Antithrombin mutation database

New	Nucleotide Position, Mutation	Codon, Amino Acid Change	Comments	Unique ID	A%	F%	Ref	CpG	S/M	Mut. type
New	2418A>C	Y-16S		1			(95)	N	S	MM
New	2436T>C	L-10P		2			(95)	N	S	MM
New	2455C>A	C-4X		3	50	50	(96)	N	S	NM
New	2463delGinsTC	-1	frameshift; stop codon 32	4	40	33	(1)	N	S	FD/FI
New	2487-8*insG	8	frameshift; stop codon 32	5			(2)	N	S	FI
New	2510-2512*delC	16	frameshift; stop codon 17	6		70	(2)	N	S	FD
New	2527C>A	C21X	Loses BspW I site	7			(95)	N	S	NM
New	2571-2580delCAGAA	36-37, or 38-39	frameshift; stop codon 70	8		57	(95)	N	S	FD
New	2599-600*delC	45 or 46	frameshift; stop codon 81	9	46	49	(3)	N	S	FD
	2601-2*delG	46	frameshift; stop codon 81	10		25/37	(4)	N	S	FD
	2606insT	48	frameshift; stop codon 72	11	45	40/43	(5)	N	S	FI
	2610-31del22bp insA	49-56	Creates Acc I site	12			(6)	N	S	ID/I
	2627-29delAAT	55	Deletes N;Double mutation, also R57C	13	60	56	(6)	N	S	ID
	2633C>T	R57C	Double mutation, also 55(-AAT)Loses Fau I site	14			(6)	Y	S	MM
	2638T>G	F58L	Type I or II? Budapest 6	15	45	55	(95)	N	S	MM
New	2652A>G	Y63C		16			(2)	N	S	MM
New	2652A>C	Y63S	Creates DdeI site	17	42	36	(1)	N	S	MM
New	2661T>C	L66P	Loses AlwN I, BstN I, EcoR I sites and gains BcN I, Nci I, Apa I and Msp I sites	18		55	(95)	N	S	MM
	2690-95delATTTTC	76-77	deletes I, F	19	49	49/51	(3)	N	S	ID
New	2702C>A	P80T		20	63	54	(7)	N	S	MM
	2705-6delCT	81	frameshift; stop codon 95	21	68	59	(6)	N	S	FD
	2706delT	81	frameshift; stop codon 89	22	53	47	(8)	N	S	FD
New	2765C>A	Q101K		23	50	50	(9)	N	S	MM
	2770insT	102	frameshift; stop codon 107	24	43	43/51	(4)	N	M (2)	FI
	2770insT	102	frameshift; stop codon 107	25	43	41/50	(4)
New	2777G>C		1st nt. intron 2loses Mnl I, Rsa I, Csp6 I sites and gains Alu I site	26	50	55	(95)	N	S	SS
New	5306G>C		last nt. intron 2Loses Sfe I site and gains Mae II, SnaB I and BsaA I sites	27			(95)	N	S	SS
	5311-5320*del6bp	106-108	deletes F and K	28	60	51	(10)	N	M (3)	ID
	5311-5320*del6bp	106-108	deletes F and K	29			(10)
	5311-5320*del6bp	106-108	deletes F and K	30	52	64	(11)
	5352delT	119	frameshift; stop codon 126	31	60	63	(12)	N	S	FD
New	5354C>T	H120Y		32	62	69	(7)	N	S	MM
	5356-64*delCTT	120-123	deletes a F	33	73	62	(6)	N	M (2)	ID
New	5356-64*delCTT	"	deletes a F	34	48	47	(11)
New	5373T>C	L126P		35	52	54	(9)	N	S	MM
New	5379G>A	C128Y	high MW complex	36	60	65	(13)	N	S	MM
	5381C>T	R129X		37, 38	<60	<60	(14)	Y	M (9)	NM
	5381C>T	"		39-42	<60	<60	(15)
	5381C>T	"		43			(96)
	5381C>T	"		44	50	50	(11)
New	5381C>T	"		45	49	50	(1)
New	5390C>T	R132X	removes Taq I site	46	50	50	(9)	Y	M (2)	NM
	5390 C>T	"		47	45	50	(96)
	5415T>A	L140X		48	50	68	(16)	N	S	NM
New	5448-50*delC	151-152	frameshift; stop codon 251	49	52	56	(17)	N	S	FD
New	5492T>C	Y166H	Creates Rsa I, Nla III sites	50	60	59	(97)	N	S	MM
Change	5493A>G	Y166C	Previously known as Whitechapel	51	55	50	(18)	N	M (3)	MM
	5493A>G	"		52	49	46	(6)
New	5493A>G	"		53	52	55	(95)
New	5501insA	169	frameshift; stop codon 192	54	42	40	(1)	N	S	FI
	5524G>A	176	exon 3A donor splice site, transcript from mutant allele lacks exon 3A	55	60	58	(19)	N	S	SS
New	6431A>G		5’ intron-exon splice site exon 3B. Alternative splice site creates stop codon 193	56	40	47	(98)	N	S	SS
New	6457-59delATC	186	deletes an Ile,loses PfIM I, BsiY I sites	57	50	56	(2)	N	S	ID
	6462C>A	N187K		58	121		(20)	N	S	MM
New	6484G>T	E195X	also GGC to GCC (G196A)	59		56/59	(2)	N	S	NM
	6490C>T	R197X		60	52	67	(16)	Y	M (2)	NM
New	6490C>T	"		61			(21)
	6523-24*insA	208	frameshift, stop codon 209	62	52	51/51	(5)	N	S	FI
New	7384T>C	W225R		63			(97)	N	S	MM
	7392-94*insA	228	frameshift, stop codon 232	64	<60	<60	(22)	N	S	FI
	7428-29delCT	239-240	frameshift, stop codon 242	65	43	49/30	(5)	N	S	FD
	7445delA	245	frameshift, stop codon 251	66	54	53	(23)	N	S	FD
	7443-46*delAG	244-245	frameshift, stop codon 264	67	54	53	(23)	N	S	FD
New	7520T>C	L270P	creates Dde I site	68	50	47	(9)	N	S	MM
New	7522G>T	Q271X	loses Tth111 II site	69			(99)	N	S	NM
	7580-83*delAG	290-291	frameshift, stop codon 309	70	<60	<60	(22)	N	S	FD
	7596delA or delG	295	frameshift, stop codon 314Valine sequence variation site	71	56	65	(6)	N	S	FD
	7634-39*del4bp	308-309	frameshift, stop codon 313	72	<60	<60	(22)	N	S	FD
	7644-49*delGGA	311-313	deletes a E	73	47	57	(6)	N	S	ID
	7756T>C	S349P		74	60	40	(24)	N	S	MM
New	7671delG	320	frameshift, stop codon 331	75	50	45	(1)	N	S	FD
New	7768-69delG	353	affects exon/intron 4 splice site and abolishes Bst NI site	76	46	46	(1)	N	S	SS
Change	9788G>A		creates cryptic splice site and high MW complex, pleiotropic effect?	77	<60	<60	(13)	Y	M (3)	SS
	9788G>A		creates cryptic splice site, removes Hpa II site	78	52	59	(6)
New	9788G>A		creates cryptic splice site	79	64	58	(17)
	9819C>T	R359X		80			(6)	Y	M (2)	NM
	9819 C>T	"		81	44	43	(97)
	9852-53*delA	370	frameshift, stop codon 375	82	50	61/69	(5)	N	S	FD
New	9858-60*delT	372	frameshift, stop codon 375	83	55	51	(2)	N	S	FD
New	9867G>T		first nt. intron 5	84	50		(2)	N	S	SS
New	13258T>G	S380R		85	51	43	(97)	N	S	MM
New	13277insACCG	387	frameshift, stop codon 433	86	52	50	(25)	N	S	FI
	13278C>T	A387V	loses BspW I and NspB II sites	87	60	50	(26)	N	S	MM
	13342insA	408	frameshift, stop codon 432	88	<60	<60	(14)	N	M (2)	FI
	13342insA	"	frameshift, stop codon 432	89			(13)
	13347-51*delT	410-411	frameshift, stop codon 412	90			(6)	N	S	FD
New	13354delAA	412	frameshift, stop codon 431	91	46	58	(25)	N	S	FD
	13354delAAGAG	412-414	frameshift, stop codon 430	92	43	30	(11)	N	S	FD
	13379insA	421	frameshift, stop codon 432	93	73		(6)	N	S	FI
New	13380T>C	I421T	abolishes Mbo II site	94	46	45	(1)	N	M (2)	MM
New	13380T>C	"	abolishes Mbo II site	95	68	68	(17)
New	13388G>C	G424R	gains Fsp I, Hha I and HinP I sites	96	51	48	(27)	N	S	MM
	13387-89*insG	423-424	frameshift, stop codon 432	97	75	52	(8)	N	S	FI
Change	13397-405del9bp	427-429	deletes A, N, P also R47H. Forms high MW complex, pleiotropic effect?	98			(13)	N	S	ID
	13398C>A	A427D	gains Acc I site	99	64	48	(11)	N	S	MM
New	13407G>A	C430F		100	60	55	(1)	N	S	MM
New	13412-4insA	432	frameshift, adds extra 18 residues to C terminus	101	50	50	(98)	N	S	FI

In this and other tables:

A%, antigen assay result as % of normal control

F%, functional assay result.

Two results indicate two types of assay were used.Nucleotide sequence numbering (28) makes no allowance for the highly polymorphic short tandem repeat region of intron 5 (29).

* Because of the repeat nature of the sequence the nucleotides affected cannot be unequivocally assigned.CpG mutation (CpG)- N no;Y yes.Single/multiple reports (S/M) - S single; M multiple, number of reports in brackets.Mutation type (Mut. type)- NM nonsense mutation; MM missense mutation; SS splice site mutation; FI frameshift insertion; FD frameshift deletion; ID inframe deletion; FD/FI deletion and insertion resulting in frameshift; ID/I deletion and insertion remaining in frame.

	Deletion	Unique Identifier	Ref
	Deletes 2761 bp, including exon 5, from 9060-9104 to 11822-11865*	102	(28)
	Deletes 5’-end; breakpoint 480bp upstream from 5’ boundary of exon 3a, 5’ to 5366	103	(30)
New	Deletes 105bp between 7432 and 7536, resulting in deletion of 35 amino acids, K241 to K275. Forms high molecular weigh complex, pleiotropic effect?	104	(13)
	Deletes 5’ end, exons 1,2	105	(31)
	Removes 3’ end of gene, including exon 6	106	(31)
	Removes 3’ end of gene, including exon 6	107	(31)
	Uncharacterised	108	(98)
	Whole gene deletion	109	(32)
	Whole gene deletion	110	(32)
	Whole gene deletion	111	(33,  34)
New	Whole gene deletion	112	(97)
New	Whole gene deletion	113	(97)

 *Precise deletion points ambiguous

	Nucleotide position, Mutation	Codon, Amino acid change	Variant; Unique Identifier	A%	F%	Comments additional data in brackets	Ref	CpG	M/S	Mut. Type
	2484T>A	I7N	Rouen III; 1			Additional carbohydrate	(57)	N	M (3)	MM
	2484T>A	"	2 unnamed families; 2, 3			Also V-3E	(98)
	2534C>T	R24C	Rouen IV; 4	105	56	loses BsiY I site	(58)	Y	S	MM
	2586C>T	P41L	Basel; 5	104	60	loses Bcn I, Nci I, Msp I and Hpa II sites and gains BstN I, EcoR II and Gsu I sites	(59)	Y	M (18)	MM
	2586C>T	"	Clichy I; 6	110	68	"	(41)
	2586C>T	"	Clichy 2; 7			"	(41)
	2586C>T	"	Franconville; 8			"	(41)
	2586C>T	"	2 unnamed families; 9, 10			"	(101)
	2586C>T	"	4 unnamed families; 11-13			"	(38)
	2586C>T	"	Dublin 2; 14			"	(60)
	2586C>T	"	unnamed; 15			"	(98)
	2586C>T	"	unnamed; 16			" (Also V-3E)	(98)
New	2586C>T	"	unnamed; 17	100	47	"	(61)
New	2586C>T	"	unnamed; 18	90	52	"	(98)
New	2586C>T	"	2 unnamed families; 19. 20	100	70-75	"	(96)
New	2586C>T	"	unnamed; 21	115	69	"	(97)
	2603C>T	R47C	Toyama; 22	100	26	(Homozygous) gains Age I site	(62)	Y	M (19)	MM
	2603C>T	"	Tours; 23			"	(63)
	2603C>T	"	Alger; 24			Homozygous "	(64)
	2603C>T	"	Paris 1; 25	127	54	"	(41)
	2603C>T	"	Paris 2; 26	100	60	"	(41)
	2603C>T	"	3 unnamed families; 27-29			"	(101)
	2603C>T	"	Padua 2; 30	100	60	"	(65)
	2603C>T	"	unnamed; 31			"	(38)
	2603C>T	"	Barcelona 2; 32	100	60	"	(66)
	2603C>T	"	Amiens; 33			"	(67)
	2603C>T	"	Kumamoto; 34	100	28	(Homozygous) "	(68)
	2603C>T	"	unnamed; 35			"	(98)
	2603C>T	"	2 unnamed families; 36, 37	90	60	"	(95)
New	2603C>T	"	Omura; 38	109	16	(Homozygous) "	(100)
New	2603C>T	"	Sasebo; 39	140	70	"	(100)
New	2603C>T	"	unnamed; 40	106	45	"	(97)
	2603C>A	R47S	Rouen II; 41	102	64	loses Cfr 10 I site	(69)	N	S	MM
	2604G>A	R47H	Rouen I; 42	111	55	gains Nsp I/NspC I, Nsp7524 I and Nla III sites	(70)	Y	M (15)	MM
	2604G>A	"	Padua I; 43	95	73	"	(71)
	2604G>A	"	Bligny; 44	100	60	"	(72)
	2604G>A	"	2 unnamed families; 45, 46			"	(38)
	2604G>A	"	3 unnamed families; 47-49			"	(101)
	2604G>A	"	unnamed; 50			"	(25)
	2604G>A	"	3 unnamed families; 51-53			"	(98)
	2604G>A	"	unnamed; 54	115	75	"	(95)
	2604G>A	"	Budapest 2; 55			"	(95)
New	2604G>A	"	unnamed; 56			"	(95)
	2759C>T	L99F	Budapest 3; 57	77		(Homozygous) loses Mnl I and Gsu I sites	(73)	N	M (5)	MM
	2759C>T	"	Budapest 7; 58	70	70	"	(95)
	2759C>T	"	unnamed; 59	54-75	19-54	(Homozygous) "	(95)
	2759C>T	"	unnamed; 60	71	55	"	(95)
New	2759C>T	"	unnamed; 61	55	56	"	(96)
New	2759C>G	L99V	Southport; 62	56	68	Variant detected by CIE loses Mnl I and Gsu I sites, gains Tth111 I site	(61)	N	S	MM
New	5342T>C	S116P	Nagasaki; 63	110	55		(74)	N	S	MM
New	5349A>C	Q118P	Vienna; 64	104	52	loses Bcl I and BstY I sites and gains Alw I site - last of little diagnostic value as another site only 5bp away	(61)	N	S	MM
	5382G>A	R129Q	Geneva; 65	100	50	loses Hinf I and Ple I sites	(75)	Y	M (4)	MM
	5382G>A	"	unnamed; 66			"	(101)
	5382G>A	"	unnamed; 67			"	(98)
	5382G>A	"	unnamed; 68	169	75	"	(95)
	7420G>A	E237K	Truro; 69			gains Mbo II and Xmn I	(102)	N	S	MM

Entries in bold and italics were the first report of this mutation

CpG - N no;Y yes.

Single/multiple reports (S/M) - S single; M multiple, number of reports in brackets.

Mut type Mutation type - MM missense mutation

	Nucleotide position, Mutation	Codon, Amino acid change	Variant; Unique Identifier	A%	F%	Comments	Ref	CpG	M/S	Mut. Type
	13323T>G	F402C	Rosny; 1	70	52		(76, 77)	N	S	MM
	13323T>C	F402S	Torino; 2	69	46	gains BsaJ I and Sty I sites	(76, 77)	N	S	MM
	13324C>A	F402L	Maisons Laffitte; 3	73	56	gains Dra I and Mse I sites	(77)	N	M (2)	MM
	13324C>A	"	unnamed; 4	73	62/41	"	(78)
	13328G>A	A404T	Oslo; 5	48	50	loses Hae III and Hae I sites - of little diagnostic value as another site only 5bp away	(77, 79)	N	M (3)	MM
	13328G>A	"	Paris 3; 6	72	48	"	(77)
	13328G>A	"	unnamed; 7	100	50/65	"	(11)
	13333C>G	N405K	La Rochelle; 8	73	55	(Also V-3E) gains Mnl I site	(77)	N	M (2)	MM
	13333C>G	"	1 family; 9		32/57	"	(98)
New	13334A>G	R406G	unnamed; 10	78	32	gains Sau 96 I site, loses Hae I and Stu I sites	(96)	N	S	MM
	13335G>T	R406M	Kyoto; 11			Described as type I deficiency loses Stu I site and gains Nsp I/NspC I and Nsp7524 sites	(80)	N	S	MM
	13337C>A	P407T	Budapest 5; 12	100	70	(Also Protein C deficiency) loses Stu I, Hae I and Hae III sites - last 2 of little diagnostic value as another site only 5bp away	(77)	N	M (2)	MM
New	13337C>A	"	unnamed; 13	86	72	"	(96)
	13338C>T	P407L	Utah; 14	50	50	loses Stu I, Hae I and Hae III sites - last 2 of little diagnostic value as another site only 5bp away	(81)	N	M (2)	MM
New	13338C>T	"	unnamed; 15			"	(95)
New	13392G>C	R425T	unnamed; 16	37	42/45	gains Bsp 1286 I site	(96)	N	M (2)	MM
New	13392G>C	"	unnamed; 17	50-56	50-59	"	(103)
	13404C>T	P429L	Budapest; 18	75	20	Homozygous, but 2 plasma forms	(82)	N	S	MM

Entries in bold and italics were the first report of this mutation

CpG mutation (CpG)- N no;Y yes.

Single/multiple reports (S/M) - S single; M multiple, number of reports in brackets.

Mutation type (Mut. type)- MM missense mutation

Nucleotide position, Mutation	Codon, Amino acid change	Variant; Unique Identifier	A%	F%	Comments additional data in brackets	Ref	CpG	S/M	Mut. type
	6460A>G	N187D	Rouen VI; 1	160	51/65	Increased heparin affinity Forms polymers	(35)	N	M (3)	MM
	6460A>G	"	unnamed; 2	98	55		(20)
	6460A>G	"	unnamed;3	77	62		(96)
New	7464G>A	M251I	unnamed;4	73	52		(7)	N	S	MM
	7562T>A	I284N	Haslar;5	69	64/82		(98)	N	S	MM
New	7615G>A	E302K	unnamed; 6	88	70	loses Mnl I site	(98)	N	S	MM
	13262G>A	A382T	Hamilton; 7	100	50	(Transformed into substrate) loses Bbv I site and Fnv4H I site	(36, 37)	Y	M (4)	MM
	13262G>A	"	unnamed; 8			"	(38)
	13262G>A	"	Glasgow II; 9	100	56	(Transformed into substrate)	(39)
	13262G>A	"	unnamed; 10	108	28/71	"	(98)
	13268G>C	A384P	Charleville; 11	100	60	(Transformed into substrate) loses Bbv I site, Fnv4H I site, BspW I site	(40, 41)	N	M (6)	MM
	13268G>C		Cambridge I; 12	95	54	"	(42)
	13268G>C	"	Vicenza; 13	105	62	(Transformed into substrate) "	(40)
	13268G>C	"	unnamed; 14			"	(38)
	13268G>C	"	Sudbury; 15	119	56	"	(43)
New	13268G>C	"	unnamed; 16	100	60	"	(95)
	13268G>T	A384S	Cambridge II; 17	103	75	loses Bbv I site, Fnv4H I site, BspW I site and Pvu II site	(44)	N	M (20)	MM
	13268G>T	"	unnamed; 18			"	(98)
	13268G>T	"	unnamed; 19	113	59	"	(98)
	13268G>T	"	unnamed; 20	108		"	(98)
	13268G>T	"	13 unnamed cases; 21-33	94	95/76	" (all but 3 asymptomatic)	(98)
	13268G>T	"	unnamed; 34	100	74	"	(95)
New	13268G>T	"	unnamed; 35	90	75	"	(96)
New	13268G>T	"	unnamed; 36	90	74	"	(98)
	13293G>A	G392D	Stockholm; 37			loses Eae I site,Gdi II site, Hae III site and BceF I site	(45)	Y	S	MM
	13295C>T	R393C	Northwick Park; 38	162	65	complex with albumin loses Eae I site,Gdi II site, Hae III site and BceF I site	(46, 47)	Y	M (3)	MM
	13295C>T	"	Milano I; 39			"	(48)
	13295C>T	"	Frankfurt I; 40	100	60	"	(49,50)
	13296G>A	R393H	Glasgow; 41	87	43	(Increased heparin affinity) loses Gdi II site and BceF I sites and gains Hae I and Msc I sites	(47)	Y	M (7)	MM
	13296G>A	"	Sheffield; 42	75	54	"	(51)
	13296G>A	"	Chicago; 43	96	37	(Increased heparin affinity) "	(52)
	13296G>A	"	Avranches; 44	100	59	"	(41)
	13296G>A	"	unnamed; 45			"	(98)
New	13296G>A	"	unnamed; 46	93	56	"	(96)
New	13296G>A	"	Kumamoto II; 47	92	61	(Increased heparin affinity) "	(100)
	13296G>C	R393P	Pescara; 48	100	62	Increased heparin affinity loses Eae I site, Gdi II site, BceF I site and gains Sau96 I site	(53, 54)	N	S	MM
	13299C>T	S394L	Denver,49	92	54	increased clearance ?	(55)	Y	M (7)	MM
	13299C>T	"	Milano 2; 50				(56)
	13299C>T	"	unnamed; 51	123	68		(11)
New	13299C>T	"	4 unnamed cases; 52-55	100	66-71		(7)

Entries in bold were the first report of this mutation.

CpG mutation (CpG)- N no;Y yes.

Single/multiple reports (S/M)) - S single; M multiple, number of reports in brackets.

Mutation type (Mut.Type) - MM missense mutation

Nucleotide Position, Sequence	Location	Detection	Comment	Ref
	(-276), 76bp dimorphism	5’ untranslated region	*	Slow 0.25, Fast 0.75	(83)
	(-159), T/C	"	DGGE	T 0.96, C 0.04 ***	(95)
	67G>A	"		Very low; found in deficient family and not in 78 normal alleles	(6)
	2457T/A	Exon 2; -3V/E	sequencing	4 families	(60)
		"	"	3 families, one also N405K	(95)
		"	"	4 families, 2 also I7N, one also P41L	(98)
		"	"	1 family	(96)
		"	"	1 family with type I deficiency	(11)
New	2523T/C	Exon 2; 20M/T	sequencing	Previously Whitechapel	(20)
New	5469A/G	Exon 3a; 158Y/C	sequencing	4 families, 3 of Danish origin	(7)
	7596G/A	Exon 4; 295V	sequencing	GTG 0.43**, GTA 0.57	(82)
	7626G/A	Exon 4; 305Q	Pst I	+ 0.5,-0.5	(33)
	7987T/C	Intron 4	Nhe I	+0.64,-0.36	(84)
	9820G/A	Exon 5; R/Q	sequencing	1 family	(102)
	8136-8153 (ATT)n	Intron 4; Alu 5 tail	sequencing	n = 6,8	(29)
	9289-9333 (ATT)n	Intron 4; Alu 8 tail	sequencing	Highly polymorphic n = 5-18	(95)
	9893C/G	Intron 5	Dde I	= +0.83,-0.17	(85)

* can be detected by visualisation of amplified DNA fragments spanning the polymorphism (8, 86)

** based upon sequencing 20 alleles

*** based on analyzing 156 alleles by denaturing gradient gel electrophoresis (DGGE)

+ presence of restriction enzyme cutting site, - absence of restriction enzyme cutting site

Distinct mutations	Total database entries
Missense mutation	60 (35)	171 (143)
Nonsense mutation	8 (0)	19 (0)
Inframe deletion	7 (0)	10 (0)
Frameshift deletion	20 (0)	20 (0)
Frameshift insertion	11 (0)	13 (0)
Splice site mutation	7 (0)	9 (0)
Major gene deletion	12 (0)	12 (0)
Frameshift deletion/Frameshift insertion	1 (0)	1 (0)
Inframe deletion/insertion	1 (0)	1 (0)
Totals	127 (35)	256 (143)

 "Distinct mutations" do not include those repeated mutations that may have arisen independently

 The entries are of total numbers in the database, while those in brackets refer to type II deficiency mutations.

