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P00748

- FA12_HUMAN

UniProt

P00748 - FA12_HUMAN

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Protein
Coagulation factor XII
Gene
F12
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei412 – 4121Charge relay system By similarity
Active sitei461 – 4611Charge relay system By similarity
Active sitei563 – 5631Charge relay system By similarity

GO - Molecular functioni

  1. misfolded protein binding Source: BHF-UCL
  2. protein binding Source: UniProtKB
  3. serine-type aminopeptidase activity Source: Ensembl
  4. serine-type endopeptidase activity Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. Factor XII activation Source: BHF-UCL
  2. blood coagulation Source: Reactome
  3. blood coagulation, intrinsic pathway Source: BHF-UCL
  4. fibrinolysis Source: UniProtKB-KW
  5. innate immune response Source: BHF-UCL
  6. plasma kallikrein-kinin cascade Source: BHF-UCL
  7. positive regulation of blood coagulation Source: BHF-UCL
  8. positive regulation of fibrinolysis Source: BHF-UCL
  9. positive regulation of plasminogen activation Source: BHF-UCL
  10. protein autoprocessing Source: BHF-UCL
  11. protein processing Source: BHF-UCL
  12. response to misfolded protein Source: BHF-UCL
  13. 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

BRENDAi3.4.21.38. 2681.
ReactomeiREACT_326. Intrinsic Pathway.

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 4 chains:
Gene namesi
Name:F12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:3530. F12.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.9 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531Y → C in FA12D; Tenri; inactive. 1 Publication
VAR_014426
Natural varianti142 – 1421R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. 1 Publication
VAR_031500
Natural varianti372 – 3721R → P in FA12D; Locarno; inactive. 1 Publication
VAR_006623
Natural varianti411 – 4111A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication
VAR_031503
Natural varianti414 – 4141L → M in FA12D; CRM-negative phenotype. 1 Publication
VAR_031504
Natural varianti417 – 4171R → Q in FA12D; CRM-negative phenotype. 1 Publication
VAR_031505
Natural varianti440 – 4401Q → K in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion. 1 Publication
VAR_031506
Natural varianti461 – 4611D → N in FA12D; CRM-positive phenotype. 1 Publication
VAR_031507
Natural varianti505 – 5051W → C in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication
VAR_031508
Natural varianti589 – 5891G → R in FA12D; CRM-positive phenotype. 2 Publications
VAR_031509
Natural varianti590 – 5901C → S in FA12D; Washington D.C.; inactive. 1 Publication
VAR_006624
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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti328 – 3281T → K in HAE3. 2 Publications
VAR_031501
Natural varianti328 – 3281T → R in HAE3. 1 Publication
VAR_031502

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 372353Coagulation factor XIIa heavy chain
PRO_0000027833Add
BLAST
Chaini354 – 3629Beta-factor XIIa part 1
PRO_0000027834
Chaini373 – 615243Beta-factor XIIa part 2
PRO_0000027835Add
BLAST
Chaini373 – 615243Coagulation factor XIIa light chain
PRO_0000027836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 73 By similarity
Disulfide bondi61 ↔ 88 By similarity
Disulfide bondi98 ↔ 110 By similarity
Disulfide bondi104 ↔ 119 By similarity
Glycosylationi109 – 1091O-linked (Fuc)1 Publication
Disulfide bondi121 ↔ 130 By similarity
Disulfide bondi135 ↔ 1631 Publication
Disulfide bondi161 ↔ 1701 Publication
Disulfide bondi178 ↔ 1891 Publication
Disulfide bondi183 ↔ 1981 Publication
Disulfide bondi200 ↔ 2091 Publication
Disulfide bondi217 ↔ 295 By similarity
Disulfide bondi238 ↔ 277 By similarity
Glycosylationi249 – 2491N-linked (GlcNAc...)3 Publications
Disulfide bondi266 ↔ 290 By similarity
Glycosylationi299 – 2991O-linked (GalNAc...)1 Publication
Glycosylationi305 – 3051O-linked (GalNAc...)1 Publication
Glycosylationi308 – 3081O-linked (GalNAc...)1 Publication
Glycosylationi328 – 3281O-linked (GalNAc...)1 Publication
Glycosylationi329 – 3291O-linked (GalNAc...)1 Publication
Glycosylationi337 – 3371O-linked (GalNAc...)1 Publication
Disulfide bondi359 ↔ 486 By similarity
Disulfide bondi397 ↔ 413 By similarity
Disulfide bondi405 ↔ 475 By similarity
Glycosylationi433 – 4331N-linked (GlcNAc...)2 Publications
Disulfide bondi436 ↔ 439 By similarity
Disulfide bondi500 ↔ 569 By similarity
Disulfide bondi532 ↔ 548 By similarity
Disulfide bondi559 ↔ 590 By similarity

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP00748.
PeptideAtlasiP00748.
PRIDEiP00748.

PTM databases

PhosphoSiteiP00748.

Miscellaneous databases

PMAP-CutDBP00748.

Expressioni

Gene expression databases

ArrayExpressiP00748.
BgeeiP00748.
CleanExiHS_F12.
GenevestigatoriP00748.

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

Protein-protein interaction databases

BioGridi108459. 9 interactions.
IntActiP00748. 2 interactions.
STRINGi9606.ENSP00000253496.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi135 – 1373
Turni138 – 1414
Beta strandi142 – 1443
Beta strandi149 – 1535
Beta strandi158 – 1636
Beta strandi165 – 1739
Beta strandi188 – 1925
Beta strandi195 – 1995
Beta strandi204 – 2063

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BDWX-ray2.50A133-215[»]
4BDXX-ray1.62A133-213[»]
ProteinModelPortaliP00748.
SMRiP00748. Positions 44-611.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 9049Fibronectin type-II
Add
BLAST
Domaini94 – 13138EGF-like 1
Add
BLAST
Domaini133 – 17341Fibronectin type-I
Add
BLAST
Domaini174 – 21037EGF-like 2
Add
BLAST
Domaini217 – 29579Kringle
Add
BLAST
Domaini373 – 614242Peptidase S1
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi296 – 34954Pro-rich
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.
Contains 1 kringle domain.

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiP00748.
KOiK01328.
OMAiPKKVKDH.
OrthoDBiEOG75B84T.
PhylomeDBiP00748.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
2.40.20.10. 1 hit.
InterProiIPR014394. 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]
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.
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

MRALLLLGFL LVSLESTLSI PPWEAPKEHK YKAEEHTVVL TVTGEPCHFP    50
FQYHRQLYHK CTHKGRPGPQ PWCATTPNFD QDQRWGYCLE PKKVKDHCSK 100
HSPCQKGGTC VNMPSGPHCL CPQHLTGNHC QKEKCFEPQL LRFFHKNEIW 150
YRTEQAAVAR CQCKGPDAHC QRLASQACRT NPCLHGGRCL EVEGHRLCHC 200
PVGYTGAFCD VDTKASCYDG RGLSYRGLAR TTLSGAPCQP WASEATYRNV 250
TAEQARNWGL GGHAFCRNPD NDIRPWCFVL NRDRLSWEYC DLAQCQTPTQ 300
AAPPTPVSPR LHVPLMPAQP APPKPQPTTR TPPQSQTPGA LPAKREQPPS 350
LTRNGPLSCG QRLRKSLSSM TRVVGGLVAL RGAHPYIAAL YWGHSFCAGS 400
LIAPCWVLTA AHCLQDRPAP EDLTVVLGQE RRNHSCEPCQ TLAVRSYRLH 450
EAFSPVSYQH DLALLRLQED ADGSCALLSP YVQPVCLPSG AARPSETTLC 500
QVAGWGHQFE GAEEYASFLQ EAQVPFLSLE RCSAPDVHGS SILPGMLCAG 550
FLEGGTDACQ GDSGGPLVCE DQAAERRLTL QGIISWGSGC GDRNKPGVYT 600
DVAYYLAWIR EHTVS 615
Length:615
Mass (Da):67,792
Last modified:January 11, 2011 - v3
Checksum:iF5B861BF635EB480
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531Y → C in FA12D; Tenri; inactive. 1 Publication
VAR_014426
Natural varianti142 – 1421R → P in FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted. 1 Publication
VAR_031500
Natural varianti207 – 2071A → P.6 Publications
Corresponds to variant rs17876030 [ dbSNP | Ensembl ].
VAR_014336
Natural varianti328 – 3281T → K in HAE3. 2 Publications
VAR_031501
Natural varianti328 – 3281T → R in HAE3. 1 Publication
VAR_031502
Natural varianti340 – 3401A → G.
Corresponds to variant rs2230938 [ dbSNP | Ensembl ].
VAR_033649
Natural varianti342 – 3421P → Q.
Corresponds to variant rs2230939 [ dbSNP | Ensembl ].
VAR_029191
Natural varianti372 – 3721R → P in FA12D; Locarno; inactive. 1 Publication
VAR_006623
Natural varianti411 – 4111A → T in FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication
VAR_031503
Natural varianti414 – 4141L → M in FA12D; CRM-negative phenotype. 1 Publication
VAR_031504
Natural varianti417 – 4171R → Q in FA12D; CRM-negative phenotype. 1 Publication
VAR_031505
Natural varianti440 – 4401Q → K in FA12D; CRM-negative phenotype; accumulation in the cell; low secretion. 1 Publication
VAR_031506
Natural varianti461 – 4611D → N in FA12D; CRM-positive phenotype. 1 Publication
VAR_031507
Natural varianti505 – 5051W → C in FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted. 1 Publication
VAR_031508
Natural varianti545 – 5451G → D.1 Publication
Corresponds to variant rs17876034 [ dbSNP | Ensembl ].
VAR_014337
Natural varianti589 – 5891G → R in FA12D; CRM-positive phenotype. 2 Publications
VAR_031509
Natural varianti590 – 5901C → S in FA12D; Washington D.C.; inactive. 1 Publication
VAR_006624
Natural varianti605 – 6051Y → H.1 Publication
Corresponds to variant rs17876035 [ dbSNP | Ensembl ].
VAR_014338

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3331P → S in AAA51986. 1 Publication
Sequence conflicti379 – 3791A → G in AAA70224. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Polymorphism databases

DMDMi317373446.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor XII entry

F12base

F12 mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS34302.1.
PIRi A29411. KFHU12.
RefSeqi NP_000496.2. NM_000505.3.
UniGenei Hs.1321.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BDW X-ray 2.50 A 133-215 [» ]
4BDX X-ray 1.62 A 133-213 [» ]
ProteinModelPortali P00748.
SMRi P00748. Positions 44-611.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108459. 9 interactions.
IntActi P00748. 2 interactions.
STRINGi 9606.ENSP00000253496.

Chemistry

BindingDBi P00748.
ChEMBLi CHEMBL2821.
GuidetoPHARMACOLOGYi 2361.

Protein family/group databases

MEROPSi S01.211.

PTM databases

PhosphoSitei P00748.

Polymorphism databases

DMDMi 317373446.

Proteomic databases

PaxDbi P00748.
PeptideAtlasi P00748.
PRIDEi P00748.

Protocols and materials databases

DNASUi 2161.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253496 ; ENSP00000253496 ; ENSG00000131187 .
GeneIDi 2161.
KEGGi hsa:2161.
UCSCi uc003mgo.4. human.

Organism-specific databases

CTDi 2161.
GeneCardsi GC05M176829.
H-InvDB HIX0005461.
HGNCi HGNC:3530. F12.
HPAi HPA003825.
MIMi 234000. phenotype.
610618. phenotype.
610619. gene.
neXtProti NX_P00748.
Orphaneti 330. Congenital factor XII deficiency.
100054. Hereditary angioedema type 3.
64738. Non rare thrombophilia.
PharmGKBi PA161.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000237314.
HOVERGENi HBG004345.
InParanoidi P00748.
KOi K01328.
OMAi PKKVKDH.
OrthoDBi EOG75B84T.
PhylomeDBi P00748.
TreeFami TF329901.

Enzyme and pathway databases

BRENDAi 3.4.21.38. 2681.
Reactomei REACT_326. Intrinsic Pathway.

Miscellaneous databases

GeneWikii Factor_XII.
GenomeRNAii 2161.
NextBioi 8731.
PMAP-CutDB P00748.
PROi P00748.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00748.
Bgeei P00748.
CleanExi HS_F12.
Genevestigatori P00748.

Family and domain databases

Gene3Di 2.10.10.10. 1 hit.
2.40.20.10. 1 hit.
InterProi IPR014394. 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 ]
Pfami PF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

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: September 3, 2014
This is version 179 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

External Data

Dasty 3

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