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P00748 (FA12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor XII

EC=3.4.21.38
Alternative name(s):
Hageman factor
Short name=HAF
Gene names
Name:F12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14

Catalytic activity

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

Subunit structure

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. Ref.14

Subcellular location

Secreted.

Post-translational modification

Factor XII is activated by kallikrein in alpha-factor XIIa, which is then further converted by trypsin into beta-factor XIIa. Alpha-factor XIIa is composed of the NH2-terminal heavy chain (Coagulation factor XIIa heavy chain) and the COOH-terminal light chain (Coagulation factor XIIa light chain), connected by a disulfide bond. Beta-factor XIIa is composed of 2 chains linked by a disulfide bond, a light chain (Beta-factor XIIa part 2), corresponding to the COOH-terminal light chain (Coagulation factor XIIa light chain) and a nonapeptide (Beta-factor XIIa part 1).

O- and N-glycosylated. The O-linked polysaccharides were not identified, but are probably the mucin type linked to GalNAc. Ref.7 Ref.10

Involvement in disease

Factor XII deficiency (FA12D) [MIM:234000]: An 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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Hereditary angioedema 3 (HAE3) [MIM:610618]: An 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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.24

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 fibronectin type-I domain.

Contains 1 fibronectin type-II domain.

Contains 1 kringle domain.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Kringle
Repeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFactor XII activation

Inferred from direct assay PubMed 18725990. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Inferred by curator PubMed 18725990. Source: BHF-UCL

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement Ref.16. Source: BHF-UCL

plasma kallikrein-kinin cascade

Inferred from direct assay PubMed 18725990PubMed 6793628. Source: BHF-UCL

positive regulation of blood coagulation

Inferred from direct assay PubMed 6793628. Source: BHF-UCL

positive regulation of fibrinolysis

Inferred from direct assay PubMed 89876. Source: BHF-UCL

positive regulation of plasminogen activation

Inferred from direct assay PubMed 89876. Source: BHF-UCL

protein autoprocessing

Inferred from direct assay PubMed 18725990. Source: BHF-UCL

protein processing

Inferred from direct assay PubMed 18725990. Source: BHF-UCL

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to misfolded protein

Inferred from direct assay PubMed 18725990. Source: BHF-UCL

zymogen activation

Inferred from direct assay PubMed 18725990PubMed 6793628PubMed 89876. Source: BHF-UCL

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 6793628. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionmisfolded protein binding

Inferred by curator PubMed 18725990. Source: BHF-UCL

serine-type aminopeptidase activity

Inferred from electronic annotation. Source: Ensembl

serine-type endopeptidase activity

Inferred from direct assay PubMed 18725990PubMed 6793628. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C1QBPQ070212EBI-6378830,EBI-347528

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7
Chain20 – 372353Coagulation factor XIIa heavy chain
PRO_0000027833
Chain354 – 3629Beta-factor XIIa part 1
PRO_0000027834
Chain373 – 615243Beta-factor XIIa part 2
PRO_0000027835
Chain373 – 615243Coagulation factor XIIa light chain
PRO_0000027836

Regions

Domain42 – 9049Fibronectin type-II
Domain94 – 13138EGF-like 1
Domain133 – 17341Fibronectin type-I
Domain174 – 21037EGF-like 2
Domain217 – 29579Kringle
Domain373 – 614242Peptidase S1
Compositional bias296 – 34954Pro-rich

Sites

Active site4121Charge relay system By similarity
Active site4611Charge relay system By similarity
Active site5631Charge relay system By similarity

Amino acid modifications

Glycosylation1091O-linked (Fuc) Ref.10
Glycosylation2491N-linked (GlcNAc...) Ref.5 Ref.7 Ref.12
Glycosylation2991O-linked (GalNAc...) Ref.7
Glycosylation3051O-linked (GalNAc...) Ref.7
Glycosylation3081O-linked (GalNAc...) Ref.7
Glycosylation3281O-linked (GalNAc...) Ref.7
Glycosylation3291O-linked (GalNAc...) Ref.7
Glycosylation3371O-linked (GalNAc...) Ref.7
Glycosylation4331N-linked (GlcNAc...) Ref.11 Ref.12
Disulfide bond47 ↔ 73 By similarity
Disulfide bond61 ↔ 88 By similarity
Disulfide bond98 ↔ 110 By similarity
Disulfide bond104 ↔ 119 By similarity
Disulfide bond121 ↔ 130 By similarity
Disulfide bond135 ↔ 163 Ref.15
Disulfide bond161 ↔ 170 Ref.15
Disulfide bond178 ↔ 189 Ref.15
Disulfide bond183 ↔ 198 Ref.15
Disulfide bond200 ↔ 209 Ref.15
Disulfide bond217 ↔ 295 By similarity
Disulfide bond238 ↔ 277 By similarity
Disulfide bond266 ↔ 290 By similarity
Disulfide bond359 ↔ 486 By similarity
Disulfide bond397 ↔ 413 By similarity
Disulfide bond405 ↔ 475 By similarity
Disulfide bond436 ↔ 439 By similarity
Disulfide bond500 ↔ 569 By similarity
Disulfide bond532 ↔ 548 By similarity
Disulfide bond559 ↔ 590 By similarity

Natural variations

Natural variant531Y → C in FA12D; Tenri; inactive. Ref.19
VAR_014426
Natural variant1421R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. Ref.20
VAR_031500
Natural variant2071A → P. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs17876030 [ dbSNP | Ensembl ].
VAR_014336
Natural variant3281T → K in HAE3. Ref.23 Ref.24
VAR_031501
Natural variant3281T → R in HAE3. Ref.23
VAR_031502
Natural variant3401A → G.
Corresponds to variant rs2230938 [ dbSNP | Ensembl ].
VAR_033649
Natural variant3421P → Q.
Corresponds to variant rs2230939 [ dbSNP | Ensembl ].
VAR_029191
Natural variant3721R → P in FA12D; Locarno; inactive. Ref.17
VAR_006623
Natural variant4111A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. Ref.22
VAR_031503
Natural variant4141L → M in FA12D; CRM-negative phenotype. Ref.18
VAR_031504
Natural variant4171R → Q in FA12D; CRM-negative phenotype. Ref.18
VAR_031505
Natural variant4401Q → K in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion. Ref.20
VAR_031506
Natural variant4611D → N in FA12D; CRM-positive phenotype. Ref.18
VAR_031507
Natural variant5051W → C in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. Ref.21
VAR_031508
Natural variant5451G → D. Ref.2
Corresponds to variant rs17876034 [ dbSNP | Ensembl ].
VAR_014337
Natural variant5891G → R in FA12D; CRM-positive phenotype. Ref.9 Ref.18
VAR_031509
Natural variant5901C → S in FA12D; Washington D.C.; inactive. Ref.16
VAR_006624
Natural variant6051Y → H. Ref.2
Corresponds to variant rs17876035 [ dbSNP | Ensembl ].
VAR_014338

Experimental info

Sequence conflict3331P → S in AAA51986. Ref.5
Sequence conflict3791A → G in AAA70224. Ref.6

Secondary structure

................. 615
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00748 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: F5B861BF635EB480

FASTA61567,792
        10         20         30         40         50         60 
MRALLLLGFL LVSLESTLSI PPWEAPKEHK YKAEEHTVVL TVTGEPCHFP FQYHRQLYHK 

        70         80         90        100        110        120 
CTHKGRPGPQ PWCATTPNFD QDQRWGYCLE PKKVKDHCSK HSPCQKGGTC VNMPSGPHCL 

       130        140        150        160        170        180 
CPQHLTGNHC QKEKCFEPQL LRFFHKNEIW YRTEQAAVAR CQCKGPDAHC QRLASQACRT 

       190        200        210        220        230        240 
NPCLHGGRCL EVEGHRLCHC PVGYTGAFCD VDTKASCYDG RGLSYRGLAR TTLSGAPCQP 

       250        260        270        280        290        300 
WASEATYRNV TAEQARNWGL GGHAFCRNPD NDIRPWCFVL NRDRLSWEYC DLAQCQTPTQ 

       310        320        330        340        350        360 
AAPPTPVSPR LHVPLMPAQP APPKPQPTTR TPPQSQTPGA LPAKREQPPS LTRNGPLSCG 

       370        380        390        400        410        420 
QRLRKSLSSM TRVVGGLVAL RGAHPYIAAL YWGHSFCAGS LIAPCWVLTA AHCLQDRPAP 

       430        440        450        460        470        480 
EDLTVVLGQE RRNHSCEPCQ TLAVRSYRLH EAFSPVSYQH DLALLRLQED ADGSCALLSP 

       490        500        510        520        530        540 
YVQPVCLPSG AARPSETTLC QVAGWGHQFE GAEEYASFLQ EAQVPFLSLE RCSAPDVHGS 

       550        560        570        580        590        600 
SILPGMLCAG FLEGGTDACQ GDSGGPLVCE DQAAERRLTL QGIISWGSGC GDRNKPGVYT 

       610 
DVAYYLAWIR EHTVS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region."
Cool D.E., McGillivray R.T.A.
J. Biol. Chem. 262:13662-13673(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-207.
[2]SeattleSNPs variation discovery resource
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-207; ASP-545 AND HIS-605.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"cDNA sequence coding for human coagulation factor XII (Hageman)."
Tripodi M., Citarella F., Guida S., Galeffi P., Fantoni A., Cortese R.
Nucleic Acids Res. 14:3146-3146(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-615, VARIANT PRO-207.
[5]"Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa."
Cool D.E., Edgell C.-J.S., Louie G.V., Zoller M.J., Brayer G.D., McGillivray R.T.A.
J. Biol. Chem. 260:13666-13676(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-615, VARIANT PRO-207.
[6]"Characterization of a cDNA coding for human factor XII (Hageman factor)."
Que B.G., Davie E.W.
Biochemistry 25:1525-1528(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 146-615, VARIANT PRO-207.
[7]"Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)."
McMullen B.A., Fujikawa K.
J. Biol. Chem. 260:5328-5341(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-379, GLYCOSYLATION AT ASN-249; THR-299; THR-305; SER-308; THR-328; THR-329 AND THR-337, VARIANT PRO-207.
[8]"Amino acid sequence of human beta-factor XIIa."
Fujikawa K., McMullen B.A.
J. Biol. Chem. 258:10924-10933(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 354-362 AND 373-615.
[9]"The novel acceptor splice site mutation 11396(G-->A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients."
Schloesser M., Hofferbert S., Bartz U., Lutze G., Lammle B., Engel W.
Hum. Mol. Genet. 4:1235-1237(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 561-615, VARIANT FA12D ARG-589.
Tissue: Blood.
[10]"O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C."
Harris R.J., Ling V.T., Spellman M.W.
J. Biol. Chem. 267:5102-5107(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-109.
[11]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-433.
Tissue: Plasma.
[12]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249 AND ASN-433.
Tissue: Plasma.
[13]"Factor XII gene alteration in Hageman trait detected by TaqI restriction enzyme."
Bernardi F., Marchetti G., Patracchini P., del Senno L., Tripodi M., Fantoni A., Bartolai S., Vannini F., Felloni L., Rossi L., Panicucci F., Conconi F.
Blood 69:1421-1424(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FA12D.
[14]"Histidine-rich glycoprotein binds factor XIIa with high affinity and inhibits contact-initiated coagulation."
Macquarrie J.L., Stafford A.R., Yau J.W., Leslie B.A., Vu T.T., Fredenburgh J.C., Weitz J.I.
Blood 117:4134-4141(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRG, FUNCTION.
[15]"The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS."
Beringer D.X., Kroon-Batenburg L.M.
Acta Crystallogr. F 69:94-102(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 133-213, DISULFIDE BONDS.
[16]"Coagulation factor XII (Hageman factor) Washington D.C.: inactive factor XIIa results from Cys-571-->Ser substitution."
Miyata T., Kawabata S., Iwanaga S., Takahashi I., Alving B., Saito H.
Proc. Natl. Acad. Sci. U.S.A. 86:8319-8322(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA12D SER-590.
[17]"Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg-353-->Pro leading to loss of a kallikrein cleavage site."
Hovinga J.K., Schaller J., Stricker H., Wuillemin W.A., Furlan M., Laemmle B.
Blood 84:1173-1181(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA12D PRO-372.
[18]"Mutations in the human factor XII gene."
Schloesser M., Zeerleder S., Lutze G., Halbmayer W.-M., Hofferbert S., Hinney B., Koestering H., Laemmle B., Pindur G., Thies K., Koehler M., Engel W.
Blood 90:3967-3977(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA12D MET-414; GLN-417; ASN-461 AND ARG-589.
[19]"Factor XII Tenri, a novel cross-reacting material negative factor XII deficiency, occurs through a proteasome-mediated degradation."
Kondo S., Tokunaga F., Kawano S., Oono Y., Kumagai S., Koide T.
Blood 93:4300-4308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA12D CYS-53.
[20]"Identification and characterization of two novel mutations (Q421K and R123P) in congenital factor XII deficiency."
Kanaji T., Kanaji S., Osaki K., Kuroiwa M., Sakaguchi M., Mihara K., Niho Y., Okamura T.
Thromb. Haemost. 86:1409-1415(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FA12D PRO-142 AND LYS-440, CHARACTERIZATION OF VARIANTS FA12D PRO-142 AND LYS-440.
[21]"Genetic analyses and expression studies identified a novel mutation (W486C) as a molecular basis of congenital coagulation factor XII deficiency."
Ishii K., Oguchi S., Moriki T., Yatabe Y., Takeshita E., Murata M., Ikeda Y., Watanabe K.
Blood Coagul. Fibrinolysis 15:367-373(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA12D CYS-505, CHARACTERIZATION OF VARIANT FA12D CYS-505.
[22]"Factor XII Shizuoka, a novel mutation (Ala392Thr) identified and characterized in a patient with congenital coagulation factor XII deficiency."
Oguchi S., Ishii K., Moriki T., Takeshita E., Murata M., Ikeda Y., Watanabe K.
Thromb. Res. 115:191-197(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FA12D THR-411, CHARACTERIZATION OF VARIANT FA12D THR-411.
[23]"Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor."
Dewald G., Bork K.
Biochem. Biophys. Res. Commun. 343:1286-1289(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HAE3 LYS-328 AND ARG-328.
[24]"Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III."
Cichon S., Martin L., Hennies H.C., Mueller F., Van Driessche K., Karpushova A., Stevens W., Colombo R., Renne T., Drouet C., Bork K., Noethen M.M.
Am. J. Hum. Genet. 79:1098-1104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE3 LYS-328.
+Additional computationally mapped references.

Web resources

Wikipedia

Factor XII entry

F12base

F12 mutation db

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKFHU12. A29411.
RefSeqNP_000496.2. NM_000505.3.
UniGeneHs.1321.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BDWX-ray2.50A133-213[»]
4BDXX-ray1.62A133-213[»]
ProteinModelPortalP00748.
SMRP00748. Positions 37-615.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108459. 9 interactions.
IntActP00748. 2 interactions.
STRING9606.ENSP00000253496.

Chemistry

BindingDBP00748.
ChEMBLCHEMBL2821.
GuidetoPHARMACOLOGY2361.

Protein family/group databases

MEROPSS01.211.

PTM databases

PhosphoSiteP00748.

Polymorphism databases

DMDM317373446.

Proteomic databases

PaxDbP00748.
PeptideAtlasP00748.
PRIDEP00748.

Protocols and materials databases

DNASU2161.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253496; ENSP00000253496; ENSG00000131187.
GeneID2161.
KEGGhsa:2161.
UCSCuc003mgo.4. human.

Organism-specific databases

CTD2161.
GeneCardsGC05M176829.
H-InvDBHIX0005461.
HGNCHGNC:3530. F12.
HPAHPA003825.
MIM234000. phenotype.
610618. phenotype.
610619. gene.
neXtProtNX_P00748.
Orphanet330. Congenital factor XII deficiency.
100054. Hereditary angioedema type 3.
64738. Non rare thrombophilia.
PharmGKBPA161.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000237314.
HOVERGENHBG004345.
InParanoidP00748.
KOK01328.
OMAPKKVKDH.
OrthoDBEOG75B84T.
PhylomeDBP00748.
TreeFamTF329901.

Enzyme and pathway databases

BRENDA3.4.21.38. 2681.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP00748.
BgeeP00748.
CleanExHS_F12.
GenevestigatorP00748.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
2.40.20.10. 1 hit.
InterProIPR014394. Coagulation_fac_XIIa/HGFA.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEPS00022. 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.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFactor_XII.
GenomeRNAi2161.
NextBio8731.
PMAP-CutDBP00748.
PROP00748.
SOURCESearch...

Entry information

Entry nameFA12_HUMAN
AccessionPrimary (citable) accession number: P00748
Secondary accession number(s): P78339
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 175 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM