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Q9UKP5

- ATS6_HUMAN

UniProt

Q9UKP5 - ATS6_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 6

Gene

ADAMTS6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi403 – 4031Zinc; catalyticBy similarity
    Active sitei404 – 4041PROSITE-ProRule annotation
    Metal bindingi407 – 4071Zinc; catalyticBy similarity
    Metal bindingi413 – 4131Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. metallopeptidase activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.230.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 6 (EC:3.4.24.-)
    Short name:
    ADAM-TS 6
    Short name:
    ADAM-TS6
    Short name:
    ADAMTS-6
    Gene namesi
    Name:ADAMTS6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:222. ADAMTS6.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24550.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 244223By similarityPRO_0000029174Add
    BLAST
    Chaini245 – 1117873A disintegrin and metalloproteinase with thrombospondin motifs 6PRO_0000029175Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi326 ↔ 387By similarity
    Disulfide bondi362 ↔ 369By similarity
    Disulfide bondi381 ↔ 463By similarity
    Disulfide bondi420 ↔ 447By similarity
    Disulfide bondi490 ↔ 512By similarity
    Disulfide bondi501 ↔ 519By similarity
    Disulfide bondi507 ↔ 542By similarity
    Disulfide bondi532 ↔ 547By similarity
    Disulfide bondi570 ↔ 607By similarity
    Disulfide bondi574 ↔ 612By similarity
    Disulfide bondi585 ↔ 597By similarity
    Glycosylationi724 – 7241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi911 ↔ 954By similarity
    Disulfide bondi915 ↔ 959By similarity
    Disulfide bondi926 ↔ 943By similarity
    Glycosylationi956 – 9561N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    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

    PaxDbiQ9UKP5.
    PRIDEiQ9UKP5.

    PTM databases

    PhosphoSiteiQ9UKP5.

    Expressioni

    Tissue specificityi

    Expressed at low levels in placenta and barely detectable in a number of other tissues.

    Inductioni

    Isoform 1 and isoform 2 expressions are up-regulated by TNF in retinal pigment epithelial cells.2 Publications

    Gene expression databases

    ArrayExpressiQ9UKP5.
    BgeeiQ9UKP5.
    CleanExiHS_ADAMTS6.
    GenevestigatoriQ9UKP5.

    Organism-specific databases

    HPAiHPA027216.

    Interactioni

    Protein-protein interaction databases

    BioGridi116345. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKP5.
    SMRiQ9UKP5. Positions 247-729.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini250 – 468219Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini495 – 55763DisintegrinAdd
    BLAST
    Domaini558 – 61356TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini840 – 90061TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini902 – 96059TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini962 – 100746TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1018 – 107356TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1079 – 111739PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni717 – 843127SpacerAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 1 PLAC domain.PROSITE-ProRule annotation
    Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG237764.
    HOGENOMiHOG000004800.
    HOVERGENiHBG004315.
    KOiK08621.
    OMAiNLIIMVL.
    OrthoDBiEOG78WKQV.
    PhylomeDBiQ9UKP5.
    TreeFamiTF313537.

    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.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF08686. PLAC. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 5 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 5 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 5 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKP5-1) [UniParc]FASTAAdd to Basket

    Also known as: Variant 2

    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

    MEILWKTLTW ILSLIMASSE FHSDHRLSYS SQEEFLTYLE HYQLTIPIRV     50
    DQNGAFLSFT VKNDKHSRRR RSMDPIDPQQ AVSKLFFKLS AYGKHFHLNL 100
    TLNTDFVSKH FTVEYWGKDG PQWKHDFLDN CHYTGYLQDQ RSTTKVALSN 150
    CVGLHGVIAT EDEEYFIEPL KNTTEDSKHF SYENGHPHVI YKKSALQQRH 200
    LYDHSHCGVS DFTRSGKPWW LNDTSTVSYS LPINNTHIHH RQKRSVSIER 250
    FVETLVVADK MMVGYHGRKD IEHYILSVMN IVAKLYRDSS LGNVVNIIVA 300
    RLIVLTEDQP NLEINHHADK SLDSFCKWQK SILSHQSDGN TIPENGIAHH 350
    DNAVLITRYD ICTYKNKPCG TLGLASVAGM CEPERSCSIN EDIGLGSAFT 400
    IAHEIGHNFG MNHDGIGNSC GTKGHEAAKL MAAHITANTN PFSWSACSRD 450
    YITSFLDSGR GTCLDNEPPK RDFLYPAVAP GQVYDADEQC RFQYGATSRQ 500
    CKYGEVCREL WCLSKSNRCV TNSIPAAEGT LCQTGNIEKG WCYQGDCVPF 550
    GTWPQSIDGG WGPWSLWGEC SRTCGGGVSS SLRHCDSPAP SGGGKYCLGE 600
    RKRYRSCNTD PCPLGSRDFR EKQCADFDNM PFRGKYYNWK PYTGGGVKPC 650
    ALNCLAEGYN FYTERAPAVI DGTQCNADSL DICINGECKH VGCDNILGSD 700
    AREDRCRVCG GDGSTCDAIE GFFNDSLPRG GYMEVVQIPR GSVHIEVREV 750
    AMSKNYIALK SEGDDYYING AWTIDWPRKF DVAGTAFHYK RPTDEPESLE 800
    ALGPTSENLI VMVLLQEQNL GIRYKFNVPI TRTGSGDNEV GFTWNHQPWS 850
    ECSATCAGGV QRQEVVCKRL DDNSIVQNNY CDPDSKPPEN QRACNTEPCP 900
    PEWFIGDWLE CSKTCDGGMR TRAVLCIRKI GPSEEETLDY SGCLTHRPVE 950
    KEPCNNQSCP PQWVALDWSE CTPKCGPGFK HRIVLCKSSD LSKTFPAAQC 1000
    PEESKPPVRI RCSLGRCPPP RWVTGDWGQC SAQCGLGQQM RTVQCLSYTG 1050
    QASSDCLETV RPPSMQQCES KCDSTPISNT EECKDVNKVA YCPLVLKFKF 1100
    CSRAYFRQMC CKTCQGH 1117
    Length:1,117
    Mass (Da):125,273
    Last modified:May 5, 2009 - v2
    Checksum:i5901E86BC82A9A87
    GO
    Isoform 2 (identifier: Q9UKP5-2) [UniParc]FASTAAdd to Basket

