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P00748

- FA12_HUMAN

UniProt

P00748 - FA12_HUMAN

Protein

Coagulation factor XII

Gene

F12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    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 systemBy similarity
    Active sitei461 – 4611Charge relay systemBy similarity
    Active sitei563 – 5631Charge relay systemBy 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

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, intrinsic pathway Source: BHF-UCL
    3. Factor XII activation 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

    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

    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).9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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).2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 PublicationAdd
    BLAST
    Chaini20 – 372353Coagulation factor XIIa heavy chainPRO_0000027833Add
    BLAST
    Chaini354 – 3629Beta-factor XIIa part 1PRO_0000027834
    Chaini373 – 615243Beta-factor XIIa part 2PRO_0000027835Add
    BLAST
    Chaini373 – 615243Coagulation factor XIIa light chainPRO_0000027836Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 73By similarity
    Disulfide bondi61 ↔ 88By similarity
    Disulfide bondi98 ↔ 110By similarity
    Disulfide bondi104 ↔ 119By similarity
    Glycosylationi109 – 1091O-linked (Fuc)1 Publication
    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
    Glycosylationi249 – 2491N-linked (GlcNAc...)3 Publications
    Disulfide bondi266 ↔ 290By 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 ↔ 486By similarity
    Disulfide bondi397 ↔ 413By similarity
    Disulfide bondi405 ↔ 475By similarity
    Glycosylationi433 – 4331N-linked (GlcNAc...)2 Publications
    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 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.4 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. 3 interactions.
    STRINGi9606.ENSP00000253496.

    Structurei

    Secondary structure

    1
    615
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 9049Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini94 – 13138EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini133 – 17341Fibronectin type-IPROSITE-ProRule annotationAdd
    BLAST
    Domaini174 – 21037EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 29579KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini373 – 614242Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

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

    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti333 – 3331P → S in AAA51986. (PubMed:3877053)Curated
    Sequence conflicti379 – 3791A → G in AAA70224. (PubMed:3011063)Curated

    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 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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108459. 9 interactions.
    IntActi P00748. 3 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

    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: October 1, 2014
    This is version 180 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

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