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UniProtKB - P07477 (TRY1_HUMAN)

Entry version 207 (05 Jun 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Trypsin-1

Gene

PRSS1

Organism
Homo sapiens (Human)
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

Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.1 Publication

Caution

Tyr-154 was proposed to be phosphorylated (PubMed:8683601) but it has been shown (PubMed:17087724) to be sulfated instead. Phosphate and sulfate groups are similar in mass and size, and this can lead to erroneous interpretation of the results.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. EC:3.4.21.4

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+Note: Binds 1 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei63Charge relay system1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi75Calcium1
Metal bindingi77Calcium; via carbonyl oxygen1
Metal bindingi80Calcium; via carbonyl oxygen1
Metal bindingi85Calcium1
Active sitei107Charge relay system1
<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>Sitei194Required for specificityBy similarity1
Active sitei200Charge relay system1

<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 functionHydrolase, Protease, Serine protease
Biological processDigestion
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-196741 Cobalamin (Cbl, vitamin B12) transport and metabolism

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.127

<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_and_taxonomy_section">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:
Trypsin-1 (EC:3.4.21.4)
Alternative name(s):
Beta-trypsin
Cationic trypsinogen
Serine protease 1
Trypsin I
Cleaved into the following 2 chains:
Alpha-trypsin chain 1
Alpha-trypsin chain 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:PRSS1
Synonyms:TRP1, TRY1, TRYP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 7

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9475 PRSS1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		276000 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P07477

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Pancreatitis, hereditary (PCTT)11 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA disease characterized by pancreas inflammation, permanent destruction of the pancreatic parenchyma, maldigestion, and severe abdominal pain attacks.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01169316A → V in PCTT; disrupts signal sequence cleavage site. 1 PublicationCorresponds to variant dbSNP:rs202003805EnsemblClinVar.1
Natural variantiVAR_01165222D → G in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs397507442EnsemblClinVar.1
Natural variantiVAR_01165323K → R in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs111033567EnsemblClinVar.1
Natural variantiVAR_00672029N → I in PCTT. 4 PublicationsCorresponds to variant dbSNP:rs111033566EnsemblClinVar.1
Natural variantiVAR_01271229N → T in PCTT. 1 PublicationCorresponds to variant dbSNP:rs111033566EnsemblClinVar.1
Natural variantiVAR_03790854N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. 1 PublicationCorresponds to variant dbSNP:rs144422014EnsemblClinVar.1
Natural variantiVAR_03790979E → K in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. 1 PublicationCorresponds to variant dbSNP:rs111033564EnsemblClinVar.1
Natural variantiVAR_011654104L → P in PCTT. 1 Publication1
Natural variantiVAR_011655116R → C in PCTT. 1 PublicationCorresponds to variant dbSNP:rs387906698EnsemblClinVar.1
Natural variantiVAR_012713122R → C in PCTT; suppresses an autocleavage site. 1 PublicationCorresponds to variant dbSNP:rs111033568EnsemblClinVar.1
Natural variantiVAR_006721122R → H in PCTT; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis. 5 PublicationsCorresponds to variant dbSNP:rs267606982EnsemblClinVar.1
Natural variantiVAR_011656139C → F in PCTT. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi154Y → F: Lack of sulfation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		5644

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		PRSS1

MalaCards human disease database

More...MalaCardsi		PRSS1
MIMi167800 phenotype

Open Targets

More...OpenTargetsi		ENSG00000204983

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		676 Hereditary chronic pancreatitis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33828

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL209

Drug and drug target database

More...DrugBanki		DB06850 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide
DB07091 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide
DB06845 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide
DB07088 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide
DB07131 (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide
DB07095 (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide
DB07985 +/-METHYL 4-(AMINOIMINOMETHYL)-BETA-[3- INH (AMINOIMINO)PHENYL]BENZENE PENTANOATE
DB03337 1-(2-Amidinophenyl)-3-(Phenoxyphenyl)Urea
DB04336 1-(4-Amidinophenyl)-3-(4-Chlorophenyl)Urea
DB03417 1-(4-Tert-Butylcarbamoyl-Piperazine-1-Carbonyl)-3-(3-Guanidino-Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid
DB08420 1-{[1-(2-AMINO-3-PHENYL-PROPIONYL)-PYRROLIDINE-2-CARBONYL]-AMINO}-2-(3-CYANO-PHENYL)-ETHANEBORONIC ACID
DB01905 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB02193 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB02463 2-(2-Hydroxy-Phenyl)-1h-Indole-5-Carboxamidine
DB02287 2-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-Carboxamidine
DB08184 2-(2-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE
DB06918 2-(2-METHYLPHENYL)-1H-INDOLE-6-CARBOXIMIDAMIDE
DB06923 2-(3-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE
DB08254 2-NAPHTHALENESULFONIC ACID
DB04325 2-Phenylethylamine
DB04410 3-Phenylpropylamine
DB07368 4-(METHYLSULFONYL)BENZENECARBOXIMIDAMIDE
DB03243 4-Fluorobenzylamine
DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine
DB04311 4-Phenylbutylamine
DB04654 4-PIPERIDIN-4-YLBUTANAL
DB02354 4-{[1-Methyl-5-(2-Methyl-Benzoimidazol-1-Ylmethyl)-1h-Benzoimidazol-2-Ylmethyl]-Amino}-Benzamidine
DB01939 5-Amidino-Benzimidazole
DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine
DB04107 [(1-{2[(4-Carbamimidoyl-Phenylamino)-Methyl]-1-Methyl-1h-Benzoimidazol-5-Yl}-Cyclopropyl)-Pyridin-2-Yl-Methyleneaminooxy]-Acetic Acid Ethyl Ester
DB02269 [4-({[5-Benzyloxy-1-(3-Carbamimidoyl-Benzyl)-1h-Indole-2-Carbonyl]-Amino}-Methyl)-Phenyl]-Trimethyl-Ammonium
DB08763 [N-(BENZYLOXYCARBONYL)AMINO](4-AMIDINOPHENYL)METHANE-PHOSPHONATE
DB04391 Aeruginosin 98-B
DB02435 Aminomethylcyclohexane
DB02045 Amylamine
DB06692 Aprotinin
DB03127 Benzamidine
DB04446 Benzo[B]Thiophene-2-Carboxamidine
DB02464 Benzylamine
DB03213 Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone
DB04301 Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone Hydrate
DB01876 Bis(5-Amidino-2-Benzimidazolyl)Methanone
DB01705 Bis(5-Amidino-Benzimidazolyl)Methane
DB04008 Bis(5-Amidino-Benzimidazolyl)Methane Zinc
DB03443 Bis(5-Amidino-Benzimidazolyl)Methanone Zinc
DB02081 Bis-Benzamidine
DB03173 CRA_10433
DB02526 CRA_10655
DB04470 CRA_10656
DB02366 CRA_10762
DB03494 CRA_10950
DB02989 CRA_10972
DB01771 CRA_10991
DB03555 CRA_11092
DB03643 CRA_1144
DB02063 CRA_16847
DB02084 CRA_17312
DB01741 CRA_17693
DB03016 CRA_1801
DB02875 CRA_1802
DB04246 CRA_23653
DB01725 CRA_7806
DB03159 CRA_8696
DB04215 CRA_9076
DB02288 CRA_9334
DB04563 CRA_9678
DB03595 CRA_9785
DB03081 Crc200 (Chiron-Behring)
DB04269 Cyclotheonamide A
DB03608 Diminazene
DB01767 Hemi-Babim
DB01805 Monoisopropylphosphorylserine
DB04125 N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)-4-Acetyl-Piperazine
DB01745 N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)Isopipecolinic Acid Methyl Ester
DB04238 N-Alpha-(2-Naphthylsulfonyl)-N-(3-Amidino-L-Phenylalaninyl)-D-Pipecolinic Acid
DB06853 N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB06858 N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB03976 Phosphorylisopropane
DB04424 RPR128515
DB02744 RPR131247
DB03251 RWJ-51084
DB02665 Trans-2-Phenylcyclopropylamine
DB01665 ZK-800270
DB04432 ZK-805623
DB02112 Zk-806450
DB03373 ZK-806711

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2397

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PRSS1

Domain mapping of disease mutations (DMDM)

More...DMDMi		136408

<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 – 152 PublicationsAdd BLAST15
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002819716 – 23Activation peptide8
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002819824 – 247Trypsin-1Add BLAST224
ChainiPRO_000031357024 – 122Alpha-trypsin chain 1Add BLAST99
ChainiPRO_0000313571123 – 247Alpha-trypsin chain 2Add BLAST125

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 bondi30 ↔ 160
Disulfide bondi48 ↔ 64
Disulfide bondi139 ↔ 206
<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 residuei154Sulfotyrosine2 Publications1
Disulfide bondi171 ↔ 185
Disulfide bondi196 ↔ 220

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.
Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader range of dietary proteins.1 Publication

Keywords - PTMi

Disulfide bond, Sulfation, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P07477

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P07477

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

More...PaxDbi		P07477

PeptideAtlas

More...PeptideAtlasi		P07477

PRoteomics IDEntifications database

More...PRIDEi		P07477

ProteomicsDB human proteome resource

More...ProteomicsDBi		52006

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07477

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P07477

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P07477

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000204983 Expressed in 87 organ(s), highest expression level in body of pancreas

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P07477 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P07477 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB025487
CAB025538
HPA062452
HPA063471

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111626, 28 interactors

Protein interaction database and analysis system

More...IntActi		P07477, 6 interactors

Molecular INTeraction database

More...MINTi		P07477

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000308720

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P07477

<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

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P07477

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P07477

<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_and_domains_section">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 – 244Peptidase S1PROSITE-ProRule annotationAdd BLAST221

<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 peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3627 Eukaryota
COG5640 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182667

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07477

KEGG Orthology (KO)

More...KOi		K01312

Database of Orthologous Groups

More...OrthoDBi		1314811at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07477

TreeFam database of animal gene trees

More...TreeFami		TF331065

Family and domain databases

Conserved Domains Database

More...CDDi		cd00190 Tryp_SPc, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00089 Trypsin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722 CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494 SSF50494, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P07477-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNPLLILTFV AAALAAPFDD DDKIVGGYNC EENSVPYQVS LNSGYHFCGG 
        60         70         80         90        100
SLINEQWVVS AGHCYKSRIQ VRLGEHNIEV LEGNEQFINA AKIIRHPQYD 
       110        120        130        140        150
RKTLNNDIML IKLSSRAVIN ARVSTISLPT APPATGTKCL ISGWGNTASS 
       160        170        180        190        200
GADYPDELQC LDAPVLSQAK CEASYPGKIT SNMFCVGFLE GGKDSCQGDS 
       210        220        230        240 
GGPVVCNGQL QGVVSWGDGC AQKNKPGVYT KVYNYVKWIK NTIAANS
Length:247
Mass (Da):26,558
Last modified:April 1, 1988 - v1
<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:iDD49A487B8062813
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A6XGL3A6XGL3_HUMAN
Protease serine 1
PRSS1
237Annotation score:

Annotation score:1 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>
E7EQ64E7EQ64_HUMAN
Trypsin-1
PRSS1
261Annotation score:

Annotation score:1 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>
H0Y8D1H0Y8D1_HUMAN
Trypsin-1
PRSS1
142Annotation score:

Annotation score:1 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 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 conflicti4L → F in AAI28227 (PubMed:15489334).Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 24348±2 Da from positions 24 - 247. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01169316A → V in PCTT; disrupts signal sequence cleavage site. 1 PublicationCorresponds to variant dbSNP:rs202003805EnsemblClinVar.1
Natural variantiVAR_01165222D → G in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs397507442EnsemblClinVar.1
Natural variantiVAR_01165323K → R in PCTT; increased rate of activation. 1 PublicationCorresponds to variant dbSNP:rs111033567EnsemblClinVar.1
Natural variantiVAR_00672029N → I in PCTT. 4 PublicationsCorresponds to variant dbSNP:rs111033566EnsemblClinVar.1
Natural variantiVAR_01271229N → T in PCTT. 1 PublicationCorresponds to variant dbSNP:rs111033566EnsemblClinVar.1
Natural variantiVAR_03790854N → S in PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation. 1 PublicationCorresponds to variant dbSNP:rs144422014EnsemblClinVar.1
Natural variantiVAR_03790979E → K in PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect. 1 PublicationCorresponds to variant dbSNP:rs111033564EnsemblClinVar.1
Natural variantiVAR_011654104L → P in PCTT. 1 Publication1
Natural variantiVAR_011655116R → C in PCTT. 1 PublicationCorresponds to variant dbSNP:rs387906698EnsemblClinVar.1
Natural variantiVAR_012713122R → C in PCTT; suppresses an autocleavage site. 1 PublicationCorresponds to variant dbSNP:rs111033568EnsemblClinVar.1
Natural variantiVAR_006721122R → H in PCTT; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis. 5 PublicationsCorresponds to variant dbSNP:rs267606982EnsemblClinVar.1
Natural variantiVAR_036299137T → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs117497341EnsemblClinVar.1
Natural variantiVAR_011656139C → F in PCTT. 1 Publication1

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
M22612 mRNA Translation: AAA61231.1
L36092 Genomic DNA Translation: AAC80207.1
AK312199 mRNA Translation: BAG35132.1
AC231380 Genomic DNA No translation available.
CH236959 Genomic DNA Translation: EAL23773.1
CH471198 Genomic DNA Translation: EAW51925.1
BC128226 mRNA Translation: AAI28227.1
AF314534 Genomic DNA Translation: AAG30943.1
U70137 Genomic DNA Translation: AAC50728.1
AF315309 Genomic DNA Translation: AAG30947.1
AF315310 Genomic DNA Translation: AAG30948.1
AF315311 Genomic DNA Translation: AAG30949.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS5872.1

Protein sequence database of the Protein Information Resource

More...PIRi		A25852
S50020
S50021

NCBI Reference Sequences

More...RefSeqi		NP_002760.1, NM_002769.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000311737; ENSP00000308720; ENSG00000204983
ENST00000616256; ENSP00000479217; ENSG00000274247

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5644

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5644

UCSC genome browser

More...UCSCi		uc003wak.3 human

Keywords - Coding sequence diversityi

Polymorphism

<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
M22612 mRNA Translation: AAA61231.1
L36092 Genomic DNA Translation: AAC80207.1
AK312199 mRNA Translation: BAG35132.1
AC231380 Genomic DNA No translation available.
CH236959 Genomic DNA Translation: EAL23773.1
CH471198 Genomic DNA Translation: EAW51925.1
BC128226 mRNA Translation: AAI28227.1
AF314534 Genomic DNA Translation: AAG30943.1
U70137 Genomic DNA Translation: AAC50728.1
AF315309 Genomic DNA Translation: AAG30947.1
AF315310 Genomic DNA Translation: AAG30948.1
AF315311 Genomic DNA Translation: AAG30949.1
CCDSiCCDS5872.1
PIRiA25852
S50020
S50021
RefSeqiNP_002760.1, NM_002769.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FXYX-ray2.15A127-247[»]
1TRNX-ray2.20A/B24-247[»]
2RA3X-ray1.46A/B24-247[»]
4WWYX-ray1.70A/B24-247[»]
4WXVX-ray2.10A/B24-247[»]
SMRiP07477
ModBaseiSearch...

Protein-protein interaction databases

BioGridi111626, 28 interactors
IntActiP07477, 6 interactors
MINTiP07477
STRINGi9606.ENSP00000308720

Chemistry databases

BindingDBiP07477
ChEMBLiCHEMBL209
DrugBankiDB06850 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide
DB07091 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide
DB06845 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide
DB07088 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide
DB07131 (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide
DB07095 (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide
DB07985 +/-METHYL 4-(AMINOIMINOMETHYL)-BETA-[3- INH (AMINOIMINO)PHENYL]BENZENE PENTANOATE
DB03337 1-(2-Amidinophenyl)-3-(Phenoxyphenyl)Urea
DB04336 1-(4-Amidinophenyl)-3-(4-Chlorophenyl)Urea
DB03417 1-(4-Tert-Butylcarbamoyl-Piperazine-1-Carbonyl)-3-(3-Guanidino-Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid
DB08420 1-{[1-(2-AMINO-3-PHENYL-PROPIONYL)-PYRROLIDINE-2-CARBONYL]-AMINO}-2-(3-CYANO-PHENYL)-ETHANEBORONIC ACID
DB01905 2-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB02193 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB02463 2-(2-Hydroxy-Phenyl)-1h-Indole-5-Carboxamidine
DB02287 2-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-Carboxamidine
DB08184 2-(2-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE
DB06918 2-(2-METHYLPHENYL)-1H-INDOLE-6-CARBOXIMIDAMIDE
DB06923 2-(3-METHYLPHENYL)-1H-INDOLE-5-CARBOXIMIDAMIDE
DB08254 2-NAPHTHALENESULFONIC ACID
DB04325 2-Phenylethylamine
DB04410 3-Phenylpropylamine
DB07368 4-(METHYLSULFONYL)BENZENECARBOXIMIDAMIDE
DB03243 4-Fluorobenzylamine
DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine
DB04311 4-Phenylbutylamine
DB04654 4-PIPERIDIN-4-YLBUTANAL
DB02354 4-{[1-Methyl-5-(2-Methyl-Benzoimidazol-1-Ylmethyl)-1h-Benzoimidazol-2-Ylmethyl]-Amino}-Benzamidine
DB01939 5-Amidino-Benzimidazole
DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine
DB04107 [(1-{2[(4-Carbamimidoyl-Phenylamino)-Methyl]-1-Methyl-1h-Benzoimidazol-5-Yl}-Cyclopropyl)-Pyridin-2-Yl-Methyleneaminooxy]-Acetic Acid Ethyl Ester
DB02269 [4-({[5-Benzyloxy-1-(3-Carbamimidoyl-Benzyl)-1h-Indole-2-Carbonyl]-Amino}-Methyl)-Phenyl]-Trimethyl-Ammonium
DB08763 [N-(BENZYLOXYCARBONYL)AMINO](4-AMIDINOPHENYL)METHANE-PHOSPHONATE
DB04391 Aeruginosin 98-B
DB02435 Aminomethylcyclohexane
DB02045 Amylamine
DB06692 Aprotinin
DB03127 Benzamidine
DB04446 Benzo[B]Thiophene-2-Carboxamidine
DB02464 Benzylamine
DB03213 Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone
DB04301 Bis(5-Amidino-2-Benzimidazolyl)Methane Ketone Hydrate
DB01876 Bis(5-Amidino-2-Benzimidazolyl)Methanone
DB01705 Bis(5-Amidino-Benzimidazolyl)Methane
DB04008 Bis(5-Amidino-Benzimidazolyl)Methane Zinc
DB03443 Bis(5-Amidino-Benzimidazolyl)Methanone Zinc
DB02081 Bis-Benzamidine
DB03173 CRA_10433
DB02526 CRA_10655
DB04470 CRA_10656
DB02366 CRA_10762
DB03494 CRA_10950
DB02989 CRA_10972
DB01771 CRA_10991
DB03555 CRA_11092
DB03643 CRA_1144
DB02063 CRA_16847
DB02084 CRA_17312
DB01741 CRA_17693
DB03016 CRA_1801
DB02875 CRA_1802
DB04246 CRA_23653
DB01725 CRA_7806
DB03159 CRA_8696
DB04215 CRA_9076
DB02288 CRA_9334
DB04563 CRA_9678
DB03595 CRA_9785
DB03081 Crc200 (Chiron-Behring)
DB04269 Cyclotheonamide A
DB03608 Diminazene
DB01767 Hemi-Babim
DB01805 Monoisopropylphosphorylserine
DB04125 N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)-4-Acetyl-Piperazine
DB01745 N-Alpha-(2-Naphthylsulfonyl)-N(3-Amidino-L-Phenylalaninyl)Isopipecolinic Acid Methyl Ester
DB04238 N-Alpha-(2-Naphthylsulfonyl)-N-(3-Amidino-L-Phenylalaninyl)-D-Pipecolinic Acid
DB06853 N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB06858 N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB03976 Phosphorylisopropane
DB04424 RPR128515
DB02744 RPR131247
DB03251 RWJ-51084
DB02665 Trans-2-Phenylcyclopropylamine
DB01665 ZK-800270
DB04432 ZK-805623
DB02112 Zk-806450
DB03373 ZK-806711
GuidetoPHARMACOLOGYi2397

Protein family/group databases

MEROPSiS01.127

PTM databases

iPTMnetiP07477
PhosphoSitePlusiP07477

Polymorphism and mutation databases

BioMutaiPRSS1
DMDMi136408

Proteomic databases

EPDiP07477
jPOSTiP07477
PaxDbiP07477
PeptideAtlasiP07477
PRIDEiP07477
ProteomicsDBi52006

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311737; ENSP00000308720; ENSG00000204983
ENST00000616256; ENSP00000479217; ENSG00000274247
GeneIDi5644
KEGGihsa:5644
UCSCiuc003wak.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5644
DisGeNETi5644

GeneCards: human genes, protein and diseases

More...GeneCardsi		PRSS1
GeneReviewsiPRSS1
HGNCiHGNC:9475 PRSS1
HPAiCAB025487
CAB025538
HPA062452
HPA063471
MalaCardsiPRSS1
MIMi167800 phenotype
276000 gene
neXtProtiNX_P07477
OpenTargetsiENSG00000204983
Orphaneti676 Hereditary chronic pancreatitis
PharmGKBiPA33828

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
GeneTreeiENSGT00950000182667
InParanoidiP07477
KOiK01312
OrthoDBi1314811at2759
PhylomeDBiP07477
TreeFamiTF331065

Enzyme and pathway databases

ReactomeiR-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-196741 Cobalamin (Cbl, vitamin B12) transport and metabolism

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PRSS1 human
EvolutionaryTraceiP07477

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Trypsin_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5644
PMAP-CutDBiP07477

Protein Ontology

More...PROi		PR:P07477

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000204983 Expressed in 87 organ(s), highest expression level in body of pancreas
ExpressionAtlasiP07477 baseline and differential
GenevisibleiP07477 HS

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 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 nameiTRY1_HUMAN
<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: P07477
Secondary accession number(s): A1A509
, A6NJ71, B2R5I5, Q5NV57, Q7M4N3, Q7M4N4, Q92955, Q9HAN4, Q9HAN5, Q9HAN6, Q9HAN7
<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_and_isoforms">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, 1988
Last sequence update: April 1, 1988
Last modified: June 5, 2019
This is version 207 of the entry and version 1 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
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.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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