	Distinct	Total
I
	Point mutations	80	101
	Partial/whole deletions	12	12
II
	RS	12	55
	HBS	12	70
	PE	11	18
Totals		127	256

RS : Reactive site mutations

HBS : Heparin binding site mutations

PE : Mutations with pleiotropic effects

RS : Reactive site mutations

HBS : Heparin binding site mutations

PE : Mutations with pleiotropic effects " Distinct mutations" do not include those repeated mutations which may have arisen independantly Type I includes point mutations, partial and whole gene deletions Numbers in brackets include total number of entries in the database for each category CpG mutations are those involving CG to TG or CA substitution mutations.

1. van Boven HH, Olds RJ, Thein SL, Reitsma PH, Lane DA, Briet E, Vandenbroucke JP, Rosendaal FR. Hereditary antithrombin deficiency: heterogeneity of the molecular basis and mortality in Dutch families. Blood 1994; 84: 4209-4213. 

2. Csurgay E, Ireland H, Thompson E, Conard J, Mannucci PM, Andrews V, Worsley A, Sas G, Lane DA. Novel mutations in seven families with type I antithrombin deficiency. Thrombosis and Haemostasis 1995; 73: 935. 

3. Daly M, Perry DJ, Bruce DB, Harper PL, Tait RC, Walker ID, Mayne EE, Daly HM, Brown K, Carrell RW. Type I antithrombin deficiency: 5 novel mutations associated with thrombosis. Blood Coagulation and Fibrinolysis 1996. 

4. Daly ME, Perry DJ, Harper PL, Carrell RW. The molecular basis of quantitative antithrombin deficiency in 8 unrelated families. British Journal of Haematology 1992; 80: 15. 

5. Daly M, Perry DJ, Harper PL, Daly HM, Roques AWW, Carrell RW. Insertions/deletions in the antithrombin gene: 3 mutations associated with non-expression. Thrombosis and Haemostasis 1992; 67: 521-525. 

6. Chowdhury V, Olds RJ, Lane DA, Conard J, Pabinger I, Ryan K, Bauer K, Bhavani M, Abildgaard U, Finazzi G, Castaman G, Mannucci PM, Thein SL. Identification of nine novel mutations in type I antithrombin deficiency by heteroduplex screening. British Journal of Haematology 1993; 84: 656-661. 

7. Millar DS, Wacey AI, Ribando J, Melissari E, Laursen B, Woods P, Kakkar VV, Cooper DN. Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis. Human Genetics 1995; 94: 509-512. 

8. Olds RJ, Lane DA, Ireland H, Leone G, De Stefano V, Wiesel ML, Cazenave JP, Thein SL. Novel point mutations leading to type I antithrombin deficiency and thrombosis. British Journal of Haematology 1991; 78: 408-413. 

9. Perry DJ. Ectopic transcript analysis in human antithrombin deficiency. Blood Coagulation and Fibrinolysis 1995; 6: 531-536. 

10. Olds RJ, Lane DA, Beresford CH, Abildgaard U, Hughes PM, Thein SL. A recurrent deletion in the antithrombin gene, AT106-108(-6bp), identified by DNA heteroduplex detection. Genomics 1993; 16: 298-299. 

11. Millar DS, Lopez A, White D, Abraham G, Laursen B, Holding S, Reverter JC, Reynand J, Martinowitz U, Hayes JPLA, Kakkar VV, Cooper DN. Screening for mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis by single strand conformation polymorphism analysis. Human Mutation 1993; 2: 324-326. 

12. Olds RJ, Lane DA, Finazzi G, Barbui T, Thein SL. A frameshift mutation leading to type 1 antithrombin deficiency and thrombosis. Blood 1990; 76: 2182-2186. 

13. Emmerich J, Vidaud D, Alhenc-Gelas M, Chadeuf G, Gouault-Heilmann M, Aillaud MF, Aiach M. Three novel mutations of antithrombin inducing high molecular mass compounds. Arteriosclerosis and Thrombosis 1994; 14: 1958-1965. 

14. Gandrille S, Vidaud D, Emmerich J, Clauser E, Sie P, Fiessinger JN, Alhenc-Gelas M, Priollet P, Aiach M. Molecular basis for hereditary antithrombin III quantitative deficiencies: a stop codon in exon IIIa and a frameshift in exon V1. British Journal of Haematology 1991; 78: 414-420. 

15. Olds RJ, Lane DA, Ireland H, Finazzi G, Barbui T, Abildgaard U, Girolami A, Thein SL. A common point mutation producing type Ia antithrombin III deficiency: AT129 CGA to TGA (Arg to Stop). Thrombosis Research 1991; 64: 621-625. 

16. Tomonori A, Iwahana H, Yoshimoto K, Shigekiyo T, Saito S, Itakura M. Two new nonsense mutations in type Ia antithrombin III deficiency at Leu140 and Arg197. Thrombosis and Haemostasis 1992; 68: 455-459. 

17. Jochmans K, Lissens W, Yin T, Michiels JJ, van der Luit L, Peerlinc- K, Vervoot R, De Wale M, Liebaers I. Molecular basis for type I antithrombin deficiency: identification of two novel mutations and evidence for a de novo splice mutation. Blood 1994; 84: 3742-3748. 

18. Perry DJ, Daly ME, Colvin BT, Brown K, Carrell RW. Two antithrombin mutations in a compound heterozygote: Met20Thr and Tyr166Cys. American Journal of Hematology 1995; 50: 215-216. 

19. Berg LP, Grundy CB, Thomas F, Millar DS, Green PJ, Slomski R, Reiss J, Kakkar VV, Cooper DN. De novo splice site mutation in the antithrombin III (AT3) gene causing recurrent venous thrombosis: demonstration of exon skipping by ectopic transcript analysis. Genomics 1992; 13: 1359-1361. 

20. Perry DJ, Marshall C, Borg JY, Tait RC, Daly ME, Walker ID, Carrell RW. Two new antithrombin variants, Asn 187 Lys, indicate a functional role for asparagine 187. Blood Coagulation and Fibrinolysis 1995; 6: 51-54. 

21. Michiels JJ, van der Luit L, van Vliet H, Jochmans K, Lissens W. Nonsense mutation in Arg 197 stop in a Dutch family with type I hereditary antithrombin deficiency causing thrombophilia. Thrombosis Research 1995; 78: 251-254. 

22. Vidaud D, Emmerich J, Sirieix ME, Sie P, Alhenc-Gelas M, Aiach M. Molecular basis for antithrombin III type I deficiency: 3 novel mutations located in exon IV. Blood 1991; 78: 2305-2309. 

23. Grundy CB, Thomas F, Millar DS, Krawczak M, Melissari E, Lindo V, Moffat E, Kakkar VV, Cooper DN. Recurrent deletion in the human antithrombin III gene. Blood 1991; 78: 1027-1032. 

24. Grundy CB, Holding S, Millar DS, Kakkar VV, Cooper DN. A novel missense mutation in the antithrombin III gene (Ser 349 to Pro) causing recurrent venous thrombosis. Human Genetics 1992; 88: 707-708.

25. Emmerich J, Chadeuf G, Alhenc-Gelas M, Gouault-Heilmann M, Toulon P, Fiessinger JN, Aiach M. Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6. Thrombosis and Haemostasis 1994; 72: 534-539. 

26. White D, Abraham G, Carter C, Kakkar VV, Cooper DN. A novel missense mutation in the antithrombin III gene (Ala 387 to Val) causing recurrent venous thrombosis. Human Genetics 1993; 90: 472-473. 

27. Jochmans K, Lissens W, Vervoot R, Peeters S, De Wale M, Liebaers I. Antithrombin-Gly 424 Arg: a novel point mutation responsible for type I antithrombin deficiency and neonatal thrombosis. Blood 1994; 83: 146-151. 

28. Olds RJ, Lane DA, Chowdury V, De Stefano V, Leone G, Thein SL. Complete nucleotide sequence of the antithrombin gene. Evidence for homologous recombination causing thrombophilia. Biochemistry 1993; 32: 4216-4224. 

29. Olds RJ, Lane DA, Chowdury V, Sas G, Pabinger I, Auberger K, Thein SL. (ATT) trinucleotide repeats in the antithrombin gene and their use in determining the origin of repeated mutations. Human Mutation 1994; 4: 31-41. 

30. Fernandez-Rachubinski RA, Rachubinski RA, Blajchman MA. Partial deletion of antithrombin III allele in a kindred with a type I deficiency. Blood 1992; 80: 1476-1485. 

31. Olds RJ, Lane DA, Chowdury V, Samson D, DeStafano V, Leone G, Wiesel ML, Cazenave JP, Conard J, Thein SL. Major rearrangements within the antithrombin gene locus: an unusual cause for antithrombin deficiency. British Journal of Haematology 1992; 40. 

32. Winter JH, Bennett B, Watt JL, Brown T, San Roman C, Schinzel A, King J, Cooke PJL. Confirmation of linkage between antithrombin III and Duffy blood group and assignment of AT3 to 1q22-25. Annals of Human Genetics 1982; 26: 29-34. 

33. Prochownik EV, Antonarakis S, Bauer KA, Rosenberg RD, Fearon ER, Orkin SH. Molecular heterogeneity of inherited antithrombin III deficiency. New England Journal of Medicine 1983; 308: 1549-1552. 

34. Bock SC, Prochownik EV. Molecular genetic survey of 16 kindreds with hereditary antithrombin III deficiency. Blood 1987; 70: 1273-1278. 

35. Bruce D, Perry DJ, Borg J-Y, Carrell RW, Wardell MR. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn to Asp). Journal of Clinical Investigation 1994; 94: 2265-2274. 

36. Devraj-Kizu- R, Chui DHK, Prochownik EV, Carter CJ, Ofosu FA, Blajchman MA. Antithrombin III Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood 1988; 72: 1518-1523. 

37. Austin RC, Rachubinski RA, Ofosu FA, Blajchman MA. Antithrombin-III-Hamilton, Ala 382 to Thr: an antithrombin -III variant that acts as a substrate but not an inhibitor of a-thrombin and Factor Xa. Blood 1991; 77: 2185-2189.  

38. Perry DJ, Carrell RW. CpG dinucleotides are "hotspots" for mutation in the antithrombin III gene. Twelve variants identified using the polymerase chain reaction. Molecular Biology in Medicine 1989; 6: 239-243. 

39. Ireland H, Lane DA, Thompson E, Walker ID, Blench I, Morris HR, Freyssinet JM, Grunebaun L, Olds R, Thein SL. Antithrombin Glasgow II: alanine to threonine mutation in the serpin P12 position, resulting in a substrate reaction with thrombin. British Journal of Haematology 1991; 79: 70-74. 

40. Caso R, Lane DA, Thompson EA, Olds RJ, Thein SL, Panico M, Blench I, Morris H, Freyssinet JM, Aiach M, Rodeghiero F, Finazzi G. Antithrombin Vicenza, Ala 384 to Pro (GCA to CCA) mutation transforming the inhibitor into a substrate. British Journal of Haematology 1991; 77: 87-92. 

41. Mohlo-Sabatier P, Aiach M, Gaillard I, Fiessinger JN, Fischer AM, Chadeuf G, Clauser E. Molecular characterization of antithrombin III (AT III) variants using polymerase chain reaction. Identification of the ATIII Charleville as an Ala384 Pro mutation. Journal of Clinical Investigation 1989; 84: 1236-1241. 

42. Perry DJ, Harper PL, Fairham S, Daly M, Carrell RW. Antithrombin Cambridge, 384 Ala to Pro: A new variant identified using the polymerase chain reaction. Federation of European Biochemical Societies Letters 1989; 254: 174-176. 

43. Penwarchuk WJ, Fernandez-Rachubinski F, Rachubinski RA, Blajchman MA. Antithrombin III Sudbury, an Ala 384 to Pro mutation with abnormal thrombin binding activity and thrombotic diathesis. Thrombosis Research. 1990; 59: 793-798. 

44. Perry DJ, Daly M, Harper PL, Tait RC, Price J, Walker ID, Carrell RW. Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpin. Federation of European Biochemical Societies Letters 1991; 285: 248-250. 

45. Blajchman MA, Fernandez-Rachubinsky F, Sheffield WP, Austin RC, Schulman S. Antithrombin III Stockholm: a codon 392 (Gly to Asp) mutation with normal heparin binding and impaired serine protease reactivity. Blood 1992; 79: 1428-1434. 

46. Erdjument H, Lane DA, Ireland H, Panico M, DiMarzo V, Blench I, Morris HR. Formation of a covalent disulfide-linked antithrombin complex by an antithrombin variant, antithrombin Northwick Park. Journal of Biological Chemistry 1987; 262: 13381-13384. 

47. Erdjument H, Lane DA, Panico M, diMarzo V, Morris HR. 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. Journal of Biological Chemistry 1988; 263: 5589-5593. 

48. Erdjument H, Lane DA, Ireland H, DiMarzo V, Panico M, Morris HR, Tripodi A, Mannucci PM. Antithrombin Milano, single amino acid substitution at the reactive site, Arg 393 to Cys. Thombosis and Haemostasis 1988; 60: 471-475. 

49. Ireland H, Lane DA, Thompson E, Olds R, Thein SL, Hach-Wunderle V, Scharrer I. Antithrombin Frankfurt I: arginine to cysteine substitution at the reactive site and formation of a variant antithrombin-albumin covalent complex. Thrombosis and Haemostasis 1991; 65: 913. 

50. van Boven HH, Reitsma PH, Rosendaal FR, Bayston TA, Chowdhury V, Bauer K, Scharrer I, Conard J, Lane DA. Factor V Leiden (FV R506Q) in families with inherited antithrombin deficiency. Thromb Haemost 1996; 75: 417-421. 

51. Lane DA, Erdjument H, Flynn A, DiMarzo V, Panico M, Morris H, Greaves M, Dolan G, Preston FE. Antithrombin Sheffield: amino acid substitution at the reactive site (Arg 393 to His) causing thrombosis. British Journal of Haematology 1989; 71: 91-96. 

52. Erdjument H, Lane DA, Panico M, DiMarzo V, Morris HR, Bauer K, Rosenberg RD. Antithrombin Chicago, amino acid substitution of arginine 393 to histidine. Thrombosis Research 1989; 54: 613-619. 

53. Lane DA, Erdjument H, Thompson E, Panico M, DiMarzo V, Morris HR, Leone G, De Stefano V, Thein SL. A novel amino acid substitution in the reactive site of a congenital variant antithrombin. Antithrombin Pescara, Arg 393 to Pro, caused by CGT to CCT mutation. Journal of Biological Chemistry 1989; 264: 10200-10204. 

54. Owen MC, George PM, Lane DA, Boswell DR. P1 variant antithrombins Glasgow (393 Arg to His) and Pescara (393 Arg to Pro) have increased heparin affinity and are resistant to catalytic cleavage by elastase. Implications for the heparin activation mechanism. Federation of European Biochemical Societies Letters 1991; 280: 216-220. 

55. Stephens AW, Thalley BS, Hirs CHW. Antithrombin Denver, a reactive site variant. Journal of Biological Chemistry 1987; 262: 1044-1048. 

56. Olds RJ, Lane D, Caso R, Tripodi A, Mannucci PM, Thein SL. Antithrombin III Milano 2: a single base substitution in the thrombin binding domain detected with PCR and direct genomic sequencing. Nucleic Acids Research 1989; 17: 10511. 

57. Brennan SO, Borg JY, George PM, Soria C, Soria J, Caen J, Carrell RW. New carbohydrate site in mutant antithrombin (7Ile-Asn) with decreased heparin affinity. Federation of European Biochemical Societies Letters 1988; 237: 118-122. 

58. Borg JY, Brennan SO, Carrell RW, George P, Perry DJ, Shaw J. Antithrombin Rouen IV 24 Arg to Cys. The amino terminal contribution to heparin binding. Federation of European Biochemical Societies Letters 1990; 266: 163-166. 

59. Chang JY, Tran TH. Antithrombin Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. Journal of Biological Chemistry 1986; 261: 1174-1176. 

60. Daly M, Bruce D, Perry DJ, Price J, Harper PL, O'Meara A, Carrell RW. Antithrombin Dublin (-3 Val to Glu): an N-terminal variant which has an aberrant signal peptide cleavage site. Federation of European Biochemical Societies Letters 1990; 273: 87-90. 

61. Chowdhury V, Mille B, Olds RJ, Lane DA, Watton J, Barrowcliffe TW, Pabinger I, Woodcock BE, Thein SL. Antithrombins Southport (99 Leu to Val) and Vienna (118 Gln to Pro): two novel antithrombin variants with abnormal heparin binding. British Journal of Haematology 1995; 89: 602-609. 

62. Koide T, Odani S, Takahashi K, Ono T, Sakuragawa N. Antithrombin III Toyama; replacement of Arginine 47 by Cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proceedings of the National Academy of Science USA 1984; 81: 289-293. 

63. Duchange N, Chasse JF, Cohen GN, Zakin MM. Identification of a mutation leading to cysteine replacement in a silent deficiency. Nucleic Acids Research 1986; 14: 2408. 

64. Brunel F, Duchange N, Fischer AM, Cohen GN, Zakin MM. Antithrombin III Alger: a new case of Arg 47 - Cys mutation. American Journal of Haematology 1987; 25: 223-224. 

65. Olds RJ, Lane DA, Caso R, Girolami A, Thein SL. Antithrombin III Padua II: a single base substitution in exon 2 detected using PCR and direct genomic sequencing. Nucleic Acids Research 1990; 18: 1926. 

66. Owen MC, Shaw GJ, Grau E, Fontcuberta J, Carrell RW, Boswell DR. Molecular characterisation of antithrombin Barcelona 2: 47 arginine to cysteine. Thrombosis Research 1989; 55: 451-457. 

67. Fernandez-Rachubinski F, Rachubinski R, Blajchman MA. Genetic characterisation of kindreds with antithrombin III (AT-III) deficiency using selected amplification of the gene. Blood 1990; 76: 506a. 

68. Ueyama H, Murakami T, Nishiguchi S, Maeda S, Hashimoto Y, Okajima K, Shimada K, Araki S. Antithrombin Kumamoto. Identification of a point mutation and genotype analysis of the family. Thrombosis and Haemostasis 1990; 63: 231-234. 

69. Borg JY, Owen MC, Soria C, Soria J, Caen J, Carrell RW. Arginine 47 is a prime heparin binding site in antithrombin. A new variant Rouen II, 47 Arg to Ser. Journal of Clinical Investigation 1988; 81: 1292-1296. 

70. Owen MC, Borg JY, Soria C, Soria J, Caen J, Carrell RW. Heparin binding defect in new antithrombin III variant: Rouen, 47 Arg to His. Blood 1987; 69: 1275-1279. 

71. Caso R, Lane DA, Thompson E, Zangouras D, Panico M, Morris H, Olds RJ, Thein SL, Girolami A. Antithrombin Padua I: impaired heparin binding caused by an Arg 47 to His (CGT to CAT) substitution. Thrombosis Research 1990; 58: 185-190. 

72. Wolf M, Boyer-Neumann C, Mohlo-Sabatier P, Neumann C, Meyer D, Larrieu MJ. Familial variant of antithrombin III (AT III Bligny, 47 Arg to His) associated with protein C deficiency. Thrombosis and Haemostasis 1990; 63: 215-219. 

73. Olds RJ, Lane DA, Boisclair M, Sas G, Bock SC, Thein SL. Antithrombin Budapest 3: an antithrombin variant with reduced heparin affinity resulting from the substitution L99F. Federation of European Societies Letters 1992; 300: 241-246. 

74. Okajima K, Abe H, Maeda S, Motomura M, Tsujihata M, Nagataki S, Okabe H, Takatsuki K. Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis. Blood 1993; 81: 1300-1305. 

75. Gandrille S, Aiach M, Lane DA, Vidaud D, Mohlo-Sabatier P, Caso R, de Moerloose P, Fiessinger JN, Clauser E. Important role of Arg 129 in heparin binding site of antithrombin III: identification of novel mutation Arg 129 to Gln. Journal of Biological Chemistry 1990; 265: 18997-19001. 

76. Olds RJ, Thein SL, Ireland H, Lane DA, Boisclair M, Conard J, Horellou MH. Identification of 402 phenylalanine as a functionally important residue in antithrombin. Thrombosis and Haemostasis 1991; 65: 670. 

77. Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, Abildgaard U, Ireland H, Thompson E, Sas G, Horellou MH, Tamponi G, Thein SL. Pleiotropic effects of antithrombin strand 1C substitution mutations. Journal of Clinical Investigation 1992; 90: 2422-2433. 

78. Emmerich J, Chadeuf G, Coetzee MJ, Alhenc-Gelas M, Friessinger J-N, Aiach M. A phenylalanine 402 to leucine mutation is responsible for a stable inactive conformation of antithrombin. Thrombosis Research 1994; 76: 307-315. 

79. Bock SC, Silberman JA, Wikoff W, Abildgaard U, Hultin MB. Identification of a threonine for alanine substitution at residue 404 of antithrombin III Oslo suggests integrity of the 404-407 region is important for maintaining normal inhibitor levels. Thrombosis and Haemostasis 1989; 62: 494. 

80. Nakagawa M, Tanaka S, Tsuji H, Takada O, Ono T. Congenital antithrombin deficiency (ATIII Kyoto): identification of a point mutation altering arginine-406 to methionine behind the reactive site. Thrombosis Research 1991; 64: 101-108. 

81. Bock SC, Marrinan JA, Radziejewska E. Antithrombin III Utah: proline 407 to leucine mutation in a highly conserved region near the inhibitor reactive site. Biochemistry 1988; 27: 6171-6178. 

82. Olds RJ, Lane DA, Caso R, Panico M, Morris HR, Sas G, Dawes J, Thein SL. Antithrombin III Budapest: a single amino acid substitution (429Pro to Leu) in a region highly conserved in the serpin super family. Blood 1992; 79: 1206-1212. 

83. Bock SC, Levitan DJ. Characterisation of an unusual length polymorphism 5' to the antithrombin III gene. Nucleic Acids Research 1983; 11: 8569-8582. 

84. Bock SC, Radziejewska E. A Nhe 1 RFLP in the human antithrombin III gene (1q23-25) (AT3). Nucleic Acids Research 1991; 19: 2519. 

85. Daly ME, Perry DJ. Dde I polymorphism in intron 5 in the antithrombin III gene. Nucleic Acid Research 1990; 18: 5583. 

86. Wu S, Seino S, Bell GI. Human antithrombin III (AT3) gene length polymorphism revealed by the polymerase chain reaction. Nucleic Acids Research 1989; 17: 6433. 

87. Whisstock J, Skinner R, Lesk AM. An atlas of serpin conformations. TIBS 1998; 63-67 

88. Desai UR, Petitou M, Bjork I, Olson ST. Mechanism of heparin activation of antithrombin. Journal of Biological Chemistry 1998; 273: 7478-7487. 

89. Huntington JA, Gettins PGW. Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin. Biochemistry 1998; 37: 3272-3277. 

90. Jin L, Abrahams JP, Skinner R, Petitou M, Pike RN, Carrell RW. The anticoagulant activation of antithrombin by heparin. Proceedings of the National Academy of Sciences USA 1997; 94: 14683-14688. 

91. Lane DA, Ireland H, Olds RJ, Thein SL, Perry DJ, Aiach M. Antithrombin III: a database of mutations.Thrombosis and Haemostasis 1991; 66: 657-661. 

92. Lane DA, Olds RJ, Boisclair M, Chowdhury V, Thein SL, Cooper DN, Blajchman M, Perry D, Emmerich J, Aiach M. 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. Thrombosis and Haemostasis 1993; 70: 361-369. 

93. Lane DA, Bayston T, Olds RJ, Fitches AC, Cooper DN, Millar DS, Jochmans K, Perry DJ, Okajima K, Thein SL, Emmerich, J. Antithrombin mutation database: 2nd (1997) update. Thrombosis and Haemostasis 1997; 77: 197-211. 

94. Antonarakis SE, Nomenclature working group. Recommendations for a nomenclature system for human gene mutations. Human Mutation 1998; 11: 1-3.

95. Olds et al, Unpublished 

96. Emmerich et al, Unpublished 

97. Jochmans et al, Unpublished 

98. Perry et al, Unpublished 

99. Blajchman et al Unpublished 

100. Okajima et al, Unpublished 

101. Aiach et al, Unpublished 

102. Daly et al, Unpublished 

103. Keeling et al Unpublished

• Compiled by members of the Plasma Coagulation Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis.

• The final version of the database was put together by Trevor Bayston and David Lane (Centre for Haematology, Imperial College London).

• Image credit - Animated antithrombin molecule: this image is derived from the co-ordinates of Professor Robin Carrell and his group at the University of Cambridge (UK).