P01008 (ANT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Antithrombin-III
Short name=ATIII

Alternative name(s):
Serpin C1

Gene names

Name:	SERPINC1
Synonyms:	AT3
ORF Names:	PRO0309

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular 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 process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Thrombophilia
Domain	Signal
Ligand	Heparin-binding
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome negative regulation of inflammatory response Inferred from electronic annotation. Source: Compara regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome response to nutrient Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from direct assay PubMed 1695900. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase inhibitor activity Non-traceable author statement PubMed 12878203. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Ref.10

Chain

33 – 464

432

Antithrombin-III

PRO_0000032489

Sites

Binding site

81

1

Heparin

Binding site

161

1

Heparin

Binding site

177

1

Heparin

Site

425 – 426

2

Reactive bond

Amino acid modifications

Glycosylation

128

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.19 Ref.21

Glycosylation

167

1

N-linked (GlcNAc...) Ref.10

Glycosylation

187

1

N-linked (GlcNAc...) (complex) Ref.10 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22

Glycosylation

224

1

N-linked (GlcNAc...) Ref.10 Ref.19 Ref.20

Disulfide bond

40 ↔ 160

Ref.10

Disulfide bond

53 ↔ 127

Ref.10

Disulfide bond

279 ↔ 462

Ref.10

Natural variations

Natural variant

17

1

Y → S in AT3D; type-I. Ref.32

VAR_027450

Natural variant

23

1

L → P in AT3D; type-I; impairs cotranslational processing. Ref.32 Ref.57

VAR_012748

Natural variant

30

1

V → E in Dublin. Ref.7 Ref.32 Ref.40
Corresponds to variant rs2227624 [ dbSNP | Ensembl ].

VAR_007032

Natural variant

32

1

C → R in AT3D; type-I. Ref.58

VAR_027451

Natural variant

39

1

I → N in AT3D; type-II; Rouen-3; lack of heparin-binding properties. Ref.32
Corresponds to variant rs28929468 [ dbSNP | Ensembl ].

VAR_007033

Natural variant

52

1

M → T Previously Whitechapel. Ref.32

VAR_007034

Natural variant

56

1

R → 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 variant

73

1

P → L in AT3D; type-II; Basel/Franconville/Clichy-1/Clichy-2/Dublin-2; lacks heparin-binding ability. Ref.32 Ref.34 Ref.58

VAR_007036

Natural variant

79

1

R → 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 variant

79

1

R → H in AT3D; type-II; Rouen-1/Padua-1/Bligny/Budapest-2; lack of heparin-binding properties. Ref.32 Ref.48

VAR_007038

Natural variant

79

1

R → S in AT3D; type-II; Rouen-2; lack of heparin-binding properties. Ref.32

VAR_007039

Natural variant

87

1

Missing in AT3D; type-I. Ref.32

VAR_007040

Natural variant

89

1

R → C in AT3D; type-I. Ref.32

VAR_007041

Natural variant

90

1

F → L in AT3D; type-I; Budapest-6. Ref.32

VAR_007042

Natural variant

95

1

Y → C in AT3D; type-I. Ref.32

VAR_027452

Natural variant

95

1

Y → S in AT3D; type-I. Ref.32 Ref.51

VAR_012316

Natural variant

98

1

L → P in AT3D; type-I. Ref.32

VAR_027453

Natural variant

108 – 109

2

Missing in AT3D; type-I.

VAR_007043

Natural variant

112

1

P → T in AT3D; type-I. Ref.32 Ref.49

VAR_007044

Natural variant

121

1

M → K in AT3D; type-I. Ref.65

VAR_027454

Natural variant

127

1

C → R in AT3D; type-I. Ref.56

VAR_027455

Natural variant

131

1

L → F in AT3D; type-II; Budapest-3/Budapest-7. Ref.32 Ref.44

VAR_007045

Natural variant

131

1

L → V in AT3D; type-II; Southport. Ref.32 Ref.53

VAR_007046

Natural variant

133

1

Q → K in AT3D; type I. Ref.32

VAR_007047

Natural variant

138 – 139

2

Missing in AT3D; type-I.

VAR_007048

Natural variant

146

1

K → E in AT3D; Dreux; complete loss af heparin binding. Ref.63

VAR_027456

Natural variant

147

1

T → A. Ref.7
Corresponds to variant rs2227606 [ dbSNP | Ensembl ].

VAR_013085

Natural variant

148

1

S → P in AT3D; type-II; Nagasaki; defective heparin binding associated with thrombosis. Ref.32 Ref.46

VAR_007049

Natural variant

150

1

Q → P in AT3D; type-II; Vienna. Ref.32 Ref.53

VAR_007050

Natural variant

152 – 154

3

Missing in AT3D; type-I.

VAR_012749

Natural variant

152

1

H → Y in AT3D; type-I. Ref.49

VAR_007051

Natural variant

153

1

Missing in AT3D; type-I.

VAR_007052

Natural variant

158

1

L → P in AT3D; type-I. Ref.32

VAR_007053

Natural variant

160

1

C → Y in AT3D; type-I. Ref.32 Ref.48

VAR_027457

Natural variant

161

1

R → Q in AT3D; type-II; Geneva. Ref.32 Ref.41

VAR_007054

Natural variant

167

1

N → T. Ref.59

VAR_012750

Natural variant

178

1

L → H in AT3D; type-I. Ref.65

VAR_027458

Natural variant

179

1

F → L in AT3D; type-I. Ref.66

VAR_027459

Natural variant

190

1

Y → C Polymorphism in population of Scandinavian origin. Ref.32 Ref.49

VAR_007055

Natural variant

198

1

Y → C in AT3D; type-I and -II; Whitechapel. Ref.32

VAR_007056

Natural variant

198

1

Y → H in AT3D; type-I. Ref.32 Ref.58

VAR_027460

Natural variant

214

1

S → F in AT3D; type-I. Ref.60

VAR_027461

Natural variant

214

1

S → Y in AT3D; type-I.

VAR_007057

Natural variant

218

1

Missing in AT3D; type-I. Ref.32

VAR_027462

Natural variant

219

1

N → D in AT3D; type-II; Rouen-6; increases affinity for heparin. Ref.32 Ref.52

VAR_007059

Natural variant

219

1

N → K in AT3D; type-II; Glasgow-3. Ref.32

VAR_007058

Natural variant

223

1

S → P in AT3D; type-I. Ref.60 Ref.62

VAR_027463

Natural variant

243

1

T → I in AT3D; type-I. Ref.60

VAR_027464

Natural variant

251

1

I → T in AT3D; type-I. Ref.60

VAR_027465

Natural variant

257

1

W → R in AT3D; type-I. Ref.32 Ref.58

VAR_027466

Natural variant

261

1

F → L in AT3D. Ref.64

VAR_027467

Natural variant

269

1

E → K in AT3D; type-II; Truro, increases affinity for heparin. Ref.32

VAR_007060

Natural variant

273 – 307

35

Missing in AT3D; type-I.

VAR_007061

Natural variant

283

1

M → I in AT3D; type-II. Ref.32 Ref.49

VAR_007062

Natural variant

283

1

M → V in AT3D; type-II. Ref.60

VAR_027468

Natural variant

302

1

L → P in AT3D; type-I.

VAR_007063

Natural variant

316

1

I → N in AT3D; type-II; Haslar/Whitechapel. Ref.32

VAR_007064

Natural variant

323

1

S → P in AT3D.

VAR_027469

Natural variant

334

1

E → K in AT3D; type-II. Ref.32

VAR_007065

Natural variant

344

1

Missing in AT3D; type-I.

VAR_007066

Natural variant

381

1

S → P in AT3D; type-I.

VAR_007067

Natural variant

391

1

R → Q.

VAR_007068

Natural variant

397

1

S → P in AT3D; type-I. Ref.60

VAR_027470

Natural variant

398

1

D → H in AT3D; type-I. Ref.67

VAR_027471

Natural variant

412

1

S → R in AT3D; type-I. Ref.32 Ref.58

VAR_027472

Natural variant

414

1

A → 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 variant

416

1

A → P in AT3D; type-II; Charleville/Sudbury/Vicenza/Cambridge-1. Ref.32
Corresponds to variant rs28930978 [ dbSNP | Ensembl ].

VAR_007070

Natural variant

416

1

A → S in AT3D; type-II; Cambridge-2. Ref.32 Ref.43

VAR_007071

Natural variant

419

1

A → V in AT3D; type-I. Ref.32

VAR_007072

Natural variant

424

1

G → D in AT3D; type-II; Stockholm. Ref.32 Ref.45

VAR_007073

Natural variant

425

1

R → C in AT3D; type-II; Northwick-Park/Milano-1/Frankfurt-1; deprived of inhibitory activity. Ref.32 Ref.37 Ref.65 Ref.66

VAR_007075

Natural variant

425

1

R → 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 variant

425

1

R → P in AT3D; type-II; Pescara; deprived of inhibitory of activity. Ref.32

VAR_007076

Natural variant

426

1

S → L in AT3D; type-II; Denver/Milano-2; deprived of inhibitory activity. Ref.32 Ref.35 Ref.66

VAR_007077

Natural variant

434

1

F → C in AT3D; type-II; Rosny. Ref.32

VAR_007078

Natural variant

434

1

F → L in AT3D; type-II; Maisons-Laffite. Ref.32

VAR_007080

Natural variant

434

1

F → S in AT3D; type-II; Torino. Ref.32

VAR_007079

Natural variant

436

1

A → T in AT3D; type-II; Oslo/Paris-3. Ref.32

VAR_007081

Natural variant

437

1

N → K in AT3D; type-II; La Rochelle. Ref.32

VAR_007082

Natural variant

438

1

R → G in AT3D; type-II. Ref.32

VAR_009258

Natural variant

438

1

R → M in AT3D; type-II; Kyoto. Ref.3 Ref.32

VAR_007083

Natural variant

439

1

P → L in AT3D; type-II; Utah; deprived of inhibitory activity. Ref.12 Ref.32

VAR_007084

Natural variant

439

1

P → T in AT3D; type-II; Budapest-5. Ref.32

VAR_007085

Natural variant

441

1

L → P in AT3D; type-II. Ref.65

VAR_027473

Natural variant

453

1

I → T in AT3D; type-I. Ref.32 Ref.51

VAR_007086

Natural variant

456

1

G → R in AT3D; type-I. Ref.32 Ref.50

VAR_007087

Natural variant

457

1

R → T in AT3D; type-II. Ref.32

VAR_007088

Natural variant

459 – 461

3

Missing in AT3D; type-I.

VAR_007089

Natural variant

459

1

A → D in AT3D; type-I. Ref.32

VAR_007090

Natural variant

461

1

P → L in AT3D; type-II; Budapest. Ref.32

VAR_007091

Natural variant

462

1

C → F in AT3D; type-I. Ref.32 Ref.51

VAR_007092

Experimental info

Mutagenesis

414

1

A → K: Reduces interaction with thrombin by 99%. Ref.42

Mutagenesis

414

1

A → Q: Reduces interaction with thrombin by 80%. Ref.42

Sequence conflict

69 – 70

2

EQ → QE AA sequence Ref.10

Sequence conflict

77

1

N → NN in BAA06212. Ref.3

Sequence conflict

97

1

H → R in AAG35525. Ref.5

Sequence conflict

120

1

A → T in BAG35537. Ref.6

Sequence conflict

226

1

T → A in BAG35537. Ref.6

Sequence conflict

247 – 249

3

Missing AA sequence Ref.10

Sequence conflict

388

1

Missing AA sequence Ref.13

Sequence conflict

395

1

Y → YA AA sequence Ref.13

Secondary structure

1

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464

Helix Strand Turn

Details...

Helix

39 – 41

3

Turn

44 – 46

3

Helix

78 – 101

24

Beta strand

108 – 110

3

Helix

112 – 123

12

Helix

128 – 137

10

Helix

140 – 142

3

Helix

145 – 149

5

Helix

151 – 166

16

Turn

167 – 169

3

Beta strand

170 – 181

12

Beta strand

184 – 186

3

Helix

188 – 198

11

Beta strand

203 – 205

3

Helix

207 – 225

19

Turn

226 – 228

3

Beta strand

237 – 239

3

Beta strand

240 – 242

3

Beta strand

245 – 255

11

Beta strand

257 – 259

3

Helix

263 – 265

3

Beta strand

267 – 272

6

Beta strand

274 – 276

3

Beta strand

278 – 294

17

Helix

296 – 298

3

Beta strand

300 – 306

7

Beta strand

309 – 317

9

Beta strand

320 – 322

3

Helix

324 – 329

6

Helix

333 – 342

10

Beta strand

344 – 353

10

Beta strand

355 – 362

8

Helix

364 – 369

6

Helix

374 – 376

3

Turn

378 – 380

3

Turn

384 – 386

3

Beta strand

389 – 392

4

Beta strand

398 – 407

10

Beta strand

409 – 413

5

Beta strand

419 – 422

4

Beta strand

423 – 426

4

Beta strand

432 – 435

4

Beta strand

440 – 446

7

Turn

447 – 450

4

Beta strand

451 – 459

9

Sequences

	Sequence		Length	Mass (Da)
	P01008 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 9A4E324F00683D9D	FASTA	464	52,602
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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

GeneReviews

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 , M21636, M21637, M21638, M21640, M21641 Genomic DNA. Translation: AAA51796.1.

