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P01033 (TIMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metalloproteinase inhibitor 1
Alternative name(s):
Erythroid-potentiating activity
Short name=EPA
Fibroblast collagenase inhibitor
Short name=Collagenase inhibitor
Tissue inhibitor of metalloproteinases 1
Short name=TIMP-1
Gene names
Name:TIMP1
Synonyms:CLGI, TIMP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Ref.1 Ref.2 Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.25 Ref.30 Ref.31 Ref.32

Subunit structure

Interacts with MMP1, MMP3, MMP10 and MMP13, but has only very low affinity for MMP14. Interacts with CD63; identified in a complex with CD63 and ITGB1. Ref.15 Ref.16 Ref.17 Ref.19 Ref.24 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32

Subcellular location

Secreted Ref.1 Ref.2 Ref.3 Ref.9 Ref.15 Ref.25.

Tissue specificity

Detected in rheumatoid synovial fluid (at protein level). Ref.9

Post-translational modification

The activity of TIMP1 is dependent on the presence of disulfide bonds.

N-glycosylated. Ref.1 Ref.2 Ref.3 Ref.22

Sequence similarities

Belongs to the protease inhibitor I35 (TIMP) family. [View classification]

Contains 1 NTR domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionGrowth factor
Metalloenzyme inhibitor
Metalloprotease inhibitor
Protease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of endopeptidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 12714508. Source: UniProtKB

negative regulation of metalloenzyme activity

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of trophoblast cell migration

Inferred from mutant phenotype PubMed 21356369. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of cell proliferation

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of integrin-mediated signaling pathway

Inferred from mutant phenotype Ref.19. Source: UniProtKB

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Non-traceable author statement Ref.10. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.1. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functioncytokine activity

Inferred from direct assay Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase inhibitor activity

Inferred from direct assay PubMed 12714508Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 2251898. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CD63P089625EBI-712536,EBI-762053

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1 Ref.2 Ref.3 Ref.9 Ref.10 Ref.11
Chain24 – 207184Metalloproteinase inhibitor 1
PRO_0000034323

Regions

Domain24 – 147124NTR
Region24 – 285Involved in metalloproteinase-binding
Region90 – 912Involved in metalloproteinase-binding

Sites

Metal binding241Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) (complex) Ref.18 Ref.20 Ref.21 Ref.22
CAR_000002
Glycosylation1011N-linked (GlcNAc...) Ref.20
CAR_000003
Disulfide bond24 ↔ 93 Ref.3 Ref.13 Ref.28 Ref.30 Ref.31 Ref.32
Disulfide bond26 ↔ 122 Ref.3 Ref.13 Ref.28 Ref.30 Ref.31 Ref.32
Disulfide bond36 ↔ 147 Ref.3 Ref.13 Ref.28 Ref.30 Ref.31 Ref.32
Disulfide bond150 ↔ 197 Ref.3 Ref.13 Ref.28 Ref.30 Ref.31 Ref.32
Disulfide bond155 ↔ 160 Ref.3 Ref.13 Ref.28 Ref.30 Ref.31 Ref.32
Disulfide bond168 ↔ 189 Ref.3 Ref.13 Ref.28 Ref.30 Ref.31 Ref.32

Experimental info

Mutagenesis251T → E, G, K, Q or R: Reduced interaction with metalloproteinase. Ref.30
Mutagenesis251T → V: Normal interaction with metalloproteinase. Ref.30
Mutagenesis301H → A: Nearly abolishes metalloproteinase inhibition. Ref.15
Mutagenesis321Q → A: Nearly abolishes metalloproteinase inhibition. Ref.15
Mutagenesis1211T → L: Decreases protein flexibility and increases affinity for MMP14. Ref.31
Sequence conflict231A → P in CAA26443. Ref.2
Sequence conflict441A → P in BAA01913. Ref.12

Secondary structure

........................................ 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01033 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5AE4F90FFAB2ECDC

FASTA20723,171
        10         20         30         40         50         60 
MAPFEPLASG ILLLLWLIAP SRACTCVPPH PQTAFCNSDL VIRAKFVGTP EVNQTTLYQR 

        70         80         90        100        110        120 
YEIKMTKMYK GFQALGDAAD IRFVYTPAME SVCGYFHRSH NRSEEFLIAG KLQDGLLHIT 

       130        140        150        160        170        180 
TCSFVAPWNS LSLAQRRGFT KTYTVGCEEC TVFPCLSIPC KLQSGTHCLW TDQLLQGSEK 

       190        200 
GFQSRHLACL PREPGLCTWQ SLRSQIA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity."
Docherty A.J.P., Lyons A., Smith B.J., Wright E.M., Stephens P.E., Harris T.J.R., Murphy G., Reynolds J.J.
Nature 318:66-69(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-51, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION.
[2]"Molecular characterization and expression of the gene encoding human erythroid-potentiating activity."
Gasson J.C., Golde D.W., Kaufman S.E., Westbrook C.A., Hewick R.M., Kaufman R.J., Wong G.G., Temple P.A., Leary A.C., Brown E.L., Orr E.C., Clark S.C.
Nature 315:768-771(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-49, SUBCELLULAR LOCATION, GLYCOSYLATION, FUNCTION.
[3]"Primary structure and cDNA cloning of human fibroblast collagenase inhibitor."
Carmichael D.F., Sommer A., Thompson R.C., Anderson D.C., Smith C.G., Welgus H.G., Stricklin G.P.
Proc. Natl. Acad. Sci. U.S.A. 83:2407-2411(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-207, DISULFIDE BOND, SUBCELLULAR LOCATION, GLYCOSYLATION.
[4]"Molecular cloning and synthesis of biologically active human tissue inhibitor of metalloproteinases in yeast."
Kaczorek M., Honore N., Ribes V., Dehoux P., Cornet P., Cartwright T., Streeck R.E.
Biotechnology (N.Y.) 5:595-598(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Characterization of three abundant mRNAs from human ovarian granulosa cells."
Rapp G., Freudenstein J., Klaudiny J., Mucha J., Wempe F., Zimmer M., Scheit K.H.
DNA Cell Biol. 9:479-485(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[6]"Characterization of a human corneal metalloproteinase inhibitor (TIMP-1)."
Opbroek A., Kenney M.C., Brown D.
Curr. Eye Res. 12:877-883(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"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: Cervix.
[8]"Genomic organization of the human TIMP-1 gene. Investigation of a causative role in the pathogenesis of X-linked retinitis pigmentosa 2."
Hardcastle A.J., Thiselton D.L., Nayudu M., Hampson R.M., Bhattacharya S.S.
Invest. Ophthalmol. Vis. Sci. 38:1893-1896(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[9]"Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid."
Osthues A., Knaueper V., Oberhoff R., Reinke H., Tschesche H.
FEBS Lett. 296:16-20(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-38, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
Tissue: Synovial fluid.
[10]"The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers."
van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F., Auwerx J., van Damme J., Opdenakker G.
Cytokine 3:231-239(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-52.
[11]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-38.
[12]Matsuda T., Kohno K., Kuwano M.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-207.
[13]"Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)."
Williamson R.A., Martson F.A.O., Angal S., Koklitis P., Panico M., Morris H.R., Carne A.F., Smith B.J., Harris T.J.R., Freedman R.B.
Biochem. J. 268:267-274(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, PARTIAL PROTEIN SEQUENCE.
[14]"Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13."
O'Shea M., Willenbrock F., Williamson R.A., Cockett M.I., Freedman R.B., Reynolds J.J., Docherty A.J.P., Murphy G.
Biochemistry 31:10146-10152(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, FUNCTION.
[15]"Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1."
Chesler L., Golde D.W., Bersch N., Johnson M.D.
Blood 86:4506-4515(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A GROWTH FACTOR AND PROTEASE INHIBITOR, INTERACTION WITH MMP3, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-30 AND GLN-32.
[16]"Biochemical characterization of human collagenase-3."
Knaeuper V., Lopez-Otin C., Smith B., Knight G., Murphy G.
J. Biol. Chem. 271:1544-1550(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MMP13, FUNCTION.
[17]"The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction."
Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H., Zardi L., Murphy G.
J. Biol. Chem. 272:7608-7616(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MMP13, FUNCTION.
[18]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
Tissue: Plasma.
[19]"Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein."
Jung K.K., Liu X.W., Chirco R., Fridman R., Kim H.R.
EMBO J. 25:3934-3942(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CD63.
[20]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53 AND ASN-101.
Tissue: Saliva.
[21]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
Tissue: Platelet.
[22]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-53.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Timp1 interacts with beta-1 integrin and CD63 along melanoma genesis and confers anoikis resistance by activating PI3-K signaling pathway independently of Akt phosphorylation."
Toricelli M., Melo F.H., Peres G.B., Silva D.C., Jasiulionis M.G.
Mol. Cancer 12:22-22(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CD63 AND ITGB1.
[25]"TIMP-1 modulates chemotaxis of human neural stem cells through CD63 and integrin signalling."
Lee S.Y., Kim J.M., Cho S.Y., Kim H.S., Shin H.S., Jeon J.Y., Kausar R., Jeong S.Y., Lee Y.S., Lee M.A.
Biochem. J. 459:565-576(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[26]"Cytokine functions of TIMP-1."
Ries C.
Cell. Mol. Life Sci. 71:659-672(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[27]"Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1."
Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R., Suzuki K., Yoshida N., Nagase H., Brew K., Bourenkov G.P., Bartunik H., Bode W.
Nature 389:77-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP3, INTERACTION WITH MMP3.
[28]"NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases."
Wu B., Arumugam S., Gao G., Lee G.I., Semenchenko V., Huang W., Brew K., Van Doren S.R.
J. Mol. Biol. 295:257-268(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-149, DISULFIDE BOND.
[29]"Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings."
Arumugam S., Van Doren S.R.
Biochemistry 42:7950-7958(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-149 IN COMPLEX WITH MMP3, INTERACTION WITH MMP3.
[30]"Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1."
Iyer S., Wei S., Brew K., Acharya K.R.
J. Biol. Chem. 282:364-371(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 24-149 IN COMPLEX WITH MMP1, FUNCTION, INTERACTION WITH MMP1 AND MMP3, DISULFIDE BOND, MUTAGENESIS OF THR-25.
[31]"The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function."
Grossman M., Tworowski D., Dym O., Lee M.H., Levy Y., Murphy G., Sagi I.
Biochemistry 49:6184-6192(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 24-148 OF MUTANT LEU-121 IN COMPLEX WITH MMP14, FUNCTION, INTERACTION WITH MMP14, DISULFIDE BOND, MUTAGENESIS OF THR-121.
[32]"Matrix metalloproteinase-10 (MMP10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure."
Batra J., Robinson J., Soares A.S., Fields A.P., Radisky D.C., Radisky E.S.
J. Biol. Chem. 287:15935-15946(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP10, FUNCTION, INTERACTION WITH MMP10, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03124 mRNA. Translation: CAA26902.1.
X02598 mRNA. Translation: CAA26443.1.
M12670 mRNA. Translation: AAA52436.1.
M59906 mRNA. Translation: AAA63234.1.
S68252 mRNA. Translation: AAD14009.1.
BC000866 mRNA. Translation: AAH00866.1.
L47361 Genomic DNA. Translation: AAA75558.1.
D11139 Genomic DNA. Translation: BAA01913.1.
CCDSCCDS14281.1.
PIRZYHUEP. A93372.
RefSeqNP_003245.1. NM_003254.2.
UniGeneHs.522632.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2BNMR-A24-149[»]
1LQNmodel-A1-207[»]
1OO9NMR-B24-149[»]
1UEAX-ray2.80B/D24-207[»]
2J0TX-ray2.54D/E/F24-149[»]
3MA2X-ray2.05B/C24-148[»]
3V96X-ray1.90A24-207[»]
ProteinModelPortalP01033.
SMRP01033. Positions 24-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112932. 9 interactions.
DIPDIP-1107N.
IntActP01033. 5 interactions.
MINTMINT-2981826.
STRING9606.ENSP00000218388.

Protein family/group databases

MEROPSI35.001.

PTM databases

PhosphoSiteP01033.
UniCarbKBP01033.

Polymorphism databases

DMDM135850.

Proteomic databases

MaxQBP01033.
PaxDbP01033.
PRIDEP01033.

Protocols and materials databases

DNASU7076.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218388; ENSP00000218388; ENSG00000102265.
GeneID7076.
KEGGhsa:7076.
UCSCuc004dif.3. human.

Organism-specific databases

CTD7076.
GeneCardsGC0XP047441.
HGNCHGNC:11820. TIMP1.
HPACAB022360.
MIM305370. gene.
neXtProtNX_P01033.
PharmGKBPA36526.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259409.
HOGENOMHOG000285981.
HOVERGENHBG068749.
InParanoidP01033.
KOK16451.
OMADKGFQSR.
OrthoDBEOG79GT74.
PhylomeDBP01033.
TreeFamTF317409.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP01033.
BgeeP01033.
CleanExHS_TIMP1.
GenevestigatorP01033.

Family and domain databases

Gene3D3.90.370.10. 1 hit.
InterProIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015611. TIMP1.
IPR027465. TIMP_C_dom.
[Graphical view]
PANTHERPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF20. PTHR11844:SF20. 1 hit.
PfamPF00965. TIMP. 1 hit.
[Graphical view]
SMARTSM00206. NTR. 1 hit.
[Graphical view]
SUPFAMSSF50242. SSF50242. 1 hit.
PROSITEPS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01033.
GeneWikiTIMP1.
GenomeRNAi7076.
NextBio27675.
PMAP-CutDBP01033.
PROP01033.
SOURCESearch...

Entry information

Entry nameTIMP1_HUMAN
AccessionPrimary (citable) accession number: P01033
Secondary accession number(s): Q14252, Q9UCU1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM