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P08030 (APT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. 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

Names and origin

Protein namesRecommended name:
Adenine phosphoribosyltransferase

Short name=APRT
EC=2.4.2.7
Gene names
Name:Aprt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. HAMAP-Rule MF_00004

Catalytic activity

AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00004

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. HAMAP-Rule MF_00004

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00004.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 180179Adenine phosphoribosyltransferase HAMAP-Rule MF_00004
PRO_0000149506

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue151Phosphoserine Ref.8
Modified residue601Phosphotyrosine By similarity
Modified residue661Phosphoserine By similarity
Modified residue1141N6-acetyllysine By similarity
Modified residue1351Phosphothreonine By similarity

Experimental info

Sequence conflict6 – 72LK → FE in BAB22029. Ref.3
Sequence conflict151S → V in AAA37255. Ref.1
Sequence conflict241V → A in BAB22029. Ref.3
Sequence conflict461L → S in BAB22029. Ref.3
Sequence conflict721G → A in BAB22029. Ref.3
Sequence conflict1071K → KVR in AAA37256. Ref.7
Sequence conflict1351T → I in BAD95572. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08030 [UniParc].

Last modified February 6, 2013. Version 2.
Checksum: A6AE4DBE0B456E42

FASTA18019,724
        10         20         30         40         50         60 
MSEPELKLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLASHL KSTHSGKIDY 

        70         80         90        100        110        120 
IAGLDSRGFL FGPSLAQELG VGCVLIRKQG KLPGPTVSAS YSLEYGKAEL EIQKDALEPG 

       130        140        150        160        170        180 
QRVVIVDDLL ATGGTMFAAC DLLHQLRAEV VECVSLVELT SLKGRERLGP IPFFSLLQYD 

« Hide

References

« Hide 'large scale' references
[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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow and Kidney.
[4]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40503.1.
PIRRTMSA. A22670.
RefSeqNP_033828.2. NM_009698.2.
UniGeneMm.1786.

3D structure databases

ProteinModelPortalP08030.
SMRP08030. Positions 2-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08030. 4 interactions.
MINTMINT-4088065.
STRING10090.ENSMUSP00000006764.

PTM databases

PhosphoSiteP08030.

Proteomic databases

PaxDbP08030.
PRIDEP08030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006764; ENSMUSP00000006764; ENSMUSG00000006589.
GeneID11821.
KEGGmmu:11821.
UCSCuc009ntf.1. mouse.

Organism-specific databases

CTD353.
MGIMGI:88061. Aprt.

Phylogenomic databases

eggNOGCOG0503.
GeneTreeENSGT00390000017259.
HOGENOMHOG000036776.
HOVERGENHBG003144.
InParanoidQ61319.
KOK00759.
OMAAGIMFRD.
OrthoDBEOG7FFMT9.
TreeFamTF300227.

Enzyme and pathway databases

UniPathwayUPA00588; UER00646.

Gene expression databases

CleanExMM_APRT.
GenevestigatorP08030.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
HAMAPMF_00004. Aden_phosphoribosyltr.
InterProIPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01090. apt. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPRT. mouse.
NextBio279721.
PROP08030.
SOURCESearch...

Entry information

Entry nameAPT_MOUSE
AccessionPrimary (citable) accession number: P08030
Secondary accession number(s): Q564P4 expand/collapse secondary AC list , Q61319, Q6PK77, Q9DCY3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 6, 2013
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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