IPI

IPI00032179.

PIR

XHHU3. A49494.

RefSeq

NP_000479.1. NM_000488.3.

UniGene

Hs.75599.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ANT	X-ray	3.00	I/L	33-464	[»]
1ATH	X-ray	3.20	A/B	33-464	[»]
1AZX	X-ray	2.90	I/L	33-464	[»]
1BR8	X-ray	2.90	I/L	33-464	[»]
1DZG	X-ray	2.80	I/L	33-464	[»]
1DZH	X-ray	2.85	I/L	33-464	[»]
1E03	X-ray	2.90	I/L	33-464	[»]
1E04	X-ray	2.60	I/L	33-464	[»]
1E05	X-ray	2.62	I/L	33-464	[»]
1JVQ	X-ray	2.60	I/L	33-464	[»]
1LK6	X-ray	2.80	I/L	33-464	[»]
1NQ9	X-ray	2.60	I/L	33-464	[»]
1OYH	X-ray	2.62	I/L	33-464	[»]
1R1L	X-ray	2.70	I/L	33-464	[»]
1SR5	X-ray	3.10	A	33-464	[»]
1T1F	X-ray	2.75	A/B/C	33-464	[»]
1TB6	X-ray	2.50	I	33-464	[»]
2ANT	X-ray	2.60	I/L	33-464	[»]
2B4X	X-ray	2.80	I/L	37-463	[»]
2B5T	X-ray	2.10	I	33-464	[»]
2BEH	X-ray	2.70	I/L	33-464	[»]
2GD4	X-ray	3.30	C/I	22-464	[»]
2HIJ	X-ray	2.90	I/L	33-464	[»]
2ZNH	X-ray	2.80	A/B	33-464	[»]
3EVJ	X-ray	3.00	I/L	33-464	[»]
3KCG	X-ray	1.70	I	33-464	[»]
4EB1	X-ray	2.80	I/L	33-464	[»]

ProteinModelPortal

P01008.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38009N.

IntAct

P01008. 3 interactions.

Protein family/group databases

MEROPS

I04.018.

PTM databases

PhosphoSite

P01008.

Polymorphism databases

DMDM

113936.

2D gel databases

DOSAC-COBS-2DPAGE

P01008.

REPRODUCTION-2DPAGE

P01008.

SWISS-2DPAGE

P01008.

Proteomic databases

PaxDb

P01008.

PRIDE

P01008.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367698; ENSP00000356671; ENSG00000117601.

GeneID

462.

KEGG

hsa:462.

UCSC

uc001gjt.3. human.

Organism-specific databases

CTD

462.

GeneCards

GC01M173872.

HGNC

HGNC:775. SERPINC1.

HPA

CAB016790.
HPA001816.
HPA024007.

MIM

107300. gene.
613118. phenotype.

neXtProt

NX_P01008.

Orphanet

82. Hereditary thrombophilia due to congenital antithrombin deficiency.

PharmGKB

PA35026.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4826.

HOVERGEN

HBG005957.

InParanoid

P01008.

KO

K03911.

OMA

ACDNTLK.

OrthoDB

EOG4SF968.

PhylomeDB

P01008.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P01008.

Bgee

P01008.

CleanEx

HS_SERPINC1.

Genevestigator

P01008.

GermOnline

ENSG00000117601. Homo sapiens.

Family and domain databases

InterPro

IPR015555. AT-III.
IPR023795. Protease_inhib_I4_serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.
PTHR11461:SF53. PTHR11461:SF53. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P01008.

ChEMBL

CHEMBL1950.

ChiTaRS

SERPINC1. human.

DrugBank

DB01225. Enoxaparin.
DB00569. Fondaparinux sodium.
DB01109. Heparin.

EvolutionaryTrace

P01008.

GenomeRNAi

462.

NextBio

1911.

PMAP-CutDB

P01008.

SOURCE

Search...

Entry information

Entry name

ANT3_HUMAN

Accession

Primary (citable) accession number: P01008
Secondary accession number(s): B2R6P0 , 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:	May 1, 2013
This is version 178 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.