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P08030

- APT_MOUSE

UniProt

P08030 - APT_MOUSE

Protein

Adenine phosphoribosyltransferase

Gene

Aprt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (06 Feb 2013)
      Previous versions | rss
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    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.

    Pathwayi

    GO - Molecular functioni

    1. adenine binding Source: MGI
    2. adenine phosphoribosyltransferase activity Source: MGI
    3. AMP binding Source: Ensembl

    GO - Biological processi

    1. adenine metabolic process Source: MGI
    2. adenine salvage Source: MGI
    3. AMP salvage Source: UniProtKB-UniPathway
    4. cellular response to insulin stimulus Source: Ensembl
    5. grooming behavior Source: MGI
    6. lactation Source: Ensembl
    7. purine ribonucleoside salvage Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Enzyme and pathway databases

    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: Chromosome 8

    Organism-specific databases

    MGIiMGI:88061. Aprt.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl

    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.
    GenevestigatoriP08030.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    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.
    InParanoidiQ61319.
    KOiK00759.
    OMAiAGIMFRD.
    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

    MSEPELKLVA RRIRSFPDFP IPGVLFRDIS PLLKDPDSFR ASIRLLASHL    50
    KSTHSGKIDY IAGLDSRGFL FGPSLAQELG VGCVLIRKQG KLPGPTVSAS 100
    YSLEYGKAEL EIQKDALEPG QRVVIVDDLL ATGGTMFAAC DLLHQLRAEV 150
    VECVSLVELT SLKGRERLGP IPFFSLLQYD 180
    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. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS40503.1.
    PIRi A22670. RTMSA.
    RefSeqi NP_033828.2. NM_009698.2.
    UniGenei Mm.1786.

    3D structure databases

    ProteinModelPortali P08030.
    SMRi P08030. Positions 2-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08030. 4 interactions.
    MINTi MINT-4088065.
    STRINGi 10090.ENSMUSP00000006764.

    PTM databases

    PhosphoSitei P08030.

    Proteomic databases

    PaxDbi P08030.
    PRIDEi P08030.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006764 ; ENSMUSP00000006764 ; ENSMUSG00000006589 .
    GeneIDi 11821.
    KEGGi mmu:11821.
    UCSCi uc009ntf.1. mouse.

    Organism-specific databases

    CTDi 353.
    MGIi MGI:88061. Aprt.

    Phylogenomic databases

    eggNOGi COG0503.
    GeneTreei ENSGT00390000017259.
    HOGENOMi HOG000036776.
    HOVERGENi HBG003144.
    InParanoidi Q61319.
    KOi K00759.
    OMAi AGIMFRD.
    OrthoDBi EOG7FFMT9.
    TreeFami TF300227.

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00646 .

    Miscellaneous databases

    ChiTaRSi APRT. mouse.
    NextBioi 279721.
    PROi P08030.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_APRT.
    Genevestigatori P08030.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    HAMAPi MF_00004. Aden_phosphoribosyltr.
    InterProi IPR005764. Ade_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view ]
    Pfami PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR01090. apt. 1 hit.
    PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 116 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