UniProt Accession

 TIMP1_HUMAN; P01033; Q14252; Q9UCU1 

Genbank Protein ID

 X03124; X02598; M12670; M59906; S68252; BC000866; L47361; D11139 

Genbank Nucleotide ID

 CAA26902.1; CAA26443.1; AAA52436.1; AAA63234.1; AAD14009.1; AAH00866.1; AAA75558.1; BAA01913.1 

Protein Name

 Metalloproteinase inhibitor 1 

Protein Synonyms/Alias

 Erythroid-potentiating activity; EPA; Fibroblast collagenase inhibitor; Collagenase inhibitor; Tissue inhibitor of metalloproteinases 1; TIMP-1 

Gene Name

 TIMP1 

Gene Synonyms/Alias

 CLGI; TIMP 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
45	SDLVIRAKFVGTPEV	ubiquitination	[1, 2]
70	IKMTKMYKGFQALGD	ubiquitination	[1, 2, 3]
141	AQRRGFTKTYTVGCE	ubiquitination	[3]
180	QLLQGSEKGFQSRHL	ubiquitination	[3]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

Functional Description

 Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14. 

Sequence Annotation

 DOMAIN 24 147 NTR.
 REGION 24 28 Involved in metalloproteinase-binding.
 REGION 90 91 Involved in metalloproteinase-binding.
 METAL 24 24 Zinc; via amino nitrogen and carbonyl
 CARBOHYD 53 53 N-linked (GlcNAc...).
 CARBOHYD 101 101 N-linked (GlcNAc...).
 DISULFID 24 93
 DISULFID 26 122
 DISULFID 36 147
 DISULFID 150 197
 DISULFID 155 160
 DISULFID 168 189  

Keyword

 3D-structure; Complete proteome; Direct protein sequencing; Disulfide bond; Erythrocyte maturation; Glycoprotein; Metal-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor; Reference proteome; Secreted; Signal; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 207 AA 

Protein Sequence

Gene Ontology

 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0005576; C:extracellular region; NAS:UniProtKB.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
 GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
 GO:1901164; P:negative regulation of trophoblast cell migration; IMP:BHF-UCL.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0034097; P:response to cytokine stimulus; IEA:Compara.
 GO:0043434; P:response to peptide hormone stimulus; IEA:Compara. 

Interpro

 IPR001134; Netrin_domain.
 IPR001820; Prot_inh_TIMP.
 IPR008993; TIMP-like_OB-fold.
 IPR015611; TIMP1.
 IPR027465; TIMP_C_dom. 

Pfam

 PF00965; TIMP 

SMART

 SM00206; NTR 

PROSITE

 PS50189; NTR
 PS00288; TIMP 

PRINTS