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Q9BQB6 (VKOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development. Ref.1 Ref.2 Ref.11 Ref.13 Ref.15 Ref.16

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. Ref.11 Ref.13 Ref.15 Ref.16

Enzyme regulation

Inhibited by warfarin. Ref.11 Ref.13 Ref.16

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.12 Ref.13 Ref.15 Ref.16.

Tissue specificity

Expressed at highest levels in fetal and adult liver, followed by fetal heart, kidney, and lung, adult heart, and pancreas. Ref.1

Domain

The number of transmembrane domains and the membrane topology are controversial; supporting evidence is available both for models with three transmembrane domains (Ref.12 and Ref.16) and four transmembrane domains (Ref.14 and Ref.15). According to Ref.12 and Ref.16 the N-terminus of the protein is in the endoplasmic reticulum lumen, while the C-terminus is in the cytosol, which is in favor of three transmembrane domains. According to Ref.14, both N-terminus and C-terminus are in the cytosol, indicating the presence of four transmembrane domains. Besides, the 3D-structure of a bacterial ortholog shows four transmembrane domains. Moreover, proteins that reside in the endoplasmic reticulum lumen can catalyze the reduction of the active site cysteines, possibly via Cys-43 and Cys-51 (Ref.14 and Ref.15), but less efficiently than the synthetic compound dithiothreitol (in vitro). Location of Cys-43 and Cys-51 in the endoplasmic reticulum lumen would be in agreement with four transmembrane domains. Again, these data are controversial, and papers do not agree on the effects of mutating Cys-43 and Cys-51, probably because of differences in the assay systems.

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 Ref.13

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.18

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 163163Vitamin K epoxide reductase complex subunit 1
PRO_0000191668

Regions

Topological domain1 – 88Lumenal Potential
Transmembrane9 – 2921Helical; Probable
Topological domain30 – 7445Cytoplasmic Potential
Transmembrane75 – 9521Helical; Potential
Transmembrane101 – 12323Helical; Probable
Topological domain124 – 1263Lumenal Probable
Transmembrane127 – 14923Helical; Probable
Topological domain150 – 16314Cytoplasmic Probable

Amino acid modifications

Disulfide bond132 ↔ 135Redox-active

Natural variations

Alternative sequence59 – 163105WGRGF…KAKRH → LPADTLGLCPDAAELPGVSR WFCLPGLDPVLRAL in isoform 3.
VSP_043407
Alternative sequence95 – 16369GCLRT…KAKRH → DGVSPCCPGWSQAICLPQPP KVLGGLQALPADTLGLCPDA AELPGVSRWFCLPGLDPVLR AL in isoform 2.
VSP_013363
Natural variant261A → T in CMRES. Ref.18
VAR_065785
Natural variant291V → L in CMRES. Ref.1 Ref.18
Corresponds to variant rs104894539 [ dbSNP | Ensembl ].
VAR_021821
Natural variant361D → G in CMRES. Ref.18
VAR_065786
Natural variant361D → Y in CMRES. Ref.18
VAR_065787
Natural variant451V → A in CMRES. Ref.1
Corresponds to variant rs104894540 [ dbSNP | Ensembl ].
VAR_021822
Natural variant521S → W in CMRES. Ref.18
VAR_065788
Natural variant561S → F in CMRES. Ref.18
VAR_065789
Natural variant581R → G in CMRES. Ref.1
Corresponds to variant rs104894541 [ dbSNP | Ensembl ].
VAR_021823
Natural variant591W → C in CMRES. Ref.18
VAR_065790
Natural variant591W → L in CMRES. Ref.18
VAR_065791
Natural variant661V → G in CMRES. Ref.18
VAR_065792
Natural variant661V → M in CMRES. Ref.18
Corresponds to variant rs72547529 [ dbSNP | Ensembl ].
VAR_065793
Natural variant711G → A in CMRES. Ref.18
VAR_065794
Natural variant771N → S in CMRES. Ref.18
VAR_065795
Natural variant771N → Y in CMRES. Ref.18
VAR_065796
Natural variant981R → W in VKCFD2; strongly reduced enzyme activity. Ref.1 Ref.13
VAR_021824
Natural variant1231I → N in CMRES. Ref.18
VAR_065797
Natural variant1281L → R in CMRES. Ref.1
Corresponds to variant rs104894542 [ dbSNP | Ensembl ].
VAR_021825
Natural variant1391Y → H in CMRES. Ref.18
VAR_065798

Experimental info

Mutagenesis161C → A or S: Reduces enzyme activity by about 80%. Ref.13
Mutagenesis351R → P: Nearly abolishes enzyme activity. Ref.11
Mutagenesis431C → A or S: Reduces enzyme activity. Ref.13 Ref.15
Mutagenesis511C → A or S: Reduces enzyme activity. Ref.13 Ref.15
Mutagenesis561S → P: Nearly abolishes enzyme activity. Ref.11
Mutagenesis571S → A: Nearly abolishes enzyme activity. Ref.13
Mutagenesis851C → A: Reduces enzyme activity by about 25%. Ref.13
Mutagenesis851C → S: Reduces enzyme activity by about 75%. Ref.13
Mutagenesis961C → A or S: Reduces enzyme activity by about 70%. Ref.13
Mutagenesis981R → D or E: Reduces enzyme activity by about 80%. Decreases inhibition by warfarin. Ref.13
Mutagenesis981R → K: No effect on enzyme activity. Decreases inhibition by warfarin. Ref.13
Mutagenesis1201L → Q: Decreases enzyme activity moderately. Decreases inhibition by warfarin. Ref.11
Mutagenesis1281L → Q or S: Decreases enzyme activity by about 80%. Decreases inhibition by warfarin. Ref.11
Mutagenesis1321C → S: Nearly abolishes enzyme activity. Ref.13
Mutagenesis1351C → S: Nearly abolishes enzyme activity. Ref.13
Mutagenesis1391Y → C, G or S: Decreases enzyme activity moderately. Strongly decreases inhibition by warfarin. Ref.11 Ref.13
Mutagenesis1391Y → F: No effect on enzyme activity. Strongly decreases inhibition by warfarin. Ref.11 Ref.13

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MST576) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2F00526A6C561D5A

FASTA16318,235
        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 

« Hide

Isoform 2 (MST134) [UniParc].

Checksum: FBB87922208F471C
Show »

FASTA15616,701
Isoform 3 [UniParc].

Checksum: CB4ADA0C5ED486BD
Show »

FASTA929,875

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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. expand/collapse author list , 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , 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]"The genetic basis of resistance to anticoagulants in rodents."
Pelz H.J., Rost S., Hunerberg M., Fregin A., Heiberg A.C., Baert K., MacNicoll A.D., Prescott C.V., Walker A.S., Oldenburg J., Muller C.R.
Genetics 170:1839-1847(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-35; SER-56; LEU-120; LEU-128 AND TYR-139, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
[12]"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, SUBCELLULAR LOCATION.
[13]"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: FUNCTION, POTENTIAL REDOX-ACTIVE SITE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-16; CYS-43; CYS-51; SER-57; CYS-85; CYS-96; ARG-98; CYS-132; CYS-135 AND TYR-139, CHARACTERIZATION OF VARIANT VKCFD2 TRP-98.
[14]"Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners."
Schulman S., Wang B., Li W., Rapoport T.A.
Proc. Natl. Acad. Sci. U.S.A. 107:15027-15032(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[15]"Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation."
Rishavy M.A., Usubalieva A., Hallgren K.W., Berkner K.L.
J. Biol. Chem. 286:7267-7278(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYS-43 AND CYS-51.
[16]"Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms."
Tie J.K., Jin D.Y., Stafford D.W.
J. Biol. Chem. 287:33945-33955(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
[17]"Membrane topology for human vitamin K epoxide reductase."
Wu S., Tie J.K., Stafford D.W., Pedersen L.G.
J. Thromb. Haemost. 12:112-114(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[18]"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

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.
CCDSCCDS10703.1. [Q9BQB6-1]
CCDS10704.1. [Q9BQB6-3]
RefSeqNP_076869.1. NM_024006.4. [Q9BQB6-1]
NP_996560.1. NM_206824.1. [Q9BQB6-3]
UniGeneHs.324844.

3D structure databases

ProteinModelPortalQ9BQB6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122472. 85 interactions.
IntActQ9BQB6. 2 interactions.
STRING9606.ENSP00000378426.

Chemistry

ChEMBLCHEMBL1930.
DrugBankDB01418. Acenocoumarol.
DB00266. Dicumarol.
DB00170. Menadione.
DB00498. Phenindione.
DB00946. Phenprocoumon.
DB00682. Warfarin.
GuidetoPHARMACOLOGY2645.

PTM databases

PhosphoSiteQ9BQB6.

Polymorphism databases

DMDM62511226.

Proteomic databases

MaxQBQ9BQB6.
PaxDbQ9BQB6.
PRIDEQ9BQB6.

Protocols and materials databases

DNASU79001.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319788; ENSP00000326135; ENSG00000167397. [Q9BQB6-2]
ENST00000354895; ENSP00000346969; ENSG00000167397. [Q9BQB6-3]
ENST00000394975; ENSP00000378426; ENSG00000167397. [Q9BQB6-1]
GeneID79001.
KEGGhsa:79001.
UCSCuc002eas.3. human. [Q9BQB6-1]
uc002eat.3. human. [Q9BQB6-3]
uc002eau.3. human. [Q9BQB6-2]

Organism-specific databases

CTD79001.
GeneCardsGC16M031105.
H-InvDBHIX0079837.
HGNCHGNC:23663. VKORC1.
HPAHPA042720.
MIM122700. phenotype.
607473. phenotype.
608547. gene.
neXtProtNX_Q9BQB6.
Orphanet240843. 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.
PharmGKBPA133787052.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46570.
HOGENOMHOG000230752.
HOVERGENHBG076672.
InParanoidQ9BQB6.
KOK05357.
OMAYSCNGSI.
PhylomeDBQ9BQB6.
TreeFamTF328467.

Enzyme and pathway databases

BRENDA1.1.4.1. 2681.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9BQB6.
BgeeQ9BQB6.
CleanExHS_VKORC1.
GenevestigatorQ9BQB6.

Family and domain databases

InterProIPR012932. VKOR.
[Graphical view]
PfamPF07884. VKOR. 1 hit.
[Graphical view]
SMARTSM00756. VKc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiVKORC1.
GenomeRNAi79001.
NextBio67615.
PROQ9BQB6.
SOURCESearch...

Entry information

Entry nameVKOR1_HUMAN
AccessionPrimary (citable) accession number: Q9BQB6
Secondary accession number(s): A6NIQ6 expand/collapse secondary AC list , B2R4Z6, Q6UX90, Q7Z2R4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM