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Q9UNA0

- ATS5_HUMAN

UniProt

Q9UNA0 - ATS5_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

ADAMTS5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (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. May play a role in proteolytic processing mostly during the peri-implantation period.

    Catalytic activityi

    Cleaves aggrecan at the 392-Glu-|-Ala-393 site.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi209 – 2091Zinc; in inhibited formBy similarity
    Metal bindingi410 – 4101Zinc; catalytic
    Active sitei411 – 41111 PublicationPROSITE-ProRule annotation
    Metal bindingi414 – 4141Zinc; catalytic
    Metal bindingi420 – 4201Zinc; catalytic

    GO - Molecular functioni

    1. integrin binding Source: ProtInc
    2. metalloendopeptidase activity Source: InterPro
    3. metallopeptidase activity Source: ProtInc
    4. protein binding Source: IntAct
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. extracellular matrix disassembly Source: Reactome
    2. extracellular matrix organization Source: Reactome
    3. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    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

    MEROPSiM12.225.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 5 (EC:3.4.24.-)
    Short name:
    ADAM-TS 5
    Short name:
    ADAM-TS5
    Short name:
    ADAMTS-5
    Alternative name(s):
    A disintegrin and metalloproteinase with thrombospondin motifs 11
    Short name:
    ADAM-TS 11
    Short name:
    ADAMTS-11
    ADMP-2
    Aggrecanase-2
    Gene namesi
    Name:ADAMTS5
    Synonyms:ADAMTS11, ADMP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:221. ADAMTS5.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 261245Sequence AnalysisPRO_0000029170Add
    BLAST
    Chaini262 – 930669A disintegrin and metalloproteinase with thrombospondin motifs 5PRO_0000029171Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi342 ↔ 3941 Publication
    Disulfide bondi371 ↔ 3761 Publication
    Disulfide bondi388 ↔ 4711 Publication
    Disulfide bondi426 ↔ 4551 Publication
    Disulfide bondi497 ↔ 5191 Publication
    Glycosylationi498 – 4981N-linked (GlcNAc...)1 Publication
    Disulfide bondi508 ↔ 5291 Publication
    Disulfide bondi514 ↔ 5481 Publication
    Disulfide bondi542 ↔ 5531 Publication
    Glycosylationi570 – 5701C-linked (Man)
    Glycosylationi573 – 5731C-linked (Man)
    Disulfide bondi579 ↔ 616By similarity
    Glycosylationi582 – 5821O-linked (Fuc...)1 Publication
    Disulfide bondi583 ↔ 621By similarity
    Disulfide bondi594 ↔ 606By similarity
    Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi802 – 8021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    C- and O-glycosylated. 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 can mediate the efficient secretion of ADAMTS family members. 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
    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

    PaxDbiQ9UNA0.
    PRIDEiQ9UNA0.

    PTM databases

    PhosphoSiteiQ9UNA0.

    Miscellaneous databases

    PMAP-CutDBQ9UNA0.

    Expressioni

    Tissue specificityi

    Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.

    Gene expression databases

    BgeeiQ9UNA0.
    CleanExiHS_ADAMTS5.
    GenevestigatoriQ9UNA0.

    Organism-specific databases

    HPAiCAB025996.
    HPA005661.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACANP136082EBI-2808663,EBI-6259246From a different organism.

    Protein-protein interaction databases

    BioGridi116277. 1 interaction.
    IntActiQ9UNA0. 3 interactions.
    STRINGi9606.ENSP00000284987.

    Structurei

    Secondary structure

    1
    930
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi267 – 2759
    Helixi277 – 2837
    Helixi284 – 2863
    Helixi287 – 30216
    Helixi305 – 3073
    Beta strandi311 – 32010
    Turni323 – 3264
    Helixi334 – 34815
    Beta strandi353 – 3564
    Beta strandi360 – 3689
    Beta strandi380 – 3823
    Helixi390 – 3923
    Beta strandi394 – 3985
    Beta strandi401 – 4033
    Helixi404 – 41512
    Helixi424 – 4307
    Beta strandi435 – 4373
    Beta strandi440 – 4423
    Helixi443 – 4453
    Helixi454 – 46512
    Turni466 – 4694
    Helixi470 – 4723
    Helixi487 – 4904
    Helixi493 – 5019
    Beta strandi509 – 5113
    Turni513 – 5153
    Beta strandi519 – 5235
    Beta strandi526 – 5305
    Beta strandi543 – 5453
    Beta strandi547 – 5493
    Beta strandi552 – 5543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RJQX-ray2.60A262-628[»]
    3B8ZX-ray1.40A/B264-480[»]
    3HY7X-ray1.69A/B262-480[»]
    3HY9X-ray2.02A/B262-480[»]
    3HYGX-ray1.40A/B262-480[»]
    3LJTX-ray1.60A264-480[»]
    ProteinModelPortaliQ9UNA0.
    SMRiQ9UNA0. Positions 259-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UNA0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini267 – 476210Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini485 – 56682DisintegrinAdd
    BLAST
    Domaini567 – 62256TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini875 – 92955TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni732 – 874143SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi207 – 2148Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi37 – 415Poly-Ala
    Compositional biasi257 – 2615Poly-Arg
    Compositional biasi624 – 731108Cys-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 2 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG302522.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiQ9UNA0.
    KOiK08620.
    OMAiRASCETP.
    OrthoDBiEOG7WDN1M.
    PhylomeDBiQ9UNA0.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013276. Pept_M12B_ADAM-TS5.
    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. 2 hits.
    [Graphical view]
    PRINTSiPR01860. ADAMTS5.
    PR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 2 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 2 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UNA0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLGWASLLL CAFRLPLAAV GPAATPAQDK AGQPPTAAAA AQPRRRQGEE    50
    VQERAEPPGH PHPLAQRRRS KGLVQNIDQL YSGGGKVGYL VYAGGRRFLL 100
    DLERDGSVGI AGFVPAGGGT SAPWRHRSHC FYRGTVDGSP RSLAVFDLCG 150
    GLDGFFAVKH ARYTLKPLLR GPWAEEEKGR VYGDGSARIL HVYTREGFSF 200
    EALPPRASCE TPASTPEAHE HAPAHSNPSG RAALASQLLD QSALSPAGGS 250
    GPQTWWRRRR RSISRARQVE LLLVADASMA RLYGRGLQHY LLTLASIANR 300
    LYSHASIENH IRLAVVKVVV LGDKDKSLEV SKNAATTLKN FCKWQHQHNQ 350
    LGDDHEEHYD AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD 400
    GLHAAFTVAH EIGHLLGLSH DDSKFCEETF GSTEDKRLMS SILTSIDASK 450
    PWSKCTSATI TEFLDDGHGN CLLDLPRKQI LGPEELPGQT YDATQQCNLT 500
    FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT PCGKGRICLQ 550
    GKCVDKTKKK YYSTSSHGNW GSWGSWGQCS RSCGGGVQFA YRHCNNPAPR 600
    NNGRYCTGKR AIYRSCSLMP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV 650
    EWVPKYAGVL PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RLYSNSVCVR 700
    GKCVRTGCDG IIGSKLQYDK CGVCGGDNSS CTKIVGTFNK KSKGYTDVVR 750
    IPEGATHIKV RQFKAKDQTR FTAYLALKKK NGEYLINGKY MISTSETIID 800
    INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT KPLDVRYSFF 850
    VPKKSTPKVN SVTSHGSNKV GSHTSQPQWV TGPWLACSRT CDTGWHTRTV 900
    QCQDGNRKLA KGCPLSQRPS AFKQCLLKKC 930
    Length:930
    Mass (Da):101,718
    Last modified:January 11, 2011 - v2
    Checksum:i8CCE448A15A29CE8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381G → A.2 Publications
    Corresponds to variant rs457947 [ dbSNP | Ensembl ].
    VAR_028199
    Natural varianti614 – 6141R → H.1 Publication
    Corresponds to variant rs2830585 [ dbSNP | Ensembl ].
    VAR_021849
    Natural varianti692 – 6921L → P.3 Publications
    Corresponds to variant rs226794 [ dbSNP | Ensembl ].
    VAR_028200

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF142099 mRNA. Translation: AAD49577.1.
    AP001698 Genomic DNA. Translation: BAA95504.1.
    AP001697 Genomic DNA. Translation: BAA95503.1.
    BC093775 mRNA. Translation: AAH93775.1.
    BC093777 mRNA. Translation: AAH93777.1.
    AF141293 mRNA. Translation: AAF02493.1.
    CCDSiCCDS13579.1.
    RefSeqiNP_008969.2. NM_007038.3.
    UniGeneiHs.58324.

    Genome annotation databases

    EnsembliENST00000284987; ENSP00000284987; ENSG00000154736.
    GeneIDi11096.
    KEGGihsa:11096.
    UCSCiuc002ymg.3. human.

    Polymorphism databases

    DMDMi317373326.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF142099 mRNA. Translation: AAD49577.1 .
    AP001698 Genomic DNA. Translation: BAA95504.1 .
    AP001697 Genomic DNA. Translation: BAA95503.1 .
    BC093775 mRNA. Translation: AAH93775.1 .
    BC093777 mRNA. Translation: AAH93777.1 .
    AF141293 mRNA. Translation: AAF02493.1 .
    CCDSi CCDS13579.1.
    RefSeqi NP_008969.2. NM_007038.3.
    UniGenei Hs.58324.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RJQ X-ray 2.60 A 262-628 [» ]
    3B8Z X-ray 1.40 A/B 264-480 [» ]
    3HY7 X-ray 1.69 A/B 262-480 [» ]
    3HY9 X-ray 2.02 A/B 262-480 [» ]
    3HYG X-ray 1.40 A/B 262-480 [» ]
    3LJT X-ray 1.60 A 264-480 [» ]
    ProteinModelPortali Q9UNA0.
    SMRi Q9UNA0. Positions 259-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116277. 1 interaction.
    IntActi Q9UNA0. 3 interactions.
    STRINGi 9606.ENSP00000284987.

    Chemistry

    BindingDBi Q9UNA0.
    ChEMBLi CHEMBL2285.

    Protein family/group databases

    MEROPSi M12.225.

    PTM databases

    PhosphoSitei Q9UNA0.

    Polymorphism databases

    DMDMi 317373326.

    Proteomic databases

    PaxDbi Q9UNA0.
    PRIDEi Q9UNA0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284987 ; ENSP00000284987 ; ENSG00000154736 .
    GeneIDi 11096.
    KEGGi hsa:11096.
    UCSCi uc002ymg.3. human.

    Organism-specific databases

    CTDi 11096.
    GeneCardsi GC21M028290.
    H-InvDB HIX0016044.
    HGNCi HGNC:221. ADAMTS5.
    HPAi CAB025996.
    HPA005661.
    MIMi 605007. gene.
    neXtProti NX_Q9UNA0.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG302522.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi Q9UNA0.
    KOi K08620.
    OMAi RASCETP.
    OrthoDBi EOG7WDN1M.
    PhylomeDBi Q9UNA0.
    TreeFami TF331949.

    Enzyme and pathway databases

    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

    EvolutionaryTracei Q9UNA0.
    GeneWikii ADAMTS5.
    GenomeRNAii 11096.
    NextBioi 42182.
    PMAP-CutDB Q9UNA0.
    PROi Q9UNA0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UNA0.
    CleanExi HS_ADAMTS5.
    Genevestigatori Q9UNA0.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013276. Pept_M12B_ADAM-TS5.
    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. 2 hits.
    [Graphical view ]
    PRINTSi PR01860. ADAMTS5.
    PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 2 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-138 AND PRO-692.
      Tissue: Liver.
    2. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 ALA-138 AND PRO-692.
      Tissue: Colon.
    4. "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] OF 413-930, VARIANTS HIS-614 AND PRO-692.
      Tissue: Fetal brain.
    5. "Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan."
      Wang L.W., Leonhard-Melief C., Haltiwanger R.S., Apte S.S.
      J. Biol. Chem. 284:30004-30015(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT TRP-570; TRP-573 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 262-628 IN COMPLEX WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, DISULFIDE BONDS, GLYCOSYLATION AT ASN-498.

    Entry informationi

    Entry nameiATS5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNA0
    Secondary accession number(s): Q52LV4, Q9UKP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 146 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 21
      Human chromosome 21: 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