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O75173

- ATS4_HUMAN

UniProt

O75173 - ATS4_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene

ADAMTS4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.

    Catalytic activityi

    Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi194 – 1941Zinc; in inhibited formBy similarity
    Metal bindingi361 – 3611Zinc; catalytic
    Active sitei362 – 36211 PublicationPROSITE-ProRule annotation
    Metal bindingi365 – 3651Zinc; catalytic
    Metal bindingi371 – 3711Zinc; catalytic

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. metallopeptidase activity Source: ProtInc
    3. peptidase activity Source: ProtInc
    4. protease binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. extracellular matrix disassembly Source: Reactome
    2. extracellular matrix organization Source: Reactome
    3. proteolysis Source: ProtInc
    4. skeletal system development Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000158859-MONOMER.
    BRENDAi3.4.24.82. 2681.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.221.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
    Short name:
    ADAM-TS 4
    Short name:
    ADAM-TS4
    Short name:
    ADAMTS-4
    Alternative name(s):
    ADMP-1
    Aggrecanase-1
    Gene namesi
    Name:ADAMTS4
    Synonyms:KIAA0688
    ORF Names:UNQ769/PRO1563
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:220. ADAMTS4.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: BHF-UCL
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24548.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5151Sequence AnalysisAdd
    BLAST
    Propeptidei52 – 212161PRO_0000029164Add
    BLAST
    Chaini213 – 837625A disintegrin and metalloproteinase with thrombospondin motifs 4PRO_0000029165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi293 ↔ 3451 Publication
    Disulfide bondi322 ↔ 3271 Publication
    Disulfide bondi339 ↔ 4231 Publication
    Disulfide bondi377 ↔ 4071 Publication
    Disulfide bondi449 ↔ 4721 Publication
    Disulfide bondi460 ↔ 4821 Publication
    Disulfide bondi467 ↔ 5011 Publication
    Disulfide bondi495 ↔ 5061 Publication
    Disulfide bondi532 ↔ 569By similarity
    Disulfide bondi536 ↔ 574By similarity
    Disulfide bondi547 ↔ 559By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.
    Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiO75173.
    PRIDEiO75173.

    PTM databases

    PhosphoSiteiO75173.

    Miscellaneous databases

    PMAP-CutDBO75173.

    Expressioni

    Tissue specificityi

    Expressed in brain, lung and heart. Expressed at very low level in placenta and skeletal muscles.

    Inductioni

    By IL1/interleukin-1.

    Gene expression databases

    ArrayExpressiO75173.
    BgeeiO75173.
    CleanExiHS_ADAMTS4.
    GenevestigatoriO75173.

    Organism-specific databases

    HPAiCAB025876.

    Interactioni

    Subunit structurei

    Interacts with SRPX2.2 Publications

    Protein-protein interaction databases

    BioGridi114885. 4 interactions.
    IntActiO75173. 2 interactions.
    STRINGi9606.ENSP00000356975.

    Structurei

    Secondary structure

    1
    837
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi218 – 2269
    Helixi228 – 2347
    Helixi235 – 2373
    Helixi238 – 25215
    Helixi256 – 2583
    Beta strandi262 – 27110
    Beta strandi274 – 2763
    Helixi285 – 29612
    Turni297 – 2993
    Beta strandi304 – 3063
    Beta strandi311 – 3177
    Turni322 – 3243
    Beta strandi331 – 3333
    Turni341 – 3433
    Beta strandi345 – 3495
    Helixi355 – 36612
    Helixi375 – 3817
    Beta strandi393 – 3953
    Helixi406 – 41712
    Turni418 – 4214
    Helixi422 – 4243
    Helixi439 – 4424
    Helixi445 – 4539
    Beta strandi463 – 4653
    Turni466 – 4683
    Beta strandi472 – 4765
    Beta strandi479 – 4835
    Beta strandi494 – 4963
    Beta strandi499 – 5024
    Beta strandi505 – 5073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RJPX-ray2.80A/B/C/D213-520[»]
    3B2ZX-ray2.80A/B/C/D/E/F/G/H213-520[»]
    ProteinModelPortaliO75173.
    SMRiO75173. Positions 215-805.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75173.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini218 – 428211Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini437 – 51983DisintegrinAdd
    BLAST
    Domaini520 – 57556TSP type-1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni686 – 837152SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi192 – 1998Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi247 – 2526Poly-Ala
    Compositional biasi577 – 685109Cys-richAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
    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.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 1 TSP type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG271890.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiO75173.
    KOiK07764.
    OMAiHAGCDRI.
    OrthoDBiEOG7WDN1M.
    PhylomeDBiO75173.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 1 hit.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O75173-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR    50
    LASPLPREEE IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEQDS 100
    GVQVEGLTVQ YLGQAPELLG GAEPGTYLTG TINGDPESVA SLHWDGGALL 150
    GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI LRRKSPASGQ GPMCNVKAPL 200
    GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR YLLTVMAAAA 250
    KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN 300
    TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED 350
    DGLQSAFTAA HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP 400
    EEPWSPCSAR FITDFLDNGY GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ 450
    LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA MCQTKHSPWA DGTPCGPAQA 500
    CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV QFSSRDCTRP 550
    VPRNGGKYCE GRRTRFRSCN TEDCPTGSAL TFREEQCAAY NHRTDLFKSF 600
    PGPMDWVPRY TGVAPQDQCK LTCQAQALGY YYVLEPRVVD GTPCSPDSSS 650
    VCVQGRCIHA GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN 700
    NVVTIPAGAT HILVRQQGNP GHRSIYLALK LPDGSYALNG EYTLMPSPTD 750
    VVLPGAVSLR YSGATAASET LSGHGPLAQP LTLQVLVAGN PQDTRLRYSF 800
    FVPRPTPSTP RPTPQDWLHR RAQILEILRR RPWAGRK 837
    Length:837
    Mass (Da):90,197
    Last modified:January 11, 2011 - v3
    Checksum:i0C05299D7FB23A8D
    GO

    Sequence cautioni

    The sequence BAA31663.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti306 – 3061D → G in AAQ89245. (PubMed:12975309)Curated
    Sequence conflicti682 – 6821G → R in AAL02262. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41T → I.1 Publication
    Corresponds to variant rs17855814 [ dbSNP | Ensembl ].
    VAR_030636
    Natural varianti77 – 771A → T.1 Publication
    Corresponds to variant rs34448954 [ dbSNP | Ensembl ].
    VAR_057073
    Natural varianti304 – 3041D → N.1 Publication
    Corresponds to variant rs17855813 [ dbSNP | Ensembl ].
    VAR_030637
    Natural varianti369 – 3691M → V.1 Publication
    Corresponds to variant rs17855812 [ dbSNP | Ensembl ].
    VAR_030638
    Natural varianti552 – 5521P → T.1 Publication
    Corresponds to variant rs17855815 [ dbSNP | Ensembl ].
    VAR_030639
    Natural varianti564 – 5641T → A.1 Publication
    Corresponds to variant rs17855816 [ dbSNP | Ensembl ].
    VAR_030640
    Natural varianti626 – 6261Q → R.3 Publications
    Corresponds to variant rs4233367 [ dbSNP | Ensembl ].
    VAR_022450
    Natural varianti836 – 8361R → K.
    Corresponds to variant rs11807350 [ dbSNP | Ensembl ].
    VAR_030641

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148213 mRNA. Translation: AAD41494.1.
    AY044847 Genomic DNA. Translation: AAL02262.1.
    AB014588 mRNA. Translation: BAA31663.2. Different initiation.
    AY358886 mRNA. Translation: AAQ89245.1.
    AL590714 Genomic DNA. Translation: CAH72146.1.
    BC063293 mRNA. Translation: AAH63293.1.
    CCDSiCCDS1223.1.
    PIRiT00355.
    RefSeqiNP_005090.3. NM_005099.4.
    UniGeneiHs.211604.

    Genome annotation databases

    EnsembliENST00000367996; ENSP00000356975; ENSG00000158859.
    GeneIDi9507.
    KEGGihsa:9507.
    UCSCiuc001fyt.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF148213 mRNA. Translation: AAD41494.1 .
    AY044847 Genomic DNA. Translation: AAL02262.1 .
    AB014588 mRNA. Translation: BAA31663.2 . Different initiation.
    AY358886 mRNA. Translation: AAQ89245.1 .
    AL590714 Genomic DNA. Translation: CAH72146.1 .
    BC063293 mRNA. Translation: AAH63293.1 .
    CCDSi CCDS1223.1.
    PIRi T00355.
    RefSeqi NP_005090.3. NM_005099.4.
    UniGenei Hs.211604.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RJP X-ray 2.80 A/B/C/D 213-520 [» ]
    3B2Z X-ray 2.80 A/B/C/D/E/F/G/H 213-520 [» ]
    ProteinModelPortali O75173.
    SMRi O75173. Positions 215-805.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114885. 4 interactions.
    IntActi O75173. 2 interactions.
    STRINGi 9606.ENSP00000356975.

    Chemistry

    BindingDBi O75173.
    ChEMBLi CHEMBL2318.

    Protein family/group databases

    MEROPSi M12.221.

    PTM databases

    PhosphoSitei O75173.

    Proteomic databases

    PaxDbi O75173.
    PRIDEi O75173.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367996 ; ENSP00000356975 ; ENSG00000158859 .
    GeneIDi 9507.
    KEGGi hsa:9507.
    UCSCi uc001fyt.4. human.

    Organism-specific databases

    CTDi 9507.
    GeneCardsi GC01M161159.
    H-InvDB HIX0001237.
    HGNCi HGNC:220. ADAMTS4.
    HPAi CAB025876.
    MIMi 603876. gene.
    neXtProti NX_O75173.
    PharmGKBi PA24548.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271890.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi O75173.
    KOi K07764.
    OMAi HAGCDRI.
    OrthoDBi EOG7WDN1M.
    PhylomeDBi O75173.
    TreeFami TF331949.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000158859-MONOMER.
    BRENDAi 3.4.24.82. 2681.
    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Miscellaneous databases

    ChiTaRSi ADAMTS4. human.
    EvolutionaryTracei O75173.
    GeneWikii ADAMTS4.
    GenomeRNAii 9507.
    NextBioi 35624.
    PMAP-CutDB O75173.
    PROi O75173.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75173.
    Bgeei O75173.
    CleanExi HS_ADAMTS4.
    Genevestigatori O75173.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-626.
    2. "ADAMTS-4 genomic locus."
      Sawaji Y., Nagase H., Saklatvala J., Clark A.R.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-77 AND ARG-626.
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-626.
    5. "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].
    6. "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], VARIANTS ILE-4; ASN-304; VAL-369; THR-552 AND ALA-564.
      Tissue: Brain.
    7. "The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage."
      Tortorella M.D., Pratta M.A., Liu R.-Q., Abbaszade I., Ross H., Burn T.C., Arner E.C.
      J. Biol. Chem. 275:25791-25797(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    8. "Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR."
      Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C., Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A., Vincentelli R., Cau P., Szepetowski P.
      Hum. Mol. Genet. 17:3617-3630(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRPX2.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 213-520 ALONE AND IN COMPLEX WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiATS4_HUMAN
    AccessioniPrimary (citable) accession number: O75173
    Secondary accession number(s): Q5VTW2
    , Q6P4Q8, Q6UWA8, Q9UN83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 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

    Caution

    Has sometimes been referred to as ADAMTS2.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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. 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