P35625 (TIMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metalloproteinase inhibitor 3

Alternative name(s):
Protein MIG-5
Tissue inhibitor of metalloproteinases 3
Short name=TIMP-3

Gene names

Name:

TIMP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with EFEMP1. Ref.16
Subcellular location	Secreted › extracellular space › extracellular matrix.
Involvement in disease	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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Sequence similarities	Belongs to the protease inhibitor I35 (TIMP) family. [View classification] Contains 1 NTR domain.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Extracellular matrix Secreted
Disease	Disease mutation
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Metalloenzyme inhibitor Metalloprotease inhibitor Protease inhibitor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to organic substance Inferred from electronic annotation. Source: Compara negative regulation of membrane protein ectodomain proteolysis Inferred from mutant phenotype PubMed 18383040. Source: BHF-UCL visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase inhibitor activity Traceable author statement Ref.17. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGTR2	P50052	7	EBI-1748085,EBI-1748067

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.14

Chain

24 – 211

188

Metalloproteinase inhibitor 3

PRO_0000034341

Regions

Domain

24 – 143

120

NTR

Region

24 – 28

5

Involved in metalloproteinase-binding

Region

88 – 89

2

Involved in metalloproteinase-binding

Region

105 – 188

84

Mediates interaction with EFEMP1

Sites

Metal binding

24

1

Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner

Amino acid modifications

Disulfide bond

24 ↔ 91

Ref.17

Disulfide bond

26 ↔ 118

Ref.17

Disulfide bond

36 ↔ 143

Ref.17

Disulfide bond

145 ↔ 192

By similarity

Disulfide bond

150 ↔ 155

By similarity

Disulfide bond

163 ↔ 184

By similarity

Natural variations

Natural variant

179

1

S → C in SFD. Ref.19

VAR_007508

Natural variant

189

1

G → C in SFD. Ref.22

VAR_008290

Natural variant

190

1

G → C in SFD. Ref.20

VAR_010901

Natural variant

191

1

Y → C in SFD. Ref.18 Ref.21

VAR_007509

Natural variant

204

1

S → C in SFD. Ref.18

VAR_007510

Experimental info

Sequence conflict

16 – 23

8

LGDWGAEA → WGTGAPR in CAA82918. Ref.4

Sequence conflict

21 – 22

2

AE → R in AAA21815. Ref.13

Secondary structure

1

.

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.

.

.

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.

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211

Helix Strand Turn

Details...

Helix

31 – 37

7

Beta strand

39 – 42

4

Beta strand

45 – 52

8

Beta strand

55 – 57

3

Beta strand

59 – 65

7

Beta strand

69 – 71

3

Turn

73 – 75

3

Beta strand

76 – 78

3

Beta strand

81 – 86

6

Helix

88 – 90

3

Beta strand

102 – 108

7

Turn

124 – 126

3

Helix

129 – 136

8

Turn

137 – 140

4

Sequences

	Sequence		Length	Mass (Da)
	P35625 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 15CF831028BABF7A	FASTA	211	24,145
	10 20 30 40 50 60 MTPWLGLIVL LGSWSLGDWG AEACTCSPSH PQDAFCNSDI VIRAKVVGKK LVKEGPFGTL 70 80 90 100 110 120 VYTIKQMKMY RGFTKMPHVQ YIHTEASESL CGLKLEVNKY QYLLTGRVYD GKMYTGLCNF 130 140 150 160 170 180 VERWDQLTLS QRKGLNYRYH LGCNCKIKSC YYLPCFVTSK NECLWTDMLS NFGYPGYQSK 190 200 210 HYACIRQKGG YCSWYRGWAP PDKSIINATD P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Night blindness in Sorsby's fundus dystrophy reversed by vitamin A." Jacobson S.G., Cideciyan A.V., Regunath G., Rodriguez F.J., Vandenburgh K., Sheffield V.C., Stone E.M. Nat. Genet. 11:27-32(1995) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Mutations of the TIMP3 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00218247.

PIR

S45317.

RefSeq

NP_000353.1. NM_000362.4.

UniGene

Hs.644633.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CKI	X-ray	2.30	B	24-144	[»]

ProteinModelPortal

P35625.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35625. 2 interactions.

STRING

9606.ENSP00000266085.

PTM databases

PhosphoSite

P35625.

Polymorphism databases

DMDM

730948.

Proteomic databases

PaxDb

P35625.

PRIDE

P35625.

Protocols and materials databases

DNASU

7078.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266085; ENSP00000266085; ENSG00000100234.

GeneID

7078.

KEGG

hsa:7078.

UCSC

uc003anb.3. human.

Organism-specific databases

CTD

7078.

GeneCards

GC22P033196.

HGNC

HGNC:11822. TIMP3.

HPA

CAB022187.

MIM

136900. phenotype.
188826. gene.

neXtProt

NX_P35625.

Orphanet

59181. Sorsby's fundus dystrophy.

PharmGKB

PA36528.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG250837.

HOGENOM

HOG000285981.

HOVERGEN

HBG068749.

InParanoid

P35625.

KO

K16866.

OMA

KEGYCSW.

OrthoDB

EOG47D9H3.

PhylomeDB

P35625.

Gene expression databases

ArrayExpress

P35625.

Bgee

P35625.

CleanEx

HS_TIMP3.

Genevestigator

P35625.

GermOnline

ENSG00000100234. Homo sapiens.

Family and domain databases

Gene3D

3.90.370.10. 1 hit.

InterPro

IPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR027465. TIMP_C_dom.
IPR015612. Tissue_inhib_metalloprotease_3.
[Graphical view]

PANTHER

PTHR11844. PTHR11844. 1 hit.
PTHR11844:SF6. PTHR11844:SF6. 1 hit.

Pfam

PF00965. TIMP. 1 hit.
[Graphical view]

SMART

SM00206. NTR. 1 hit.
[Graphical view]

SUPFAM

SSF50242. TIMP_like. 1 hit.

PROSITE

PS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35625.

GenomeRNAi

7078.

NextBio

27685.

SOURCE

Search...

Entry information

Entry name

TIMP3_HUMAN

Accession

Primary (citable) accession number: P35625
Secondary accession number(s): B2RBY9 , Q5THV4, Q9UC74, Q9UGS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.