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P59510

- ATS20_HUMAN

UniProt

P59510 - ATS20_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 20

Gene

ADAMTS20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    May play a role in tissue-remodeling process occurring in both normal and pathological conditions. May have a protease-independent function in the transport from the endoplasmic reticulum to the Golgi apparatus of secretory cargos, mediated by the GON domain.

    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: Ensembl
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. extracellular matrix organization Source: Ensembl
    2. negative regulation of apoptotic process Source: Ensembl
    3. positive regulation of melanocyte differentiation Source: Ensembl
    4. positive regulation of signal transduction Source: Ensembl

    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

    MEROPSiM12.246.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 20 (EC:3.4.24.-)
    Short name:
    ADAM-TS 20
    Short name:
    ADAM-TS20
    Short name:
    ADAMTS-20
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:17178. ADAMTS20.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134901626.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 253232By similarityPRO_0000029206Add
    BLAST
    Chaini254 – 19101657A disintegrin and metalloproteinase with thrombospondin motifs 20PRO_0000029207Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi334 ↔ 387By similarity
    Disulfide bondi363 ↔ 369By similarity
    Disulfide bondi381 ↔ 462By similarity
    Disulfide bondi419 ↔ 446By similarity
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi489 ↔ 511By similarity
    Disulfide bondi500 ↔ 521By similarity
    Disulfide bondi506 ↔ 540By similarity
    Disulfide bondi534 ↔ 545By similarity
    Disulfide bondi568 ↔ 605By similarity
    Disulfide bondi572 ↔ 610By similarity
    Disulfide bondi583 ↔ 595By similarity
    Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi809 – 8091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi870 – 8701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1061 – 10611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1456 – 14561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1542 – 15421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1572 – 15721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1781 – 17811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1852 – 18521N-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

    PaxDbiP59510.
    PRIDEiP59510.

    PTM databases

    PhosphoSiteiP59510.

    Expressioni

    Tissue specificityi

    Very sparingly expressed, although is detected at low levels in testis, prostate, ovary, heart, placenta, lung and pancreas. Overexpressed in several brain, colon and breast carcinomas.

    Gene expression databases

    BgeeiP59510.
    CleanExiHS_ADAMTS20.
    GenevestigatoriP59510.

    Organism-specific databases

    HPAiHPA027608.
    HPA027609.

    Interactioni

    Protein-protein interaction databases

    IntActiP59510. 1 interaction.
    STRINGi9606.ENSP00000374071.

    Structurei

    3D structure databases

    ProteinModelPortaliP59510.
    SMRiP59510. Positions 259-729.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini259 – 467209Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini468 – 55588DisintegrinAdd
    BLAST
    Domaini556 – 61156TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini846 – 90459TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini905 – 96157TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini966 – 102358TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1024 – 107350TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1076 – 113560TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1152 – 120655TSP type-1 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1207 – 126458TSP type-1 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1304 – 135653TSP type-1 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1358 – 141659TSP type-1 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1417 – 147559TSP type-1 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1476 – 153156TSP type-1 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1535 – 158854TSP type-1 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1589 – 165264TSP type-1 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1654 – 171057TSP type-1 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1711 – 1910200GONPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni724 – 846123SpacerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi612 – 723112Cys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 GON domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 15 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG237764.
    HOGENOMiHOG000004798.
    HOVERGENiHBG037334.
    InParanoidiP59510.
    KOiK09609.
    OMAiPWGPYSS.
    OrthoDBiEOG7WDN1M.
    PhylomeDBiP59510.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR012314. Pept_M12B_GON-ADAMTSs.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF08685. GON. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 11 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 13 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 12 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS51046. GON. 1 hit.
    PS50092. TSP1. 12 hits.
    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. Align

    Isoform 1 (identifier: P59510-1) [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

    MWVAKWLTGL LYHLSLFITR SWEVDFHPRQ EALVRTLTSY EVVIPERVNE     50
    FGEVFPQSHH FSRQKRSSEA LEPMPFRTHY RFTAYGQLFQ LNLTADASFL 100
    AAGYTEVHLG TPERGAWESD AGPSDLRHCF YRGQVNSQED YKAVVSLCGG 150
    LTGTFKGQNG EYFLEPIMKA DGNEYEDGHN KPHLIYRQDL NNSFLQTLKY 200
    CSVSESQIKE TSLPFHTYSN MNEDLNVMKE RVLGHTSKNV PLKDERRHSR 250
    KKRLISYPRY IEIMVTADAK VVSAHGSNLQ NYILTLMSIV ATIYKDPSIG 300
    NLIHIVVVKL VMIHREEEGP VINFDGATTL KNFCSWQQTQ NDLDDVHPSH 350
    HDTAVLITRE DICSSKEKCN MLGLSYLGTI CDPLQSCFIN EEKGLISAFT 400
    IAHELGHTLG VQHDDNPRCK EMKVTKYHVM APALSFHMSP WSWSNCSRKY 450
    VTEFLDTGYG ECLLDKPDEE IYNLPSELPG SRYDGNKQCE LAFGPGSQMC 500
    PHINICMHLW CTSTEKLHKG CFTQHVPPAD GTDCGPGMHC RHGLCVNKET 550
    ETRPVNGEWG PWEPYSSCSR TCGGGIESAT RRCNRPEPRN GGNYCVGRRM 600
    KFRSCNTDSC PKGTQDFREK QCSDFNGKHL DISGIPSNVR WLPRYSGIGT 650
    KDRCKLYCQV AGTNYFYLLK DMVEDGTPCG TETHDICVQG QCMAAGCDHV 700
    LNSSAKIDKC GVCGGDNSSC KTITGVFNSS HYGYNVVVKI PAGATNVDIR 750
    QYSYSGQPDD SYLALSDAEG NFLFNGNFLL STSKKEINVQ GTRTVIEYSG 800
    SNNAVERINS TNRQEKEILI EVLCVGNLYN PDVHYSFNIP LEERSDMFTW 850
    DPYGPWEGCT KMCQGLQRRN ITCIHKSDHS VVSDKECDHL PLPSFVTQSC 900
    NTDCELRWHV IGKSECSSQC GQGYRTLDIH CMKYSIHEGQ TVQVDDHYCG 950
    DQLKPPTQEL CHGNCVFTRW HYSEWSQCSR SCGGGERSRE SYCMNNFGHR 1000
    LADNECQELS RVTRENCNEF SCPSWAASEW SECLVTCGKG TKQRQVWCQL 1050
    NVDHLSDGFC NSSTKPESLS PCELHTCASW QVGPWGPCTT TCGHGYQMRD 1100
    VKCVNELASA VLEDTECHEA SRPSDRQSCV LTPCSFISKL ETALLPTVLI 1150
    KKMAQWRHGS WTPCSVSCGR GTQARYVSCR DALDRIADES YCAHLPRPAE 1200
    IWDCFTPCGE WQAGDWSPCS ASCGHGKTTR QVLCMNYHQP IDENYCDPEV 1250
    RPLMEQECSL AACPPAHSHF PSSPVQPSYY LSTNLPLTQK LEDNENQVVH 1300
    PSVRGNQWRT GPWGSCSSSC SGGLQHRAVV CQDENGQSAS YCDAASKPPE 1350
    LQQCGPGPCP QWNYGNWGEC SQTCGGGIKS RLVICQFPNG QILEDHNCEI 1400
    VNKPPSVIQC HMHACPADVS WHQEPWTSCS ASCGKGRKYR EVFCIDQFQR 1450
    KLEDTNCSQV QKPPTHKACR SVRCPSWKAN SWNECSVTCG SGVQQRDVYC 1500
    RLKGVGQVVE EMCDQSTRPC SQRRCWSQDC VQHKGMERGR LNCSTSCERK 1550
    DSHQRMECTD NQIRQVNEIV YNSSTISLTS KNCRNPPCNY IVVTADSSQC 1600
    ANNCGFSYRQ RITYCTEIPS TKKHKLHRLR PIVYQECPVV PSSQVYQCIN 1650
    SCLHLATWKV GKWSKCSVTC GIGIMKRQVK CITKHGLSSD LCLNHLKPGA 1700
    QKKCYANDCK SFTTCKEIQV KNHIRKDGDY YLNIKGRIIK IYCADMYLEN 1750
    PKEYLTLVQG EENFSEVYGF RLKNPYQCPF NGSRREDCEC DNGHLAAGYT 1800
    VFSKIRIDLT SMQIKTTDLL FSKTIFGNAV PFATAGDCYS AFRCPQGQFS 1850
    INLSGTGMKI SSTAKWLTQG SYTSVSIRRS EDGTRFFGKC GGYCGKCLPH 1900
    MTTGLPIQVI 1910
    Length:1,910
    Mass (Da):214,721
    Last modified:December 16, 2008 - v2
    Checksum:iD7FFCB0D56F4B6D9
    GO
    Isoform 2 (identifier: P59510-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         683-693: THDICVQGQCM → SYNIDCNCVLK
         1429-1504: CSASCGKGRK...QRDVYCRLKG → EDLKVKLLPQ...GDLKYYKNSL
         1505-1910: Missing.

    Show »
    Length:1,504
    Mass (Da):169,506
    Checksum:i2F9D75248EE885DF
    GO
    Isoform 3 (identifier: P59510-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         818-821: ILIE → LILQ

    Show »
    Length:1,910
    Mass (Da):214,720
    Checksum:i93AA3B0AC1B9C6D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521T → V in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti152 – 1521T → V in CAD56160. (PubMed:12562771)Curated
    Sequence conflicti360 – 3601E → Y in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti360 – 3601E → Y in CAD56160. (PubMed:12562771)Curated
    Sequence conflicti371 – 3711M → T in AAO15766. (PubMed:12514189)Curated
    Sequence conflicti456 – 4561D → E in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti456 – 4561D → E in CAD56160. (PubMed:12562771)Curated
    Sequence conflicti648 – 6481I → V in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti648 – 6481I → V in CAD56160. (PubMed:12562771)Curated
    Sequence conflicti792 – 7932Missing in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti792 – 7932Missing in CAD56160. (PubMed:12562771)Curated
    Sequence conflicti908 – 9125WHVIG → GMLLAK in AAO15766. (PubMed:12514189)Curated
    Sequence conflicti1315 – 13151S → Q in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti1315 – 13151S → Q in CAD56160. (PubMed:12562771)Curated
    Sequence conflicti1327 – 13271R → T in AAO15766. (PubMed:12514189)Curated
    Sequence conflicti1816 – 18161T → A in CAD56159. (PubMed:12562771)Curated
    Sequence conflicti1881 – 18811E → Q in CAD56159. (PubMed:12562771)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti876 – 8761K → M.
    Corresponds to variant rs7302446 [ dbSNP | Ensembl ].
    VAR_057088
    Natural varianti1000 – 10001R → H.
    Corresponds to variant rs7297737 [ dbSNP | Ensembl ].
    VAR_057089
    Natural varianti1273 – 12731S → F.
    Corresponds to variant rs7310011 [ dbSNP | Ensembl ].
    VAR_057090

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei683 – 69311THDICVQGQCM → SYNIDCNCVLK in isoform 2. 1 PublicationVSP_007106Add
    BLAST
    Alternative sequencei818 – 8214ILIE → LILQ in isoform 3. 1 PublicationVSP_047084
    Alternative sequencei1429 – 150476CSASC…CRLKG → EDLKVKLLPQRTIILWELMK NIFCHGKHSHMYLINVVTDH LLYPRHCDPETIETYFLSLW SLQFTWGDLKYYKNSL in isoform 2. 1 PublicationVSP_007107Add
    BLAST
    Alternative sequencei1505 – 1910406Missing in isoform 2. 1 PublicationVSP_007108Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF488804 mRNA. Translation: AAO15766.1.
    AJ515153 mRNA. Translation: CAD56159.3.
    AJ515154 mRNA. Translation: CAD56160.2.
    AC090525 Genomic DNA. No translation available.
    AC107018 Genomic DNA. No translation available.
    AC120104 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57861.1.
    CCDSiCCDS31778.2. [P59510-3]
    RefSeqiNP_079279.3. NM_025003.3.
    UniGeneiHs.287554.

    Genome annotation databases

    EnsembliENST00000389420; ENSP00000374071; ENSG00000173157. [P59510-3]
    GeneIDi80070.
    KEGGihsa:80070.
    UCSCiuc010skx.2. human.

    Polymorphism databases

    DMDMi218511943.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF488804 mRNA. Translation: AAO15766.1 .
    AJ515153 mRNA. Translation: CAD56159.3 .
    AJ515154 mRNA. Translation: CAD56160.2 .
    AC090525 Genomic DNA. No translation available.
    AC107018 Genomic DNA. No translation available.
    AC120104 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57861.1 .
    CCDSi CCDS31778.2. [P59510-3 ]
    RefSeqi NP_079279.3. NM_025003.3.
    UniGenei Hs.287554.

    3D structure databases

    ProteinModelPortali P59510.
    SMRi P59510. Positions 259-729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P59510. 1 interaction.
    STRINGi 9606.ENSP00000374071.

    Protein family/group databases

    MEROPSi M12.246.

    PTM databases

    PhosphoSitei P59510.

    Polymorphism databases

    DMDMi 218511943.

    Proteomic databases

    PaxDbi P59510.
    PRIDEi P59510.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389420 ; ENSP00000374071 ; ENSG00000173157 . [P59510-3 ]
    GeneIDi 80070.
    KEGGi hsa:80070.
    UCSCi uc010skx.2. human.

    Organism-specific databases

    CTDi 80070.
    GeneCardsi GC12M043715.
    HGNCi HGNC:17178. ADAMTS20.
    HPAi HPA027608.
    HPA027609.
    MIMi 611681. gene.
    neXtProti NX_P59510.
    PharmGKBi PA134901626.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237764.
    HOGENOMi HOG000004798.
    HOVERGENi HBG037334.
    InParanoidi P59510.
    KOi K09609.
    OMAi PWGPYSS.
    OrthoDBi EOG7WDN1M.
    PhylomeDBi P59510.
    TreeFami TF331949.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GenomeRNAii 80070.
    NextBioi 35537418.
    PROi P59510.
    SOURCEi Search...

    Gene expression databases

    Bgeei P59510.
    CleanExi HS_ADAMTS20.
    Genevestigatori P59510.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR012314. Pept_M12B_GON-ADAMTSs.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF08685. GON. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 11 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 13 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 12 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS51046. GON. 1 hit.
    PS50092. TSP1. 12 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
      Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
      J. Biol. Chem. 278:9503-9513(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. "Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain."
      Llamazares M., Cal S., Quesada V., Lopez-Otin C.
      J. Biol. Chem. 278:13382-13389(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Liver.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiATS20_HUMAN
    AccessioniPrimary (citable) accession number: P59510
    Secondary accession number(s): A6NNC9, J3QT00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2003
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 118 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 12
      Human chromosome 12: 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

    External Data

    Dasty 3