Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Metalloproteinase inhibitor 3

Gene

TIMP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. protease binding Source: GO_Central

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. negative regulation of metalloenzyme activity Source: GO_Central
  5. response to cytokine Source: GO_Central
  6. response to hormone Source: GO_Central
  7. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiI35.003.

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 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11822. TIMP3.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. extracellular space Source: GO_Central
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. proteinaceous extracellular matrix Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Sorsby fundus dystrophy (SFD)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionRare 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.

See also OMIM:136900
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.

Polymorphism and mutation databases

BioMutaiTIMP3.
DMDMi730948.

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 ↔ 91PROSITE-ProRule annotation1 Publication
Disulfide bondi26 ↔ 118PROSITE-ProRule annotation1 Publication
Disulfide bondi36 ↔ 143PROSITE-ProRule annotation1 Publication
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. 8 interactions.
IntActiP35625. 2 interactions.
STRINGi9606.ENSP00000266085.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000004555.
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.
IPR030490. TIMP_CS.
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

        10         20         30         40         50
MTPWLGLIVL LGSWSLGDWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK
60 70 80 90 100
LVKEGPFGTL VYTIKQMKMY RGFTKMPHVQ YIHTEASESL CGLKLEVNKY
110 120 130 140 150
QYLLTGRVYD GKMYTGLCNF VERWDQLTLS QRKGLNYRYH LGCNCKIKSC
160 170 180 190 200
YYLPCFVTSK NECLWTDMLS NFGYPGYQSK HYACIRQKGG YCSWYRGWAP
210
PDKSIINATD P
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiTIMP3.

Cross-referencesi

Web resourcesi

Mutations of the TIMP3 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi112934. 8 interactions.
IntActiP35625. 2 interactions.
STRINGi9606.ENSP00000266085.

Protein family/group databases

MEROPSiI35.003.

PTM databases

PhosphoSiteiP35625.

Polymorphism and mutation databases

BioMutaiTIMP3.
DMDMi730948.

Proteomic databases

MaxQBiP35625.
PaxDbiP35625.
PRIDEiP35625.

Protocols and materials databases

DNASUi7078.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7078.
GeneCardsiGC22P033196.
HGNCiHGNC:11822. TIMP3.
HPAiCAB022187.
MIMi136900. phenotype.
188826. gene.
neXtProtiNX_P35625.
Orphaneti59181. Sorsby's fundus dystrophy.
PharmGKBiPA36528.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250837.
GeneTreeiENSGT00390000004555.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiP35625.
KOiK16866.
OMAiKEGYCSW.
OrthoDBiEOG79GT74.
PhylomeDBiP35625.
TreeFamiTF317409.

Miscellaneous databases

EvolutionaryTraceiP35625.
GeneWikiiTIMP3.
GenomeRNAii7078.
NextBioi27685.
PROiP35625.
SOURCEiSearch...

Gene expression databases

BgeeiP35625.
CleanExiHS_TIMP3.
GenevestigatoriP35625.

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.
IPR030490. TIMP_CS.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.