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O43708 (MAAI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maleylacetoacetate isomerase

Short name=MAAI
EC=5.2.1.2
Alternative name(s):
GSTZ1-1
Glutathione S-transferase zeta 1
EC=2.5.1.18
Gene names
Name:GSTZ1
Synonyms:MAAI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. Ref.15

Catalytic activity

4-maleylacetoacetate = 4-fumarylacetoacetate. Ref.15

RX + glutathione = HX + R-S-glutathione. Ref.15

Cofactor

Glutathione. Required for the MAAI activity.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.

Subunit structure

Homodimer. Ref.16

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Mostly expressed in liver followed by kidney, skeletal muscle and brain. Also expressed in melanocytes, synovium, placenta, breast and fetal liver and heart.

Sequence similarities

Belongs to the GST superfamily. Zeta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Biological processPhenylalanine catabolism
Tyrosine catabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionIsomerase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processL-phenylalanine catabolic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

glutathione derivative biosynthetic process

Traceable author statement. Source: Reactome

glutathione metabolic process

Inferred from direct assay Ref.15. Source: UniProtKB

oxidation-reduction process

Traceable author statement Ref.2. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

tyrosine catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutathione peroxidase activity

Traceable author statement Ref.2. Source: ProtInc

glutathione transferase activity

Inferred from direct assay Ref.15. Source: UniProtKB

maleylacetoacetate isomerase activity

Inferred from direct assay Ref.15. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-748043,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43708-1)

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: O43708-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
Isoform 3 (identifier: O43708-3)

The sequence of this isoform differs from the canonical sequence as follows:
     73-114: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216Maleylacetoacetate isomerase
PRO_0000186022

Regions

Domain4 – 8784GST N-terminal
Domain92 – 212121GST C-terminal
Region14 – 196Glutathione binding
Region71 – 722Glutathione binding
Region115 – 1173Glutathione binding

Sites

Binding site451Glutathione
Binding site591Glutathione; via amide nitrogen and carbonyl oxygen
Binding site1111Glutathione

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14
Modified residue321N6-acetyllysine Ref.12
Modified residue571N6-succinyllysine By similarity
Modified residue1361Phosphothreonine By similarity
Modified residue1771N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 5555Missing in isoform 2.
VSP_039862
Alternative sequence73 – 11442Missing in isoform 3.
VSP_047392
Natural variant321K → E in allele GSTZ1*C. Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.15
Corresponds to variant rs7975 [ dbSNP | Ensembl ].
VAR_009705
Natural variant421R → G in allele GSTZ1*B and allele GSTZ1*C. Ref.1 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.15
Corresponds to variant rs7972 [ dbSNP | Ensembl ].
VAR_009706
Natural variant821M → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs1046428 [ dbSNP | Ensembl ].
VAR_009707
Natural variant1331N → H. Ref.7
Corresponds to variant rs2234955 [ dbSNP | Ensembl ].
VAR_014505

Secondary structure

.................................. 216
Helix Strand Turn

Details...

Sequences

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

Last modified November 24, 2009. Version 3.
Checksum: 2B3112B8AE6B55E0

FASTA21624,212
        10         20         30         40         50         60 
MQAGKPILYS YFRSSCSWRV RIALALKGID YKTVPINLIK DRGQQFSKDF QALNPMKQVP 

        70         80         90        100        110        120 
TLKIDGITIH QSLAIIEYLE EMRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK 

       130        140        150        160        170        180 
QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL 

       190        200        210 
TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA 

« Hide

Isoform 2 [UniParc].

Checksum: 8EF7E58223F1C0E3
Show »

FASTA16117,896
Isoform 3 [UniParc].

Checksum: 9C4636C87F67ADED
Show »

FASTA17419,472

References

« Hide 'large scale' references
[1]"Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue."
Fernandez-Canon J.M., Penalva M.A.
J. Biol. Chem. 273:329-337(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, VARIANTS GLY-42 AND THR-82.
[2]"Zeta, a novel class of glutathione transferases in a range of species from plants to humans."
Board P.G., Baker R.T., Chelvanayagam G., Jermiin L.S.
Biochem. J. 328:929-935(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT THR-82, CHARACTERIZATION.
[3]"Characterization and chromosome location of the gene GSTZ1 encoding the human zeta class glutathione transferase and maleylacetoacetate isomerase."
Blackburn A.C., Woollatt E., Sutherland G.R., Board P.G.
Cytogenet. Cell Genet. 83:109-114(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS GLU-32; GLY-42 AND THR-82.
[4]"Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase."
Fernandez-Canon J.M., Hejna J., Reifsteck C., Olson S., Grompe M.
Genomics 58:263-269(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS GLY-42 AND THR-82.
[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] (ISOFORM 2), VARIANT THR-82.
Tissue: Skeletal muscle.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLY-42 AND THR-82.
[7]NIEHS SNPs program
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS GLU-32; GLY-42; THR-82 AND HIS-133.
[8]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-32 AND GLY-42.
[9]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], VARIANTS GLU-32 AND GLY-42.
[10]"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), VARIANTS GLU-32 AND GLY-42.
Tissue: Placenta.
[11]"Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid."
Tong Z., Board P.G., Anders M.W.
Biochem. J. 331:371-374(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[12]"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-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis."
Blackburn A.C., Tzeng H.F., Anders M.W., Board P.G.
Pharmacogenetics 10:49-57(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-32 AND GLY-42, FUNCTION, CATALYTIC ACTIVITY.
[16]"Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity."
Polekhina G., Board P.G., Blackburn A.C., Parker M.W.
Biochemistry 40:1567-1576(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001838 mRNA. Translation: CAA05045.1.
U86529 mRNA. Translation: AAB96392.1.
AF053545 expand/collapse EMBL AC list , AF053539, AF053540, AF053541, AF053542, AF053543, AF053544 Genomic DNA. Translation: AAC33591.1.
AF098318 expand/collapse EMBL AC list , AF095582, AF098311, AF098312, AF098313, AF098314, AF098315, AF098316, AF098317 Genomic DNA. Translation: AAD43007.1.
AK315154 mRNA. Translation: BAG37600.1.
CR456987 mRNA. Translation: CAG33268.1.
AY316305 Genomic DNA. Translation: AAP69526.1.
AC007954 Genomic DNA. Translation: AAF62559.1.
CH471061 Genomic DNA. Translation: EAW81278.1.
CH471061 Genomic DNA. Translation: EAW81279.1.
BC001453 mRNA. Translation: AAH01453.1.
RefSeqNP_001504.2. NM_001513.3.
NP_665877.1. NM_145870.2.
NP_665878.2. NM_145871.2.
XP_005267616.1. XM_005267559.1.
UniGeneHs.655292.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FW1X-ray1.90A1-216[»]
ProteinModelPortalO43708.
SMRO43708. Positions 5-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109209. 5 interactions.
IntActO43708. 5 interactions.
MINTMINT-1444642.
STRING9606.ENSP00000216465.

Chemistry

ChEMBLCHEMBL4949.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteO43708.

Proteomic databases

PaxDbO43708.
PRIDEO43708.

Protocols and materials databases

DNASU2954.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216465; ENSP00000216465; ENSG00000100577.
ENST00000361389; ENSP00000354959; ENSG00000100577. [O43708-2]
ENST00000393734; ENSP00000377335; ENSG00000100577. [O43708-2]
ENST00000557639; ENSP00000451927; ENSG00000100577. [O43708-2]
GeneID2954.
KEGGhsa:2954.
UCSCuc001xtm.3. human. [O43708-1]

Organism-specific databases

CTD2954.
GeneCardsGC14P077787.
HGNCHGNC:4643. GSTZ1.
HPAHPA004701.
MIM603758. gene.
neXtProtNX_O43708.
PharmGKBPA29031.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0625.
HOVERGENHBG001501.
KOK01800.
OrthoDBEOG7TF79P.
PhylomeDBO43708.
TreeFamTF105324.

Enzyme and pathway databases

BioCycMetaCyc:HS02114-MONOMER.
BRENDA5.2.1.2. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00139; UER00340.

Gene expression databases

ArrayExpressO43708.
BgeeO43708.
CleanExHS_GSTZ1.
GenevestigatorO43708.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005955. Mal_ac_isom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01262. maiA. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSTZ1. human.
EvolutionaryTraceO43708.
GeneWikiGSTZ1.
GenomeRNAi2954.
NextBio11706.
PROO43708.
SOURCESearch...

Entry information

Entry nameMAAI_HUMAN
AccessionPrimary (citable) accession number: O43708
Secondary accession number(s): A6NED0 expand/collapse secondary AC list , A6NNB8, A8MWD7, B2RCK3, O15308, O75430, Q6IB17, Q7Z610, Q9BV63
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 155 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 14

Human chromosome 14: entries, gene names and cross-references to MIM