Q9BQB6 (VKOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vitamin K epoxide reductase complex subunit 1
EC=1.1.4.1

Alternative name(s):
Vitamin K1 2,3-epoxide reductase subunit 1

Gene names

Name:	VKORC1
Synonyms:	VKOR
ORF Names:	MSTP134, MSTP576, UNQ308/PRO351

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	163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Ref.1 Ref.2
Catalytic activity	2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Expressed at highest levels in fetal and adult liver, followed by fetal heart, kidney, and lung, adult heart, and pancreas. Ref.1
Involvement in disease	Combined deficiency of vitamin K-dependent clotting factors 2 (VKCFD2) [MIM:607473]: VKCFD leads to a bleeding tendency that is usually reversed by oral administration of vitamin K. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Coumarin resistance (CMRES) [MIM:122700]: A condition characterized by partial or complete resistance to warfarin or other 4-hydroxycoumarin derivatives. These drugs are used as anti-coagulants for the prevention of thromboembolic diseases in subjects with deep vein thrombosis, atrial fibrillation, or mechanical heart valve replacement. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.13
Miscellaneous	The location of two cysteine active-site residues within a proposed transmembrane is consistent both with the known hydrophobic environment of the thiol redox site of the enzyme and with the lipophilicity of vitamin K and warfarin.
Sequence similarities	Belongs to the VKOR family.
Sequence caution	The sequence AAQ88821.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Redox-active center Transmembrane Transmembrane helix
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	drug metabolic process Inferred from mutant phenotype PubMed 21127708. Source: UniProtKB peptidyl-glutamic acid carboxylation Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	vitamin-K-epoxide reductase (warfarin-sensitive) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BQB6-1)

Also known as: MST576;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BQB6-2)

Also known as: MST134;

The sequence of this isoform differs from the canonical sequence as follows:
     95-163: GCLRTRWASV...QEPQGKAKRH → DGVSPCCPGW...PGLDPVLRAL

Isoform 3 (identifier: Q9BQB6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     59-163: WGRGFGLVEH...QEPQGKAKRH → LPADTLGLCPDAAELPGVSRWFCLPGLDPVLRAL

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 163	163	Vitamin K epoxide reductase complex subunit 1		PRO_0000191668
Regions
	Topological domain	1 – 8	8	Lumenal Potential
	Transmembrane	9 – 29	21	Helical; Potential
	Topological domain	30 – 100	71	Cytoplasmic Potential
	Transmembrane	101 – 123	23	Helical; Potential
	Topological domain	124 – 126	3	Lumenal Potential
	Transmembrane	127 – 149	23	Helical; Potential
	Topological domain	150 – 163	14	Cytoplasmic Potential
Amino acid modifications
	Disulfide bond	132 ↔ 135		Redox-active Potential
Natural variations
	Alternative sequence	59 – 163	105	WGRGF…KAKRH → LPADTLGLCPDAAELPGVSR WFCLPGLDPVLRAL in isoform 3.		VSP_043407
	Alternative sequence	95 – 163	69	GCLRT…KAKRH → DGVSPCCPGWSQAICLPQPP KVLGGLQALPADTLGLCPDA AELPGVSRWFCLPGLDPVLR AL in isoform 2.		VSP_013363
	Natural variant	26	1	A → T in CMRES. Ref.13		VAR_065785
	Natural variant	29	1	V → L in CMRES. Ref.1 Ref.13 Corresponds to variant rs104894539 [ dbSNP | Ensembl ].		VAR_021821
	Natural variant	36	1	D → G in CMRES. Ref.13		VAR_065786
	Natural variant	36	1	D → Y in CMRES. Ref.13		VAR_065787
	Natural variant	45	1	V → A in CMRES. Ref.1 Corresponds to variant rs104894540 [ dbSNP | Ensembl ].		VAR_021822
	Natural variant	52	1	S → W in CMRES. Ref.13		VAR_065788
	Natural variant	56	1	S → F in CMRES. Ref.13		VAR_065789
	Natural variant	58	1	R → G in CMRES. Ref.1 Corresponds to variant rs104894541 [ dbSNP | Ensembl ].		VAR_021823
	Natural variant	59	1	W → C in CMRES. Ref.13		VAR_065790
	Natural variant	59	1	W → L in CMRES. Ref.13		VAR_065791
	Natural variant	66	1	V → G in CMRES. Ref.13		VAR_065792
	Natural variant	66	1	V → M in CMRES. Ref.13 Corresponds to variant rs72547529 [ dbSNP | Ensembl ].		VAR_065793
	Natural variant	71	1	G → A in CMRES. Ref.13		VAR_065794
	Natural variant	77	1	N → S in CMRES. Ref.13		VAR_065795
	Natural variant	77	1	N → Y in CMRES. Ref.13		VAR_065796
	Natural variant	98	1	R → W in VKCFD2. Ref.1		VAR_021824
	Natural variant	123	1	I → N in CMRES. Ref.13		VAR_065797
	Natural variant	128	1	L → R in CMRES. Ref.1 Corresponds to variant rs104894542 [ dbSNP | Ensembl ].		VAR_021825
	Natural variant	139	1	Y → H in CMRES. Ref.13		VAR_065798

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MST576) [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2F00526A6C561D5A	FASTA	163	18,235
	10 20 30 40 50 60 MGSTWGSPGW VRLALCLTGL VLSLYALHVK AARARDRDYR ALCDVGTAIS CSRVFSSRWG 70 80 90 100 110 120 RGFGLVEHVL GQDSILNQSN SIFGCIFYTL QLLLGCLRTR WASVLMLLSS LVSLAGSVYL 130 140 150 160 AWILFFVLYD FCIVCITTYA INVSLMWLSF RKVQEPQGKA KRH
	Isoform 2 (MST134) [UniParc]. Checksum: FBB87922208F471C	FASTA	156	16,701
	10 20 30 40 50 60 MGSTWGSPGW VRLALCLTGL VLSLYALHVK AARARDRDYR ALCDVGTAIS CSRVFSSRWG 70 80 90 100 110 120 RGFGLVEHVL GQDSILNQSN SIFGCIFYTL QLLLDGVSPC CPGWSQAICL PQPPKVLGGL 130 140 150 QALPADTLGL CPDAAELPGV SRWFCLPGLD PVLRAL
	Isoform 3 [UniParc]. Checksum: CB4ADA0C5ED486BD	FASTA	92	9,875
	10 20 30 40 50 60 MGSTWGSPGW VRLALCLTGL VLSLYALHVK AARARDRDYR ALCDVGTAIS CSRVFSSRLP 70 80 90 ADTLGLCPDA AELPGVSRWF CLPGLDPVLR AL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2." Rost S., Fregin A., Ivaskevicius V., Conzelmann E., Hoertnagel K., Pelz H.-J., Lappegard K., Seifried E., Scharrer I., Tuddenham E.G.D., Mueller C.R., Strom T.M., Oldenburg J. Nature 427:537-541(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS CMRES LEU-29; ALA-45; GLY-58 AND ARG-128, VARIANT VKCFD2 TRP-98. Tissue: Kidney.
[2]	"Identification of the gene for vitamin K epoxide reductase." Li T., Chang C.-Y., Jin D.-Y., Lin P.-J., Khvorova A., Stafford D.W. Nature 427:541-544(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[3]	Liu B., Qin B.M., Sheng H., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q., Song L., Lu H., Xu H.S., Zheng W.Y., Gong J., Wang Y.B., Liu Y.Q., Zhang C.N., Shi Y., Wang W., Zhang Z. , Yang X., Han Y., Chen J.Z., Liu B.H., Hui R.T. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Aorta.
[4]	SeattleSNPs variation discovery resource Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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] (ISOFORMS 1 AND 3). Tissue: Brain.
[6]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[9]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-163 (ISOFORM 1).
[10]	"Vitamin K epoxide reductase: homology, active site and catalytic mechanism." Goodstadt L., Ponting C.P. Trends Biochem. Sci. 29:289-292(2004) [PubMed] [Europe PMC] [Abstract] Cited for: POTENTIAL REDOX-ACTIVE SITE.
[11]	"Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation." Tie J.-K., Nicchitta C., von Heijne G., Stafford D.W. J. Biol. Chem. 280:16410-16416(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[12]	"Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin." Rost S., Fregin A., Hunerberg M., Bevans C.G., Muller C.R., Oldenburg J. Thromb. Haemost. 94:780-786(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS, POTENTIAL REDOX-ACTIVE SITE.
[13]	"Thirteen novel VKORC1 mutations associated with oral anticoagulant resistance: insights into improved patient diagnosis and treatment." Watzka M., Geisen C., Bevans C.G., Sittinger K., Spohn G., Rost S., Seifried E., Muller C.R., Oldenburg J. J. Thromb. Haemost. 9:109-118(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMRES THR-26; LEU-29; GLY-36; TYR-36; TRP-52; PHE-56; LEU-59; CYS-59; GLY-66; MET-66; ALA-71; SER-77; TYR-77; ASN-123 AND HIS-139.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY423044 mRNA. Translation: AAR82914.1. AY521634 mRNA. Translation: AAS01052.1. AF176924 mRNA. Translation: AAQ13668.1. AY466113 mRNA. Translation: AAR28759.1. AY587020 Genomic DNA. Translation: AAS83106.1. AK289790 mRNA. Translation: BAF82479.1. AK312005 mRNA. Translation: BAG34943.1. AC135050 Genomic DNA. No translation available. CH471192 Genomic DNA. Translation: EAW52167.1. CH471192 Genomic DNA. Translation: EAW52168.1. BC002911 mRNA. Translation: AAH02911.1. AY358456 mRNA. Translation: AAQ88821.1. Different initiation.
IPI	IPI00031000. IPI00384902. IPI00410112.
RefSeq	NP_076869.1. NM_024006.4. NP_996560.1. NM_206824.1.
UniGene	Hs.324844.
3D structure databases
ProteinModelPortal	Q9BQB6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BQB6. 1 interaction.
STRING	9606.ENSP00000378426.
PTM databases
PhosphoSite	Q9BQB6.
Polymorphism databases
DMDM	62511226.
Proteomic databases
PaxDb	Q9BQB6.
PRIDE	Q9BQB6.
Protocols and materials databases
DNASU	79001.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000319788; ENSP00000326135; ENSG00000167397. ENST00000354895; ENSP00000346969; ENSG00000167397. ENST00000394975; ENSP00000378426; ENSG00000167397.
GeneID	79001.
KEGG	hsa:79001.
UCSC	uc002eas.3. human. uc002eau.3. human.
Organism-specific databases
CTD	79001.
GeneCards	GC16M031105.
H-InvDB	HIX0079837.
HGNC	HGNC:23663. VKORC1.
HPA	HPA042720.
MIM	122700. phenotype. 607473. phenotype. 608547. gene.
neXtProt	NX_Q9BQB6.
Orphanet	240843. Acenocoumarol toxicity. 240873. Fluindione toxicity. 98434. Hereditary combined deficiency of vitamin K-dependent clotting factors. 240897. Phenprocoumon toxicity. 240929. Resistance to acenocoumarol in venous thrombosis and atrial fibrillation. 240937. Resistance to fluindione in venous thrombosis and atrial fibrillation. 240943. Resistance to phenprocoumon in venous thrombosis and atrial fibrillation. 240953. Resistance to warfarine in venous thrombosis and atrial fibrillation. 240991. Susceptibility to bleeding due to acenocoumarol treatment. 240993. Susceptibility to bleeding due to fluindione treatment. 240995. Susceptibility to bleeding due to phenprocoumon treatment. 240997. Susceptibility to bleeding due to warfarine treatment. 241045. Warfarine dose selection in the treatment of venous thrombosis and atrial fibrillation. 240923. Warfarine toxicity.
PharmGKB	PA133787052.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG46570.
HOGENOM	HOG000230752.
HOVERGEN	HBG076672.
InParanoid	Q9BQB6.
KO	K05357.
OMA	INVGLTV.
OrthoDB	EOG4ZGPDK.
Enzyme and pathway databases
BRENDA	1.1.4.1. 2681.
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9BQB6.
Bgee	Q9BQB6.
CleanEx	HS_VKORC1.
Genevestigator	Q9BQB6.
GermOnline	ENSG00000167397. Homo sapiens.
Family and domain databases
InterPro	IPR012932. VKOR. [Graphical view]
Pfam	PF07884. VKOR. 1 hit. [Graphical view]
SMART	SM00756. VKc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1930.
DrugBank	DB01418. Acenocoumarol. DB00266. Dicumarol. DB00170. Menadione. DB00498. Phenindione. DB00946. Phenprocoumon. DB00682. Warfarin.
GenomeRNAi	79001.
NextBio	67615.
SOURCE	Search...

Entry information

Entry name

VKOR1_HUMAN

Accession

Primary (citable) accession number: Q9BQB6
Secondary accession number(s): A6NIQ6 , B2R4Z6, Q6UX90, Q7Z2R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 96 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.