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P08030

- APT_MOUSE

UniProt

P08030 - APT_MOUSE

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Protein
Adenine phosphoribosyltransferase
Gene
Aprt
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

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

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 180179Adenine phosphoribosyltransferaseUniRule annotation
PRO_0000149506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei60 – 601Phosphotyrosine By similarity
Modified residuei66 – 661Phosphoserine By similarity
Modified residuei114 – 1141N6-acetyllysine By similarity
Modified residuei135 – 1351Phosphothreonine By 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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72LK → FE in BAB22029. 1 Publication
Sequence conflicti15 – 151S → V in AAA37255. 1 Publication
Sequence conflicti24 – 241V → A in BAB22029. 1 Publication
Sequence conflicti46 – 461L → S in BAB22029. 1 Publication
Sequence conflicti72 – 721G → A in BAB22029. 1 Publication
Sequence conflicti107 – 1071K → KVR in AAA37256. 1 Publication
Sequence conflicti135 – 1351T → I in BAD95572. 1 Publication

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

« 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: July 9, 2014
This is version 115 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