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Q9C0B1 (FTO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Alpha-ketoglutarate-dependent dioxygenase FTO

EC=1.14.11.-
Alternative name(s):
Fat mass and obesity-associated protein
Gene names
Name:FTO
Synonyms:KIAA1752
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dioxygenase that repairs alkylated DNA and RNA by oxidative demethylation. Has highest activity towards single-stranded RNA containing 3-methyluracil, followed by single-stranded DNA containing 3-methylthymine. Has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Has no activity towards 1-methylguanine. Has no detectable activity towards double-stranded DNA. Requires molecular oxygen, alpha-ketoglutarate and iron. Contributes to the regulation of the global metabolic rate, energy expenditure and energy homeostasis. Contributes to the regulation of body size and body fat accumulation. Ref.6 Ref.9 Ref.10

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.10

Enzyme regulation

Activated by ascorbate. Inhibited by N-oxalylglycine, fumarate and succinate By similarity. Ref.10

Subunit structure

Monomer. May also exist as homodimer By similarity.

Subcellular location

Nucleus. Nucleus speckle Ref.9.

Tissue specificity

Ubiquitously expressed, with relatively high expression in adrenal glands and brain; especially in hypothalamus and pituitary. Ref.4 Ref.5

Domain

The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases. Ref.10

Polymorphism

At least one intronic variation within the gene predisposes to childhood and adult obesity.

Involvement in disease

Growth retardation developmental delay coarse facies early death (GDFD) [MIM:612938]: A severe polymalformation syndrome characterized by postnatal growth retardation, microcephaly, severe psychomotor delay, functional brain deficits and characteristic facial dysmorphism. In some patients, structural brain malformations, cardiac defects, genital anomalies, and cleft palate are observed. Early death occurs by the age of 3 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11

Sequence similarities

Belongs to the fto family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5-6. Ref.6

Sequence caution

The sequence BAB21843.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
RNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Obesity
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA dealkylation involved in DNA repair

Inferred from direct assay Ref.10. Source: UniProtKB

DNA demethylation

Inferred from direct assay Ref.6. Source: BHF-UCL

RNA repair

Inferred from direct assay Ref.6. Source: BHF-UCL

adipose tissue development

Inferred from electronic annotation. Source: Ensembl

oxidative demethylation

Inferred from direct assay Ref.6. Source: BHF-UCL

oxidative single-stranded DNA demethylation

Inferred from direct assay Ref.10. Source: UniProtKB

oxidative single-stranded RNA demethylation

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of lipid storage

Inferred from electronic annotation. Source: Ensembl

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

regulation of respiratory system process

Inferred from electronic annotation. Source: Ensembl

regulation of white fat cell proliferation

Inferred from electronic annotation. Source: Ensembl

temperature homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnuclear speck

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity PubMed 17991826. Source: BHF-UCL

   Molecular_functionDNA-N1-methyladenine dioxygenase activity

Inferred from direct assay Ref.10. Source: UniProtKB

ferrous iron binding

Inferred from direct assay Ref.10. Source: UniProtKB

oxidative DNA demethylase activity

Inferred from direct assay Ref.10. Source: UniProtKB

oxidative RNA demethylase activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C0B1-1)

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: Q9C0B1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-378: Missing.
     379-413: LRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGV → MEWRKVSECNSVEPCREVKKWPYRCIHHGKNFSRM
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9C0B1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-445: Missing.
     446-455: QNLRREWHAR → MACQGREECW
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9C0B1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-399: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Alpha-ketoglutarate-dependent dioxygenase FTO
PRO_0000286163

Regions

Region32 – 327296Fe2OG dioxygenase domain
Region213 – 22412Loop L1; predicted to block binding of double-stranded DNA or RNA
Region231 – 2344Substrate binding
Region316 – 3183Alpha-ketoglutarate binding

Sites

Metal binding2311Iron; catalytic
Metal binding2331Iron; catalytic
Metal binding3071Iron; catalytic
Binding site961Substrate
Binding site1081Substrate
Binding site2051Alpha-ketoglutarate
Binding site2951Alpha-ketoglutarate
Binding site3201Alpha-ketoglutarate
Binding site3221Alpha-ketoglutarate

Amino acid modifications

Modified residue2161N6-acetyllysine Ref.7

Natural variations

Alternative sequence1 – 445445Missing in isoform 3.
VSP_025002
Alternative sequence1 – 399399Missing in isoform 4.
VSP_025003
Alternative sequence1 – 378378Missing in isoform 2.
VSP_025004
Alternative sequence379 – 41335LRQFW…KMEGV → MEWRKVSECNSVEPCREVKK WPYRCIHHGKNFSRM in isoform 2.
VSP_025005
Alternative sequence446 – 45510QNLRREWHAR → MACQGREECW in isoform 3.
VSP_025006
Natural variant3161R → Q in GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. Ref.9 Ref.11
VAR_063252
Natural variant4051A → V.
Corresponds to variant rs16952624 [ dbSNP | Ensembl ].
VAR_032078

