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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 By similarity.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi338 – 3381Zinc; catalytic By similarity
Metal bindingi340 – 3401Zinc; catalytic By similarity
Binding sitei340 – 3401Substrate By similarity
Metal bindingi607 – 6071Zinc; catalytic By similarity
Binding sitei610 – 6101Substrate By similarity
Active sitei629 – 6291Proton acceptor By similarity
Metal bindingi684 – 6841Zinc; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. IMP biosynthetic process Source: MGI
  2. IMP salvage Source: UniProtKB-UniPathway
  3. energy homeostasis Source: MGI
  4. 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

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.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9DBT5.
PaxDbiQ9DBT5.
PRIDEiQ9DBT5.

PTM databases

PhosphoSiteiQ9DBT5.

Expressioni

Gene expression databases

ArrayExpressiQ9DBT5.
BgeeiQ9DBT5.
CleanExiMM_AMPD2.
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.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiA2AE28.
KOiK01490.
OrthoDBiEOG70ZZMQ.
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]

Sequencei

Sequence statusi: Complete.

Q9DBT5-1 [UniParc]FASTAAdd to Basket

« Hide

MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF    50
SRSLAESELR SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA 100
KQDFLKTDSD SDLQLYKEQG EGQGDRGLWE RDVVLEREFQ RVIISGEEKC 150
GVPFTDLLDA AKSVVRALFI REKYMALSLQ SFCPTTRRYL QQLAEKPLET 200
RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG LGLRMVRGVV 250
HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ 300
YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL 350
LRFIKRAMKR HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD 400
RNTFHRFDKF NAKYNPIGES VLREIFIKTD NKISGKYFAH IIKEVMADLE 450
ESKYQNAELR LSIYGRSRDE WDKLARWAVN HKVHSPNVRW LVQVPRLFDV 500
YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH VDGFDSVDDE 550
SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH 600
TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI 650
AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY 700
SIATQVWKLS SCDMCELARN SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI 750
RRTNVPDIRV GYRYETLCQE LALITQAVQS EMLETIPEEV GIVMSPGP 798
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 A2AE28.
KOi K01490.
OrthoDBi EOG70ZZMQ.
TreeFami TF300439.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .

Miscellaneous databases

NextBioi 362553.
PROi Q9DBT5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9DBT5.
Bgeei Q9DBT5.
CleanExi MM_AMPD2.
Genevestigatori Q9DBT5.

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

  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.

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: September 3, 2014
This is version 102 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

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