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

P07741 (APT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenine phosphoribosyltransferase

Short name=APRT
EC=2.4.2.7
Gene names
Name:APRT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. HAMAP-Rule MF_00004

Catalytic activity

AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00004

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. HAMAP-Rule MF_00004

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00004.

Involvement in disease

Adenine phosphoribosyltransferase deficiency (APRTD) [MIM:614723]: An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processAMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

adenine salvage

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

grooming behavior

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

purine-containing compound salvage

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionAMP binding

Inferred from direct assay Ref.16. Source: MGI

adenine binding

Inferred from electronic annotation. Source: Ensembl

adenine phosphoribosyltransferase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07741-1)

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: P07741-2)

The sequence of this isoform differs from the canonical sequence as follows:
     134-180: GTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE → V
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 180179Adenine phosphoribosyltransferase HAMAP-Rule MF_00004
PRO_0000149504

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Modified residue41Phosphoserine Ref.11
Modified residue151Phosphoserine Ref.11
Modified residue601Phosphotyrosine Ref.11
Modified residue661Phosphoserine Ref.11
Modified residue1141N6-acetyllysine Ref.12
Modified residue1351Phosphothreonine Ref.11

Natural variations

Alternative sequence134 – 18047GTMNA…LLQYE → V in isoform 2.
VSP_045705
Natural variant331L → P in APRTD. Ref.24
VAR_069049
Natural variant651D → V in APRTD; Icelandic type. Ref.17
VAR_006747
Natural variant841V → M in APRTD. Ref.23
Corresponds to variant rs200392753 [ dbSNP | Ensembl ].
VAR_069050
Natural variant1101L → P in APRTD; Newfoundland type. Ref.18
VAR_006748
Natural variant1211Q → R. Ref.4
Corresponds to variant rs8191494 [ dbSNP | Ensembl ].
VAR_019055
Natural variant1331G → D in APRTD. Ref.23
VAR_069051
Natural variant1361M → T in APRTD; Japanese type; allele APRT*J; most common mutation. Ref.19 Ref.20 Ref.21 Ref.24
Corresponds to variant rs28999113 [ dbSNP | Ensembl ].
VAR_006749
Natural variant1501V → F in APRTD. Ref.22
VAR_022608
Natural variant1531C → R in APRTD. Ref.22
VAR_022609
Natural variant1731Missing in APRTD. Ref.20
VAR_037575

Secondary structure

................................. 180
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: CDC7703337A6E453

FASTA18019,608
        10         20         30         40         50         60 
MADSELQLVE QRIRSFPDFP TPGVVFRDIS PVLKDPASFR AAIGLLARHL KATHGGRIDY 

        70         80         90        100        110        120 
IAGLDSRGFL FGPSLAQELG LGCVLIRKRG KLPGPTLWAS YSLEYGKAEL EIQKDALEPG 

       130        140        150        160        170        180 
QRVVVVDDLL ATGGTMNAAC ELLGRLQAEV LECVSLVELT SLKGREKLAP VPFFSLLQYE 

« Hide

Isoform 2 [UniParc].

Checksum: 404EC4ACAE4C29DE
Show »

FASTA13414,557

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the human APRT gene."
Hidaka Y., Tarle S.A., Toole T.E.O., Kelley W.N., Palella T.D.
Nucleic Acids Res. 15:9086-9086(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement."
Broderick T.P., Schaff D.A., Bertino A.M., Dush M.K., Tischfield J.A., Stambrook P.J.
Proc. Natl. Acad. Sci. U.S.A. 84:3349-3353(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterine endothelium.
[4]NIEHS SNPs program
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-121.
[5]"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].
[6]Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 1 AND 2).
Tissue: Astrocytoma.
[8]"Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme."
Wilson J.M., O'Toole T.E., Argos P., Shewach D.S., Daddona P.E., Kelley W.N.
J. Biol. Chem. 261:13677-13683(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-180.
[9]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12, ACETYLATION AT ALA-2.
Tissue: Platelet.
[10]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-15; TYR-60; SER-66 AND THR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-114, 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]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis."
Silva M., Silva C.H., Iulek J., Thiemann O.H.
Biochemistry 43:7663-7671(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[17]"Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient."
Chen J., Sahota A., Laxdal T., Scrine M., Bowman S., Cui C., Stambrook P.J., Tischfield J.A.
Am. J. Hum. Genet. 49:1306-1311(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APRTD VAL-65.
[18]"Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis."
Sahota A., Chen J., Boyadjiev S.A., Gault M.H., Tischfield J.A.
Hum. Mol. Genet. 3:817-818(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APRTD PRO-110.
[19]"Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme."
Hidaka Y., Palella T.D., O'Toole T.E., Tarle S.A., Kelley W.N.
J. Clin. Invest. 80:1409-1415(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APRTD THR-136.
[20]"Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese."
Hidaka Y., Tarle S.A., Fujimori S., Kamatani N., Kelley W.N.
J. Clin. Invest. 81:945-950(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APRTD THR-136 AND PHE-173 DEL.
[21]"Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients."
Kamatani N., Hakoda M., Otsuka S., Yoshikawa H., Kashiwazaki S.
J. Clin. Invest. 90:130-135(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT APRTD THR-136.
[22]"2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT."
Deng L., Yang M., Fruend S., Wessel T., De Abreu R.A., Tischfield J.A., Sahota A.
Mol. Genet. Metab. 72:260-264(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APRTD PHE-150 AND ARG-153.
[23]"Identification of two novel mutations in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis."
Taniguchi A., Tsuchida S., Kuno S., Mita M., Machida T., Ioritani N., Terai C., Yamanaka H., Kamatani N.
Nucleosides Nucleotides Nucleic Acids 23:1141-1145(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APRTD MET-84 AND ASP-133.
[24]"A Japanese boy with adenine phosphoribosyltransferase (APRT) deficiency caused by compound heterozygosity including a novel missense mutation in APRT gene."
Nozue H., Kamoda T., Saitoh H., Ichikawa K., Taniguchi A.
Acta Paediatr. 100:E285-E288(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APRTD PRO-33 AND THR-136.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Adenine phosphoribosyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00486 Genomic DNA. Translation: CAA68543.1.
M16446 Genomic DNA. Translation: AAA51769.1.
CR749423 mRNA. Translation: CAH18261.1.
AY306126 Genomic DNA. Translation: AAP45051.1.
AC092384 Genomic DNA. No translation available.
CH471184 Genomic DNA. Translation: EAW66761.1.
BC107151 mRNA. Translation: AAI07152.1.
BM550173 mRNA. No translation available.
CCDSCCDS32511.1. [P07741-1]
CCDS45546.1. [P07741-2]
PIRRTHUA. S06232.
RefSeqNP_000476.1. NM_000485.2. [P07741-1]
NP_001025189.1. NM_001030018.1. [P07741-2]
UniGeneHs.28914.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OPUmodel-A1-180[»]
1OREX-ray2.10A1-180[»]
1ZN7X-ray1.83A/B1-180[»]
1ZN8X-ray1.76A/B2-180[»]
1ZN9X-ray2.05A/B1-180[»]
ProteinModelPortalP07741.
SMRP07741. Positions 2-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106849. 14 interactions.
IntActP07741. 2 interactions.
MINTMINT-4999823.
STRING9606.ENSP00000367615.

Chemistry

DrugBankDB00173. Adenine.
DB00131. Adenosine monophosphate.

PTM databases

PhosphoSiteP07741.

Polymorphism databases

DMDM114074.

2D gel databases

SWISS-2DPAGEP07741.

Proteomic databases

MaxQBP07741.
PaxDbP07741.
PRIDEP07741.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378364; ENSP00000367615; ENSG00000198931. [P07741-1]
ENST00000426324; ENSP00000397007; ENSG00000198931. [P07741-2]
GeneID353.
KEGGhsa:353.
UCSCuc002flv.3. human. [P07741-1]
uc002flw.3. human.

Organism-specific databases

CTD353.
GeneCardsGC16M088875.
GeneReviewsAPRT.
HGNCHGNC:626. APRT.
HPAHPA026681.
MIM102600. gene.
614723. phenotype.
neXtProtNX_P07741.
Orphanet976. Adenine phosphoribosyltransferase deficiency.
PharmGKBPA24914.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0503.
HOGENOMHOG000036776.
HOVERGENHBG003144.
InParanoidP07741.
KOK00759.
OMATTYSERD.
OrthoDBEOG7FFMT9.
PhylomeDBP07741.
TreeFamTF300227.

Enzyme and pathway databases

BRENDA2.4.2.7. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP07741.
UniPathwayUPA00588; UER00646.

Gene expression databases

ArrayExpressP07741.
BgeeP07741.
CleanExHS_APRT.
GenevestigatorP07741.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
HAMAPMF_00004. Aden_phosphoribosyltr.
InterProIPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01090. apt. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07741.
GeneWikiAdenine_phosphoribosyltransferase.
GenomeRNAi353.
NextBio1453.
PROP07741.
SOURCESearch...

Entry information

Entry nameAPT_HUMAN
AccessionPrimary (citable) accession number: P07741
Secondary accession number(s): G5E9J2, Q3KP55, Q68DF9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 164 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM