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Protein

Adenine phosphoribosyltransferase

Gene

Aprt

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

Functioni

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.

Catalytic activityi

AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.

Pathway:iAMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from adenine.
Proteins known to be involved in this subpathway in this organism are:
  1. Adenine phosphoribosyltransferase (Aprt)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from adenine, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

GO - Molecular functioni

  • adenine binding Source: MGI
  • adenine phosphoribosyltransferase activity Source: MGI
  • AMP binding Source: MGI

GO - Biological processi

  • adenine metabolic process Source: MGI
  • adenine salvage Source: MGI
  • AMP salvage Source: UniProtKB-UniPathway
  • cellular response to insulin stimulus Source: Ensembl
  • grooming behavior Source: MGI
  • lactation Source: Ensembl
  • purine ribonucleoside salvage Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

ReactomeiREACT_345398. Purine salvage.
UniPathwayiUPA00588; UER00646.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenine phosphoribosyltransferase (EC:2.4.2.7)
Short name:
APRT
Gene namesi
Name:Aprt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88061. Aprt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 180179Adenine phosphoribosyltransferasePRO_0000149506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei60 – 601PhosphotyrosineBy similarity
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei114 – 1141N6-acetyllysineBy similarity
Modified residuei135 – 1351PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08030.
PRIDEiP08030.

PTM databases

PhosphoSiteiP08030.

Expressioni

Gene expression databases

CleanExiMM_APRT.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi198168. 3 interactions.
IntActiP08030. 4 interactions.
MINTiMINT-4088065.
STRINGi10090.ENSMUSP00000006764.

Structurei

3D structure databases

ProteinModelPortaliP08030.
SMRiP08030. Positions 2-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0503.
GeneTreeiENSGT00390000017259.
HOGENOMiHOG000036776.
HOVERGENiHBG003144.
InParanoidiP08030.
KOiK00759.
OMAiPTVWASY.
OrthoDBiEOG7FFMT9.
TreeFamiTF300227.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_00004. Aden_phosphoribosyltr.
InterProiIPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01090. apt. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08030-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPELKLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLASHL
60 70 80 90 100
KSTHSGKIDY IAGLDSRGFL FGPSLAQELG VGCVLIRKQG KLPGPTVSAS
110 120 130 140 150
YSLEYGKAEL EIQKDALEPG QRVVIVDDLL ATGGTMFAAC DLLHQLRAEV
160 170 180
VECVSLVELT SLKGRERLGP IPFFSLLQYD
Length:180
Mass (Da):19,724
Last modified:February 6, 2013 - v2
Checksum:iA6AE4DBE0B456E42
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72LK → FE in BAB22029 (PubMed:16141072).Curated
Sequence conflicti15 – 151S → V in AAA37255 (PubMed:3921964).Curated
Sequence conflicti24 – 241V → A in BAB22029 (PubMed:16141072).Curated
Sequence conflicti46 – 461L → S in BAB22029 (PubMed:16141072).Curated
Sequence conflicti72 – 721G → A in BAB22029 (PubMed:16141072).Curated
Sequence conflicti107 – 1071K → KVR in AAA37256 (PubMed:8433377).Curated
Sequence conflicti135 – 1351T → I in BAD95572 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11310 mRNA. Translation: AAA37255.1.
AB033539 mRNA. Translation: BAD95571.1.
AB033540 mRNA. Translation: BAD95572.1.
AK002350 mRNA. Translation: BAB22029.1.
AK153201 mRNA. Translation: BAE31801.1.
AC114917 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11692.1.
BC005667 mRNA. Translation: AAH05667.1.
M86439 Genomic DNA. Translation: AAA37256.1.
CCDSiCCDS40503.1.
PIRiA22670. RTMSA.
RefSeqiNP_033828.2. NM_009698.2.
UniGeneiMm.1786.

Genome annotation databases

EnsembliENSMUST00000006764; ENSMUSP00000006764; ENSMUSG00000006589.
GeneIDi11821.
KEGGimmu:11821.
UCSCiuc009ntf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11310 mRNA. Translation: AAA37255.1.
AB033539 mRNA. Translation: BAD95571.1.
AB033540 mRNA. Translation: BAD95572.1.
AK002350 mRNA. Translation: BAB22029.1.
AK153201 mRNA. Translation: BAE31801.1.
AC114917 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11692.1.
BC005667 mRNA. Translation: AAH05667.1.
M86439 Genomic DNA. Translation: AAA37256.1.
CCDSiCCDS40503.1.
PIRiA22670. RTMSA.
RefSeqiNP_033828.2. NM_009698.2.
UniGeneiMm.1786.

3D structure databases

ProteinModelPortaliP08030.
SMRiP08030. Positions 2-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198168. 3 interactions.
IntActiP08030. 4 interactions.
MINTiMINT-4088065.
STRINGi10090.ENSMUSP00000006764.

PTM databases

PhosphoSiteiP08030.

Proteomic databases

PaxDbiP08030.
PRIDEiP08030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006764; ENSMUSP00000006764; ENSMUSG00000006589.
GeneIDi11821.
KEGGimmu:11821.
UCSCiuc009ntf.1. mouse.

Organism-specific databases

CTDi353.
MGIiMGI:88061. Aprt.

Phylogenomic databases

eggNOGiCOG0503.
GeneTreeiENSGT00390000017259.
HOGENOMiHOG000036776.
HOVERGENiHBG003144.
InParanoidiP08030.
KOiK00759.
OMAiPTVWASY.
OrthoDBiEOG7FFMT9.
TreeFamiTF300227.

Enzyme and pathway databases

UniPathwayiUPA00588; UER00646.
ReactomeiREACT_345398. Purine salvage.

Miscellaneous databases

ChiTaRSiAprt. mouse.
NextBioi279721.
PROiP08030.
SOURCEiSearch...

Gene expression databases

CleanExiMM_APRT.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_00004. Aden_phosphoribosyltr.
InterProiIPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01090. apt. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and organization of the mouse adenine phosphoribosyltransferase gene: presence of a coding region common to animal and bacterial phosphoribosyltransferases that has a variable intron/exon arrangement."
    Dush M.K., Sikela J.M., Khan S.A., Tischfield J.A., Stambrook P.J.
    Proc. Natl. Acad. Sci. U.S.A. 82:2731-2735(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "mRNA aprt (wild-type allele) in murine SR-1 cell line."
    Fujimori A.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Carcinoma.
  3. "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.
    Tissue: Bone marrow and Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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: FVB/N-3.
    Tissue: Mammary tumor.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Region-specific rates of molecular evolution: a fourfold reduction in the rate of accumulation of 'silent' mutations in transcribed versus nontranscribed regions of homologous DNA fragments derived from two closely related mouse species."
    Turker M.S., Cooper G.E., Bishop P.L.
    J. Mol. Evol. 36:31-40(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-133.
  8. "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-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiAPT_MOUSE
AccessioniPrimary (citable) accession number: P08030
Secondary accession number(s): Q564P4
, Q61319, Q6PK77, Q9DCY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 6, 2013
Last modified: June 24, 2015
This is version 124 of the entry and version 2 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.