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Q01432

- AMPD3_HUMAN

UniProt

Q01432 - AMPD3_HUMAN

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Protein
AMP deaminase 3
Gene
AMPD3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi317 – 3171Zinc; catalytic By similarity
Metal bindingi319 – 3191Zinc; catalytic By similarity
Binding sitei319 – 3191Substrate By similarity
Metal bindingi586 – 5861Zinc; catalytic By similarity
Binding sitei589 – 5891Substrate By similarity
Active sitei608 – 6081Proton acceptor By similarity
Metal bindingi663 – 6631Zinc; catalytic By similarity

GO - Molecular functioni

  1. AMP deaminase activity Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. AMP catabolic process Source: ProtInc
  2. IMP salvage Source: UniProtKB-UniPathway
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. purine nucleobase metabolic process Source: Reactome
  5. purine-containing compound salvage Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1923. Purine salvage.
SABIO-RKQ01432.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 3 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform E
Erythrocyte AMP deaminase
Gene namesi
Name:AMPD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:470. AMPD3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti310 – 3101N → K in AMPDDE. 1 Publication
VAR_042606
Natural varianti311 – 3111V → L in AMPDDE. 1 Publication
Corresponds to variant rs117706710 [ dbSNP | Ensembl ].
VAR_042607
Natural varianti320 – 3201A → V in AMPDDE. 1 Publication
VAR_042608
Natural varianti324 – 3241M → T in AMPDDE. 1 Publication
VAR_042609
Natural varianti331 – 3311R → C in AMPDDE. 1 Publication
VAR_042610
Natural varianti402 – 4021R → C in AMPDDE. 1 Publication
VAR_042611
Natural varianti450 – 4501W → R in AMPDDE. 2 Publications
VAR_042612
Natural varianti573 – 5731R → C in AMPDDE; enzyme inactive. 1 Publication
Corresponds to variant rs3741040 [ dbSNP | Ensembl ].
VAR_009881
Natural varianti585 – 5851P → L in AMPDDE. 1 Publication
VAR_042614
Natural varianti712 – 7121Q → P in AMPDDE. 1 Publication
VAR_042615

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi612874. phenotype.
Orphaneti45. Adenosine monophosphate deaminase deficiency.
PharmGKBiPA24778.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767AMP deaminase 3
PRO_0000194410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01432.
PaxDbiQ01432.
PRIDEiQ01432.

PTM databases

PhosphoSiteiQ01432.

Expressioni

Tissue specificityi

Isoform 1 is 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.

Gene expression databases

ArrayExpressiQ01432.
BgeeiQ01432.
CleanExiHS_AMPD3.
GenevestigatoriQ01432.

Organism-specific databases

HPAiHPA047408.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106769. 3 interactions.
IntActiQ01432. 2 interactions.
STRINGi9606.ENSP00000256183.

Structurei

3D structure databases

ProteinModelPortaliQ01432.
SMRiQ01432. Positions 219-762.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni388 – 3936Substrate binding By similarity
Regioni664 – 6674Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ01432.
KOiK01490.
OMAiFSLHEML.
OrthoDBiEOG70ZZMQ.
PhylomeDBiQ01432.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1B (identifier: Q01432-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPRQFPKLNI SEVDEQVRLL AEKVFAKVLR EEDSKDALSL FTVPEDCPIG    50
QKEAKERELQ KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PPQQDWKGPP 100
AASPAMSPTT PVVTGATSLP TPAPYAMPEF QRVTISGDYC AGITLEDYEQ 150
AAKSLAKALM IREKYARLAY HRFPRITSQY LGHPRADTAP PEEGLPDFHP 200
PPLPQEDPYC LDDAPPNLDY LVHMQGGILF VYDNKKMLEH QEPHSLPYPD 250
LETYTVDMSH ILALITDGPT KTYCHRRLNF LESKFSLHEM LNEMSEFKEL 300
KSNPHRDFYN VRKVDTHIHA AACMNQKHLL RFIKHTYQTE PDRTVAEKRG 350
RKITLRQVFD GLHMDPYDLT VDSLDVHAGR QTFHRFDKFN SKYNPVGASE 400
LRDLYLKTEN YLGGEYFARM VKEVARELEE SKYQYSEPRL SIYGRSPEEW 450
PNLAYWFIQH KVYSPNMRWI IQVPRIYDIF RSKKLLPNFG KMLENIFLPL 500
FKATINPQDH RELHLFLKYV TGFDSVDDES KHSDHMFSDK SPNPDVWTSE 550
QNPPYSYYLY YMYANIMVLN NLRRERGLST FLFRPHCGEA GSITHLVSAF 600
LTADNISHGL LLKKSPVLQY LYYLAQIPIA MSPLSNNSLF LEYSKNPLRE 650
FLHKGLHVSL STDDPMQFHY TKEALMEEYA IAAQVWKLST CDLCEIARNS 700
VLQSGLSHQE KQKFLGQNYY KEGPEGNDIR KTNVAQIRMA FRYETLCNEL 750
SFLSDAMKSE EITALTN 767
Length:767
Mass (Da):88,812
Last modified:July 1, 1993 - v1
Checksum:i2E0A2C629003B98C
GO
Isoform 1A (identifier: Q01432-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM
     208-767: Missing.

Show »
Length:216
Mass (Da):24,119
Checksum:i77821100D9737811
GO
Isoform 1C (identifier: Q01432-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM
     652-767: Missing.

Show »
Length:658
Mass (Da):76,269
Checksum:i0FDFC779DC4996F2
GO
Isoform 2 (identifier: Q01432-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALSSEPAEM

Show »
Length:776
Mass (Da):89,728
Checksum:i53FFE0714FC9BC45
GO
Isoform 3 (identifier: Q01432-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPGSAEM

Show »
Length:774
Mass (Da):89,514
Checksum:i208BFD79F9053BA2
GO
Isoform 4 (identifier: Q01432-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:608
Mass (Da):71,222
Checksum:i04814500471AE377
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851R → W.
Corresponds to variant rs11042836 [ dbSNP | Ensembl ].
VAR_033499
Natural varianti310 – 3101N → K in AMPDDE. 1 Publication
VAR_042606
Natural varianti311 – 3111V → L in AMPDDE. 1 Publication
Corresponds to variant rs117706710 [ dbSNP | Ensembl ].
VAR_042607
Natural varianti320 – 3201A → V in AMPDDE. 1 Publication
VAR_042608
Natural varianti324 – 3241M → T in AMPDDE. 1 Publication
VAR_042609
Natural varianti331 – 3311R → C in AMPDDE. 1 Publication
VAR_042610
Natural varianti402 – 4021R → C in AMPDDE. 1 Publication
VAR_042611
Natural varianti450 – 4501W → R in AMPDDE. 2 Publications
VAR_042612
Natural varianti455 – 4551Y → H.
Corresponds to variant rs36003153 [ dbSNP | Ensembl ].
VAR_042613
Natural varianti573 – 5731R → C in AMPDDE; enzyme inactive. 1 Publication
Corresponds to variant rs3741040 [ dbSNP | Ensembl ].
VAR_009881
Natural varianti585 – 5851P → L in AMPDDE. 1 Publication
VAR_042614
Natural varianti712 – 7121Q → P in AMPDDE. 1 Publication
VAR_042615

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 159159Missing in isoform 4.
VSP_044230Add
BLAST
Alternative sequencei1 – 11M → MALSSEPAEM in isoform 1A and isoform 2.
VSP_001275
Alternative sequencei1 – 11M → MEPGSAEM in isoform 1C and isoform 3.
VSP_001276
Alternative sequencei208 – 767560Missing in isoform 1A.
VSP_001277Add
BLAST
Alternative sequencei652 – 767116Missing in isoform 1C.
VSP_001278Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12775 mRNA. Translation: BAA02240.1.
M84720 mRNA. Translation: AAA58365.1.
M84721 mRNA. Translation: AAA58366.1.
M84722 mRNA. Translation: AAA58367.1.
U29926
, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60410.1.
U29926
, U29912, U29929, U29907, U29909, U29910, U29911, U29916, U29917, U29918, U29922, U29924, U29925 Genomic DNA. Translation: AAB60408.1.
U29926
, 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.
CCDSiCCDS41617.1. [Q01432-1]
CCDS44537.1. [Q01432-5]
CCDS53601.1. [Q01432-6]
CCDS7802.1. [Q01432-4]
PIRiS68146.
S68147.
RefSeqiNP_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]
UniGeneiHs.501890.

Genome annotation databases

EnsembliENST00000396553; ENSP00000379801; ENSG00000133805. [Q01432-1]
ENST00000396554; ENSP00000379802; ENSG00000133805. [Q01432-4]
ENST00000444303; ENSP00000396000; ENSG00000133805. [Q01432-6]
ENST00000528723; ENSP00000436987; ENSG00000133805. [Q01432-5]
ENST00000529507; ENSP00000431648; ENSG00000133805. [Q01432-1]
GeneIDi272.
KEGGihsa:272.
UCSCiuc001min.1. human. [Q01432-4]
uc001mio.1. human. [Q01432-1]
uc001mip.1. human. [Q01432-5]

Polymorphism databases

DMDMi399033.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12775 mRNA. Translation: BAA02240.1 .
M84720 mRNA. Translation: AAA58365.1 .
M84721 mRNA. Translation: AAA58366.1 .
M84722 mRNA. Translation: AAA58367.1 .
U29926
, U29929 , U29907 , U29909 , U29910 , U29911 , U29916 , U29917 , U29918 , U29922 , U29924 , U29925 Genomic DNA. Translation: AAB60410.1 .
U29926
, U29912 , U29929 , U29907 , U29909 , U29910 , U29911 , U29916 , U29917 , U29918 , U29922 , U29924 , U29925 Genomic DNA. Translation: AAB60408.1 .
U29926
, 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 .
CCDSi CCDS41617.1. [Q01432-1 ]
CCDS44537.1. [Q01432-5 ]
CCDS53601.1. [Q01432-6 ]
CCDS7802.1. [Q01432-4 ]
PIRi S68146.
S68147.
RefSeqi NP_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 ]
UniGenei Hs.501890.

3D structure databases

ProteinModelPortali Q01432.
SMRi Q01432. Positions 219-762.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106769. 3 interactions.
IntActi Q01432. 2 interactions.
STRINGi 9606.ENSP00000256183.

Chemistry

BindingDBi Q01432.
ChEMBLi CHEMBL2912.

PTM databases

PhosphoSitei Q01432.

Polymorphism databases

DMDMi 399033.

Proteomic databases

MaxQBi Q01432.
PaxDbi Q01432.
PRIDEi Q01432.

Protocols and materials databases

DNASUi 272.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396553 ; ENSP00000379801 ; ENSG00000133805 . [Q01432-1 ]
ENST00000396554 ; ENSP00000379802 ; ENSG00000133805 . [Q01432-4 ]
ENST00000444303 ; ENSP00000396000 ; ENSG00000133805 . [Q01432-6 ]
ENST00000528723 ; ENSP00000436987 ; ENSG00000133805 . [Q01432-5 ]
ENST00000529507 ; ENSP00000431648 ; ENSG00000133805 . [Q01432-1 ]
GeneIDi 272.
KEGGi hsa:272.
UCSCi uc001min.1. human. [Q01432-4 ]
uc001mio.1. human. [Q01432-1 ]
uc001mip.1. human. [Q01432-5 ]

Organism-specific databases

CTDi 272.
GeneCardsi GC11P010329.
HGNCi HGNC:470. AMPD3.
HPAi HPA047408.
MIMi 102772. gene.
612874. phenotype.
neXtProti NX_Q01432.
Orphaneti 45. Adenosine monophosphate deaminase deficiency.
PharmGKBi PA24778.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1816.
HOGENOMi HOG000092200.
HOVERGENi HBG050494.
InParanoidi Q01432.
KOi K01490.
OMAi FSLHEML.
OrthoDBi EOG70ZZMQ.
PhylomeDBi Q01432.
TreeFami TF300439.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .
Reactomei REACT_1923. Purine salvage.
SABIO-RK Q01432.

Miscellaneous databases

ChiTaRSi AMPD3. human.
GeneWikii AMPD3.
GenomeRNAii 272.
NextBioi 1073.
PROi Q01432.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01432.
Bgeei Q01432.
CleanExi HS_AMPD3.
Genevestigatori Q01432.

Family and domain databases

InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
[Graphical view ]
PANTHERi PTHR11359. PTHR11359. 1 hit.
Pfami PF00962. A_deaminase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
PROSITEi PS00485. A_DEAMINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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.

Entry informationi

Entry nameiAMPD3_HUMAN
AccessioniPrimary (citable) accession number: Q01432
Secondary accession number(s): A0AUX0
, B7Z2S2, B7Z763, B7Z877
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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