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Q9DBT5

- AMPD2_MOUSE

UniProt

Q9DBT5 - AMPD2_MOUSE

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Protein

AMP deaminase 2

Gene

Ampd2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 .
CCDSi CCDS17749.1.
RefSeqi NP_001276648.1. NM_001289719.1.
NP_001276649.1. NM_001289720.1.
NP_083055.1. NM_028779.5.
UniGenei Mm.274335.
Mm.487815.

3D structure databases

ProteinModelPortali Q9DBT5.
SMRi Q9DBT5. Positions 226-763.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9DBT5. 1 interaction.
MINTi MINT-4616236.

PTM databases

PhosphoSitei Q9DBT5.

Proteomic databases

MaxQBi Q9DBT5.
PaxDbi Q9DBT5.
PRIDEi Q9DBT5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102637 ; ENSMUSP00000099697 ; ENSMUSG00000027889 .
ENSMUST00000102638 ; ENSMUSP00000099698 ; ENSMUSG00000027889 .
GeneIDi 109674.
KEGGi mmu:109674.
UCSCi uc008qxz.1. mouse.

Organism-specific databases

CTDi 271.
MGIi MGI:88016. Ampd2.

Phylogenomic databases

eggNOGi COG1816.
GeneTreei ENSGT00390000008190.
HOGENOMi HOG000092200.
HOVERGENi HBG050494.
InParanoidi Q9DBT5.
KOi K01490.
OrthoDBi EOG70ZZMQ.
TreeFami TF300439.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .
Reactomei REACT_244050. Purine salvage.

Miscellaneous databases

NextBioi 362553.
PROi Q9DBT5.
SOURCEi Search...

Gene expression databases

Bgeei Q9DBT5.
CleanExi MM_AMPD2.
ExpressionAtlasi Q9DBT5. baseline and differential.
Genevestigatori Q9DBT5.

Family and domain databases

InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029749. AMPD2.
[Graphical view ]
PANTHERi PTHR11359. PTHR11359. 1 hit.
PTHR11359:SF3. PTHR11359:SF3. 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. "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: November 26, 2014
This is version 105 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