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Q06210 (GFPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

EC=2.6.1.16
Alternative name(s):
D-fructose-6-phosphate amidotransferase 1
Glutamine:fructose-6-phosphate amidotransferase 1
Short name=GFAT 1
Short name=GFAT1
Hexosephosphate aminotransferase 1
Gene names
Name:GFPT1
Synonyms:GFAT, GFPT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length699 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1.

Catalytic activity

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.

Subunit structure

Homotetramer Probable, may also exist as homodimers. Ref.15

Tissue specificity

Isoform 1 is predominantly expressed in skeletal muscle. Not expressed in brain. Seems to be selectively expressed in striated muscle. Ref.4

Involvement in disease

Myasthenic syndrome, congenital, with tubular aggregates, 1 (CMSTA1) [MIM:610542]: A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Contains 1 glutamine amidotransferase type-2 domain.

Contains 2 SIS domains.

Ontologies

Keywords
   Biological processBiological rhythms
   Coding sequence diversityAlternative splicing
   DiseaseCongenital myasthenic syndrome
Disease mutation
   DomainGlutamine amidotransferase
Repeat
   Molecular functionAminotransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine biosynthetic process

Traceable author statement. Source: Reactome

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

carbohydrate biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

dolichol-linked oligosaccharide biosynthetic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

energy reserve metabolic process

Traceable author statement Ref.1. Source: ProtInc

fructose 6-phosphate metabolic process

Traceable author statement PubMed 8144040. Source: ProtInc

glucosamine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to sucrose

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: Ensembl

carbohydrate binding

Inferred from electronic annotation. Source: Ensembl

glutamine-fructose-6-phosphate transaminase (isomerizing) activity

Traceable author statement PubMed 8144040. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q06210-1)

Also known as: GFAT1m;

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: Q06210-2)

The sequence of this isoform differs from the canonical sequence as follows:
     229-246: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 699698Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
PRO_0000135280

Regions

Domain2 – 305304Glutamine amidotransferase type-2
Domain377 – 516140SIS 1
Domain548 – 689142SIS 2
Region313 – 680368Isomerase
Region394 – 3952Substrate-binding
Region439 – 4413Substrate-binding

Sites

Active site21For GATase activity By similarity
Binding site4441Substrate
Binding site5841Substrate

Amino acid modifications

Modified residue2611Phosphoserine Ref.6 Ref.7 Ref.11

Natural variations

Alternative sequence229 – 24618Missing in isoform 2.
VSP_007497
Natural variant151T → A in CMSTA1. Ref.16
VAR_065339
Natural variant151T → M in CMSTA1. Ref.16
VAR_065340
Natural variant431D → V in CMSTA1. Ref.16
VAR_065341
Natural variant1111R → C in CMSTA1. Ref.16
Corresponds to variant rs201322234 [ dbSNP | Ensembl ].
VAR_065342
Natural variant1211I → T in CMSTA1. Ref.16
VAR_065343
Natural variant1991V → F in CMSTA1. Ref.16
VAR_065344
Natural variant3661D → Y in CMSTA1. Ref.16
VAR_065345
Natural variant4031R → H in CMSTA1. Ref.16
VAR_065346
Natural variant4521R → H in CMSTA1. Ref.16
VAR_065347
Natural variant5091M → T in CMSTA1. Ref.16
VAR_065348
Natural variant5101M → T in CMSTA1. Ref.16
VAR_065349
Natural variant5141R → W in CMSTA1. Ref.16
VAR_065350
Natural variant5301R → W in CMSTA1. Ref.16
VAR_065351

Secondary structure

.................................................................... 699
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GFAT1m) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F0533A7B762C7B98

FASTA69978,806
        10         20         30         40         50         60 
MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GFDGGNDKDW EANACKIQLI 

        70         80         90        100        110        120 
KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPSPVNSHPQ RSDKNNEFIV 

       130        140        150        160        170        180 
IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNRESQDTSF TTLVERVIQQ 

       190        200        210        220        230        240 
LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSKFTRW 

       250        260        270        280        290        300 
GSQGERGKDK KGSCNLSRVD STTCLFPVEE KAVEYYFASD ASAVIEHTNR VIFLEDDDVA 

       310        320        330        340        350        360 
AVVDGRLSIH RIKRTAGDHP GRAVQTLQME LQQIMKGNFS SFMQKEIFEQ PESVVNTMRG 

       370        380        390        400        410        420 
RVNFDDYTVN LGGLKDHIKE IQRCRRLILI ACGTSYHAGV ATRQVLEELT ELPVMVELAS 

       430        440        450        460        470        480 
DFLDRNTPVF RDDVCFFLSQ SGETADTLMG LRYCKERGAL TVGITNTVGS SISRETDCGV 

       490        500        510        520        530        540 
HINAGPEIGV ASTKAYTSQF VSLVMFALMM CDDRISMQER RKEIMLGLKR LPDLIKEVLS 

       550        560        570        580        590        600 
MDDEIQKLAT ELYHQKSVLI MGRGYHYATC LEGALKIKEI TYMHSEGILA GELKHGPLAL 

       610        620        630        640        650        660 
VDKLMPVIMI IMRDHTYAKC QNALQQVVAR QGRPVVICDK EDTETIKNTK RTIKVPHSVD 

       670        680        690 
CLQGILSVIP LQLLAFHLAV LRGYDVDFPR NLAKSVTVE 

« Hide

Isoform 2 [UniParc].

Checksum: 5CB56FDB5E4F76FA
Show »

FASTA68176,759

References

« Hide 'large scale' references
[1]"Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase."
McKnight G.L., Mudri S.L., Mathewes S.L., Traxinger R.R., Marshall S., Sheppard P.O., O'Hara P.J.
J. Biol. Chem. 267:25208-25212(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2).
[4]"A novel variant of glutamine:fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle."
DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G.
Diabetes 50:2419-2424(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-275 (ISOFORM 1), TISSUE SPECIFICITY.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes."
Nakaishi Y., Bando M., Shimizu H., Watanabe K., Goto F., Tsuge H., Kondo K., Komatsu M.
FEBS Lett. 583:163-167(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 332-699, SUBUNIT, SUBSTRATE-BINDING SITES.
[16]"Hexosamine biosynthetic pathway mutations cause neuromuscular transmission defect."
Senderek J., Muller J.S., Dusl M., Strom T.M., Guergueltcheva V., Diepolder I., Laval S.H., Maxwell S., Cossins J., Krause S., Muelas N., Vilchez J.J., Colomer J., Mallebrera C.J., Nascimento A., Nafissi S., Kariminejad A., Nilipour Y. expand/collapse author list , Bozorgmehr B., Najmabadi H., Rodolico C., Sieb J.P., Steinlein O.K., Schlotter B., Schoser B., Kirschner J., Herrmann R., Voit T., Oldfors A., Lindbergh C., Urtizberea A., von der Hagen M., Hubner A., Palace J., Bushby K., Straub V., Beeson D., Abicht A., Lochmuller H.
Am. J. Hum. Genet. 88:162-172(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMSTA1 ALA-15; MET-15; VAL-43; CYS-111; THR-121; PHE-199; TYR-366; HIS-403; HIS-452; THR-509; THR-510; TRP-514 AND TRP-530.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90516 mRNA. Translation: AAA58502.1.
AC114772 Genomic DNA. Translation: AAY14827.1.
BC045641 mRNA. Translation: AAH45641.1.
AF334737 mRNA. Translation: AAK15342.1.
PIRA45055.
RefSeqNP_001231639.1. NM_001244710.1.
NP_002047.2. NM_002056.3.
UniGeneHs.580300.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4MX-ray2.29A/B/C/D332-699[»]
2ZJ3X-ray1.90A332-699[»]
2ZJ4X-ray2.20A332-699[»]
ProteinModelPortalQ06210.
SMRQ06210. Positions 2-699.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108941. 22 interactions.
IntActQ06210. 4 interactions.
MINTMINT-5001216.
STRING9606.ENSP00000354347.

Chemistry

BindingDBQ06210.
ChEMBLCHEMBL1909481.

Protein family/group databases

MEROPSC44.970.

PTM databases

PhosphoSiteQ06210.

Polymorphism databases

DMDM30923274.

Proteomic databases

PaxDbQ06210.
PRIDEQ06210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357308; ENSP00000349860; ENSG00000198380. [Q06210-1]
ENST00000361060; ENSP00000354347; ENSG00000198380. [Q06210-2]
GeneID2673.
KEGGhsa:2673.
UCSCuc002sfh.3. human. [Q06210-2]
uc002sfi.2. human. [Q06210-1]

Organism-specific databases

CTD2673.
GeneCardsGC02M069546.
HGNCHGNC:4241. GFPT1.
HPAHPA047240.
MIM138292. gene.
610542. phenotype.
neXtProtNX_Q06210.
Orphanet353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBPA28651.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0449.
HOGENOMHOG000258898.
HOVERGENHBG051724.
InParanoidQ06210.
KOK00820.
OMALGIGENF.
OrthoDBEOG73NG2S.
PhylomeDBQ06210.
TreeFamTF300864.

Enzyme and pathway databases

BioCycMetaCyc:HS09974-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00113; UER00528.

Gene expression databases

BgeeQ06210.
CleanExHS_GFPT1.
GenevestigatorQ06210.

Family and domain databases

InterProIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]
PfamPF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01135. glmS. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGFPT1. human.
EvolutionaryTraceQ06210.
GeneWikiGFPT1.
GenomeRNAi2673.
NextBio10550.
PROQ06210.
SOURCESearch...

Entry information

Entry nameGFPT1_HUMAN
AccessionPrimary (citable) accession number: Q06210
Secondary accession number(s): Q53QE6, Q9BXF8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 139 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 2

Human chromosome 2: entries, gene names and cross-references to MIM