Experimental info

Mutagenesis961R → M or W: Almost abolishes enzyme activity. Ref.10
Mutagenesis1081Y → A: Abolishes enzyme activity. Ref.10
Mutagenesis1141F → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. Ref.10
Mutagenesis231 – 2333HHD → AHA: Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs. Ref.9
Mutagenesis2341E → P: Abolishes enzyme activity. Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs; when associated with Q-322. Ref.10
Mutagenesis3921C → D: Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity. Ref.10
Sequence conflict3161R → W in BAB21843. Ref.1
Sequence conflict3161R → W in AAH03583. Ref.3
Sequence conflict3161R → W in AAH30798. Ref.3
Sequence conflict3161R → W in AAI32893. Ref.3

Secondary structure

................................................................... 505
Helix Strand Turn

Details...

Sequences

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

Last modified May 29, 2007. Version 3.
Checksum: 3498A92C6E6D81B1

FASTA50558,282
        10         20         30         40         50         60 
MKRTPTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLI LREASSVSEE 

        70         80         90        100        110        120 
LHKEVQEAFL TLHKHGCLFR DLVRIQGKDL LTPVSRILIG NPGCTYKYLN TRLFTVPWPV 

       130        140        150        160        170        180 
KGSNIKHTEA EIAAACETFL KLNDYLQIET IQALEELAAK EKANEDAVPL CMSADFPRVG 

       190        200        210        220        230        240 
MGSSYNGQDE VDIKSRAAYN VTLLNFMDPQ KMPYLKEEPY FGMGKMAVSW HHDENLVDRS 

       250        260        270        280        290        300 
AVAVYSYSCE GPEEESEDDS HLEGRDPDIW HVGFKISWDI ETPGLAIPLH QGDCYFMLDD 

       310        320        330        340        350        360 
LNATHQHCVL AGSQPRFSST HRVAECSTGT LDYILQRCQL ALQNVCDDVD NDDVSLKSFE 

       370        380        390        400        410        420 
PAVLKQGEEI HNEVEFEWLR QFWFQGNRYR KCTDWWCQPM AQLEALWKKM EGVTNAVLHE 

       430        440        450        460        470        480 
VKREGLPVEQ RNEILTAILA SLTARQNLRR EWHARCQSRI ARTLPADQKP ECRPYWEKDD 

       490        500 
ASMPLPFDLT DIVSELRGQL LEAKP 

« Hide

Isoform 2 [UniParc].

Checksum: 5FA0B71723B0564B
Show »

FASTA12714,936
Isoform 3 [UniParc].

Checksum: 54A786243F09AF34
Show »

FASTA606,924
Isoform 4 [UniParc].

Checksum: AFE4D8E4F34B2F74
Show »

FASTA10612,218

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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].
Tissue: Brain.
[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] (ISOFORMS 2; 3 AND 4).
Tissue: Cervix, Eye and Lung.
[4]"Variation in FTO contributes to childhood obesity and severe adult obesity."
Dina C., Meyre D., Gallina S., Durand E., Korner A., Jacobson P., Carlsson L.M.S., Kiess W., Vatin V., Lecoeur C., Delplanque J., Vaillant E., Pattou F., Ruiz J., Weill J., Levy-Marchal C., Horber F., Potoczna N. expand/collapse author list , Hercberg S., Le Stunff C., Bougneres P., Kovacs P., Marre M., Balkau B., Cauchi S., Chevre J.-C., Froguel P.
Nat. Genet. 39:724-726(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PREDISPOSITION OF OBESITY, TISSUE SPECIFICITY.
[5]"A common variant in the FTO gene is associated with body mass index and predisposes to childhood and adult obesity."
Frayling T.M., Timpson N.J., Weedon M.N., Zeggini E., Freathy R.M., Lindgren C.M., Perry J.R., Elliott K.S., Lango H., Rayner N.W., Shields B., Harries L.W., Barrett J.C., Ellard S., Groves C.J., Knight B., Patch A.M., Ness A.R. expand/collapse author list , Ebrahim S., Lawlor D.A., Ring S.M., Ben-Shlomo Y., Jarvelin M.-R., Sovio U., Bennett A.J., Melzer D., Ferrucci L., Loos R.J., Barroso I., Wareham N.J., Karpe F., Owen K.R., Cardon L.R., Walker M., Hitman G.A., Palmer C.N., Doney A.S., Morris A.D., Davey-Smith G., Hattersley A.T., McCarthy M.I.
Science 316:889-894(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PREDISPOSITION OF OBESITY, TISSUE SPECIFICITY.
[6]"Oxidative demethylation of 3-methylthymine and 3-methyluracil in single-stranded DNA and RNA by mouse and human FTO."
Jia G., Yang C.G., Yang S., Jian X., Yi C., Zhou Z., He C.
FEBS Lett. 582:3313-3319(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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].
[9]"N6-methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO."
Jia G., Fu Y., Zhao X., Dai Q., Zheng G., Yang Y., Yi C., Lindahl T., Pan T., Yang Y.G., He C.
Nat. Chem. Biol. 7:885-887(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 231-HIS--ASP-233, CHARACTERIZATION OF VARIANT GDFD GLN-316.
[10]"Crystal structure of the FTO protein reveals basis for its substrate specificity."
Han Z., Niu T., Chang J., Lei X., Zhao M., Wang Q., Cheng W., Wang J., Feng Y., Chai J.
Nature 464:1205-1209(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-505 IN COMPLEX WITH IRON IONS; N-OXALYLGLYCINE AND 3-METHYLTHYMIDINE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ARG-96; TYR-108; PHE-114; GLU-234 AND CYS-392, CIRCULAR DICHROISM, DOMAIN.
[11]"Loss-of-function mutation in the dioxygenase-encoding FTO gene causes severe growth retardation and multiple malformations."
Boissel S., Reish O., Proulx K., Kawagoe-Takaki H., Sedgwick B., Yeo G.S., Meyre D., Golzio C., Molinari F., Kadhom N., Etchevers H.C., Saudek V., Farooqi I.S., Froguel P., Lindahl T., O'Rahilly S., Munnich A., Colleaux L.
Am. J. Hum. Genet. 85:106-111(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GDFD GLN-316, CHARACTERIZATION OF VARIANT GDFD GLN-316.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB051539 mRNA. Translation: BAB21843.1. Different initiation.
AC007347 Genomic DNA. No translation available.
AC007496 Genomic DNA. No translation available.
AC007909 Genomic DNA. No translation available.
BC003583 mRNA. Translation: AAH03583.1.
BC030798 mRNA. Translation: AAH30798.1.
BC132892 mRNA. Translation: AAI32893.1.
BC137091 mRNA. Translation: AAI37092.1.
RefSeqNP_001073901.1. NM_001080432.2.
UniGeneHs.528833.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LFMX-ray2.50A32-505[»]
4IDZX-ray2.46A32-505[»]
4IE0X-ray2.53A32-505[»]
4IE4X-ray2.50A32-505[»]
4IE5X-ray1.95A32-505[»]
4IE6X-ray2.50A32-505[»]
4IE7X-ray2.60A32-505[»]
ProteinModelPortalQ9C0B1.
SMRQ9C0B1. Positions 30-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122520. 14 interactions.
IntActQ9C0B1. 2 interactions.
STRING9606.ENSP00000418823.

Chemistry

ChEMBLCHEMBL2331065.

PTM databases

PhosphoSiteQ9C0B1.

Polymorphism databases

DMDM148841515.

Proteomic databases

PaxDbQ9C0B1.
PRIDEQ9C0B1.

Protocols and materials databases

DNASU79068.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000431610; ENSP00000415636; ENSG00000140718. [Q9C0B1-4]
ENST00000460382; ENSP00000417422; ENSG00000140718. [Q9C0B1-4]
ENST00000463855; ENSP00000417843; ENSG00000140718. [Q9C0B1-2]
ENST00000471389; ENSP00000418823; ENSG00000140718. [Q9C0B1-1]
GeneID79068.
KEGGhsa:79068.
UCSCuc002ehr.3. human. [Q9C0B1-1]
uc010cbz.3. human. [Q9C0B1-4]

Organism-specific databases

CTD79068.
GeneCardsGC16P053737.
H-InvDBHIX0013037.
HIX0134382.
HIX0204005.
HGNCHGNC:24678. FTO.
HPACAB017123.
MIM610966. gene.
612938. phenotype.
neXtProtNX_Q9C0B1.
Orphanet210144. Lethal polymalformative syndrome, Boissel type.
PharmGKBPA152208656.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45792.
HOGENOMHOG000273870.
HOVERGENHBG101847.
InParanoidQ9C0B1.
OMAAVYNYSC.
OrthoDBEOG7CK36T.
PhylomeDBQ9C0B1.
TreeFamTF333296.

Gene expression databases

ArrayExpressQ9C0B1.
BgeeQ9C0B1.
CleanExHS_FTO.
GenevestigatorQ9C0B1.

Family and domain databases

InterProIPR024366. FTO_C.
IPR024367. FTO_cat_dom.
[Graphical view]
PfamPF12934. FTO_CTD. 1 hit.
PF12933. FTO_NTD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFTO. human.
GeneWikiFTO_gene.
GenomeRNAi79068.
NextBio67845.
PROQ9C0B1.
SOURCESearch...

Entry information

Entry nameFTO_HUMAN
AccessionPrimary (citable) accession number: Q9C0B1
Secondary accession number(s): A2RUH1 expand/collapse secondary AC list , B2RNS0, Q0P676, Q7Z785
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 85 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

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