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P01008 (ANT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 192. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Antithrombin-III

Short name=ATIII
Alternative name(s):
Serpin C1
Gene names
Name:SERPINC1
Synonyms:AT3
ORF Names:PRO0309
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. Ref.18

Subunit structure

Forms protease inhibiting heterodimer with TMPRSS7.

Subcellular location

Secretedextracellular space.

Tissue specificity

Found in plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium.

Involvement in disease

Antithrombin III deficiency (AT3D) [MIM:613118]: An important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. Antithrombin-III deficiency is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.12 Ref.13 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67

Sequence similarities

Belongs to the serpin family.

Mass spectrometry

Molecular mass is 57863 Da from positions 33 - 464. Determined by ESI. Ref.13

Molecular mass is 57911 Da from positions 33 - 464. Determined by ESI. Variant Thr-414. Ref.13

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Thrombophilia
   DomainSignal
   LigandHeparin-binding
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

regulation of blood coagulation, intrinsic pathway

Inferred from electronic annotation. Source: InterPro

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to nutrient

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 1695900. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protease binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12878203. Source: UniProtKB

serine-type endopeptidase inhibitor activity

Non-traceable author statement PubMed 12878203. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.10
Chain33 – 464432Antithrombin-III
PRO_0000032489

Sites

Binding site811Heparin
Binding site1611Heparin
Binding site1771Heparin
Site425 – 4262Reactive bond

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Ref.10 Ref.17 Ref.19 Ref.21
Glycosylation1671N-linked (GlcNAc...) Ref.10
Glycosylation1871N-linked (GlcNAc...) (complex) Ref.10 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22
Glycosylation2241N-linked (GlcNAc...) Ref.10 Ref.19 Ref.20
Disulfide bond40 ↔ 160 Ref.10
Disulfide bond53 ↔ 127 Ref.10
Disulfide bond279 ↔ 462 Ref.10

