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Protein

AMP deaminase 2

Gene

Ampd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle (By similarity).By similarity

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi338 – 3381Zinc; catalyticBy similarity
Metal bindingi340 – 3401Zinc; catalyticBy similarity
Binding sitei340 – 3401SubstrateBy similarity
Metal bindingi607 – 6071Zinc; catalyticBy similarity
Binding sitei610 – 6101SubstrateBy similarity
Active sitei629 – 6291Proton acceptorPROSITE-ProRule annotation
Metal bindingi684 – 6841Zinc; catalyticBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cyclic purine nucleotide metabolic process Source: UniProtKB
  2. energy homeostasis Source: MGI
  3. IMP biosynthetic process Source: MGI
  4. IMP salvage Source: UniProtKB-UniPathway
  5. nucleotide metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_244050. Purine salvage.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 2 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform L
Gene namesi
Name:Ampd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:88016. Ampd2.

Pathology & Biotechi

Disruption phenotypei

Mice have normal brain histology.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798AMP deaminase 2PRO_0000194408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei64 – 641Phosphotyrosine1 Publication
Modified residuei70 – 701PhosphoserineBy similarity
Modified residuei87 – 871Phosphoserine2 Publications
Modified residuei107 – 1071PhosphothreonineBy similarity
Modified residuei109 – 1091Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9DBT5.
PaxDbiQ9DBT5.
PRIDEiQ9DBT5.

PTM databases

PhosphoSiteiQ9DBT5.

Expressioni

Gene expression databases

BgeeiQ9DBT5.
CleanExiMM_AMPD2.
ExpressionAtlasiQ9DBT5. baseline and differential.
GenevestigatoriQ9DBT5.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9DBT5. 1 interaction.
MINTiMINT-4616236.

Structurei

3D structure databases

ProteinModelPortaliQ9DBT5.
SMRiQ9DBT5. Positions 226-763.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni409 – 4146Substrate bindingBy similarity
Regioni685 – 6884Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ9DBT5.
KOiK01490.
OrthoDBiEOG70ZZMQ.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 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]

Sequencei

Sequence statusi: Complete.

Q9DBT5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF
60 70 80 90 100
SRSLAESELR SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA
110 120 130 140 150
KQDFLKTDSD SDLQLYKEQG EGQGDRGLWE RDVVLEREFQ RVIISGEEKC
160 170 180 190 200
GVPFTDLLDA AKSVVRALFI REKYMALSLQ SFCPTTRRYL QQLAEKPLET
210 220 230 240 250
RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG LGLRMVRGVV
260 270 280 290 300
HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ
310 320 330 340 350
YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL
360 370 380 390 400
LRFIKRAMKR HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD
410 420 430 440 450
RNTFHRFDKF NAKYNPIGES VLREIFIKTD NKISGKYFAH IIKEVMADLE
460 470 480 490 500
ESKYQNAELR LSIYGRSRDE WDKLARWAVN HKVHSPNVRW LVQVPRLFDV
510 520 530 540 550
YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH VDGFDSVDDE
560 570 580 590 600
SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH
610 620 630 640 650
TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI
660 670 680 690 700
AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY
710 720 730 740 750
SIATQVWKLS SCDMCELARN SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI
760 770 780 790
RRTNVPDIRV GYRYETLCQE LALITQAVQS EMLETIPEEV GIVMSPGP
Length:798
Mass (Da):92,024
Last modified:June 1, 2001 - v1
Checksum:i2BC4F37E4006C7D5
GO

Sequence cautioni

The sequence AAH16662.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004759 mRNA. Translation: BAB23540.1.
AK169980 mRNA. Translation: BAE41495.1.
AL671854 Genomic DNA. Translation: CAM27248.1.
BC016662 mRNA. Translation: AAH16662.2. Different initiation.
BC049119 mRNA. Translation: AAH49119.1.
CCDSiCCDS17749.1.
RefSeqiNP_001276648.1. NM_001289719.1.
NP_001276649.1. NM_001289720.1.
NP_083055.1. NM_028779.5.
UniGeneiMm.274335.
Mm.487815.

Genome annotation databases

EnsembliENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889.
ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889.
GeneIDi109674.
KEGGimmu:109674.
UCSCiuc008qxz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004759 mRNA. Translation: BAB23540.1.
AK169980 mRNA. Translation: BAE41495.1.
AL671854 Genomic DNA. Translation: CAM27248.1.
BC016662 mRNA. Translation: AAH16662.2. Different initiation.
BC049119 mRNA. Translation: AAH49119.1.
CCDSiCCDS17749.1.
RefSeqiNP_001276648.1. NM_001289719.1.
NP_001276649.1. NM_001289720.1.
NP_083055.1. NM_028779.5.
UniGeneiMm.274335.
Mm.487815.

3D structure databases

ProteinModelPortaliQ9DBT5.
SMRiQ9DBT5. Positions 226-763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBT5. 1 interaction.
MINTiMINT-4616236.

PTM databases

PhosphoSiteiQ9DBT5.

Proteomic databases

MaxQBiQ9DBT5.
PaxDbiQ9DBT5.
PRIDEiQ9DBT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889.
ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889.
GeneIDi109674.
KEGGimmu:109674.
UCSCiuc008qxz.1. mouse.

Organism-specific databases

CTDi271.
MGIiMGI:88016. Ampd2.

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiQ9DBT5.
KOiK01490.
OrthoDBiEOG70ZZMQ.
TreeFamiTF300439.

Enzyme and pathway databases

UniPathwayiUPA00591; UER00663.
ReactomeiREACT_244050. Purine salvage.

Miscellaneous databases

NextBioi362553.
PROiQ9DBT5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBT5.
CleanExiMM_AMPD2.
ExpressionAtlasiQ9DBT5. baseline and differential.
GenevestigatoriQ9DBT5.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiAMPD2_MOUSE
AccessioniPrimary (citable) accession number: Q9DBT5
Secondary accession number(s): A2AE28, Q91YI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.