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P35625

- TIMP3_HUMAN

UniProt

P35625 - TIMP3_HUMAN

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Protein
Metalloproteinase inhibitor 3
Gene
TIMP3
Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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 Publication
Add
BLAST
Chaini24 – 211188Metalloproteinase inhibitor 3
PRO_0000034341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 911 Publication
Disulfide bondi26 ↔ 1181 Publication
Disulfide bondi36 ↔ 1431 Publication
Disulfide bondi145 ↔ 192 By similarity
Disulfide bondi150 ↔ 155 By similarity
Disulfide bondi163 ↔ 184 By similarity

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 EFEMP1.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP35625.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 143120NTR
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 285Involved in metalloproteinase-binding
Regioni88 – 892Involved in metalloproteinase-binding
Regioni105 – 18884Mediates interaction with EFEMP1
Add
BLAST

Sequence similaritiesi

Contains 1 NTR domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 238LGDWGAEA → WGTGAPR in CAA82918. 1 Publication
Sequence conflicti21 – 222AE → R in AAA21815. 1 Publication

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

« 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: September 3, 2014
This is version 151 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

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