    Also known as: Variant 1

    The sequence of this isoform differs from the canonical sequence as follows:
         422-504: TKGHEAAKLM...GATSRQCKYG → RKVMKQQNYGSSHYCEYQSFFLVCLQSRFHHQLFR
         860-908: VQRQEVVCKR...CPPEWFIGDW → KMPTRQPTQR...SCNLAKETLL
         909-1117: Missing.

    Note: Contains critical point mutations in the region encoding the catalytic domain as well as 2 point mutations compared with genomic sequence. May either be a rare polymorphism or may have arisen through a combination of aberrant RNA editing and point mutation/sequencing error.

    Show »
    Length:860
    Mass (Da):97,152
    Checksum:iEA137275B9A465C2
    GO
    Isoform 3 (identifier: Q9UKP5-3) [UniParc]FASTAAdd to Basket

    Also known as: Variant 3

    The sequence of this isoform differs from the canonical sequence as follows:
         457-468: DSGRGTCLDNEP → EFLKLGDSISGS
         469-1117: Missing.

    Show »
    Length:468
    Mass (Da):53,165
    Checksum:iE8D2E75EF8A1C468
    GO
    Isoform 4 (identifier: Q9UKP5-4) [UniParc]FASTAAdd to Basket

    Also known as: Variant 4

    The sequence of this isoform differs from the canonical sequence as follows:
         283-292: AKLYRDSSLG → RLPNFTVIPA
         293-1117: Missing.

    Show »
    Length:292
    Mass (Da):34,189
    Checksum:i01A54680DCEFABD7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41L → S in AAW47399. (PubMed:16129570)Curated
    Sequence conflicti24 – 241D → G in AAW47398. (PubMed:16129570)Curated
    Sequence conflicti83 – 831S → P in AAW47398. (PubMed:16129570)Curated
    Sequence conflicti229 – 2291Y → H in AAW47397. (PubMed:16129570)Curated
    Sequence conflicti406 – 4061G → V in AAD56357. (PubMed:10464288)Curated
    Sequence conflicti426 – 4261E → G in AAD56357. (PubMed:10464288)Curated
    Sequence conflicti426 – 4261E → G in AAW47397. (PubMed:16129570)Curated
    Sequence conflicti588 – 5892PA → LK in BAD92922. 1 PublicationCurated
    Sequence conflicti712 – 7121D → G in AAD56357. (PubMed:10464288)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei283 – 29210AKLYRDSSLG → RLPNFTVIPA in isoform 4. 1 PublicationVSP_037093
    Alternative sequencei293 – 1117825Missing in isoform 4. 1 PublicationVSP_037094Add
    BLAST
    Alternative sequencei422 – 50483TKGHE…QCKYG → RKVMKQQNYGSSHYCEYQSF FLVCLQSRFHHQLFR in isoform 2. 1 PublicationVSP_037095Add
    BLAST
    Alternative sequencei457 – 46812DSGRG…LDNEP → EFLKLGDSISGS in isoform 3. 1 PublicationVSP_037096Add
    BLAST
    Alternative sequencei469 – 1117649Missing in isoform 3. 1 PublicationVSP_037097Add
    BLAST
    Alternative sequencei860 – 90849VQRQE…FIGDW → KMPTRQPTQRARWRTKHILS YALCLLKKLIGNISCRFASS CNLAKETLL in isoform 2. 1 PublicationVSP_037098Add
    BLAST
    Alternative sequencei909 – 1117209Missing in isoform 2. 1 PublicationVSP_037099Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF140674 mRNA. Translation: AAD56357.1.
    AY692424 mRNA. Translation: AAW47397.1.
    AY692425 mRNA. Translation: AAW47398.1.
    AY692426 mRNA. Translation: AAW47399.1.
    AC008847 Genomic DNA. No translation available.
    AC008868 Genomic DNA. No translation available.
    AC025176 Genomic DNA. No translation available.
    AC025186 Genomic DNA. No translation available.
    AC099505 Genomic DNA. No translation available.
    AB209685 mRNA. Translation: BAD92922.1.
    CR749356 mRNA. Translation: CAH18209.1.
    CCDSiCCDS3983.2. [Q9UKP5-1]
    RefSeqiNP_922932.2. NM_197941.2. [Q9UKP5-1]
    UniGeneiHs.482291.

    Genome annotation databases

    EnsembliENST00000381052; ENSP00000424377; ENSG00000049192. [Q9UKP5-4]
    ENST00000381055; ENSP00000370443; ENSG00000049192. [Q9UKP5-1]
    GeneIDi11174.
    KEGGihsa:11174.
    UCSCiuc003jto.4. human. [Q9UKP5-1]

    Polymorphism databases

    DMDMi229462816.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF140674 mRNA. Translation: AAD56357.1 .
    AY692424 mRNA. Translation: AAW47397.1 .
    AY692425 mRNA. Translation: AAW47398.1 .
    AY692426 mRNA. Translation: AAW47399.1 .
    AC008847 Genomic DNA. No translation available.
    AC008868 Genomic DNA. No translation available.
    AC025176 Genomic DNA. No translation available.
    AC025186 Genomic DNA. No translation available.
    AC099505 Genomic DNA. No translation available.
    AB209685 mRNA. Translation: BAD92922.1 .
    CR749356 mRNA. Translation: CAH18209.1 .
    CCDSi CCDS3983.2. [Q9UKP5-1 ]
    RefSeqi NP_922932.2. NM_197941.2. [Q9UKP5-1 ]
    UniGenei Hs.482291.

    3D structure databases

    ProteinModelPortali Q9UKP5.
    SMRi Q9UKP5. Positions 247-729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116345. 2 interactions.

    Protein family/group databases

    MEROPSi M12.230.

    PTM databases

    PhosphoSitei Q9UKP5.

    Polymorphism databases

    DMDMi 229462816.

    Proteomic databases

    PaxDbi Q9UKP5.
    PRIDEi Q9UKP5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381052 ; ENSP00000424377 ; ENSG00000049192 . [Q9UKP5-4 ]
    ENST00000381055 ; ENSP00000370443 ; ENSG00000049192 . [Q9UKP5-1 ]
    GeneIDi 11174.
    KEGGi hsa:11174.
    UCSCi uc003jto.4. human. [Q9UKP5-1 ]

    Organism-specific databases

    CTDi 11174.
    GeneCardsi GC05M064526.
    HGNCi HGNC:222. ADAMTS6.
    HPAi HPA027216.
    MIMi 605008. gene.
    neXtProti NX_Q9UKP5.
    PharmGKBi PA24550.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237764.
    HOGENOMi HOG000004800.
    HOVERGENi HBG004315.
    KOi K08621.
    OMAi NLIIMVL.
    OrthoDBi EOG78WKQV.
    PhylomeDBi Q9UKP5.
    TreeFami TF313537.

    Enzyme and pathway databases

    Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    GenomeRNAii 11174.
    NextBioi 42521.
    PROi Q9UKP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKP5.
    Bgeei Q9UKP5.
    CleanExi HS_ADAMTS6.
    Genevestigatori Q9UKP5.

    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.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF08686. PLAC. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 5 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 5 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 5 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
      Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
      J. Biol. Chem. 274:25555-25563(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Analysis of full length ADAMTS6 transcript reveals alternative splicing and a role for the 5' untranslated region in translational control."
      Bevitt D.J., Li Z., Lindrop J.L., Barker M.D., Clarke M.P., McKie N.
      Gene 359:99-110(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), INDUCTION.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1117 (ISOFORM 1).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 804-1117 (ISOFORM 1).
      Tissue: Uterus.
    6. "Expression of ADAMTS metalloproteinases in the retinal pigment epithelium derived cell line ARPE-19: transcriptional regulation by TNFalpha."
      Bevitt D.J., Mohamed J., Catterall J.B., Li Z., Arris C.E., Hiscott P., Sheridan C., Langton K.P., Barker M.D., Clarke M.P., McKie N.
      Biochim. Biophys. Acta 1626:83-91(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiATS6_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKP5
    Secondary accession number(s): Q59EX6
    , Q5IR87, Q5IR88, Q5IR89, Q68DL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 133 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3