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Q01432 (AMPD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. 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:
AMP deaminase 3

EC=3.5.4.6
Alternative name(s):
AMP deaminase isoform E
Erythrocyte AMP deaminase
Gene names
Name:AMPD3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AMP deaminase plays a critical role in energy metabolism.

Catalytic activity

AMP + H2O = IMP + NH3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1.

Subunit structure

Homotetramer.

Tissue specificity

Isoform 1is the predominant form in skeletal muscle; Isoform 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; Isoform 3 is found in erythrocytes.

Involvement in disease

Adenosine monophosphate deaminase deficiency erythrocyte type (AMPDDE) [MIM:612874]: A metabolic disorder due to lack of activity of the erythrocyte isoform of AMP deaminase. It is a clinically asymptomatic condition characterized by a 50% increase in steady-state levels of ATP in affected cells. Individuals with complete deficiency of erythrocyte AMP deaminase are healthy and have no hematologic disorders.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1B (identifier: Q01432-1)

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 1A (identifier: Q01432-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM
     208-767: Missing.
Isoform 1C (identifier: Q01432-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM
     652-767: Missing.
Isoform 2 (identifier: Q01432-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM
Isoform 3 (identifier: Q01432-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM
Isoform 4 (identifier: Q01432-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 767767AMP deaminase 3
PRO_0000194410

Regions

Region388 – 3936Substrate binding By similarity
Region664 – 6674Substrate binding By similarity

Sites

Active site6081Proton acceptor By similarity
Metal binding3171Zinc; catalytic By similarity
Metal binding3191Zinc; catalytic By similarity
Metal binding5861Zinc; catalytic By similarity
Metal binding6631Zinc; catalytic By similarity
Binding site3191Substrate By similarity
Binding site5891Substrate By similarity

Amino acid modifications

Modified residue1071Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 159159Missing in isoform 4.
VSP_044230
Alternative sequence11M → MALSSEPAEM in isoform 1A and isoform 2.
VSP_001275
Alternative sequence11M → MEPGSAEM in isoform 1C and isoform 3.
VSP_001276
Alternative sequence208 – 767560Missing in isoform 1A.
VSP_001277
Alternative sequence652 – 767116Missing in isoform 1C.
VSP_001278
Natural variant1851R → W.
Corresponds to variant rs11042836 [ dbSNP | Ensembl ].
VAR_033499
Natural variant3101N → K in AMPDDE. Ref.10
VAR_042606
Natural variant3111V → L in AMPDDE. Ref.11
Corresponds to variant rs117706710 [ dbSNP | Ensembl ].
VAR_042607
Natural variant3201A → V in AMPDDE. Ref.10
VAR_042608
Natural variant3241M → T in AMPDDE. Ref.10
VAR_042609
Natural variant3311R → C in AMPDDE. Ref.10
VAR_042610
Natural variant4021R → C in AMPDDE. Ref.10
VAR_042611
Natural variant4501W → R in AMPDDE. Ref.10 Ref.12
VAR_042612
Natural variant4551Y → H.
Corresponds to variant rs36003153 [ dbSNP | Ensembl ].
VAR_042613
Natural variant5731R → C in AMPDDE; enzyme inactive. Ref.4
Corresponds to variant rs3741040 [ dbSNP | Ensembl ].
VAR_009881
Natural variant5851P → L in AMPDDE. Ref.10
VAR_042614
Natural variant7121Q → P in AMPDDE. Ref.12
VAR_042615

Sequences

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

Last modified July 1, 1993. Version 1.
Checksum: 2E0A2C629003B98C

FASTA76788,812
        10         20         30         40         50         60 
MPRQFPKLNI SEVDEQVRLL AEKVFAKVLR EEDSKDALSL FTVPEDCPIG QKEAKERELQ 

        70         80         90        100        110        120 
KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PPQQDWKGPP AASPAMSPTT PVVTGATSLP 

       130        140        150        160        170        180 
TPAPYAMPEF QRVTISGDYC AGITLEDYEQ AAKSLAKALM IREKYARLAY HRFPRITSQY 

       190        200        210        220        230        240 
LGHPRADTAP PEEGLPDFHP PPLPQEDPYC LDDAPPNLDY LVHMQGGILF VYDNKKMLEH 

       250        260        270        280        290        300 
QEPHSLPYPD LETYTVDMSH ILALITDGPT KTYCHRRLNF LESKFSLHEM LNEMSEFKEL 

       310        320        330        340        350        360 
KSNPHRDFYN VRKVDTHIHA AACMNQKHLL RFIKHTYQTE PDRTVAEKRG RKITLRQVFD 

       370        380        390        400        410        420 
GLHMDPYDLT VDSLDVHAGR QTFHRFDKFN SKYNPVGASE LRDLYLKTEN YLGGEYFARM 

       430        440        450        460        470        480 
VKEVARELEE SKYQYSEPRL SIYGRSPEEW PNLAYWFIQH KVYSPNMRWI IQVPRIYDIF 

       490        500        510        520        530        540 
RSKKLLPNFG KMLENIFLPL FKATINPQDH RELHLFLKYV TGFDSVDDES KHSDHMFSDK 

       550        560        570        580        590        600 
SPNPDVWTSE QNPPYSYYLY YMYANIMVLN NLRRERGLST FLFRPHCGEA GSITHLVSAF 

       610        620        630        640        650        660 
LTADNISHGL LLKKSPVLQY LYYLAQIPIA MSPLSNNSLF LEYSKNPLRE FLHKGLHVSL 

       670        680        690        700        710        720 
STDDPMQFHY TKEALMEEYA IAAQVWKLST CDLCEIARNS VLQSGLSHQE KQKFLGQNYY 

       730        740        750        760 
KEGPEGNDIR KTNVAQIRMA FRYETLCNEL SFLSDAMKSE EITALTN 

« Hide

Isoform 1A [UniParc].

Checksum: 77821100D9737811
Show »

FASTA21624,119
Isoform 1C [UniParc].

Checksum: 0FDFC779DC4996F2
Show »

FASTA65876,269
Isoform 2 [UniParc].

Checksum: 53FFE0714FC9BC45
Show »

FASTA77689,728
Isoform 3 [UniParc].

Checksum: 208BFD79F9053BA2
Show »

FASTA77489,514
Isoform 4 [UniParc].

Checksum: 04814500471AE377
Show »

FASTA60871,222

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the cDNA encoding human erythrocyte-specific AMP deaminase."
Yamada Y., Goto H., Ogasawara N.
Biochim. Biophys. Acta 1171:125-128(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1B).
[2]"Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons."
Mahnke-Zizelman D.K., Sabina R.L.
J. Biol. Chem. 267:20866-20877(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C).
Tissue: Keratinocyte.
[3]"Characterization of the human AMPD3 gene reveals that 5' exon useage is subject to transcriptional control by three tandem promoters and alternative splicing."
Mahnke-Zizelman D.K., Eddy R., Shows T.B., Sabina R.L.
Biochim. Biophys. Acta 1306:75-92(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1B; 2 AND 3), ALTERNATIVE SPLICING.
[4]"A point mutation responsible for human erythrocyte AMP deaminase deficiency."
Yamada Y., Goto H., Ogasawara N.
Hum. Mol. Genet. 3:331-334(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1B), VARIANT AMPDDE CYS-573.
[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] (ISOFORMS 1B; 2; 3 AND 4).
Tissue: Brain, Synovium and Testis.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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).
[9]"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-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Molecular basis for human erythrocyte AMP deaminase deficiency: screening for the major point mutation and identification of other mutations."
Yamada Y., Goto H., Murase T., Ogasawara N.
Hum. Mol. Genet. 3:2243-2245(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMPDDE LYS-310; VAL-320; THR-324; CYS-331; CYS-402; ARG-450 AND LEU-585.
[11]"Gene mutations responsible for human erythrocyte AMP deaminase deficiency in Poles."
Yamada Y., Makarewicz W., Goto H., Nomura N., Kitoh H., Ogasawara N.
Adv. Exp. Med. Biol. 431:347-350(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMPDDE LEU-311.
[12]"A rare case of complete human erythrocyte AMP deaminase deficiency due to two novel missense mutations in AMPD3."
Yamada Y., Goto H., Wakamatsu N., Ogasawara N.
Hum. Mutat. 17:78-78(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMPDDE ARG-450 AND PRO-712.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D12775 mRNA. Translation: BAA02240.1.
M84720 mRNA. Translation: AAA58365.1.
M84721 mRNA. Translation: AAA58366.1.
M84722 mRNA. Translation: AAA58367.1.
U29926 expand/collapse EMBL AC list , U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60410.1.
U29926 expand/collapse EMBL AC list , U29912, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60408.1.
U29926 expand/collapse EMBL AC list , U29927, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60409.1.
D31646 Genomic DNA. Translation: BAA06505.1.
AK289998 mRNA. Translation: BAF82687.1.
AK295046 mRNA. Translation: BAH11958.1.
AK301507 mRNA. Translation: BAH13499.1.
AK302970 mRNA. Translation: BAH13863.1.
AC084117 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68567.1.
CH471064 Genomic DNA. Translation: EAW68568.1.
CH471064 Genomic DNA. Translation: EAW68569.1.
BC126118 mRNA. Translation: AAI26119.1.
CCDSCCDS41617.1. [Q01432-1]
CCDS44537.1. [Q01432-5]
CCDS53601.1. [Q01432-6]
CCDS7802.1. [Q01432-4]
PIRS68146.
S68147.
RefSeqNP_000471.1. NM_000480.2. [Q01432-4]
NP_001020560.1. NM_001025389.1. [Q01432-1]
NP_001020561.1. NM_001025390.1. [Q01432-5]
NP_001165901.1. NM_001172430.1. [Q01432-1]
NP_001165902.1. NM_001172431.1. [Q01432-6]
UniGeneHs.501890.

3D structure databases

ProteinModelPortalQ01432.
SMRQ01432. Positions 219-762.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106769. 3 interactions.
IntActQ01432. 2 interactions.
STRING9606.ENSP00000256183.

Chemistry

BindingDBQ01432.
ChEMBLCHEMBL2912.

PTM databases

PhosphoSiteQ01432.

Polymorphism databases

DMDM399033.

Proteomic databases

MaxQBQ01432.
PaxDbQ01432.
PRIDEQ01432.

Protocols and materials databases

DNASU272.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396553; ENSP00000379801; ENSG00000133805. [Q01432-1]
ENST00000396554; ENSP00000379802; ENSG00000133805. [Q01432-4]
ENST00000444303; ENSP00000396000; ENSG00000133805. [Q01432-6]
ENST00000528723; ENSP00000436987; ENSG00000133805. [Q01432-5]
ENST00000529507; ENSP00000431648; ENSG00000133805. [Q01432-1]
GeneID272.
KEGGhsa:272.
UCSCuc001min.1. human. [Q01432-4]
uc001mio.1. human. [Q01432-1]
uc001mip.1. human. [Q01432-5]

Organism-specific databases

CTD272.
GeneCardsGC11P010329.
HGNCHGNC:470. AMPD3.
HPAHPA047408.
MIM102772. gene.
612874. phenotype.
neXtProtNX_Q01432.
Orphanet45. Adenosine monophosphate deaminase deficiency.
PharmGKBPA24778.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000092200.
HOVERGENHBG050494.
InParanoidQ01432.
KOK01490.
OMAFSLHEML.
OrthoDBEOG70ZZMQ.
PhylomeDBQ01432.
TreeFamTF300439.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKQ01432.
UniPathwayUPA00591; UER00663.

Gene expression databases

ArrayExpressQ01432.
BgeeQ01432.
CleanExHS_AMPD3.
GenevestigatorQ01432.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
PANTHERPTHR11359. PTHR11359. 1 hit.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsTIGR01429. AMP_deaminase. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAMPD3. human.
GeneWikiAMPD3.
GenomeRNAi272.
NextBio1073.
PROQ01432.
SOURCESearch...

Entry information

Entry nameAMPD3_HUMAN
AccessionPrimary (citable) accession number: Q01432
Secondary accession number(s): A0AUX0 expand/collapse secondary AC list , B7Z2S2, B7Z763, B7Z877
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 139 of the entry and version 1 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 11

Human chromosome 11: entries, gene names and cross-references to MIM