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P35625

- TIMP3_HUMAN

UniProt

P35625 - TIMP3_HUMAN

Protein

Metalloproteinase inhibitor 3

Gene

TIMP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi24 – 241Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase inhibitor activity Source: BHF-UCL
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to organic substance Source: Ensembl
    2. negative regulation of endopeptidase activity Source: GOC
    3. negative regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
    4. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

    Keywords - Biological processi

    Sensory transduction, Vision

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metalloproteinase inhibitor 3
    Alternative name(s):
    Protein MIG-5
    Tissue inhibitor of metalloproteinases 3
    Short name:
    TIMP-3
    Gene namesi
    Name:TIMP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11822. TIMP3.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Sorsby fundus dystrophy (SFD) [MIM:136900]: Rare autosomal dominant macular disorder with an age of onset in the fourth decade. It is characterized by loss of central vision from subretinal neovascularization and atrophy of the ocular tissues. Generally, macular disciform degeneration develops in the patients eye within 6 months to 6 years.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791S → C in SFD. 1 Publication
    VAR_007508
    Natural varianti189 – 1891G → C in SFD. 1 Publication
    VAR_008290
    Natural varianti190 – 1901G → C in SFD. 1 Publication
    VAR_010901
    Natural varianti191 – 1911Y → C in SFD. 2 Publications
    VAR_007509
    Natural varianti204 – 2041S → C in SFD. 1 Publication
    VAR_007510

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi136900. phenotype.
    Orphaneti59181. Sorsby's fundus dystrophy.
    PharmGKBiPA36528.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 211188Metalloproteinase inhibitor 3PRO_0000034341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 911 PublicationPROSITE-ProRule annotation
    Disulfide bondi26 ↔ 1181 PublicationPROSITE-ProRule annotation
    Disulfide bondi36 ↔ 1431 PublicationPROSITE-ProRule annotation
    Disulfide bondi145 ↔ 192PROSITE-ProRule annotation
    Disulfide bondi150 ↔ 155PROSITE-ProRule annotation
    Disulfide bondi163 ↔ 184PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP35625.
    PaxDbiP35625.
    PRIDEiP35625.

    PTM databases

    PhosphoSiteiP35625.

    Expressioni

    Gene expression databases

    BgeeiP35625.
    CleanExiHS_TIMP3.
    GenevestigatoriP35625.

    Organism-specific databases

    HPAiCAB022187.

    Interactioni

    Subunit structurei

    Interacts with EFEMP1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGTR2P500527EBI-1748085,EBI-1748067

    Protein-protein interaction databases

    BioGridi112934. 3 interactions.
    IntActiP35625. 2 interactions.
    STRINGi9606.ENSP00000266085.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 377
    Beta strandi39 – 424
    Beta strandi45 – 528
    Beta strandi55 – 573
    Beta strandi59 – 657
    Beta strandi69 – 713
    Turni73 – 753
    Beta strandi76 – 783
    Beta strandi81 – 866
    Helixi88 – 903
    Beta strandi102 – 1087
    Turni124 – 1263
    Helixi129 – 1368
    Turni137 – 1404

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CKIX-ray2.30B24-144[»]
    ProteinModelPortaliP35625.
    SMRiP35625. Positions 24-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35625.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 143120NTRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 285Involved in metalloproteinase-binding
    Regioni88 – 892Involved in metalloproteinase-binding
    Regioni105 – 18884Mediates interaction with EFEMP1Add
    BLAST

    Sequence similaritiesi

    Contains 1 NTR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250837.
    HOGENOMiHOG000285981.
    HOVERGENiHBG068749.
    InParanoidiP35625.
    KOiK16866.
    OMAiKEGYCSW.
    OrthoDBiEOG79GT74.
    PhylomeDBiP35625.
    TreeFamiTF317409.

    Family and domain databases

    Gene3Di3.90.370.10. 1 hit.
    InterProiIPR001134. Netrin_domain.
    IPR001820. Prot_inh_TIMP.
    IPR008993. TIMP-like_OB-fold.
    IPR027465. TIMP_C_dom.
    IPR015612. Tissue_inhib_metalloprotease_3.
    [Graphical view]
    PANTHERiPTHR11844. PTHR11844. 1 hit.
    PTHR11844:SF6. PTHR11844:SF6. 1 hit.
    PfamiPF00965. TIMP. 1 hit.
    [Graphical view]
    SMARTiSM00206. NTR. 1 hit.
    [Graphical view]
    SUPFAMiSSF50242. SSF50242. 1 hit.
    PROSITEiPS50189. NTR. 1 hit.
    PS00288. TIMP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P35625-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTPWLGLIVL LGSWSLGDWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK    50
    LVKEGPFGTL VYTIKQMKMY RGFTKMPHVQ YIHTEASESL CGLKLEVNKY 100
    QYLLTGRVYD GKMYTGLCNF VERWDQLTLS QRKGLNYRYH LGCNCKIKSC 150
    YYLPCFVTSK NECLWTDMLS NFGYPGYQSK HYACIRQKGG YCSWYRGWAP 200
    PDKSIINATD P 211
    Length:211
    Mass (Da):24,145
    Last modified:February 1, 1995 - v2
    Checksum:i15CF831028BABF7A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 238LGDWGAEA → WGTGAPR in CAA82918. (PubMed:8034652)Curated
    Sequence conflicti21 – 222AE → R in AAA21815. (PubMed:8188246)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791S → C in SFD. 1 Publication
    VAR_007508
    Natural varianti189 – 1891G → C in SFD. 1 Publication
    VAR_008290
    Natural varianti190 – 1901G → C in SFD. 1 Publication
    VAR_010901
    Natural varianti191 – 1911Y → C in SFD. 2 Publications
    VAR_007509
    Natural varianti204 – 2041S → C in SFD. 1 Publication
    VAR_007510

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76227 mRNA. Translation: CAA53813.1.
    S78453 mRNA. Translation: AAB34532.1.
    U14394 mRNA. Translation: AAB60373.1.
    U02571 mRNA. Translation: AAA17672.1.
    Z30183 Genomic DNA. Translation: CAA82918.1.
    U33114
    , U33110, U33111, U33112, U33113 Genomic DNA. Translation: AAC50393.1.
    U67195 mRNA. Translation: AAB07547.1.
    CR456593 mRNA. Translation: CAG30479.1.
    BT006848 mRNA. Translation: AAP35494.1.
    AK314871 mRNA. Translation: BAG37386.1.
    AL023282, Z98256 Genomic DNA. Translation: CAI17996.1.
    Z98256, AL023282 Genomic DNA. Translation: CAI20115.1.
    CH471095 Genomic DNA. Translation: EAW60038.1.
    BC014277 mRNA. Translation: AAH14277.1.
    L15078 mRNA. Translation: AAA21815.1.
    U38955
    , U38952, U38953, U38954 Genomic DNA. Translation: AAB17602.1.
    CCDSiCCDS13911.1.
    PIRiS45317.
    RefSeqiNP_000353.1. NM_000362.4.
    UniGeneiHs.644633.

    Genome annotation databases

    EnsembliENST00000266085; ENSP00000266085; ENSG00000100234.
    GeneIDi7078.
    KEGGihsa:7078.
    UCSCiuc003anb.3. human.

    Polymorphism databases

    DMDMi730948.

    Cross-referencesi

    Web resourcesi

    Mutations of the TIMP3 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76227 mRNA. Translation: CAA53813.1 .
    S78453 mRNA. Translation: AAB34532.1 .
    U14394 mRNA. Translation: AAB60373.1 .
    U02571 mRNA. Translation: AAA17672.1 .
    Z30183 Genomic DNA. Translation: CAA82918.1 .
    U33114
    , U33110 , U33111 , U33112 , U33113 Genomic DNA. Translation: AAC50393.1 .
    U67195 mRNA. Translation: AAB07547.1 .
    CR456593 mRNA. Translation: CAG30479.1 .
    BT006848 mRNA. Translation: AAP35494.1 .
    AK314871 mRNA. Translation: BAG37386.1 .
    AL023282 , Z98256 Genomic DNA. Translation: CAI17996.1 .
    Z98256 , AL023282 Genomic DNA. Translation: CAI20115.1 .
    CH471095 Genomic DNA. Translation: EAW60038.1 .
    BC014277 mRNA. Translation: AAH14277.1 .
    L15078 mRNA. Translation: AAA21815.1 .
    U38955
    , U38952 , U38953 , U38954 Genomic DNA. Translation: AAB17602.1 .
    CCDSi CCDS13911.1.
    PIRi S45317.
    RefSeqi NP_000353.1. NM_000362.4.
    UniGenei Hs.644633.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CKI X-ray 2.30 B 24-144 [» ]
    ProteinModelPortali P35625.
    SMRi P35625. Positions 24-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112934. 3 interactions.
    IntActi P35625. 2 interactions.
    STRINGi 9606.ENSP00000266085.

    PTM databases

    PhosphoSitei P35625.

    Polymorphism databases

    DMDMi 730948.

    Proteomic databases

    MaxQBi P35625.
    PaxDbi P35625.
    PRIDEi P35625.

    Protocols and materials databases

    DNASUi 7078.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266085 ; ENSP00000266085 ; ENSG00000100234 .
    GeneIDi 7078.
    KEGGi hsa:7078.
    UCSCi uc003anb.3. human.

    Organism-specific databases

    CTDi 7078.
    GeneCardsi GC22P033196.
    HGNCi HGNC:11822. TIMP3.
    HPAi CAB022187.
    MIMi 136900. phenotype.
    188826. gene.
    neXtProti NX_P35625.
    Orphaneti 59181. Sorsby's fundus dystrophy.
    PharmGKBi PA36528.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250837.
    HOGENOMi HOG000285981.
    HOVERGENi HBG068749.
    InParanoidi P35625.
    KOi K16866.
    OMAi KEGYCSW.
    OrthoDBi EOG79GT74.
    PhylomeDBi P35625.
    TreeFami TF317409.

    Miscellaneous databases

    EvolutionaryTracei P35625.
    GeneWikii TIMP3.
    GenomeRNAii 7078.
    NextBioi 27685.
    PROi P35625.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35625.
    CleanExi HS_TIMP3.
    Genevestigatori P35625.

    Family and domain databases

    Gene3Di 3.90.370.10. 1 hit.
    InterProi IPR001134. Netrin_domain.
    IPR001820. Prot_inh_TIMP.
    IPR008993. TIMP-like_OB-fold.
    IPR027465. TIMP_C_dom.
    IPR015612. Tissue_inhib_metalloprotease_3.
    [Graphical view ]
    PANTHERi PTHR11844. PTHR11844. 1 hit.
    PTHR11844:SF6. PTHR11844:SF6. 1 hit.
    Pfami PF00965. TIMP. 1 hit.
    [Graphical view ]
    SMARTi SM00206. NTR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50242. SSF50242. 1 hit.
    PROSITEi PS50189. NTR. 1 hit.
    PS00288. TIMP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression in breast tumors of human TIMP-3, a new member of the metalloproteinase inhibitor family."
      Uria J.A., Ferrando A.A., Velasco G., Freije J.M., Lopez-Otin C.
      Cancer Res. 54:2091-2094(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    2. "Cloning and characterization of human tissue inhibitor of metalloproteinases-3."
      Wilde C.G., Hawkins P.R., Coleman R.T., Levine W.B., Delegeane A.M., Okamoto P.M., Ito L.Y., Scott R.W., Seilhamer J.J.
      DNA Cell Biol. 13:711-718(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family."
      Silbiger S.M., Jacobsen V.L., Cupples R.L., Koski R.A.
      Gene 141:293-297(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    4. "A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during G1 progression, mitogenic stimulation, differentiation, and senescence."
      Wick M., Buerger C., Bruesselbach S., Lucibello F., Mueller R.
      J. Biol. Chem. 269:18953-18960(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Genomic organization of the human tissue inhibitor of metalloproteinases-3 (TIMP3)."
      Stoehr H., Roomp K., Felbor U., Weber B.H.F.
      Genome Res. 5:483-487(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "TIMP-3 is expressed in the human retinal pigment epithelium."
      Ruiz A.C., Brett P., Bok D.
      Biochem. Biophys. Res. Commun. 226:467-474(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    10. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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].
      Tissue: Pancreas.
    13. "Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22."
      Apte S.S., Mattei M.-G., Olsen B.R.
      Genomics 19:86-90(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-211.
      Tissue: Placenta.
    14. "Identification and characterization of human tissue inhibitor of metalloproteinase-3 and detection of three additional metalloproteinase inhibitor activities in extracellular matrix."
      Kishnani N.S., Staskus P.W., Yang T.-T., Masiarz F.R., Hawkes S.P.
      Matrix Biol. 14:479-488(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-41.
    15. "Cloning and partial structure of the gene encoding human tissue inhibitor of metalloproteinases-3."
      Hammani K., Henriet P.M., Silbiger S.M., DeClerck Y.A.
      Gene 170:287-288(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-211.
      Tissue: Placenta.
    16. "Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations."
      Klenotic P.A., Munier F.L., Marmorstein L.Y., Anand-Apte B.
      J. Biol. Chem. 279:30469-30473(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EFEMP1.
    17. "Structural determinants of the ADAM inhibition by TIMP-3: crystal structure of the TACE-N-TIMP-3 complex."
      Wisniewska M., Goettig P., Maskos K., Belouski E., Winters D., Hecht R., Black R., Bode W.
      J. Mol. Biol. 381:1307-1319(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 24-144 IN COMPLEX WITH TACE, DISULFIDE BONDS.
    18. "Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy."
      Weber B.H.F., Vogt G., Pruett R.C., Stoehr H., Felbor U.
      Nat. Genet. 8:352-356(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SFD CYS-191 AND CYS-204.
    19. "A novel Ser156Cys mutation in the tissue inhibitor of metalloproteinases-3 (TIMP3) in Sorsby's fundus dystrophy with unusual clinical features."
      Felbor U., Stoehr H., Amann T., Schoenherr U., Weber B.H.F.
      Hum. Mol. Genet. 4:2415-2416(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SFD CYS-179.
    20. Cited for: VARIANT SFD CYS-190.
    21. "A second independent Tyr168Cys mutation in the tissue inhibitor of metalloproteinases-3 (TIMP3) in Sorsby's fundus dystrophy."
      Felbor U., Stoehr H., Amann T., Schoenherr U., Apfelstedt-Sylla E., Weber B.H.F.
      J. Med. Genet. 33:233-236(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SFD CYS-191.
    22. "Autosomal recessive Sorsby fundus dystrophy revisited: molecular evidence for dominant inheritance."
      Felbor U., Suvanto E.A., Forsius H.R., Eriksson A.W., Weber B.H.
      Am. J. Hum. Genet. 60:57-62(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SFD CYS-189.

    Entry informationi

    Entry nameiTIMP3_HUMAN
    AccessioniPrimary (citable) accession number: P35625
    Secondary accession number(s): B2RBY9
    , Q5THV4, Q9UC74, Q9UGS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 152 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3