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Q9DBT5 (AMPD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP deaminase 2
EC=3.5.4.6
Alternative name(s):
AMP deaminase isoform L
Gene names
Name:Ampd2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length798 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AMP deaminase plays a critical role in energy metabolism By similarity.

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 By similarity.

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Sequence caution

The sequence AAH16662.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 798798AMP deaminase 2
PRO_0000194408

Regions

Region409 – 4146Substrate binding By similarity
Region685 – 6884Substrate binding By similarity

Sites

Active site6291Proton acceptor By similarity
Metal binding3381Zinc; catalytic By similarity
Metal binding3401Zinc; catalytic By similarity
Metal binding6071Zinc; catalytic By similarity
Metal binding6841Zinc; catalytic By similarity
Binding site3401Substrate By similarity
Binding site6101Substrate By similarity

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue371Phosphoserine By similarity
Modified residue641Phosphotyrosine Ref.4
Modified residue701Phosphoserine By similarity
Modified residue871Phosphoserine Ref.6
Modified residue1091Phosphoserine By similarity
Modified residue1111Phosphoserine Ref.5
Modified residue4141Phosphotyrosine By similarity
Modified residue4201Phosphoserine By similarity
Modified residue4361N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DBT5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2BC4F37E4006C7D5

FASTA79892,024
        10         20         30         40         50         60 
MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF SRSLAESELR 

        70         80         90        100        110        120 
SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA KQDFLKTDSD SDLQLYKEQG 

       130        140        150        160        170        180 
EGQGDRGLWE RDVVLEREFQ RVIISGEEKC GVPFTDLLDA AKSVVRALFI REKYMALSLQ 

       190        200        210        220        230        240 
SFCPTTRRYL QQLAEKPLET RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG 

       250        260        270        280        290        300 
LGLRMVRGVV HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ 

       310        320        330        340        350        360 
YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL LRFIKRAMKR 

       370        380        390        400        410        420 
HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD RNTFHRFDKF NAKYNPIGES 

       430        440        450        460        470        480 
VLREIFIKTD NKISGKYFAH IIKEVMADLE ESKYQNAELR LSIYGRSRDE WDKLARWAVN 

       490        500        510        520        530        540 
HKVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH 

       550        560        570        580        590        600 
VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH 

       610        620        630        640        650        660 
TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI AMSPLSNNSL 

       670        680        690        700        710        720 
FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIATQVWKLS SCDMCELARN 

       730        740        750        760        770        780 
SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV GYRYETLCQE LALITQAVQS 

       790 
EMLETIPEEV GIVMSPGP

« Hide

References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Lung.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[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: 15489334] [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: 17947660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, MASS SPECTROMETRY.
Tissue: Mast cell.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, MASS SPECTROMETRY.
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: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00406639.
RefSeqNP_083055.1. NM_028779.4.
UniGeneMm.274335.

3D structure databases

ProteinModelPortalQ9DBT5.
SMRQ9DBT5. Positions 137-784.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DBT5.

PTM databases

PhosphoSiteQ9DBT5.

Proteomic databases

PRIDEQ9DBT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889.
ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889.
GeneID109674.
KEGGmmu:109674.
UCSCuc008qxz.1. mouse.

Organism-specific databases

CTD271.
MGIMGI:88016. Ampd2.

Phylogenomic databases

GeneTreeENSGT00390000008190.
HOGENOMHBG713563.
HOVERGENHBG050494.
InParanoidQ9DBT5.
OrthoDBEOG41JZBP.
PhylomeDBQ9DBT5.

Gene expression databases

ArrayExpressQ9DBT5.
BgeeQ9DBT5.
CleanExMM_AMPD2.
GenevestigatorQ9DBT5.
GermOnlineENSMUSG00000027889. Mus musculus.

Family and domain databases

InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMP_deaminase.
[Graphical view]
KOK01490.
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

NextBio362553.
SOURCESearch...

Entry information

Entry nameAMPD2_MOUSE
AccessionPrimary (citable) accession number: Q9DBT5
Secondary accession number(s): A2AE28, Q91YI2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2001
Last modified: December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents