Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BQB6 (VKOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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. 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.

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; Potential
Topological domain30 – 10071Cytoplasmic Potential
Transmembrane101 – 12323Helical; Potential
Topological domain124 – 1263Lumenal Potential
Transmembrane127 – 14923Helical; Potential
Topological domain150 – 16314Cytoplasmic Potential

Amino acid modifications

Disulfide bond132 ↔ 135Redox-active Potential

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.13
VAR_065785
Natural variant291V → L in CMRES. Ref.1 Ref.13
Corresponds to variant rs104894539 [ dbSNP | Ensembl ].
VAR_021821
Natural variant361D → G in CMRES. Ref.13
VAR_065786
Natural variant361D → Y in CMRES. Ref.13
VAR_065787
Natural variant451V → A in CMRES. Ref.1
Corresponds to variant rs104894540 [ dbSNP | Ensembl ].
VAR_021822
Natural variant521S → W in CMRES. Ref.13
VAR_065788
Natural variant561S → F in CMRES. Ref.13
VAR_065789
Natural variant581R → G in CMRES. Ref.1
Corresponds to variant rs104894541 [ dbSNP | Ensembl ].
VAR_021823
Natural variant591W → C in CMRES. Ref.13
VAR_065790
Natural variant591W → L in CMRES. Ref.13
VAR_065791
Natural variant661V → G in CMRES. Ref.13
VAR_065792
Natural variant661V → M in CMRES. Ref.13
Corresponds to variant rs72547529 [ dbSNP | Ensembl ].
VAR_065793
Natural variant711G → A in CMRES. Ref.13
VAR_065794
Natural variant771N → S in CMRES. Ref.13
VAR_065795
Natural variant771N → Y in CMRES. Ref.13
VAR_065796
Natural variant981R → W in VKCFD2. Ref.1
VAR_021824
Natural variant1231I → N in CMRES. Ref.13
VAR_065797
Natural variant1281L → R in CMRES. Ref.1
Corresponds to variant rs104894542 [ dbSNP | Ensembl ].
VAR_021825
Natural variant1391Y → H in CMRES. Ref.13
VAR_065798

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]"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

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.
RefSeqNP_076869.1. NM_024006.4.
NP_996560.1. NM_206824.1.
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

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.
OMARARWASI.
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: April 16, 2014
This is version 106 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