZ11.
TreeFamiTF314733.

Miscellaneous databases

EvolutionaryTraceiQ9BZ11.
GeneWikiiADAM33.
GenomeRNAii80332.
NextBioi70880.
PROiQ9BZ11.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZ11.
CleanExiHS_ADAM33.
ExpressionAtlasiQ9BZ11. baseline and differential.
GenevestigatoriQ9BZ11.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity."
    Yoshinaka T., Nishii K., Yamada K., Sawada H., Nishiwaki E., Smith K., Yoshino K., Ishiguro H., Higashiyama S.
    Gene 282:227-236(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INVOLVEMENT IN ASTHMA.
    Tissue: Uterus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. NIEHS SNPs program
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-109; ALA-178; MET-272; ILE-316; SER-336; SER-365; GLU-441; ARG-515; HIS-612; ILE-710; GLY-739; TYR-742; THR-764 AND SER-774.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "ADAM33 haplotypes are associated with asthma in a large Australian population."
    Kedda M.A., Duffy D.L., Bradley B., O'Hehir R.E., Thompson P.J.
    Eur. J. Hum. Genet. 14:1027-1036(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
  7. "Positionally cloned asthma susceptibility gene polymorphisms and disease risk in the British 1958 Birth Cohort."
    Blakey J.D., Sayers I., Ring S.M., Strachan D.P., Hall I.P.
    Thorax 64:381-387(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 204-410 IN COMPLEX WITH METALLOPROTEASE INHIBITOR MARIMASTAT, X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 204-410.
  9. "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma."
    Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.
    Hum. Mutat. 32:E2148-E2175(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-305.

Entry informationi

Entry nameiADA33_HUMAN
AccessioniPrimary (citable) accession number: Q9BZ11
Secondary accession number(s): A0A1K6
, Q5JT75, Q5JT76, Q8N0W6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: February 4, 2015
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.