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Protein

Coagulation factor XII

Gene

F12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei412Charge relay systemBy similarity1
Active sitei461Charge relay systemBy similarity1
Active sitei563Charge relay systemBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • blood coagulation, intrinsic pathway Source: BHF-UCL
  • Factor XII activation Source: BHF-UCL
  • fibrinolysis Source: UniProtKB-KW
  • innate immune response Source: BHF-UCL
  • plasma kallikrein-kinin cascade Source: BHF-UCL
  • positive regulation of blood coagulation Source: BHF-UCL
  • positive regulation of fibrinolysis Source: BHF-UCL
  • positive regulation of plasminogen activation Source: BHF-UCL
  • protein autoprocessing Source: BHF-UCL
  • protein processing Source: BHF-UCL
  • response to misfolded protein Source: BHF-UCL
  • zymogen activation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Enzyme and pathway databases

BioCyciZFISH:HS05500-MONOMER.
BRENDAi3.4.21.38. 2681.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.

Protein family/group databases

MEROPSiS01.211.

Names & Taxonomyi

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:
Gene namesi
Name:F12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3530. F12.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

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
Natural variantiVAR_01442653Y → C in FA12D; Tenri; inactive. 1 PublicationCorresponds to variant rs118204455dbSNPEnsembl.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 rs118204454dbSNPEnsembl.1
Natural variantiVAR_031503411A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication1
Natural variantiVAR_031504414L → M in FA12D; CRM-negative phenotype. 1 Publication1
Natural variantiVAR_031505417R → Q in FA12D; CRM-negative phenotype. 1 Publication1
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 rs766505234dbSNPEnsembl.1
Natural variantiVAR_006624590C → S in FA12D; Washington D.C.; inactive. 1 Publication1
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 rs118204456dbSNPEnsembl.1
Natural variantiVAR_031502328T → R in HAE3. 1 PublicationCorresponds to variant rs118204456dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2161.
MalaCardsiF12.
MIMi234000. phenotype.
610618. phenotype.
OpenTargetsiENSG00000131187.
Orphaneti330. Congenital factor XII deficiency.
100054. Hereditary angioedema type 3.
64738. Non rare thrombophilia.
PharmGKBiPA161.

Chemistry databases

ChEMBLiCHEMBL2821.
DrugBankiDB06689. Ethanolamine Oleate.
GuidetoPHARMACOLOGYi2361.

Polymorphism and mutation databases

BioMutaiF12.
DMDMi317373446.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
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
Disulfide bondi47 ↔ 73By similarity
Disulfide bondi61 ↔ 88By similarity
Disulfide bondi98 ↔ 110By similarity
Disulfide bondi104 ↔ 119By similarity
Glycosylationi109O-linked (Fuc)1 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...)3 Publications1
Disulfide bondi266 ↔ 290By similarity
Glycosylationi299O-linked (GalNAc...)1 Publication1
Glycosylationi305O-linked (GalNAc...)1 Publication1
Glycosylationi308O-linked (GalNAc...)1 Publication1
Glycosylationi328O-linked (GalNAc...)1 Publication1
Glycosylationi329O-linked (GalNAc...)1 Publication1
Glycosylationi337O-linked (GalNAc...)1 Publication1
Disulfide bondi359 ↔ 486By similarity
Disulfide bondi397 ↔ 413By similarity
Disulfide bondi405 ↔ 475By similarity
Glycosylationi433N-linked (GlcNAc...)2 Publications1
Disulfide bondi436 ↔ 439By similarity
Disulfide bondi500 ↔ 569By similarity
Disulfide bondi532 ↔ 548By similarity
Disulfide bondi559 ↔ 590By similarity

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

PaxDbiP00748.
PeptideAtlasiP00748.
PRIDEiP00748.

PTM databases

iPTMnetiP00748.
PhosphoSitePlusiP00748.

Miscellaneous databases

PMAP-CutDBP00748.

Expressioni

Gene expression databases

BgeeiENSG00000131187.
CleanExiHS_F12.
GenevisibleiP00748. HS.

Organism-specific databases

HPAiHPA003825.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
C1QBPQ070212EBI-6378830,EBI-347528

GO - Molecular functioni

  • misfolded protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108459. 15 interactors.
IntActiP00748. 3 interactors.
STRINGi9606.ENSP00000253496.

Chemistry databases

BindingDBiP00748.

Structurei

Secondary structure

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi135 – 137Combined sources3
Turni138 – 141Combined sources4
Beta strandi142 – 144Combined sources3
Beta strandi149 – 153Combined sources5
Beta strandi158 – 163Combined sources6
Beta strandi165 – 173Combined sources9
Beta strandi188 – 192Combined sources5
Beta strandi195 – 199Combined sources5
Beta strandi204 – 206Combined sources3
Beta strandi380 – 383Combined sources4
Beta strandi387 – 392Combined sources6
Beta strandi395 – 403Combined sources9
Beta strandi406 – 409Combined sources4
Helixi411 – 414Combined sources4
Helixi420 – 422Combined sources3
Beta strandi424 – 428Combined sources5
Beta strandi440 – 449Combined sources10
Turni455 – 457Combined sources3
Beta strandi463 – 467Combined sources5
Turni471 – 473Combined sources3
Beta strandi490 – 492Combined sources3
Beta strandi499 – 504Combined sources6
Helixi513 – 515Combined sources3
Beta strandi520 – 527Combined sources8
Helixi529 – 532Combined sources4
Turni535 – 538Combined sources4
Helixi539 – 541Combined sources3
Beta strandi546 – 550Combined sources5
Turni558 – 560Combined sources3
Beta strandi566 – 570Combined sources5
Beta strandi572 – 586Combined sources15
Beta strandi597 – 601Combined sources5
Helixi602 – 605Combined sources4
Helixi606 – 611Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BDWX-ray2.50A133-215[»]
4BDXX-ray1.62A133-213[»]
4XDEX-ray2.14A373-615[»]
4XE4X-ray2.40A373-615[»]
ProteinModelPortaliP00748.
SMRiP00748.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Compositional biasi296 – 349Pro-richAdd BLAST54

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-I domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiP00748.
KOiK01328.
OMAiPCHFPFQ.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00748.
TreeFamiTF329901.

Family and domain databases

CDDicd00062. FN2. 1 hit.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. Coagulation_fac_XIIa/HGFA.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. 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.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Complete.

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
Checksum:iF5B861BF635EB480
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 rs118204455dbSNPEnsembl.1
Natural variantiVAR_031500142R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. 1 Publication1
Natural variantiVAR_014336207A → P.6 PublicationsCorresponds to variant rs17876030dbSNPEnsembl.1
Natural variantiVAR_031501328T → K in HAE3. 2 PublicationsCorresponds to variant rs118204456dbSNPEnsembl.1
Natural variantiVAR_031502328T → R in HAE3. 1 PublicationCorresponds to variant rs118204456dbSNPEnsembl.1
Natural variantiVAR_033649340A → G.Corresponds to variant rs2230938dbSNPEnsembl.1
Natural variantiVAR_029191342P → Q.Corresponds to variant rs2230939dbSNPEnsembl.1
Natural variantiVAR_006623372R → P in FA12D; Locarno; inactive. 1 PublicationCorresponds to variant rs118204454dbSNPEnsembl.1
Natural variantiVAR_031503411A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication1
Natural variantiVAR_031504414L → M in FA12D; CRM-negative phenotype. 1 Publication1
Natural variantiVAR_031505417R → Q in FA12D; CRM-negative phenotype. 1 Publication1
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 → D.1 PublicationCorresponds to variant rs17876034dbSNPEnsembl.1
Natural variantiVAR_031509589G → R in FA12D; CRM-positive phenotype. 2 PublicationsCorresponds to variant rs766505234dbSNPEnsembl.1
Natural variantiVAR_006624590C → S in FA12D; Washington D.C.; inactive. 1 Publication1
Natural variantiVAR_014338605Y → H.1 PublicationCorresponds to variant rs17876035dbSNPEnsembl.1

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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BDWX-ray2.50A133-215[»]
4BDXX-ray1.62A133-213[»]
4XDEX-ray2.14A373-615[»]
4XE4X-ray2.40A373-615[»]
ProteinModelPortaliP00748.
SMRiP00748.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108459. 15 interactors.
IntActiP00748. 3 interactors.
STRINGi9606.ENSP00000253496.

Chemistry databases

BindingDBiP00748.
ChEMBLiCHEMBL2821.
DrugBankiDB06689. Ethanolamine Oleate.
GuidetoPHARMACOLOGYi2361.

Protein family/group databases

MEROPSiS01.211.

PTM databases

iPTMnetiP00748.
PhosphoSitePlusiP00748.

Polymorphism and mutation databases

BioMutaiF12.
DMDMi317373446.

Proteomic databases

PaxDbiP00748.
PeptideAtlasiP00748.
PRIDEiP00748.

Protocols and materials databases

DNASUi2161.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2161.
DisGeNETi2161.
GeneCardsiF12.
H-InvDBHIX0005461.
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 thrombophilia.
PharmGKBiPA161.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3627. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiP00748.
KOiK01328.
OMAiPCHFPFQ.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00748.
TreeFamiTF329901.

Enzyme and pathway databases

BioCyciZFISH:HS05500-MONOMER.
BRENDAi3.4.21.38. 2681.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.

Miscellaneous databases

GeneWikiiFactor_XII.
GenomeRNAii2161.
PMAP-CutDBP00748.
PROiP00748.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131187.
CleanExiHS_F12.
GenevisibleiP00748. HS.

Family and domain databases

CDDicd00062. FN2. 1 hit.
cd00190. Tryp_SPc. 1 hit.
Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. Coagulation_fac_XIIa/HGFA.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. 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.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. 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.
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Entry informationi

Entry nameiFA12_HUMAN
AccessioniPrimary (citable) accession number: P00748
Secondary accession number(s): P78339
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 203 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.