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UniProtKB - P04070 (PROC_HUMAN)

Entry version 241 (08 May 2019)
Sequence version 1 (01 Nov 1986)
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Protein

Vitamin K-dependent protein C

Gene

PROC

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

Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845).2 Publications

Miscellaneous

Calcium also binds, with stronger affinity to another site, beyond the GLA domain. This GLA-independent binding site is necessary for the recognition of the thrombin-thrombomodulin complex.

<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

  • Degradation of blood coagulation factors Va and VIIIa. EC:3.4.21.69

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei253Charge relay system1
Active sitei299Charge relay system1
Active sitei402Charge 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

  • calcium ion binding Source: InterPro
  • serine-type endopeptidase activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 processBlood coagulation, Hemostasis
LigandCalcium

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.69 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8957275 Post-translational protein phosphorylation

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P04070

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.218

<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:
Vitamin K-dependent protein C (EC:3.4.21.69)
Alternative name(s):
Anticoagulant protein C
Autoprothrombin IIA
Blood coagulation factor XIV
Cleaved into the following 3 chains:
Vitamin K-dependent protein C light chain
Vitamin K-dependent protein C heavy chain
Activation peptide
<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:PROC
<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 2

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9451 PROC

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		612283 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P04070

<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

Endoplasmic reticulum, Golgi apparatus, 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

Thrombophilia due to protein C deficiency, autosomal dominant (THPH3)16 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. Individuals with decreased amounts of protein C are classically referred to as having type I protein C deficiency and those with normal amounts of a functionally defective protein as having type II deficiency.
See also OMIM:176860
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_00663532R → C in THPH3. 1 Publication1
Natural variantiVAR_05507442R → S in THPH3; type II; Osaka-10; alters proteolytic processing so that S-42 is the N-terminus of the mature protein. 1 PublicationCorresponds to variant dbSNP:rs774572099Ensembl.1
Natural variantiVAR_00664257R → W in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs757583846EnsemblClinVar.1
Natural variantiVAR_00664562E → A in THPH3; Vermont-1. 1 PublicationCorresponds to variant dbSNP:rs121918148EnsemblClinVar.1
Natural variantiVAR_00664676V → M in THPH3; Vermont-1. 1 PublicationCorresponds to variant dbSNP:rs121918149EnsemblClinVar.1
Natural variantiVAR_006651114G → R in THPH3. 1 PublicationCorresponds to variant dbSNP:rs374476971EnsemblClinVar.1
Natural variantiVAR_006656145G → R in THPH3. 1 PublicationCorresponds to variant dbSNP:rs370813536Ensembl.1
Natural variantiVAR_073147163A → V in THPH3; drastically reduced secretion; colocalizes with 26S proteasome. 1 Publication1
Natural variantiVAR_006664210P → L in THPH3. 1 PublicationCorresponds to variant dbSNP:rs121918145EnsemblClinVar.1
Natural variantiVAR_006665211R → W in THPH3; London-1/Tochigi. 2 PublicationsCorresponds to variant dbSNP:rs121918143EnsemblClinVar.1
Natural variantiVAR_006669220R → Q in THPH3; Vermont-3. 3 PublicationsCorresponds to variant dbSNP:rs121918153EnsemblClinVar.1
Natural variantiVAR_006668220R → W in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs121918152EnsemblClinVar.1
Natural variantiVAR_006671243I → T in THPH3. 1 PublicationCorresponds to variant dbSNP:rs774584131Ensembl.1
Natural variantiVAR_006677272R → C in THPH3. 1 PublicationCorresponds to variant dbSNP:rs121918154EnsemblClinVar.1
Natural variantiVAR_074303297D → H in THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity; decreased Golgi localization. 2 PublicationsCorresponds to variant dbSNP:rs199469471Ensembl.1
Natural variantiVAR_006687321P → L in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs1321566264Ensembl.1
Natural variantiVAR_006688324G → R in THPH3. 1 Publication1
Natural variantiVAR_006689328R → C in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs201907715Ensembl.1
Natural variantiVAR_006692340T → M in THPH3; Vermont-2. 2 PublicationsCorresponds to variant dbSNP:rs766261022Ensembl.1
Natural variantiVAR_006696369P → L in THPH3; Osaka-6. 2 PublicationsCorresponds to variant dbSNP:rs1211098698Ensembl.1
Natural variantiVAR_006700392G → R in THPH3; Osaka-9. 1 PublicationCorresponds to variant dbSNP:rs756467027EnsemblClinVar.1
Natural variantiVAR_006702401D → N in THPH3; La Jolla-2/Osaka-7 and -8. 1 PublicationCorresponds to variant dbSNP:rs142742242EnsemblClinVar.1
Natural variantiVAR_074307420V → L in THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity. 2 PublicationsCorresponds to variant dbSNP:rs199469472Ensembl.1
Natural variantiVAR_006704423G → S in THPH3. 1 Publication1
Natural variantiVAR_006705426C → Y in THPH3. 1 Publication1
Natural variantiVAR_006707436T → N in THPH3. 1 Publication1
Natural variantiVAR_006708441Y → H in THPH3; Osaka-4. 1 PublicationCorresponds to variant dbSNP:rs753436021Ensembl.1
Natural variantiVAR_006709444W → C in THPH3. 1 PublicationCorresponds to variant dbSNP:rs121918142EnsemblClinVar.1
Thrombophilia due to protein C deficiency, autosomal recessive (THPH4)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemostatic disorder characterized by impaired regulation of blood coagulation and a tendency to recurrent venous thrombosis. It results in a thrombotic condition that can manifest as a severe neonatal disorder or as a milder disorder with late-onset thrombophilia. The severe form leads to neonatal death through massive neonatal venous thrombosis. Often associated with ecchymotic skin lesions which can turn necrotic called purpura fulminans, this disorder is very rare.
See also OMIM:612304
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07314577D → G in THPH4; no effect on secretion; no effect on catalytic activity in vitro. 1 Publication1
Natural variantiVAR_006655144 – 145NG → K in THPH4; neonatal purpura fulminans. 1 Publication2
Natural variantiVAR_073146163A → E in THPH4; drastically reduced secretion; colocalizes with 26S proteasome. 1 Publication1
Natural variantiVAR_006660178A → P in THPH4; Clamart. 1 PublicationCorresponds to variant dbSNP:rs1254257945Ensembl.1
Natural variantiVAR_006679289P → L in THPH4. 1 PublicationCorresponds to variant dbSNP:rs121918151EnsemblClinVar.1
Natural variantiVAR_006690328R → H in THPH4; Muenchen. 1 Publication1
Natural variantiVAR_006691334G → S in THPH4. 1 PublicationCorresponds to variant dbSNP:rs121918150EnsemblClinVar.1
Natural variantiVAR_006695367V → A in THPH4; neonatal purpura fulminans. 1 PublicationCorresponds to variant dbSNP:rs767730328Ensembl.1
Natural variantiVAR_006703418G → D in THPH4; Hong Kong-2. 1 Publication1

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNET

More...DisGeNETi		5624

MalaCards human disease database

More...MalaCardsi		PROC
MIMi176860 phenotype
612304 phenotype

Open Targets

More...OpenTargetsi		ENSG00000115718

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

More...Orphaneti		64738 NON RARE IN EUROPE: Non rare thrombophilia
745 Severe hereditary thrombophilia due to congenital protein C deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33799

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4444

Drug and drug target database

More...DrugBanki		DB00025 Antihemophilic Factor (Recombinant)
DB00170 Menadione
DB00464 Sodium Tetradecyl Sulfate

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2396

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PROC

Domain mapping of disease mutations (DMDM)

More...DMDMi		131067

<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 – 18Sequence analysisAdd BLAST18
<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_000002810719 – 42Add BLAST24
<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_000002810843 – 461Vitamin K-dependent protein CAdd BLAST419
ChainiPRO_000002810943 – 197Vitamin K-dependent protein C light chainAdd BLAST155
ChainiPRO_0000028110200 – 461Vitamin K-dependent protein C heavy chainAdd BLAST262
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000028111200 – 211Activation peptideAdd BLAST12

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi19O-linked (GalNAc...) threonine1 Publication1
<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 residuei484-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei494-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei584-carboxyglutamatePROSITE-ProRule annotation1 Publication1
<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 bondi59 ↔ 64
Modified residuei614-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei624-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei684-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei714-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi92 ↔ 111
Disulfide bondi101 ↔ 106
Disulfide bondi105 ↔ 120
Modified residuei113(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi122 ↔ 131
Glycosylationi139N-linked (GlcNAc...) asparagine1
Disulfide bondi140 ↔ 151
Disulfide bondi147 ↔ 160
Disulfide bondi162 ↔ 175
Disulfide bondi183 ↔ 319Interchain (between light and heavy chains)
Disulfide bondi238 ↔ 254
Glycosylationi290N-linked (GlcNAc...) asparagine2 Publications1
Modified residuei347Phosphoserine; by FAM20C1 Publication1
Glycosylationi355N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi371N-linked (GlcNAc...) asparagine; atypical; partial2 Publications1
Disulfide bondi373 ↔ 387
Disulfide bondi398 ↔ 426

<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

The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not N-glycosylated at Asn-371, is beta. O-glycosylated with core 1 or possibly core 8 glycans.4 Publications
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.2 Publications
May be phosphorylated on a Ser or Thr in a region (AA 25-30) of the propeptide.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei211 – 212Cleavage; by thrombin2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Zymogen

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P04070

MaxQB - The MaxQuant DataBase

More...MaxQBi		P04070

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

More...PaxDbi		P04070

PeptideAtlas

More...PeptideAtlasi		P04070

PRoteomics IDEntifications database

More...PRIDEi		P04070

ProteomicsDB human proteome resource

More...ProteomicsDBi		51646

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		620

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P04070

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

More...PhosphoSitePlusi		P04070

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P04070

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P04070

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000115718 Expressed in 94 organ(s), highest expression level in right lobe of liver

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P04070 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P04070 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB016721
CAB016792
HPA005550

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
MMP15P515112EBI-1383018,EBI-1383043

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111608, 11 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P04070

Protein interaction database and analysis system

More...IntActi		P04070, 5 interactors

Molecular INTeraction database

More...MINTi		P04070

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000234071

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P04070

<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

1461
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1AUTX-ray2.80C212-461[»]
L84-197[»]
1LQVX-ray1.60C/D43-75[»]
1PCUmodel-A175-450[»]
2PCTmodel-A175-450[»]
3F6UX-ray2.80H212-451[»]
L91-188[»]
3JTCX-ray1.60C/D43-75[»]
4DT7X-ray1.90E/F204-223[»]

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

More...SMRi		P04070

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P04070

<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>Domaini43 – 88GlaPROSITE-ProRule annotationAdd BLAST46
Domaini97 – 132EGF-like 1PROSITE-ProRule annotationAdd BLAST36
Domaini136 – 176EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini212 – 450Peptidase S1PROSITE-ProRule annotationAdd BLAST239

<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

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IJRM Eukaryota
COG5640 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154505

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000251821

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P04070

KEGG Orthology (KO)

More...KOi		K01344

Database of Orthologous Groups

More...OrthoDBi		311898at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P04070

TreeFam database of animal gene trees

More...TreeFami		TF327329

Family and domain databases

Conserved Domains Database

More...CDDi		cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.740.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
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
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001143 Factor_X, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722 CHYMOTRYPSIN
PR00001 GLABLOOD

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS00011 GLA_1, 1 hit
PS50998 GLA_2, 1 hit
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P04070-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL 
        60         70         80         90        100
RHSSLERECI EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP 
       110        120        130        140        150
CASLCCGHGT CIDGIGSFSC DCRSGWEGRF CQREVSFLNC SLDNGGCTHY 
       160        170        180        190        200
CLEEVGWRRC SCAPGYKLGD DLLQCHPAVK FPCGRPWKRM EKKRSHLKRD 
       210        220        230        240        250
TEDQEDQVDP RLIDGKMTRR GDSPWQVVLL DSKKKLACGA VLIHPSWVLT 
       260        270        280        290        300
AAHCMDESKK LLVRLGEYDL RRWEKWELDL DIKEVFVHPN YSKSTTDNDI 
       310        320        330        340        350
ALLHLAQPAT LSQTIVPICL PDSGLAEREL NQAGQETLVT GWGYHSSREK 
       360        370        380        390        400
EAKRNRTFVL NFIKIPVVPH NECSEVMSNM VSENMLCAGI LGDRQDACEG 
       410        420        430        440        450
DSGGPMVASF HGTWFLVGLV SWGEGCGLLH NYGVYTKVSR YLDWIHGHIR 
       460 
DKEAPQKSWA P
Length:461
Mass (Da):52,071
Last modified:November 1, 1986 - 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:i3531B0AE5345B39A
GO
Isoform 2 (identifier: P04070-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAAGRRTCSISTTRPCASASRM
     133-133: R → RGEGERWMLAGGGAGLGPGWGRGTSTSCPRPPLPA

Note: No experimental confirmation available.
Show »
Length:516
Mass (Da):57,556
Checksum:i6F21DD7C17317C88
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7END6E7END6_HUMAN
Vitamin K-dependent protein C
PROC
495Annotation score:

Annotation score:2 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>
E7ENR9E7ENR9_HUMAN
Vitamin K-dependent protein C
PROC
175Annotation 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>
E7EVH6E7EVH6_HUMAN
Vitamin K-dependent protein C
PROC
126Annotation 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>
E7EU72E7EU72_HUMAN
Vitamin K-dependent protein C
PROC
116Annotation 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>
H7BYX9H7BYX9_HUMAN
Vitamin K-dependent protein C
PROC
236Annotation 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>
F2Z2A0F2Z2A0_HUMAN
Vitamin K-dependent protein C
PROC
52Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence S76088 differs from that shown. Reason: Erroneous termination at position 151. Translated as Cys.Curated

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 conflicti106C → Q in AAA60164 (PubMed:6589623).Curated1
Sequence conflicti445I → IL in AAA60165 (PubMed:3511471).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00663414W → G in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_00663532R → C in THPH3. 1 Publication1
Natural variantiVAR_00663638R → W in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs769900251Ensembl.1
Natural variantiVAR_00663842R → C in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs774572099Ensembl.1
Natural variantiVAR_00663742R → H in Malakoff; low anticoagulant activity. 1 PublicationCorresponds to variant dbSNP:rs369504169EnsemblClinVar.1
Natural variantiVAR_05507442R → S in THPH3; type II; Osaka-10; alters proteolytic processing so that S-42 is the N-terminus of the mature protein. 1 PublicationCorresponds to variant dbSNP:rs774572099Ensembl.1
Natural variantiVAR_00663943A → T1 PublicationCorresponds to variant dbSNP:rs767626189Ensembl.1
Natural variantiVAR_00664049E → D in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_00664151R → C in patients with PROC deficiency. Corresponds to variant dbSNP:rs764546127Ensembl.1
Natural variantiVAR_00664357R → G in Yonago; defective anticoagulant activity. 1 Publication1
Natural variantiVAR_00664457R → Q in patients with PROC deficiency. Corresponds to variant dbSNP:rs574949343Ensembl.1
Natural variantiVAR_00664257R → W in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs757583846EnsemblClinVar.1
Natural variantiVAR_00664562E → A in THPH3; Vermont-1. 1 PublicationCorresponds to variant dbSNP:rs121918148EnsemblClinVar.1
Natural variantiVAR_07429670K → E in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs199469481Ensembl.1
Natural variantiVAR_00664676V → M in THPH3; Vermont-1. 1 PublicationCorresponds to variant dbSNP:rs121918149EnsemblClinVar.1
Natural variantiVAR_07314577D → G in THPH4; no effect on secretion; no effect on catalytic activity in vitro. 1 Publication1
Natural variantiVAR_00664789G → C in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_074297106C → G in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs199469479Ensembl.1
Natural variantiVAR_006648108H → N in patients with PROC deficiency; La Jolla-1. Corresponds to variant dbSNP:rs200234655EnsemblClinVar.1
Natural variantiVAR_006649109G → R in patients with PROC deficiency. 1
Natural variantiVAR_006650114 – 118Missing in patients with PROC deficiency. 5
Natural variantiVAR_006651114G → R in THPH3. 1 PublicationCorresponds to variant dbSNP:rs374476971EnsemblClinVar.1
Natural variantiVAR_074298118F → A in patients with PROC deficiency; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_006652118F → L in patients with PROC deficiency. 1
Natural variantiVAR_006653119 – 124Missing in patients with PROC deficiency; St Louis-2. 6
Natural variantiVAR_006654120 – 125Missing in patients with PROC deficiency; St Louis-3. 6
Natural variantiVAR_006655144 – 145NG → K in THPH4; neonatal purpura fulminans. 1 Publication2
Natural variantiVAR_006656145G → R in THPH3. 1 PublicationCorresponds to variant dbSNP:rs370813536Ensembl.1
Natural variantiVAR_006657147C → Y in patients with PROC deficiency. Corresponds to variant dbSNP:rs1247269491Ensembl.1
Natural variantiVAR_006658149H → P in patients with PROC deficiency. Corresponds to variant dbSNP:rs121918159EnsemblClinVar.1
Natural variantiVAR_006659161S → R in patients with PROC deficiency. Corresponds to variant dbSNP:rs1433503391Ensembl.1
Natural variantiVAR_073146163A → E in THPH4; drastically reduced secretion; colocalizes with 26S proteasome. 1 Publication1
Natural variantiVAR_073147163A → V in THPH3; drastically reduced secretion; colocalizes with 26S proteasome. 1 Publication1
Natural variantiVAR_074299175C → Y in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs199469474Ensembl.1
Natural variantiVAR_006660178A → P in THPH4; Clamart. 1 PublicationCorresponds to variant dbSNP:rs1254257945Ensembl.1
Natural variantiVAR_074300181F → V in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs199469470Ensembl.1
Natural variantiVAR_006661183C → R in patients with PROC deficiency. Corresponds to variant dbSNP:rs748920874Ensembl.1
Natural variantiVAR_006662189R → W in patients with PROC deficiency; La Jolla-3. 1 PublicationCorresponds to variant dbSNP:rs146922325EnsemblClinVar.1
Natural variantiVAR_006663194R → C in patients with PROC deficiency. Corresponds to variant dbSNP:rs371071104EnsemblClinVar.1
Natural variantiVAR_006664210P → L in THPH3. 1 PublicationCorresponds to variant dbSNP:rs121918145EnsemblClinVar.1
Natural variantiVAR_006666211R → Q in patients with PROC deficiency. 2 PublicationsCorresponds to variant dbSNP:rs199469476Ensembl.1
Natural variantiVAR_006665211R → W in THPH3; London-1/Tochigi. 2 PublicationsCorresponds to variant dbSNP:rs121918143EnsemblClinVar.1
Natural variantiVAR_006667220R → P in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_006669220R → Q in THPH3; Vermont-3. 3 PublicationsCorresponds to variant dbSNP:rs121918153EnsemblClinVar.1
Natural variantiVAR_006668220R → W in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs121918152EnsemblClinVar.1
Natural variantiVAR_074301223S → R in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs199469483Ensembl.1
Natural variantiVAR_006670226Q → H in patients with PROC deficiency. Corresponds to variant dbSNP:rs121918155EnsemblClinVar.1
Natural variantiVAR_074302240A → G in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_006671243I → T in THPH3. 1 PublicationCorresponds to variant dbSNP:rs774584131Ensembl.1
Natural variantiVAR_006672244H → Y in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs759557871Ensembl.1
Natural variantiVAR_006673253H → Q in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs1458669732Ensembl.1
Natural variantiVAR_006674265L → F in patients with PROC deficiency. Corresponds to variant dbSNP:rs121918156EnsemblClinVar.1
Natural variantiVAR_006675271R → Q in Marseille; low anticoagulant activity. 1 PublicationCorresponds to variant dbSNP:rs752290840Ensembl.1
Natural variantiVAR_006676271R → W in patients with PROC deficiency. Corresponds to variant dbSNP:rs767112991EnsemblClinVar.1
Natural variantiVAR_006677272R → C in THPH3. 1 PublicationCorresponds to variant dbSNP:rs121918154EnsemblClinVar.1
Natural variantiVAR_006678281D → DLD in patients with PROC deficiency. 1
Natural variantiVAR_006679289P → L in THPH4. 1 PublicationCorresponds to variant dbSNP:rs121918151EnsemblClinVar.1
Natural variantiVAR_006680294S → N in Paris; low anticoagulant activity. 1 PublicationCorresponds to variant dbSNP:rs200721675Ensembl.1
Natural variantiVAR_074303297D → H in THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity; decreased Golgi localization. 2 PublicationsCorresponds to variant dbSNP:rs199469471Ensembl.1
Natural variantiVAR_006681298N → D in patients with PROC deficiency. 1
Natural variantiVAR_006682301A → T in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs1343264503Ensembl.1
Natural variantiVAR_006683301A → V in patients with PROC deficiency. Corresponds to variant dbSNP:rs121918144EnsemblClinVar.1
Natural variantiVAR_006684309A → T in patients with PROC deficiency. Corresponds to variant dbSNP:rs121918146EnsemblClinVar.1
Natural variantiVAR_006685312S → L in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs121918160EnsemblClinVar.1
Natural variantiVAR_006686312S → P in a patient with PROC deficiency; sporadic case. 1 Publication1
Natural variantiVAR_074304317P → S in patients with PROC deficiency; abolishes Golgi localization. 1 Publication1
Natural variantiVAR_006687321P → L in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs1321566264Ensembl.1
Natural variantiVAR_006688324G → R in THPH3. 1 Publication1
Natural variantiVAR_074305327E → V in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs199469480Ensembl.1
Natural variantiVAR_006689328R → C in THPH3. 2 PublicationsCorresponds to variant dbSNP:rs201907715Ensembl.1
Natural variantiVAR_006690328R → H in THPH4; Muenchen. 1 Publication1
Natural variantiVAR_006691334G → S in THPH4. 1 PublicationCorresponds to variant dbSNP:rs121918150EnsemblClinVar.1
Natural variantiVAR_006692340T → M in THPH3; Vermont-2. 2 PublicationsCorresponds to variant dbSNP:rs766261022Ensembl.1
Natural variantiVAR_006693343G → D in patients with PROC deficiency. 1
Natural variantiVAR_074306357T → A Gain of function mutation; abolishes glycosylation at N-313; decreases its catalytic activity; significant loss of its protective effect on endothelial barrier function; increased activation by thrombin. 1 Publication1
Natural variantiVAR_006694363Missing in patients with PROC deficiency. 1
Natural variantiVAR_006695367V → A in THPH4; neonatal purpura fulminans. 1 PublicationCorresponds to variant dbSNP:rs767730328Ensembl.1
Natural variantiVAR_006696369P → L in THPH3; Osaka-6. 2 PublicationsCorresponds to variant dbSNP:rs1211098698Ensembl.1
Natural variantiVAR_006697385M → I in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_006698388A → T in patients with PROC deficiency. 1 Publication1
Natural variantiVAR_006699388A → V in patients with PROC deficiency. 1 PublicationCorresponds to variant dbSNP:rs769277939Ensembl.1
Natural variantiVAR_006700392G → R in THPH3; Osaka-9. 1 PublicationCorresponds to variant dbSNP:rs756467027EnsemblClinVar.1
Natural variantiVAR_006701394R → W in patients with PROC deficiency. Corresponds to variant dbSNP:rs759316085Ensembl.1
Natural variantiVAR_006702401D → N in THPH3; La Jolla-2/Osaka-7 and -8. 1 PublicationCorresponds to variant dbSNP:rs142742242EnsemblClinVar.1
Natural variantiVAR_006703418G → D in THPH4; Hong Kong-2. 1 Publication1
Natural variantiVAR_074307420V → L in THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity. 2 PublicationsCorresponds to variant dbSNP:rs199469472Ensembl.1
Natural variantiVAR_006704423G → S in THPH3. 1 Publication1
Natural variantiVAR_006705426C → Y in THPH3. 1 Publication1
Natural variantiVAR_006706433G → S in patients with PROC deficiency; Purmerend. Corresponds to variant dbSNP:rs1266965698Ensembl.1
Natural variantiVAR_006707436T → N in THPH3. 1 Publication1
Natural variantiVAR_006708441Y → H in THPH3; Osaka-4. 1 PublicationCorresponds to variant dbSNP:rs753436021Ensembl.1
Natural variantiVAR_006709444W → C in THPH3. 1 PublicationCorresponds to variant dbSNP:rs121918142EnsemblClinVar.1
Natural variantiVAR_006710445I → M in patients with PROC deficiency. Corresponds to variant dbSNP:rs121918157EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0543931M → MAAGRRTCSISTTRPCASAS RM in isoform 2. 1 Publication1
Alternative sequenceiVSP_054394133R → RGEGERWMLAGGGAGLGPGW GRGTSTSCPRPPLPA in isoform 2. 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
X02750 mRNA Translation: CAA26528.1
M11228 Genomic DNA Translation: AAA60166.1
M12712
, M12683, M12684, M12685, M12686, M12687 Genomic DNA Translation: AAA60165.1
AF378903 Genomic DNA Translation: AAK56377.1
AK298454 mRNA Translation: BAG60669.1
AC068282 Genomic DNA Translation: AAY15044.1
CH471103 Genomic DNA Translation: EAW95320.1
BC034377 mRNA Translation: AAH34377.1
S58668 Genomic DNA Translation: AAB26335.1
K02059 mRNA Translation: AAA60164.1
S76088 Genomic DNA No translation available.
S76090 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS2145.1 [P04070-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A22331 KXHU

NCBI Reference Sequences

More...RefSeqi		NP_000303.1, NM_000312.3 [P04070-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000234071; ENSP00000234071; ENSG00000115718 [P04070-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5624

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5624

UCSC genome browser

More...UCSCi		uc002tok.4 human [P04070-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Protein C entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02750 mRNA Translation: CAA26528.1
M11228 Genomic DNA Translation: AAA60166.1
M12712
, M12683, M12684, M12685, M12686, M12687 Genomic DNA Translation: AAA60165.1
AF378903 Genomic DNA Translation: AAK56377.1
AK298454 mRNA Translation: BAG60669.1
AC068282 Genomic DNA Translation: AAY15044.1
CH471103 Genomic DNA Translation: EAW95320.1
BC034377 mRNA Translation: AAH34377.1
S58668 Genomic DNA Translation: AAB26335.1
K02059 mRNA Translation: AAA60164.1
S76088 Genomic DNA No translation available.
S76090 Genomic DNA No translation available.
CCDSiCCDS2145.1 [P04070-1]
PIRiA22331 KXHU
RefSeqiNP_000303.1, NM_000312.3 [P04070-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AUTX-ray2.80C212-461[»]
L84-197[»]
1LQVX-ray1.60C/D43-75[»]
1PCUmodel-A175-450[»]
2PCTmodel-A175-450[»]
3F6UX-ray2.80H212-451[»]
L91-188[»]
3JTCX-ray1.60C/D43-75[»]
4DT7X-ray1.90E/F204-223[»]
SMRiP04070
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111608, 11 interactors
ELMiP04070
IntActiP04070, 5 interactors
MINTiP04070
STRINGi9606.ENSP00000234071

Chemistry databases

BindingDBiP04070
ChEMBLiCHEMBL4444
DrugBankiDB00025 Antihemophilic Factor (Recombinant)
DB00170 Menadione
DB00464 Sodium Tetradecyl Sulfate
GuidetoPHARMACOLOGYi2396

Protein family/group databases

MEROPSiS01.218

PTM databases

GlyConnecti620
iPTMnetiP04070
PhosphoSitePlusiP04070
UniCarbKBiP04070

Polymorphism and mutation databases

BioMutaiPROC
DMDMi131067

Proteomic databases

jPOSTiP04070
MaxQBiP04070
PaxDbiP04070
PeptideAtlasiP04070
PRIDEiP04070
ProteomicsDBi51646

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5624
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234071; ENSP00000234071; ENSG00000115718 [P04070-1]
GeneIDi5624
KEGGihsa:5624
UCSCiuc002tok.4 human [P04070-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5624
DisGeNETi5624

GeneCards: human genes, protein and diseases

More...GeneCardsi		PROC
HGNCiHGNC:9451 PROC
HPAiCAB016721
CAB016792
HPA005550
MalaCardsiPROC
MIMi176860 phenotype
612283 gene
612304 phenotype
neXtProtiNX_P04070
OpenTargetsiENSG00000115718
Orphaneti64738 NON RARE IN EUROPE: Non rare thrombophilia
745 Severe hereditary thrombophilia due to congenital protein C deficiency
PharmGKBiPA33799

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IJRM Eukaryota
COG5640 LUCA
GeneTreeiENSGT00940000154505
HOGENOMiHOG000251821
InParanoidiP04070
KOiK01344
OrthoDBi311898at2759
PhylomeDBiP04070
TreeFamiTF327329

Enzyme and pathway databases

BRENDAi3.4.21.69 2681
ReactomeiR-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8957275 Post-translational protein phosphorylation
SABIO-RKiP04070

Miscellaneous databases

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

More...ChiTaRSi		PROC human
EvolutionaryTraceiP04070

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Protein_C

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

More...GenomeRNAii		5624
PMAP-CutDBiP04070

Protein Ontology

More...PROi		PR:P04070

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000115718 Expressed in 94 organ(s), highest expression level in right lobe of liver
ExpressionAtlasiP04070 baseline and differential
GenevisibleiP04070 HS

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS00011 GLA_1, 1 hit
PS50998 GLA_2, 1 hit
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiPROC_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: P04070
Secondary accession number(s): B4DPQ7
, Q15189, Q15190, Q16001, Q53S74, Q9UC55
<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: November 1, 1986
Last sequence update: November 1, 1986
Last modified: May 8, 2019
This is version 241 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. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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