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Q99798 (ACON_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aconitate hydratase, mitochondrial

Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
Name:ACO2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit. Binding of a 3Fe-4S cluster leads to an inactive enzyme By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion By similarity.

Involvement in disease

Infantile cerebellar-retinal degeneration (ICRD) [MIM:614559]: A severe autosomal recessive neurodegenerative disorder characterized by onset between ages 2 and 6 months of truncal hypotonia, athetosis, seizures, and ophthalmologic abnormalities, particularly optic atrophy and retinal degeneration. Affected individuals show profound psychomotor retardation, with only some achieving rolling, sitting, or recognition of family. Brain MRI shows progressive cerebral and cerebellar degeneration.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Neurodegeneration
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Pyrrolidone carboxylic acid
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular metabolic process

Traceable author statement. Source: Reactome

citrate metabolic process

Inferred from direct assay Ref.2. Source: MGI

generation of precursor metabolites and energy

Traceable author statement Ref.2. Source: ProtInc

isocitrate metabolic process

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

tricarboxylic acid cycle

Inferred from direct assay Ref.2. Source: MGI

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_function3 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: Ensembl

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

aconitate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron ion binding

Inferred from direct assay Ref.2. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 780753Aconitate hydratase, mitochondrial
PRO_0000000541

Regions

Region192 – 1943Substrate binding By similarity
Region670 – 6712Substrate binding By similarity

Sites

Metal binding3851Iron-sulfur (4Fe-4S) By similarity
Metal binding4481Iron-sulfur (4Fe-4S) By similarity
Metal binding4511Iron-sulfur (4Fe-4S) By similarity
Binding site991Substrate By similarity
Binding site4741Substrate By similarity
Binding site4791Substrate By similarity
Binding site6071Substrate By similarity

Amino acid modifications

Modified residue281Pyrrolidone carboxylic acid By similarity
Modified residue311N6-succinyllysine By similarity
Modified residue501N6-acetyllysine; alternate By similarity
Modified residue501N6-succinyllysine; alternate By similarity
Modified residue1381N6-acetyllysine; alternate By similarity
Modified residue1381N6-succinyllysine; alternate By similarity
Modified residue1441N6-acetyllysine; alternate By similarity
Modified residue1441N6-succinyllysine; alternate By similarity
Modified residue2331N6-acetyllysine; alternate By similarity
Modified residue2331N6-succinyllysine; alternate By similarity
Modified residue4111N6-succinyllysine By similarity
Modified residue5491N6-succinyllysine By similarity
Modified residue5591Phosphoserine Ref.10
Modified residue5731N6-acetyllysine; alternate Ref.9
Modified residue5731N6-succinyllysine; alternate By similarity
Modified residue5771N6-succinyllysine By similarity
Modified residue5911N6-succinyllysine By similarity
Modified residue6051N6-acetyllysine; alternate Ref.9
Modified residue6051N6-succinyllysine; alternate By similarity
Modified residue6281N6-succinyllysine By similarity
Modified residue6891N6-succinyllysine By similarity
Modified residue7231N6-acetyllysine; alternate By similarity
Modified residue7231N6-succinyllysine; alternate By similarity
Modified residue7301N6-acetyllysine; alternate By similarity
Modified residue7301N6-succinyllysine; alternate By similarity
Modified residue7361N6-acetyllysine By similarity
Modified residue7391N6-acetyllysine By similarity
Modified residue7431N6-acetyllysine By similarity
Cross-link144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Natural variations

Natural variant1121S → R in ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt. Ref.13
VAR_067543
Natural variant6971T → N in a breast cancer sample; somatic mutation. Ref.12
VAR_036572
Natural variant7681A → S.
Corresponds to variant rs1804785 [ dbSNP | Ensembl ].
VAR_033297

Experimental info

Sequence conflict351S → T in AAB38416. Ref.1
Sequence conflict1361G → D in AAB38416. Ref.1
Sequence conflict1591A → D in AAB38416. Ref.1
Sequence conflict1671K → S in AAB38416. Ref.1
Sequence conflict1991G → D in CAG38805. Ref.4
Sequence conflict2071G → R in AAH26196. Ref.6
Sequence conflict2421S → T in AAB38416. Ref.1
Sequence conflict2701P → H in AAH26196. Ref.6
Sequence conflict2751I → M in AAB38416. Ref.1
Sequence conflict4441L → P in CAG38805. Ref.4
Sequence conflict5171T → K in AAB38416. Ref.1
Sequence conflict5531G → R in AAB38416. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99798 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 58C9FFBDBDC63D5E

FASTA78085,425
        10         20         30         40         50         60 
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPN EYIHYDLLEK NINIVRKRLN 

        70         80         90        100        110        120 
RPLTLSEKIV YGHLDDPASQ EIERGKSYLR LRPDRVAMQD ATAQMAMLQF ISSGLSKVAV 

       130        140        150        160        170        180 
PSTIHCDHLI EAQVGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWKPGS GIIHQIILEN 

       190        200        210        220        230        240 
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG 

       250        260        270        280        290        300 
WSSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN 

       310        320        330        340        350        360 
HRMKKYLSKT GREDIANLAD EFKDHLVPDP GCHYDQLIEI NLSELKPHIN GPFTPDLAHP 

       370        380        390        400        410        420 
VAEVGKVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS 

       430        440        450        460        470        480 
EQIRATIERD GYAQILRDLG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN 

       490        500        510        520        530        540 
DANPETHAFV TSPEIVTALA IAGTLKFNPE TDYLTGTDGK KFRLEAPDAD ELPKGEFDPG 

       550        560        570        580        590        600 
QDTYQHPPKD SSGQHVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA 

       610        620        630        640        650        660 
GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI 

       670        680        690        700        710        720 
GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP 

       730        740        750        760        770        780 
VDKLTIQGLK DFTPGKPLKC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and structural characterization of human mitochondrial aconitase."
Juang H.H., Chiou B.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Characterization of the human mitochondrial aconitase gene (ACO2)."
Mirel D.B., Marder K., Graziano J., Freyer G., Zhao Q., Mayeux R., Wilhelmsen K.C.
Gene 213:205-218(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain and Uterus.
[7]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 69-84; 234-245; 313-323; 379-395; 412-424; 430-437; 507-520; 565-573; 608-628; 634-648 AND 657-671, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]"Purification and partial amino acid sequence of human aconitase."
Baldwin G.S., Seet K.L., Callaghan J., Toncich G., Toh B.H., Moritz R.L., Rubira M.R., Simpson R.
Protein Seq. Data Anal. 4:63-67(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-83; 96-107; 371-396 AND 524-534.
[9]"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-573 AND LYS-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-697.
[13]"Infantile Cerebellar-Retinal Degeneration Associated with a Mutation in Mitochondrial Aconitase, ACO2."
Spiegel R., Pines O., Ta-Shma A., Burak E., Shaag A., Halvardson J., Edvardson S., Mahajna M., Zenvirt S., Saada A., Shalev S., Feuk L., Elpeleg O.
Am. J. Hum. Genet. 90:518-523(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ICRD ARG-112, CHARACTERIZATION OF VARIANT ICRD ARG-112.
+Additional computationally mapped references.

Web resources

Wikipedia

Aconitase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U80040 mRNA. Translation: AAB38416.1.
U87939 expand/collapse EMBL AC list , U87926, U87927, U87928, U87929, U87930, U87931, U87932, U87933, U87934, U87935, U87936, U87937, U87938 Genomic DNA. Translation: AAC39921.1.
CR456365 mRNA. Translation: CAG30251.1.
CR536568 mRNA. Translation: CAG38805.1.
AL023553, AL008582 Genomic DNA. Translation: CAI20278.1.
AL008582, AL023553 Genomic DNA. Translation: CAI17931.1.
BC014092 mRNA. Translation: AAH14092.1.
BC026196 mRNA. Translation: AAH26196.1.
PIRS17526.
T52543.
RefSeqNP_001089.1. NM_001098.2.
UniGeneHs.643610.

3D structure databases

ProteinModelPortalQ99798.
SMRQ99798. Positions 29-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106566. 12 interactions.
IntActQ99798. 2 interactions.
MINTMINT-2856402.
STRING9606.ENSP00000216254.

PTM databases

PhosphoSiteQ99798.

Polymorphism databases

DMDM6686275.

2D gel databases

DOSAC-COBS-2DPAGEQ99798.
REPRODUCTION-2DPAGEIPI00017855.
Q99798.
SWISS-2DPAGEQ99798.
UCD-2DPAGEQ99798.

Proteomic databases

PaxDbQ99798.
PRIDEQ99798.

Protocols and materials databases

DNASU50.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216254; ENSP00000216254; ENSG00000100412.
GeneID50.
KEGGhsa:50.
UCSCuc003bac.3. human.

Organism-specific databases

CTD50.
GeneCardsGC22P041865.
HGNCHGNC:118. ACO2.
HPAHPA001097.
MIM100850. gene.
614559. phenotype.
neXtProtNX_Q99798.
Orphanet313850. Infantile cerebellar-retinal degeneration.
PharmGKBPA24443.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000224293.
HOVERGENHBG000248.
KOK01681.
OrthoDBEOG74FF06.
PhylomeDBQ99798.
TreeFamTF300627.

Enzyme and pathway databases

BioCycMetaCyc:HS02077-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00223; UER00718.

Gene expression databases

ArrayExpressQ99798.
BgeeQ99798.
CleanExHS_ACO2.
GenevestigatorQ99798.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF5. PTHR11670:SF5. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsTIGR01340. aconitase_mito. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACO2. human.
GenomeRNAi50.
NextBio195.
PROQ99798.
SOURCESearch...

Entry information

Entry nameACON_HUMAN
AccessionPrimary (citable) accession number: Q99798
Secondary accession number(s): O75809 expand/collapse secondary AC list , Q5JZ41, Q6FHX0, Q8TAQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 147 of the entry and version 2 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

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 22

Human chromosome 22: entries, gene names and cross-references to MIM