Natural variations

Natural variant171Y → S in AT3D; type-I. Ref.32
VAR_027450
Natural variant231L → P in AT3D; type-I; does not undergo post-translational glycosylation. Ref.32 Ref.57
VAR_012748
Natural variant301V → E in Dublin. Ref.7 Ref.32 Ref.40
Corresponds to variant rs2227624 [ dbSNP | Ensembl ].
VAR_007032
Natural variant321C → R in AT3D; type-I. Ref.58
VAR_027451
Natural variant391I → N in AT3D; type-II; Rouen-3; lack of heparin-binding properties. Ref.32
Corresponds to variant rs28929468 [ dbSNP | Ensembl ].
VAR_007033
Natural variant521M → T Previously Whitechapel. Ref.32
VAR_007034
Natural variant561R → C in AT3D; type-II; Rouen-4; lack of heparin-binding properties. Ref.32 Ref.39
Corresponds to variant rs28929469 [ dbSNP | Ensembl ].
VAR_007035
Natural variant731P → L in AT3D; type-II; Basel/Franconville/Clichy-1/Clichy-2/Dublin-2; lacks heparin-binding ability. Ref.32 Ref.34 Ref.58
Corresponds to variant rs121909551 [ dbSNP | Ensembl ].
VAR_007036
Natural variant791R → C in AT3D; Tours/Alger/Amiens/Toyama/Paris-1/Paris-2/Padua-2/Barcelona-2/Kumamoto/Omura/Sasebo; lacks heparin-binding ability. Ref.32 Ref.33 Ref.58
VAR_007037
Natural variant791R → H in AT3D; type-II; Rouen-1/Padua-1/Bligny/Budapest-2; lack of heparin-binding properties. Ref.32 Ref.48
Corresponds to variant rs121909552 [ dbSNP | Ensembl ].
VAR_007038
Natural variant791R → S in AT3D; type-II; Rouen-2; lack of heparin-binding properties. Ref.32
VAR_007039
Natural variant871Missing in AT3D; type-I. Ref.32
VAR_007040
Natural variant891R → C in AT3D; type-I. Ref.32
Corresponds to variant rs147266200 [ dbSNP | Ensembl ].
VAR_007041
Natural variant901F → L in AT3D; type-I; Budapest-6. Ref.32
VAR_007042
Natural variant951Y → C in AT3D; type-I. Ref.32
VAR_027452
Natural variant951Y → S in AT3D; type-I. Ref.32 Ref.51
VAR_012316
Natural variant981L → P in AT3D; type-I. Ref.32
VAR_027453
Natural variant108 – 1092Missing in AT3D; type-I.
VAR_007043
Natural variant1121P → T in AT3D; type-I. Ref.32 Ref.49
VAR_007044
Natural variant1211M → K in AT3D; type-I. Ref.65
VAR_027454
Natural variant1271C → R in AT3D; type-I. Ref.56
VAR_027455
Natural variant1311L → F in AT3D; type-II; Budapest-3/Budapest-7. Ref.32 Ref.44
VAR_007045
Natural variant1311L → V in AT3D; type-II; Southport. Ref.32 Ref.53
VAR_007046
Natural variant1331Q → K in AT3D; type I. Ref.32
VAR_007047
Natural variant138 – 1392Missing in AT3D; type-I.
VAR_007048
Natural variant1461K → E in AT3D; Dreux; complete loss af heparin binding. Ref.63
VAR_027456
Natural variant1471T → A. Ref.7
Corresponds to variant rs2227606 [ dbSNP | Ensembl ].
VAR_013085
Natural variant1481S → P in AT3D; type-II; Nagasaki; defective heparin binding associated with thrombosis. Ref.32 Ref.46
VAR_007049
Natural variant1501Q → P in AT3D; type-II; Vienna. Ref.32 Ref.53
VAR_007050
Natural variant152 – 1543Missing in AT3D; type-I.
VAR_012749
Natural variant1521H → Y in AT3D; type-I. Ref.49
VAR_007051
Natural variant1531Missing in AT3D; type-I.
VAR_007052
Natural variant1581L → P in AT3D; type-I. Ref.32
VAR_007053
Natural variant1601C → Y in AT3D; type-I. Ref.32 Ref.48
VAR_027457
Natural variant1611R → Q in AT3D; type-II; Geneva. Ref.32 Ref.41
VAR_007054
Natural variant1671N → T. Ref.59
VAR_012750
Natural variant1781L → H in AT3D; type-I. Ref.65
VAR_027458
Natural variant1791F → L in AT3D; type-I. Ref.66
VAR_027459
Natural variant1901Y → C Polymorphism in population of Scandinavian origin. Ref.32 Ref.49
VAR_007055
Natural variant1981Y → C in AT3D; type-I and -II; Whitechapel. Ref.32
VAR_007056
Natural variant1981Y → H in AT3D; type-I. Ref.32 Ref.58
VAR_027460
Natural variant2141S → F in AT3D; type-I. Ref.60
VAR_027461
Natural variant2141S → Y in AT3D; type-I.
VAR_007057
Natural variant2181Missing in AT3D; type-I. Ref.32
VAR_027462
Natural variant2191N → D in AT3D; type-II; Rouen-6; increases affinity for heparin. Ref.32 Ref.52
VAR_007059
Natural variant2191N → K in AT3D; type-II; Glasgow-3. Ref.32
VAR_007058
Natural variant2231S → P in AT3D; type-I. Ref.60 Ref.62
VAR_027463
Natural variant2431T → I in AT3D; type-I. Ref.60
VAR_027464
Natural variant2511I → T in AT3D; type-I. Ref.60
VAR_027465
Natural variant2571W → R in AT3D; type-I. Ref.32 Ref.58
VAR_027466
Natural variant2611F → L in AT3D. Ref.64
VAR_027467
Natural variant2691E → K in AT3D; type-II; Truro, increases affinity for heparin. Ref.32
VAR_007060
Natural variant273 – 30735Missing in AT3D; type-I.
VAR_007061
Natural variant2831M → I in AT3D; type-II. Ref.32 Ref.49
VAR_007062
Natural variant2831M → V in AT3D; type-II. Ref.60
VAR_027468
Natural variant3021L → P in AT3D; type-I.
VAR_007063
Natural variant3161I → N in AT3D; type-II; Haslar/Whitechapel. Ref.32
VAR_007064
Natural variant3231S → P in AT3D.
VAR_027469
Natural variant3341E → K in AT3D; type-II. Ref.32
VAR_007065
Natural variant3441Missing in AT3D; type-I.
VAR_007066
Natural variant3811S → P in AT3D; type-I.
VAR_007067
Natural variant3911R → Q.
VAR_007068
Natural variant3971S → P in AT3D; type-I. Ref.60
VAR_027470
Natural variant3981D → H in AT3D; type-I. Ref.67
VAR_027471
Natural variant4121S → R in AT3D; type-I. Ref.32 Ref.58
VAR_027472
Natural variant4141A → T in AT3D; type-II; Hamilton/Glasgow-2; reduces interaction with thrombin by 90%. Ref.13 Ref.32 Ref.36 Ref.42
VAR_007069
Natural variant4161A → P in AT3D; type-II; Charleville/Sudbury/Vicenza/Cambridge-1. Ref.32
Corresponds to variant rs28930978 [ dbSNP | Ensembl ].
VAR_007070
Natural variant4161A → S in AT3D; type-II; Cambridge-2. Ref.32 Ref.43
Corresponds to variant rs121909548 [ dbSNP | Ensembl ].
VAR_007071
Natural variant4191A → V in AT3D; type-I. Ref.32
VAR_007072
Natural variant4241G → D in AT3D; type-II; Stockholm. Ref.32 Ref.45
VAR_007073
Natural variant4251R → C in AT3D; type-II; Northwick-Park/Milano-1/Frankfurt-1; deprived of inhibitory activity. Ref.32 Ref.37 Ref.65 Ref.66
Corresponds to variant rs121909554 [ dbSNP | Ensembl ].
VAR_007075
Natural variant4251R → H in AT3D; type-II; Glasgow/Sheffield/Chicago/Avranches/Kumamoto-2; increases affinity for heparin; deprived of inhibitory activity. Ref.32 Ref.37 Ref.38 Ref.55 Ref.65
VAR_007074
Natural variant4251R → P in AT3D; type-II; Pescara; deprived of inhibitory of activity. Ref.32
VAR_007076
Natural variant4261S → L in AT3D; type-II; Denver/Milano-2; deprived of inhibitory activity. Ref.32 Ref.35 Ref.66
VAR_007077
Natural variant4341F → C in AT3D; type-II; Rosny. Ref.32
VAR_007078
Natural variant4341F → L in AT3D; type-II; Maisons-Laffite. Ref.32
VAR_007080
Natural variant4341F → S in AT3D; type-II; Torino. Ref.32
VAR_007079
Natural variant4361A → T in AT3D; type-II; Oslo/Paris-3. Ref.32
VAR_007081
Natural variant4371N → K in AT3D; type-II; La Rochelle. Ref.32
VAR_007082
Natural variant4381R → G in AT3D; type-II. Ref.32
VAR_009258
Natural variant4381R → M in AT3D; type-II; Kyoto. Ref.3 Ref.32
VAR_007083
Natural variant4391P → L in AT3D; type-II; Utah; deprived of inhibitory activity. Ref.12 Ref.32
VAR_007084
Natural variant4391P → T in AT3D; type-II; Budapest-5. Ref.32
VAR_007085
Natural variant4411L → P in AT3D; type-II. Ref.65
VAR_027473
Natural variant4531I → T in AT3D; type-I. Ref.32 Ref.51
VAR_007086
Natural variant4561G → R in AT3D; type-I. Ref.32 Ref.50
VAR_007087
Natural variant4571R → T in AT3D; type-II. Ref.32
VAR_007088
Natural variant459 – 4613Missing in AT3D; type-I.
VAR_007089
Natural variant4591A → D in AT3D; type-I. Ref.32
VAR_007090
Natural variant4611P → L in AT3D; type-II; Budapest. Ref.32
VAR_007091
Natural variant4621C → F in AT3D; type-I. Ref.32 Ref.51
VAR_007092

Experimental info

Mutagenesis4141A → K: Reduces interaction with thrombin by 99%. Ref.42
Mutagenesis4141A → Q: Reduces interaction with thrombin by 80%. Ref.42
Sequence conflict69 – 702EQ → QE AA sequence Ref.10
Sequence conflict771N → NN in BAA06212. Ref.3
Sequence conflict971H → R in AAG35525. Ref.5
Sequence conflict1201A → T in BAG35537. Ref.6
Sequence conflict2261T → A in BAG35537. Ref.6
Sequence conflict247 – 2493Missing AA sequence Ref.10
Sequence conflict3881Missing AA sequence Ref.13
Sequence conflict3951Y → YA AA sequence Ref.13

Secondary structure

........................................................................................ 464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01008 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9A4E324F00683D9D

FASTA46452,602
        10         20         30         40         50         60 
MYSNVIGTVT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC TAKPRDIPMN PMCIYRSPEK 

        70         80         90        100        110        120 
KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA 

       130        140        150        160        170        180 
MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG 

       190        200        210        220        230        240 
DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPSEAIN 

       250        260        270        280        290        300 
ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ 

       310        320        330        340        350        360 
VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG 

       370        380        390        400        410        420 
FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV 

       430        440        450        460 
VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of the cDNA for human antithrombin III."
Bock S.C., Wion K.L., Vehar G.A., Lawn R.M.
Nucleic Acids Res. 10:8113-8125(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Isolation and sequence characterization of a cDNA clone of human antithrombin III."
Chandra T., Stackhouse R., Kidd V.J., Woo S.L.C.
Proc. Natl. Acad. Sci. U.S.A. 80:1845-1848(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Hereditary antithrombin III deficiency: identification of an arginine-406 to methionine point mutation near protease reactive site."
Tsuji H., Takada O., Nakagawa M., Tanaka S., Hashimoto-Gotoh T.
(In) Yoshida T.O., Wilson J.M. (eds.); Molecular approaches to the study and treatment of Human diseases, pp.51-55, Elsevier, Amsterdam (1992)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT AT3D MET-438.
[4]"Complete nucleotide sequence of the antithrombin gene: evidence for homologous recombination causing thrombophilia."
Olds R.J., Lane D.A., Chowdhury V., de Stefano V., Leone G., Thein S.L.
Biochemistry 32:4216-4224(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal liver.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[7]SeattleSNPs variation discovery resource
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-30 AND ALA-147.
[8]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III."
Petersen T.E., Dudek-Wojciechowska G., Sottrup-Jensen L., Magnusson S.
(In) Collen D., Wiman B., Verstraete M. (eds.); The physiological inhibitors of blood coagulation and fibrinolysis, pp.43-54, Elsevier, Amsterdam (1979)
Cited for: PROTEIN SEQUENCE OF 33-464, GLYCOSYLATION AT ASN-128; ASN-167; ASN-187 AND ASN-224, DISULFIDE BONDS.
[11]"Isolation of a cDNA clone for human antithrombin III."
Prochownik E.V., Markham A.F., Orkin S.H.
J. Biol. Chem. 258:8389-8394(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-464.
[12]"Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site."
Bock S.C., Marrinan J.A., Radziejewska E.
Biochemistry 27:6171-6178(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-208, VARIANT AT3D LEU-439.
[13]"Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin."
Lindo V.S., Kakkar V.V., Learmonth M., Melissari E., Zappacosta F., Panico M., Morris H.R.
Br. J. Haematol. 89:589-601(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 371-425, MASS SPECTROMETRY, VARIANT AT3D THR-414.
Tissue: Plasma.
[14]"The site in human antithrombin for functional proteolytic cleavage by human thrombin."
Bjoerk I., Danielsson A., Fenton J.W. II, Joernvall H.
FEBS Lett. 126:257-260(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: REACTIVE SITE.
[15]"The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence."
Blackburn M.N., Smith R.L., Carson J., Sibley C.C.
J. Biol. Chem. 259:939-941(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: HEPARIN-BINDING SITE.
[16]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187.
Tissue: Bile.
[17]"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-128 AND ASN-187.
Tissue: Plasma.
[18]"Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity."
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.
Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
[19]"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-128; ASN-187 AND ASN-224.
Tissue: Plasma.
[20]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224.
Tissue: Platelet.
[21]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187.
Tissue: Liver.
[22]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Biological implications of a 3 A structure of dimeric antithrombin."
Carrell R.W., Stein P.E., Fermi G., Wardell M.R.
Structure 2:257-270(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[25]"The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions."
Schreuder H.A., de Boer B., Dijkema R., Mulders J., Theunissen H.J.M., Grootenhuis P.D.J., Hol W.G.J.
Nat. Struct. Biol. 1:48-54(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[26]"The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site."
Skinner R., Abrahams J.P., Whisstock J.C., Lesk A.M., Carrel R.W., Wardell M.R.
J. Mol. Biol. 266:601-609(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[27]"Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin."
Skinner R., Chang W.-S.W., Jin L., Pei X.Y., Huntington J.A., Abrahams J.P., Carrell R.W., Lomas D.A.
J. Mol. Biol. 283:9-14(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[28]"Antithrombin III: structural and functional aspects."
Mourey L., Samama J.-P., Delarue M., Choay J., Lormeau J.C., Petitou M., Moras D.
Biochimie 72:599-608(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[29]"Antithrombin III mutation database: first update. For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis."
Lane D.A., Olds R.J., Boisclair M., Chowdhury V., Thein S.L., Cooper D.N., Blajchman M., Perry D., Emmerich J., Aiach M.
Thromb. Haemost. 70:361-369(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[30]"What do dysfunctional serpins tell us about molecular mobility and disease?"
Stein P.E., Carrell R.W.
Nat. Struct. Biol. 2:96-113(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[31]"Molecular genetics of human antithrombin deficiency."
Perry D.J., Carrell R.W.
Hum. Mutat. 7:7-22(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[32]"Antithrombin mutation database: 2nd (1997) update."
The plasma coagulation inhibitors subcommittee of the scientific and standardization committee of the international society on thrombosis and haemostasis
Lane D.A., Bayston T., Olds R.J., Fitches A.C., Cooper D.N., Millar D.S., Jochmans K., Perry D.J., Okajima K., Thein S.L., Emmerich J.
Thromb. Haemost. 77:197-211(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D SER-17; PRO-23; ASN-39; CYS-56; LEU-73; CYS-79; HIS-79; SER-79; ASN-87 DEL; CYS-89; LEU-90; CYS-95; SER-95; PRO-98; THR-112; PHE-131; VAL-131; LYS-133; PHE-138-139-LYS DEL; PRO-148; PRO-150; PRO-158; TYR-160; GLN-161; CYS-198; HIS-198; ILE-218 DEL; ASP-219; LYS-219; ARG-257; LYS-269; ILE-283; ASN-316; LYS-334; ARG-412; THR-414; PRO-416; SER-416; VAL-419; ASP-424; CYS-425; HIS-425; PRO-425; LEU-426; CYS-434; LEU-434; SER-434; THR-436; LYS-437; GLY-438; MET-438; LEU-439; THR-439; THR-453; ARG-456; THR-457; ASP-459; LEU-461 AND PHE-462, VARIANTS GLU-30; THR-52 AND CYS-190.
[33]"Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability."
Koide T., Odani S., Takahashi K., Ono T., Sakuragawa N.
Proc. Natl. Acad. Sci. U.S.A. 81:289-293(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D CYS-79.
[34]"Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity."
Chang J.Y., Tran T.H.
J. Biol. Chem. 261:1174-1176(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D LEU-73.
[35]"Antithrombin-III Denver, a reactive site variant."
Stephens A.W., Thalley B.S., Hirs C.H.W.
J. Biol. Chem. 262:1044-1048(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D LEU-426.
[36]"Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity."
Devrak-Kizuk R., Chui D.H.K., Prochownik E.V., Carter C.J., Ofosu F.A., Blajchman M.A.
Blood 72:1518-1523(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D THR-414.
[37]"Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow."
Erdjument H., Laned D.A., Panico M., di Marzo V., Morris H.R.
J. Biol. Chem. 263:5589-5593(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D CYS-425 AND HIS-425.
[38]"Antithrombin Chicago, amino acid substitution of arginine 393 to histidine."
Erdjument H., Lane D.A., Panico M., di Marzo V., Morris H.R., Bauer K., Rosenberg R.D.
Thromb. Res. 54:613-619(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D HIS-425.
[39]"Antithrombin Rouen-IV 24 Arg-->Cys. The amino-terminal contribution to heparin binding."
Borg J.Y., Brennan S.O., Carrell R.W., George P., Perry D.J., Shaw J.
FEBS Lett. 266:163-166(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D CYS-56.
[40]"Antithrombin Dublin (-3 Val-->Glu): an N-terminal variant which has an aberrant signal peptidase cleavage site."
Daly M., Bruce D., Perry D.J., Price J., Harper P.L., O'Meara A., Carrell R.W.
FEBS Lett. 273:87-90(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-30.
[41]"Important role of arginine 129 in heparin-binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine."
Gandrille S., Aiach M., Lane D.A., Vidaud D., Molho-Sabatier P., Caso R., de Moerloose P., Fiessinger J.-N., Clauser E.
J. Biol. Chem. 265:18997-19001(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D GLN-161.
[42]"Site-directed mutagenesis of alanine-382 of human antithrombin III."
Austin R.C., Rachubinski R.A., Blachjman M.A.
FEBS Lett. 280:254-258(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT AT3D THR-414, MUTAGENESIS OF ALA-414.
[43]"Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins."
Perry D.J., Daly M., Harper P.L., Tait R.C., Price J., Walker I.D., Carrell R.W.
FEBS Lett. 285:248-250(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D SER-416.
[44]"Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F."
Olds R.J., Lane D.A., Boisclair M., Sas G., Bock S.C., Thein S.L.
FEBS Lett. 300:241-246(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D PHE-131.
[45]"Antithrombin-III Stockholm: a codon 392 (Gly-->Asp) mutation with normal heparin binding and impaired serine protease reactivity."
Blajchman M.A., Fernandez-Rachubinski F., Sheffield W.P., Austin R.C., Schulman S.
Blood 79:1428-1434(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D ASP-424.
[46]"Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis."
Okajima K., Abe H., Maeda S., Motomura M., Tsujihata M., Nagataki S., Okabe H., Takatsuki K.
Blood 81:1300-1305(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D PRO-148.
[47]"A recurrent deletion in the antithrombin gene, AT106-108(-6 bp), identified by DNA heteroduplex detection."
Olds R.J., Lane D.A., Beresford C.H., Abildgaard U., Hughes P.M., Thein S.L.
Genomics 16:298-299(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D 138-PHE-LYS-139 DEL.
[48]"Three novel mutations of antithrombin inducing high-molecular-mass compounds."
Emmerich J., Vidaud D., Alhenc-Gelas M., Chadeuf G., Gouault-Heilmann M., Aillaud M.-F., Aiach M.
Arterioscler. Thromb. 14:1958-1965(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D HIS-79 AND TYR-160.
[49]"Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis."
Millar D.S., Wacey A.I., Ribando J., Melissari E., Laursen B., Woods P., Kakkar V.V., Cooper D.N.
Hum. Genet. 94:509-512(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D THR-112; TYR-152 AND ILE-283, VARIANT CYS-190.
[50]"Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1 antithrombin deficiency and neonatal thrombosis."
Jochmans K., Lissens W., Vervoort R., Peeters S., de Waelwe M., Liebaers I.
Blood 83:146-151(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D ARG-456.
[51]"Hereditary antithrombin deficiency: heterogeneity of the molecular basis and mortality in Dutch families."
van Boven H.H., Olds R.J., Thein S.L., Reitsma P.H., Lane D.A., Briet E., Vandenbroucke J.P., Rosendaal F.R.
Blood 84:4209-4213(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D SER-95; THR-453 AND PHE-462.
[52]"Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp)."
Bruce D., Perry D.J., Borg J.-Y., Carrell R.W., Wardell M.R.
J. Clin. Invest. 94:2265-2274(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D ASP-219.
[53]"Two novel antithrombin variants (L99V and Q118P) which alter the heparin binding domain."
Chowdhury V., Olds R.J., Lane D.A., Mille B., Pabinger I., Thein S.L.
Nouv. Rev. Fr. Hematol. 86:268-268(1994)
Cited for: VARIANTS AT3D VAL-131 AND PRO-150.
[54]"Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6."
Emmerich J., Chadeuf G., Alhenc-Gelas M., Gouault-Heilman M., Toulon P., Fiessinger J.-N., Aiach M.
Thromb. Haemost. 72:534-539(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D 273-LYS--LYS-307 DEL.
[55]"Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin."
Okajima K., Abe H., Wagatsuma M., Okabe H., Takatsuki K.
Am. J. Hematol. 48:12-18(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D HIS-425.
[56]"Antithrombin Morioka (Cys 95-Arg): a novel missense mutation causing type I antithrombin deficiency."
Ozawa T., Takikawa Y., Niiya K., Fujiwara T., Suzuki K., Sato S., Sakuragawa N.
Thromb. Haemost. 77:403-403(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D ARG-127.
[57]"Impaired cotranslational processing as a mechanism for type I antithrombin deficiency."
Fitches A.C., Appleby R., Lane D.A., De Stefano V., Leone G., Olds R.J.
Blood 92:4671-4676(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D PRO-23.
[58]"The molecular basis of antithrombin deficiency in Belgian and Dutch families."
Jochmans K., Lissens W., Seneca S., Capel P., Chatelain B., Meeus P., Osselaer J.C., Peerlinck K., Seghers J., Slacmeulder M., Stibbe J., van de Loo J., Vermylen J., Liebaers I., De Waele M.
Thromb. Haemost. 80:376-381(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412.
[59]"Familial overexpression of beta-antithrombin caused by an Asn135-to-Thr substitution."
Bayston T.A., Tripodi A., Mannucci P.M., Thompson E., Ireland H., Fitches A.C., Hananeia L., Olds R.J., Lane D.A.
Blood 93:4242-4247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-167.
[60]"Molecular bases of antithrombin deficiency in French families: identification of seven novel mutations in the antithrombin gene."
Picard V., Bura A., Emmerich J., Alhenc-Gelas M., Biron C., Houbouyan-Reveillard L.L., Molho P., Labatide-Alanore A., Sie P., Toulon P., Verdy E., Aiach M.
Br. J. Haematol. 110:731-734(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D PHE-214; PRO-223; ILE-243; THR-251; VAL-283 AND PRO-397.
[61]"Two novel gene mutations in type I antithrombin deficiency."
Niiya K., Kiguchi T., Dansako H., Fujimura K., Fujimoto T., Iijima K., Tanimoto M., Harada M.
Int. J. Hematol. 74:469-472(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D 152-HIS--PHE-154 DEL.
[62]"Intracerebral hemorrhage associated with a novel antithrombin gene mutation in a neonate."
Baud O., Picard V., Durand P., Duchemin J., Proulle V., Alhenc-Gelas M., Devictor D., Dreyfus M.
J. Pediatr. 139:741-743(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D PRO-223.
[63]"Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of heparin affinity."
Mushunje A., Zhou A., Huntington J.A., Conard J., Carrell R.W.
Thromb. Haemost. 88:436-443(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D GLU-146.
[64]"Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous antithrombin polymerization in vivo associated with severe childhood thrombosis."
Picard V., Dautzenberg M.-D., Villoutreix B.O., Orliaguet G., Alhenc-Gelas M., Aiach M.
Blood 102:919-925(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D LEU-261.
[65]"Five novel and four recurrent point mutations in the antithrombin gene causing venous thrombosis."
Nagaizumi K., Inaba H., Amano K., Suzuki M., Arai M., Fukutake K.
Int. J. Hematol. 78:79-83(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441.
[66]"Molecular basis of inherited antithrombin deficiency in Portuguese families: identification of genetic alterations and screening for additional thrombotic risk factors."
David D., Ribeiro S., Ferrao L., Gago T., Crespo F.
Am. J. Hematol. 76:163-171(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT3D LEU-179; CYS-425 AND LEU-426.
[67]"Retinal vein occlusion associated with antithrombin deficiency secondary to a novel G9840C missense mutation."
Kuhli C., Jochmans K., Scharrer I., Luechtenberg M., Hattenbach L.-O.
Arch. Ophthalmol. 124:1165-1169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT3D HIS-398.
+Additional computationally mapped references.

Web resources

Wikipedia

Antithrombin entry

Antithrombin mutation database
SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00185 Genomic DNA. No translation available.
L00186 Genomic DNA. No translation available.
L00190 Genomic DNA. Translation: AAB40025.1.
D29832 mRNA. Translation: BAA06212.1.
X68793 Genomic DNA. Translation: CAA48690.1.
AF130100 mRNA. Translation: AAG35525.1.
AK312654 mRNA. Translation: BAG35537.1.
AF386078 Genomic DNA. Translation: AAK60337.1.
AL136170 Genomic DNA. Translation: CAI19423.1.
CH471067 Genomic DNA. Translation: EAW90969.1.
M21643 Genomic DNA. Translation: AAA51793.1.
M21644, M21643 Genomic DNA. Translation: AAA51794.1.
M21642 expand/collapse EMBL AC list , M21636, M21637, M21638, M21640, M21641 Genomic DNA. Translation: AAA51796.1.
CCDSCCDS1313.1.
PIRXHHU3. A49494.
RefSeqNP_000479.1. NM_000488.3.
UniGeneHs.75599.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ANTX-ray3.00I/L33-464[»]
1ATHX-ray3.20A/B33-464[»]
1AZXX-ray2.90I/L33-464[»]
1BR8X-ray2.90I/L33-464[»]
1DZGX-ray2.80I/L33-464[»]
1DZHX-ray2.85I/L33-464[»]
1E03X-ray2.90I/L33-464[»]
1E04X-ray2.60I/L33-464[»]
1E05X-ray2.62I/L33-464[»]
1JVQX-ray2.60I/L33-464[»]
1LK6X-ray2.80I/L33-464[»]
1NQ9X-ray2.60I/L33-464[»]
1OYHX-ray2.62I/L33-464[»]
1R1LX-ray2.70I/L33-464[»]
1SR5X-ray3.10A33-464[»]
1T1FX-ray2.75A/B/C33-464[»]
1TB6X-ray2.50I33-464[»]
2ANTX-ray2.60I/L33-464[»]
2B4XX-ray2.80I/L37-463[»]
2B5TX-ray2.10I33-464[»]
2BEHX-ray2.70I/L33-464[»]
2GD4X-ray3.30C/I22-464[»]
2HIJX-ray2.90I/L33-464[»]
2ZNHX-ray2.80A/B33-464[»]
3EVJX-ray3.00I/L33-464[»]
3KCGX-ray1.70I33-464[»]
4EB1X-ray2.80I/L33-464[»]
ProteinModelPortalP01008.
SMRP01008. Positions 37-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106953. 1 interaction.
DIPDIP-38009N.
IntActP01008. 3 interactions.

Chemistry

BindingDBP01008.
ChEMBLCHEMBL1950.
DrugBankDB01225. Enoxaparin.
DB00569. Fondaparinux sodium.
DB01109. Heparin.
GuidetoPHARMACOLOGY2632.

Protein family/group databases

MEROPSI04.018.

PTM databases

PhosphoSiteP01008.

Polymorphism databases

DMDM113936.

2D gel databases

DOSAC-COBS-2DPAGEP01008.
REPRODUCTION-2DPAGEP01008.
SWISS-2DPAGEP01008.

Proteomic databases

MaxQBP01008.
PaxDbP01008.
PRIDEP01008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367698; ENSP00000356671; ENSG00000117601.
GeneID462.
KEGGhsa:462.
UCSCuc001gjt.3. human.

Organism-specific databases

CTD462.
GeneCardsGC01M173872.
HGNCHGNC:775. SERPINC1.
HPACAB016790.
HPA001816.
HPA024007.
MIM107300. gene.
613118. phenotype.
neXtProtNX_P01008.
Orphanet82. Hereditary thrombophilia due to congenital antithrombin deficiency.
PharmGKBPA35026.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOVERGENHBG005957.
InParanoidP01008.
KOK03911.
OMAKADGESC.
OrthoDBEOG7327PB.
PhylomeDBP01008.
TreeFamTF343094.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP01008.
BgeeP01008.
CleanExHS_SERPINC1.
GenevestigatorP01008.

Family and domain databases

InterProIPR015555. AT-III.
IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PTHR11461:SF53. PTHR11461:SF53. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPINC1. human.
EvolutionaryTraceP01008.
GeneWikiAntithrombin.
GenomeRNAi462.
NextBio1911.
PMAP-CutDBP01008.
PROP01008.
SOURCESearch...

Entry information

Entry nameANT3_HUMAN
AccessionPrimary (citable) accession number: P01008
Secondary accession number(s): B2R6P0 expand/collapse secondary AC list , P78439, P78447, Q13815, Q5TC78, Q7KZ43, Q7KZ97, Q9UC78
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 192 of the entry and version 1 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM