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UniProtKB - P30120 (TIMP1_RAT)

Entry version 162 (07 Oct 2020)
Sequence version 2 (01 Nov 1995)
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Protein

Metalloproteinase inhibitor 1

Gene

Timp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Also stimulates steroidogenesis by Leydig and ovarian granuloma cells; procathepsin L is required for maximal activity.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi24Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partnerBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei37Involved in metalloproteinase-bindingBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGrowth factor, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor
Biological processSteroidogenesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-114608, Platelet degranulation
R-RNO-1592389, Activation of Matrix Metalloproteinases
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-8957275, Post-translational protein phosphorylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Metalloproteinase inhibitor 1
Alternative name(s):
Tissue inhibitor of metalloproteinases 1
Short name:
TIMP-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Timp1
Synonyms:Timp-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Rat genome database

More...RGDi		621675, Timp1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 232 PublicationsAdd BLAST23
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003432924 – 217Metalloproteinase inhibitor 1Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi24 ↔ 93PROSITE-ProRule annotation
Disulfide bondi26 ↔ 122PROSITE-ProRule annotation
Disulfide bondi36 ↔ 147PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi77N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi101N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi150 ↔ 197PROSITE-ProRule annotation
Disulfide bondi155 ↔ 160PROSITE-ProRule annotation
Disulfide bondi168 ↔ 189PROSITE-ProRule annotation
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei178PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The activity of TIMP1 is dependent on the presence of disulfide bonds.By similarity
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P30120

PRoteomics IDEntifications database

More...PRIDEi		P30120

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P30120, 2 sites

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By follicle-stimulating hormone (FSH).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000010208, Expressed in female gonad and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P30120, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000013745

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P30120

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 147NTRPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni24 – 27Involved in metalloproteinase-bindingBy similarity4
Regioni90 – 91Involved in metalloproteinase-bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4745, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161081

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_084029_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P30120

KEGG Orthology (KO)

More...KOi		K16451

Identification of Orthologs from Complete Genome Data

More...OMAi		CTVFPCS

Database of Orthologous Groups

More...OrthoDBi		1122531at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P30120

TreeFam database of animal gene trees

More...TreeFami		TF317409

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.50.120, 1 hit
3.90.370.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001134, Netrin_domain
IPR001820, TIMP
IPR008993, TIMP-like_OB-fold
IPR015611, TIMP1
IPR027465, TIMP_C
IPR030490, TIMP_CS

The PANTHER Classification System

More...PANTHERi		PTHR11844, PTHR11844, 1 hit
PTHR11844:SF20, PTHR11844:SF20, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00965, TIMP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00206, NTR, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50242, SSF50242, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50189, NTR, 1 hit
PS00288, TIMP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P30120-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPFASLASG ILLLLSLIAS SKACSCAPTH PQTAFCNSDL VIRAKFMGSP 
        60         70         80         90        100
EIIETTLYQR YEIKMTKMLK GFDAVGNATG FRFAYTPAME SLCGYVHKSQ 
       110        120        130        140        150
NRSEEFLIAG RLRNGNLHIT ACSFLVPWHN LSPAQQKAFV KTYSAGCGVC 
       160        170        180        190        200
TVFPCSAIPC KLESDSHCLW TDQILMGSEK GYQSDHFACL PRNPDLCTWQ 
       210 
YLGVSMTRSL PLAKAEA
Length:217
Mass (Da):23,794
Last modified:November 1, 1995 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC5AC240A61C1A1DF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti80 – 81GF → DI in AAB08483 (PubMed:8707259).Curated2
Sequence conflicti88A → V in AAA51653 (PubMed:7777858).Curated1
Sequence conflicti103S → R in AAB08483 (PubMed:8707259).Curated1
Sequence conflicti129 – 130HN → AS in AAB08483 (PubMed:8707259).Curated2
Sequence conflicti136 – 140QKAFV → RKGLT in AAB08483 (PubMed:8707259).Curated5
Sequence conflicti149V → L in AAA51653 (PubMed:7777858).Curated1
Sequence conflicti157A → V in AAB08483 (PubMed:8707259).Curated1
Sequence conflicti166S → T in AAB08483 (PubMed:8707259).Curated1
Sequence conflicti185 – 187DHF → RHL in AAB08483 (PubMed:8707259).Curated3
Sequence conflicti195D → G in AAB08483 (PubMed:8707259).Curated1
Sequence conflicti201Y → S in AAB08483 (PubMed:8707259).Curated1
Sequence conflicti204 – 205VS → SR in AAB08483 (PubMed:8707259).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U06179 mRNA Translation: AAA85780.1
L31883 mRNA Translation: AAA85373.1
AY550026 mRNA Translation: AAS55641.1
BC099821 mRNA Translation: AAH99821.1
L29512 mRNA Translation: AAB08483.1
U16022 mRNA Translation: AAA51653.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...PIRi		JC2557

NCBI Reference Sequences

More...RefSeqi		NP_446271.1, NM_053819.1
XP_006256670.1, XM_006256608.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000013745; ENSRNOP00000013745; ENSRNOG00000010208

Database of genes from NCBI RefSeq genomes

More...GeneIDi		116510

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:116510

UCSC genome browser

More...UCSCi		RGD:621675, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06179 mRNA Translation: AAA85780.1
L31883 mRNA Translation: AAA85373.1
AY550026 mRNA Translation: AAS55641.1
BC099821 mRNA Translation: AAH99821.1
L29512 mRNA Translation: AAB08483.1
U16022 mRNA Translation: AAA51653.1 Sequence problems.
PIRiJC2557
RefSeqiNP_446271.1, NM_053819.1
XP_006256670.1, XM_006256608.2

3D structure databases

SMRiP30120
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013745

PTM databases

GlyGeniP30120, 2 sites

Proteomic databases

PaxDbiP30120
PRIDEiP30120

Genome annotation databases

EnsembliENSRNOT00000013745; ENSRNOP00000013745; ENSRNOG00000010208
GeneIDi116510
KEGGirno:116510
UCSCiRGD:621675, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7076
RGDi621675, Timp1

Phylogenomic databases

eggNOGiKOG4745, Eukaryota
GeneTreeiENSGT00940000161081
HOGENOMiCLU_084029_0_0_1
InParanoidiP30120
KOiK16451
OMAiCTVFPCS
OrthoDBi1122531at2759
PhylomeDBiP30120
TreeFamiTF317409

Enzyme and pathway databases

ReactomeiR-RNO-114608, Platelet degranulation
R-RNO-1592389, Activation of Matrix Metalloproteinases
R-RNO-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-RNO-8957275, Post-translational protein phosphorylation

Miscellaneous databases

Protein Ontology

More...PROi		PR:P30120

Gene expression databases

BgeeiENSRNOG00000010208, Expressed in female gonad and 22 other tissues
GenevisibleiP30120, RN

Family and domain databases

Gene3Di2.40.50.120, 1 hit
3.90.370.10, 1 hit
InterProiView protein in InterPro
IPR001134, Netrin_domain
IPR001820, TIMP
IPR008993, TIMP-like_OB-fold
IPR015611, TIMP1
IPR027465, TIMP_C
IPR030490, TIMP_CS
PANTHERiPTHR11844, PTHR11844, 1 hit
PTHR11844:SF20, PTHR11844:SF20, 1 hit
PfamiView protein in Pfam
PF00965, TIMP, 1 hit
SMARTiView protein in SMART
SM00206, NTR, 1 hit
SUPFAMiSSF50242, SSF50242, 1 hit
PROSITEiView protein in PROSITE
PS50189, NTR, 1 hit
PS00288, TIMP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTIMP1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P30120
Secondary accession number(s): P70533, Q53YM7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: October 7, 2020
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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