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Protein

Coagulation factor XII

Gene

F12

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

Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa.1 Publication

<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

  • Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa. EC:3.4.21.38

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 sitei412Charge relay systemBy similarity1
Active sitei461Charge relay systemBy similarity1
Active sitei563Charge relay systemBy similarity1

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

  • calcium ion binding Source: InterPro
  • misfolded protein binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

<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, Fibrinolysis, Hemostasis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.38 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P00748

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.211

<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:
Coagulation factor XII (EC:3.4.21.38)
Alternative name(s):
Hageman factor
Short name:
HAF
Cleaved into the following 3 chains:
<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:F12
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000131187.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3530 F12

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
610619 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P00748

<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; 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

Factor XII deficiency (FA12D)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn asymptomatic anomaly of in vitro blood coagulation. Its diagnosis is based on finding a low plasma activity of the factor in coagulating assays. It is usually only accidentally discovered through pre-operative blood tests. Factor XII deficiency is divided into two categories, a cross-reacting material (CRM)-negative group (negative F12 antigen detection) and a CRM-positive group (positive F12 antigen detection).
See also OMIM:234000
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_01442653Y → C in FA12D; Tenri; inactive. 1 PublicationCorresponds to variant dbSNP:rs118204455EnsemblClinVar.1
Natural variantiVAR_031500142R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. 1 Publication1
Natural variantiVAR_006623372R → P in FA12D; Locarno; inactive. 1 PublicationCorresponds to variant dbSNP:rs118204454EnsemblClinVar.1
Natural variantiVAR_031503411A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 PublicationCorresponds to variant dbSNP:rs865853663Ensembl.1
Natural variantiVAR_031504414L → M in FA12D; CRM-negative phenotype. 1 Publication1
Natural variantiVAR_031505417R → Q in FA12D; CRM-negative phenotype. 1 PublicationCorresponds to variant dbSNP:rs932430490Ensembl.1
Natural variantiVAR_031506440Q → K in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion. 1 Publication1
Natural variantiVAR_031507461D → N in FA12D; CRM-positive phenotype. 1 Publication1
Natural variantiVAR_031508505W → C in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication1
Natural variantiVAR_031509589G → R in FA12D; CRM-positive phenotype. 2 PublicationsCorresponds to variant dbSNP:rs766505234Ensembl.1
Natural variantiVAR_006624590C → S in FA12D; Washington D.C.; inactive. 1 PublicationCorresponds to variant dbSNP:rs1157280571Ensembl.1
Hereditary angioedema 3 (HAE3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn hereditary angioedema occurring only in women. Hereditary angioedema is an autosomal dominant disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. Hereditary angioedema type 3 differs from types 1 and 2 in that both concentration and function of C1 esterase inhibitor are normal. Hereditary angioedema type 3 is precipitated or worsened by high estrogen levels (e.g., during pregnancy or treatment with oral contraceptives).
See also OMIM:610618
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031501328T → K in HAE3. 2 PublicationsCorresponds to variant dbSNP:rs118204456EnsemblClinVar.1
Natural variantiVAR_031502328T → R in HAE3. 1 PublicationCorresponds to variant dbSNP:rs118204456EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2161

MalaCards human disease database

More...
MalaCardsi
F12
MIMi234000 phenotype
610618 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000131187

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

More...
Orphaneti
330 Congenital factor XII deficiency
100054 Hereditary angioedema type 3
64738 NON RARE IN EUROPE: Non rare thrombophilia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA161

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2821

Drug and drug target database

More...
DrugBanki
DB06404 C1 Esterase Inhibitor (Human)
DB09228 C1 Esterase Inhibitor (Recombinant)
DB06689 Ethanolamine Oleate

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2361

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
F12

Domain mapping of disease mutations (DMDM)

More...
DMDMi
317373446

<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 – 191 PublicationAdd BLAST19
<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_000002783320 – 372Coagulation factor XIIa heavy chainAdd BLAST353
ChainiPRO_0000027834354 – 362Beta-factor XIIa part 19
ChainiPRO_0000027835373 – 615Coagulation factor XIIa light chainAdd BLAST243

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 bondi47 ↔ 73By similarity
Disulfide bondi61 ↔ 88By similarity
Disulfide bondi98 ↔ 110By similarity
Disulfide bondi104 ↔ 119By similarity
<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>Glycosylationi109O-linked (Fuc) threonine1 Publication1
Disulfide bondi121 ↔ 130By similarity
Disulfide bondi135 ↔ 1631 Publication
Disulfide bondi161 ↔ 1701 Publication
Disulfide bondi178 ↔ 1891 Publication
Disulfide bondi183 ↔ 1981 Publication
Disulfide bondi200 ↔ 2091 Publication
Disulfide bondi217 ↔ 295By similarity
Disulfide bondi238 ↔ 277By similarity
Glycosylationi249N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi266 ↔ 290By similarity
Glycosylationi299O-linked (GalNAc...) threonine1 Publication1
Glycosylationi305O-linked (GalNAc...) threonine1 Publication1
Glycosylationi308O-linked (GalNAc...) serine1 Publication1
Glycosylationi328O-linked (GalNAc...) threonine1 Publication1
Glycosylationi329O-linked (GalNAc...) threonine1 Publication1
Glycosylationi337O-linked (GalNAc...) threonine1 Publication1
Disulfide bondi359 ↔ 486By similarity
Disulfide bondi397 ↔ 413By similarity
Disulfide bondi405 ↔ 475By similarity
Glycosylationi433N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi436 ↔ 439By similarity
Disulfide bondi500 ↔ 569By similarity
Disulfide bondi532 ↔ 548By similarity
Disulfide bondi559 ↔ 590By similarity

<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

Factor XII is activated by kallikrein in alpha-factor XIIa, which is further converted by trypsin into beta-factor XIIa. Alpha-factor XIIa is composed of an NH2-terminal heavy chain, called coagulation factor XIIa heavy chain, and a COOH-terminal light chain, called coagulation factor XIIa light chain, connected by a disulfide bond. Beta-factor XIIa is composed of 2 chains linked by a disulfide bond, an N-terminal nonapeptide, called beta-factor XIIa part 1, and coagulation factor XIIa light chain, also known in this context as beta-factor XIIa part 2.
O- and N-glycosylated. The O-linked polysaccharides were not identified, but are probably the mucin type linked to GalNAc.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

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

More...
PaxDbi
P00748

PeptideAtlas

More...
PeptideAtlasi
P00748

PRoteomics IDEntifications database

More...
PRIDEi
P00748

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51278

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1121

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00748

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

More...
PhosphoSitePlusi
P00748

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P00748

<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
ENSG00000131187 Expressed in 128 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_F12

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P00748 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA003825

<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

Interacts with HRG; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding, inhibits factor XII autoactivation and contact-initiated coagulation.1 Publication

<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
C1QBPQ070212EBI-6378830,EBI-347528

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108459, 15 interactors

Protein interaction database and analysis system

More...
IntActi
P00748, 3 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000253496

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00748

<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

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00748

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

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SMRi
P00748

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_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>Domaini42 – 90Fibronectin type-IIPROSITE-ProRule annotationAdd BLAST49
Domaini94 – 131EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini133 – 173Fibronectin type-IPROSITE-ProRule annotationAdd BLAST41
Domaini174 – 210EGF-like 2PROSITE-ProRule annotationAdd BLAST37
Domaini217 – 295KringlePROSITE-ProRule annotationAdd BLAST79
Domaini373 – 614Peptidase S1PROSITE-ProRule annotationAdd BLAST242

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi296 – 349Pro-richAdd BLAST54

<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, Kringle, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1217 Eukaryota
KOG3627 Eukaryota
COG5640 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000161657

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000237314

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004345

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00748

KEGG Orthology (KO)

More...
KOi
K01328

Identification of Orthologs from Complete Genome Data

More...
OMAi
EKCFEPQ

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0AH5

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00748

TreeFam database of animal gene trees

More...
TreeFami
TF329901

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00061 FN1, 1 hit
cd00062 FN2, 1 hit
cd00108 KR, 1 hit
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.10.10, 1 hit
2.40.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014394 Coagulation_fac_XII/HGFA
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000083 Fibronectin_type1
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
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, 2 hits
PF00039 fn1, 1 hit
PF00040 fn2, 1 hit
PF00051 Kringle, 1 hit
PF00089 Trypsin, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001146 Factor_XII_HGFA, 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
SM00181 EGF, 2 hits
SM00179 EGF_CA, 2 hits
SM00058 FN1, 1 hit
SM00059 FN2, 1 hit
SM00130 KR, 1 hit
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022 EGF_1, 2 hits
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 2 hits
PS01253 FN1_1, 1 hit
PS51091 FN1_2, 1 hit
PS00023 FN2_1, 1 hit
PS51092 FN2_2, 1 hit
PS00021 KRINGLE_1, 1 hit
PS50070 KRINGLE_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>Sequencei

<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.

P00748-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRALLLLGFL LVSLESTLSI PPWEAPKEHK YKAEEHTVVL TVTGEPCHFP
60 70 80 90 100
FQYHRQLYHK CTHKGRPGPQ PWCATTPNFD QDQRWGYCLE PKKVKDHCSK
110 120 130 140 150
HSPCQKGGTC VNMPSGPHCL CPQHLTGNHC QKEKCFEPQL LRFFHKNEIW
160 170 180 190 200
YRTEQAAVAR CQCKGPDAHC QRLASQACRT NPCLHGGRCL EVEGHRLCHC
210 220 230 240 250
PVGYTGAFCD VDTKASCYDG RGLSYRGLAR TTLSGAPCQP WASEATYRNV
260 270 280 290 300
TAEQARNWGL GGHAFCRNPD NDIRPWCFVL NRDRLSWEYC DLAQCQTPTQ
310 320 330 340 350
AAPPTPVSPR LHVPLMPAQP APPKPQPTTR TPPQSQTPGA LPAKREQPPS
360 370 380 390 400
LTRNGPLSCG QRLRKSLSSM TRVVGGLVAL RGAHPYIAAL YWGHSFCAGS
410 420 430 440 450
LIAPCWVLTA AHCLQDRPAP EDLTVVLGQE RRNHSCEPCQ TLAVRSYRLH
460 470 480 490 500
EAFSPVSYQH DLALLRLQED ADGSCALLSP YVQPVCLPSG AARPSETTLC
510 520 530 540 550
QVAGWGHQFE GAEEYASFLQ EAQVPFLSLE RCSAPDVHGS SILPGMLCAG
560 570 580 590 600
FLEGGTDACQ GDSGGPLVCE DQAAERRLTL QGIISWGSGC GDRNKPGVYT
610
DVAYYLAWIR EHTVS
Length:615
Mass (Da):67,792
Last modified:January 11, 2011 - v3
<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:iF5B861BF635EB480
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti333P → S in AAA51986 (PubMed:3877053).Curated1
Sequence conflicti379A → G in AAA70224 (PubMed:3011063).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01442653Y → C in FA12D; Tenri; inactive. 1 PublicationCorresponds to variant dbSNP:rs118204455EnsemblClinVar.1
Natural variantiVAR_031500142R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. 1 Publication1
Natural variantiVAR_014336207A → P6 PublicationsCorresponds to variant dbSNP:rs17876030EnsemblClinVar.1
Natural variantiVAR_031501328T → K in HAE3. 2 PublicationsCorresponds to variant dbSNP:rs118204456EnsemblClinVar.1
Natural variantiVAR_031502328T → R in HAE3. 1 PublicationCorresponds to variant dbSNP:rs118204456EnsemblClinVar.1
Natural variantiVAR_029191342P → Q. Corresponds to variant dbSNP:rs2230939Ensembl.1
Natural variantiVAR_006623372R → P in FA12D; Locarno; inactive. 1 PublicationCorresponds to variant dbSNP:rs118204454EnsemblClinVar.1
Natural variantiVAR_031503411A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 PublicationCorresponds to variant dbSNP:rs865853663Ensembl.1
Natural variantiVAR_031504414L → M in FA12D; CRM-negative phenotype. 1 Publication1
Natural variantiVAR_031505417R → Q in FA12D; CRM-negative phenotype. 1 PublicationCorresponds to variant dbSNP:rs932430490Ensembl.1
Natural variantiVAR_031506440Q → K in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion. 1 Publication1
Natural variantiVAR_031507461D → N in FA12D; CRM-positive phenotype. 1 Publication1
Natural variantiVAR_031508505W → C in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication1
Natural variantiVAR_014337545G → D1 PublicationCorresponds to variant dbSNP:rs17876034Ensembl.1
Natural variantiVAR_031509589G → R in FA12D; CRM-positive phenotype. 2 PublicationsCorresponds to variant dbSNP:rs766505234Ensembl.1
Natural variantiVAR_006624590C → S in FA12D; Washington D.C.; inactive. 1 PublicationCorresponds to variant dbSNP:rs1157280571Ensembl.1
Natural variantiVAR_014338605Y → H1 PublicationCorresponds to variant dbSNP:rs17876035Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M17466, M17464, M17465 Genomic DNA Translation: AAB59490.1
AF538691 Genomic DNA Translation: AAM97932.1
AC145098 Genomic DNA No translation available.
M31315 mRNA Translation: AAA70225.1
M11723 mRNA Translation: AAA51986.1
M13147 mRNA Translation: AAA70224.1
U71274 Genomic DNA Translation: AAB51203.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34302.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A29411 KFHU12

NCBI Reference Sequences

More...
RefSeqi
NP_000496.2, NM_000505.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.1321

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000253496; ENSP00000253496; ENSG00000131187

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2161

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2161

UCSC genome browser

More...
UCSCi
uc003mgo.5 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

<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

Factor XII entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17466, M17464, M17465 Genomic DNA Translation: AAB59490.1
AF538691 Genomic DNA Translation: AAM97932.1
AC145098 Genomic DNA No translation available.
M31315 mRNA Translation: AAA70225.1
M11723 mRNA Translation: AAA51986.1
M13147 mRNA Translation: AAA70224.1
U71274 Genomic DNA Translation: AAB51203.1
CCDSiCCDS34302.1
PIRiA29411 KFHU12
RefSeqiNP_000496.2, NM_000505.3
UniGeneiHs.1321

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BDWX-ray2.50A133-215[»]
4BDXX-ray1.62A133-213[»]
4XDEX-ray2.14A373-615[»]
4XE4X-ray2.40A373-615[»]
6B74X-ray2.32A354-362[»]
B373-615[»]
6B77X-ray2.37A354-362[»]
B373-615[»]
ProteinModelPortaliP00748
SMRiP00748
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108459, 15 interactors
IntActiP00748, 3 interactors
STRINGi9606.ENSP00000253496

Chemistry databases

BindingDBiP00748
ChEMBLiCHEMBL2821
DrugBankiDB06404 C1 Esterase Inhibitor (Human)
DB09228 C1 Esterase Inhibitor (Recombinant)
DB06689 Ethanolamine Oleate
GuidetoPHARMACOLOGYi2361

Protein family/group databases

MEROPSiS01.211

PTM databases

GlyConnecti1121
iPTMnetiP00748
PhosphoSitePlusiP00748

Polymorphism and mutation databases

BioMutaiF12
DMDMi317373446

Proteomic databases

PaxDbiP00748
PeptideAtlasiP00748
PRIDEiP00748
ProteomicsDBi51278

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2161
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253496; ENSP00000253496; ENSG00000131187
GeneIDi2161
KEGGihsa:2161
UCSCiuc003mgo.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2161
DisGeNETi2161
EuPathDBiHostDB:ENSG00000131187.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
F12

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0005461
HGNCiHGNC:3530 F12
HPAiHPA003825
MalaCardsiF12
MIMi234000 phenotype
610618 phenotype
610619 gene
neXtProtiNX_P00748
OpenTargetsiENSG00000131187
Orphaneti330 Congenital factor XII deficiency
100054 Hereditary angioedema type 3
64738 NON RARE IN EUROPE: Non rare thrombophilia
PharmGKBiPA161

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1217 Eukaryota
KOG3627 Eukaryota
COG5640 LUCA
GeneTreeiENSGT00940000161657
HOGENOMiHOG000237314
HOVERGENiHBG004345
InParanoidiP00748
KOiK01328
OMAiEKCFEPQ
OrthoDBiEOG091G0AH5
PhylomeDBiP00748
TreeFamiTF329901

Enzyme and pathway databases

BRENDAi3.4.21.38 2681
ReactomeiR-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
SIGNORiP00748

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Factor_XII

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

More...
GenomeRNAii
2161
PMAP-CutDBiP00748

Protein Ontology

More...
PROi
PR:P00748

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000131187 Expressed in 128 organ(s), highest expression level in liver
CleanExiHS_F12
GenevisibleiP00748 HS

Family and domain databases

CDDicd00061 FN1, 1 hit
cd00062 FN2, 1 hit
cd00108 KR, 1 hit
cd00190 Tryp_SPc, 1 hit
Gene3Di2.10.10.10, 1 hit
2.40.20.10, 1 hit
InterProiView protein in InterPro
IPR014394 Coagulation_fac_XII/HGFA
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000083 Fibronectin_type1
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 2 hits
PF00039 fn1, 1 hit
PF00040 fn2, 1 hit
PF00051 Kringle, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001146 Factor_XII_HGFA, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 2 hits
SM00058 FN1, 1 hit
SM00059 FN2, 1 hit
SM00130 KR, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 2 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 2 hits
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 2 hits
PS01253 FN1_1, 1 hit
PS51091 FN1_2, 1 hit
PS00023 FN2_1, 1 hit
PS51092 FN2_2, 1 hit
PS00021 KRINGLE_1, 1 hit
PS50070 KRINGLE_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 nameiFA12_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: P00748
Secondary accession number(s): P78339
<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: July 21, 1986
Last sequence update: January 11, 2011
Last modified: December 5, 2018
This is version 222 of the entry and version 3 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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