Reviewed, UniProtKB/Swiss-Prot P01008 (ANT3_HUMAN)

Names and origin

Protein names

Recommended name:
    Antithrombin-III
      Short name=ATIII

Gene names

Name:	SERPINC1
Synonyms:	AT3
ORF Names:	PRO0309

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Found in plasma. Ref.21
Post-translational modification	Phosphorylation sites are present in the extracelllular medium.
Involvement in disease	Defects in SERPINC1 are the cause of antithrombin-III deficiency (AT3D) [MIM:107300]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D 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. Ref.12 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 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.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65
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
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
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW protease binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase inhibitor activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PLCG1	P19174	1	EBI-1039832,EBI-79387

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

Modified residue

68

1

Phosphoserine Ref.21

Glycosylation

128

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18 Ref.20

Glycosylation

167

1

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

Glycosylation

187

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18 Ref.20 Ref.16

Glycosylation

224

1

N-linked (GlcNAc...) Ref.10 Ref.18 Ref.19

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.30

VAR_027450

Natural variant

23

1

L → P in AT3D; type-I; impairs cotranslational processing. Ref.30 Ref.55

VAR_012748

Natural variant

30

1

V → E in Dublin. dbSNP rs2227624. Ref.30 Ref.7 Ref.38

VAR_007032

Natural variant

32

1

C → R in AT3D; type-I. Ref.56

VAR_027451

Natural variant

39

1

I → N in AT3D; type-II; Rouen-3; lack of heparin-binding properties. dbSNP rs28929468. Ref.30

VAR_007033

Natural variant

52

1

M → T Previously Whitechapel. Ref.30

VAR_007034

Natural variant

56

1

R → C in AT3D; type-II; Rouen-4; lack of heparin-binding properties. dbSNP rs28929469. Ref.30 Ref.37

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.30 Ref.32 Ref.56

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.30 Ref.31 Ref.56

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.30 Ref.46

VAR_007038

Natural variant

79

1

R → S in AT3D; type-II; Rouen-2; lack of heparin-binding properties. Ref.30

VAR_007039

Natural variant

87

1

Missing in AT3D; type-I.

VAR_007040

Natural variant

89

1

R → C in AT3D; type-I. Ref.30

VAR_007041

Natural variant

90

1

F → L in AT3D; type-I; Budapest-6. Ref.30

VAR_007042

Natural variant

95

1

Y → C in AT3D; type-I. Ref.30

VAR_027452

Natural variant

95

1

Y → S in AT3D; type-I. Ref.30 Ref.49

VAR_012316

Natural variant

98

1

L → P in AT3D; type-I. Ref.30

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.30 Ref.47

VAR_007044

Natural variant

121

1

M → K in AT3D; type-I. Ref.63

VAR_027454

Natural variant

127

1

C → R in AT3D; type-I. Ref.54

VAR_027455

Natural variant

131

1

L → F in AT3D; type-II; Budapest-3/Budapest-7. Ref.30 Ref.42

VAR_007045

Natural variant

131

1

L → V in AT3D; type-II; Southport. Ref.30 Ref.51

VAR_007046

Natural variant

133

1

Q → K in AT3D; type I. Ref.30

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.61

VAR_027456

Natural variant

147

1

T → A: dbSNP rs2227606. Ref.7

VAR_013085

Natural variant

148

1

S → P in AT3D; type-II; Nagasaki; defective heparin binding associated with thrombosis. Ref.30 Ref.44

VAR_007049

Natural variant

150

1

Q → P in AT3D; type-II; Vienna. Ref.30 Ref.51

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.47

VAR_007051

Natural variant

153

1

Missing in AT3D; type-I.

VAR_007052

Natural variant

158

1

L → P in AT3D; type-I. Ref.30

VAR_007053

Natural variant

160

1

C → Y in AT3D; type-I. Ref.30 Ref.46

VAR_027457

Natural variant

161

1

R → Q in AT3D; type-II; Geneva. Ref.30 Ref.39

VAR_007054

Natural variant

167

1

N → T

VAR_012750

Natural variant

178

1

L → H in AT3D; type-I. Ref.63

VAR_027458

Natural variant

179

1

F → L in AT3D; type-I. Ref.64

VAR_027459

Natural variant

190

1

Y → C Polymorphism in population of Scandinavian origin. Ref.30 Ref.47

VAR_007055

Natural variant

198

1

Y → C in AT3D; type-I and -II; Whitechapel. Ref.30

VAR_007056

Natural variant

198

1

Y → H in AT3D; type-I. Ref.30 Ref.56

VAR_027460

Natural variant

214

1

S → F in AT3D; type-I. Ref.58

VAR_027461

Natural variant

214

1

S → Y in AT3D; type-I.

VAR_007057

Natural variant

218

1

Missing in AT3D; type-I.

VAR_027462

Natural variant

219

1

N → D in AT3D; type-II; Rouen-6; increases affinity for heparin. Ref.30 Ref.50

VAR_007059

Natural variant

219

1

N → K in AT3D; type-II; Glasgow-3. Ref.30

VAR_007058

Natural variant

223

1

S → P in AT3D; type-I. Ref.58 Ref.60

VAR_027463

Natural variant

243

1

T → I in AT3D; type-I. Ref.58

VAR_027464

Natural variant

251

1

I → T in AT3D; type-I. Ref.58

VAR_027465

Natural variant

257

1

W → R in AT3D; type-I. Ref.30 Ref.56

VAR_027466

Natural variant

261

1

F → L in AT3D. Ref.62

VAR_027467

Natural variant

269

1

E → K in AT3D; type-II; Truro, increases affinity for heparin. Ref.30

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.30 Ref.47

VAR_007062

Natural variant

283

1

M → V in AT3D; type-II. Ref.58

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.30

VAR_007064

Natural variant

323

1

S → P in AT3D.

VAR_027469

Natural variant

334

1

E → K in AT3D; type-II. Ref.30

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.58

VAR_027470

Natural variant

398

1

D → H in AT3D; type-I. Ref.65

VAR_027471

Natural variant

412

1

S → R in AT3D; type-I. Ref.30 Ref.56

VAR_027472

Natural variant

414

1

A → T in AT3D; type-II; Hamilton/Glasgow-2; reduces interaction with thrombin by 90%. Ref.13 Ref.30 Ref.34 Ref.40

VAR_007069

Natural variant

416

1

A → P in AT3D; type-II; Charleville/Sudbury/Vicenza/Cambridge-1. dbSNP rs28930978. Ref.30

VAR_007070

Natural variant

416

1

A → S in AT3D; type-II; Cambridge-2. Ref.30 Ref.41

VAR_007071

Natural variant

419

1

A → V in AT3D; type-I. Ref.30

VAR_007072

Natural variant

424

1

G → D in AT3D; type-II; Stockholm. Ref.30 Ref.43

VAR_007073

Natural variant

425

1

R → C in AT3D; type-II; Northwick-Park/Milano-1/Frankfurt-1; deprived of inhibitory activity. Ref.30 Ref.35 Ref.63 Ref.64

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.30 Ref.35 Ref.36 Ref.53 Ref.63

VAR_007074

Natural variant

425

1

R → P in AT3D; type-II; Pescara; deprived of inhibitory of activity. Ref.30

VAR_007076

Natural variant

426

1

S → L in AT3D; type-II; Denver/Milano-2; deprived of inhibitory activity. Ref.30 Ref.33 Ref.64

VAR_007077

Natural variant

434

1

F → C in AT3D; type-II; Rosny. Ref.30

VAR_007078

Natural variant

434

1

F → L in AT3D; type-II; Maisons-Laffite. Ref.30

VAR_007080

Natural variant

434

1

F → S in AT3D; type-II; Torino. Ref.30

VAR_007079

Natural variant

436

1

A → T in AT3D; type-II; Oslo/Paris-3. Ref.30

VAR_007081

Natural variant

437

1

N → K in AT3D; type-II; La Rochelle. Ref.30

VAR_007082

Natural variant

438

1

R → G in AT3D; type-II. Ref.30

VAR_009258

Natural variant

438

1

R → M in AT3D; type-II; Kyoto. Ref.30 Ref.3

VAR_007083

Natural variant

439

1

P → L in AT3D; type-II; Utah; deprived of inhibitory activity. Ref.12 Ref.30

VAR_007084

Natural variant

439

1

P → T in AT3D; type-II; Budapest-5. Ref.30

VAR_007085

Natural variant

441

1

L → P in AT3D; type-II. Ref.63

VAR_027473

Natural variant

453

1

I → T in AT3D; type-I. Ref.30 Ref.49

VAR_007086

Natural variant

456

1

G → R in AT3D; type-I. Ref.30 Ref.48

VAR_007087

Natural variant

457

1

R → T in AT3D; type-II. Ref.30

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.30

VAR_007090

Natural variant

461

1

P → L in AT3D; type-II; Budapest. Ref.30

VAR_007091

Natural variant

462

1

C → F in AT3D; type-I. Ref.30 Ref.49

VAR_007092

Experimental info

Mutagenesis

414

1

A → K: Reduces interaction with thrombin by 99%. Ref.40

Mutagenesis

414

1

A → Q: Reduces interaction with thrombin by 80%. Ref.40

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...

Turn

39 – 41

3

Turn

44 – 46

3

Helix

78 – 100

23

Beta strand

108 – 110

3

Helix

112 – 123

12

Helix

128 – 137

10

Helix

140 – 142

3

Helix

145 – 149

5

Helix

151 – 162

12

Beta strand

168 – 181

14

Helix

188 – 198

11

Beta strand

203 – 205

3

Turn

207 – 209

3

Helix

211 – 225

15

Turn

226 – 228

3

Beta strand

245 – 259

15

Helix

263 – 265

3

Beta strand

267 – 271

5

Beta strand

274 – 276

3

Beta strand

279 – 294

16

Helix

296 – 298

3

Beta strand

300 – 306

7

Beta strand

309 – 317

9

Beta strand

320 – 322

3

Helix

324 – 330

7

Helix

333 – 342

10

Beta strand

344 – 353

10

Beta strand

355 – 358

4

Helix

363 – 368

6

Turn

369 – 371

3

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

440 – 446

7

Turn

447 – 449

3

Beta strand

452 – 459

8

Sequences

	Sequence		Length	Mass (Da)
	P01008-1 [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: 6298709] [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: 6572945] [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 AT-III DEFICIENCY 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: 8476848] [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: 14702039] [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: 16710414] [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: 6305982] [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: 3191114] [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: 7734359] [Abstract] Cited for: PROTEIN SEQUENCE OF 371-425, MASS SPECTROMETRY, VARIANT AT-III DEFICIENCY 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: 7238875] [Abstract] Cited for: ACTIVE 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: 6693405] [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: 15084671] [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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187, MASS SPECTROMETRY. Tissue: Plasma.
[18]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-187 AND ASN-224, MASS SPECTROMETRY. Tissue: Plasma.
[19]	"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: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224, MASS SPECTROMETRY. Tissue: Platelet.
[20]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187, MASS SPECTROMETRY. Tissue: Liver.
[21]	"An initial characterization of the serum phosphoproteome." Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A., Liotta L.A., Petricoin E.F. III J. Proteome Res. 8:5523-5531(2009) [PubMed: 19824718] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Serum.
[22]	"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: 8087553] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[23]	"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: 7656006] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[24]	"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: 9067613] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[25]	"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: 9761669] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[26]	"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: 2126464] [Abstract] Cited for: REVIEW.
[27]	"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: 8236149] [Abstract] Cited for: REVIEW ON VARIANTS.
[28]	"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: 7749926] [Abstract] Cited for: REVIEW ON VARIANTS.
[29]	"Molecular genetics of human antithrombin deficiency." Perry D.J., Carrell R.W. Hum. Mutat. 7:7-22(1996) [PubMed: 8664906] [Abstract] Cited for: REVIEW ON VARIANTS.
[30]	"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: 9031473] [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.
[31]	"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: 6582486] [Abstract] Cited for: VARIANT AT3D CYS-79.
[32]	"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: 3080419] [Abstract] Cited for: VARIANT AT3D LEU-73.
[33]	"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: 3805013] [Abstract] Cited for: VARIANT AT3D LEU-426.
[34]	"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: 3179438] [Abstract] Cited for: VARIANT AT3D THR-414.
[35]	"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: 3162733] [Abstract] Cited for: VARIANTS AT3D CYS-425 AND HIS-425.
[36]	"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: 2781509] [Abstract] Cited for: VARIANT AT3D HIS-425.
[37]	"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: 2365065] [Abstract] Cited for: VARIANT AT3D CYS-56.
[38]	"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: 1977621] [Abstract] Cited for: VARIANT GLU-30.
[39]	"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: 2229057] [Abstract] Cited for: VARIANT AT3D GLN-161.
[40]	"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: 2013320] [Abstract] Cited for: CHARACTERIZATION OF VARIANT AT3D THR-414, MUTAGENESIS OF ALA-414.
[41]	"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: 1906811] [Abstract] Cited for: VARIANT AT3D SER-416.
[42]	"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: 1555650] [Abstract] Cited for: VARIANT AT3D PHE-131.
[43]	"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: 1547341] [Abstract] Cited for: VARIANT AT3D ASP-424.
[44]	"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: 8443391] [Abstract] Cited for: VARIANT AT3D PRO-148.
[45]	"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: 8486379] [Abstract] Cited for: VARIANT AT3D 138-PHE-LYS-139 DEL.
[46]	"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: 7981186] [Abstract] Cited for: VARIANTS AT3D HIS-79 AND TYR-160.
[47]	"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: 7959685] [Abstract] Cited for: VARIANTS AT3D THR-112; TYR-152 AND ILE-283, VARIANT CYS-190.
[48]	"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: 8274732] [Abstract] Cited for: VARIANT AT3D ARG-456.
[49]	"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: 7994035] [Abstract] Cited for: VARIANTS AT3D SER-95; THR-453 AND PHE-462.
[50]	"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: 7989582] [Abstract] Cited for: VARIANT AT3D ASP-219.
[51]	"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.
[52]	"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: 7878627] [Abstract] Cited for: VARIANT AT3D 273-LYS--LYS-307 DEL.
[53]	"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: 7832187] [Abstract] Cited for: VARIANT AT3D HIS-425.
[54]	"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: 9157604] [Abstract] Cited for: VARIANT AT3D ARG-127.
[55]	"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: 9845533] [Abstract] Cited for: VARIANT AT3D PRO-23.
[56]	"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: 9759613] [Abstract] Cited for: VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412.
[57]	"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: 10361121] [Abstract] Cited for: VARIANT THR-167.
[58]	"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: 10997988] [Abstract] Cited for: VARIANTS AT3D PHE-214; PRO-223; ILE-243; THR-251; VAL-283 AND PRO-397.
[59]	"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: 11794707] [Abstract] Cited for: VARIANT AT3D 152-HIS--PHE-154 DEL.
[60]	"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: 11713457] [Abstract] Cited for: VARIANT AT3D PRO-223.
[61]	"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: 12353073] [Abstract] Cited for: VARIANT AT3D GLU-146.
[62]	"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: 12595305] [Abstract] Cited for: VARIANT AT3D LEU-261.
[63]	"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: 12894857] [Abstract] Cited for: VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441.
[64]	"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: 15164384] [Abstract] Cited for: VARIANTS AT3D LEU-179; CYS-425 AND LEU-426.
[65]	"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: 16908819] [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.

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P01008. 2 interactions.

STRING

P01008.

Protein family/group databases

MEROPS

I04.018.

2-D gel databases

SWISS-2DPAGE

P01008.

Cornea-2DPAGE

P01008.

DOSAC-COBS-2DPAGE

P01008.

REPRODUCTION-2DPAGE

P01008.

Proteomic databases

PRIDE

P01008.

Genome annotation databases

Ensembl

ENST00000367698; ENSP00000356671; ENSG00000117601; Homo sapiens. [Genome view]

GeneID

462.

KEGG

hsa:462.

UCSC

uc001gjt.1. human.

Organism-specific databases

CTD

462.

GeneCards

GC01M172139.

H-InvDB

HIX0001345.

HGNC

HGNC:775. SERPINC1.

HPA

CAB016790.
HPA001816.
HPA024007.

MIM

107300. gene+phenotype.
188050. phenotype.

Orphanet

82. Antithrombin deficiency, congenital.

PharmGKB

PA35026.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17846.

HOVERGEN

P01008.

InParanoid

P01008.

OMA

FRYRRVA.

OrthoDB

EOG9FJBVV.

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

IPR000215. Protease_inhib_I4_serpin.
IPR015555. Protease_inhib_serpin_AT-III.
[Graphical view]

PANTHER

PTHR11461. Prot_inh_serpin. 1 hit.
PTHR11461:SF53. Serpin_ATIII. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

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

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:	February 9, 2010
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.