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Q9D0M1

- KPRA_MOUSE

UniProt

Q9D0M1 - KPRA_MOUSE

Protein

Phosphoribosyl pyrophosphate synthase-associated protein 1

Gene

Prpsap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.By similarity

    GO - Molecular functioni

    1. enzyme regulator activity Source: Ensembl
    2. magnesium ion binding Source: InterPro
    3. ribose phosphate diphosphokinase activity Source: InterPro

    GO - Biological processi

    1. negative regulation of kinase activity Source: Ensembl
    2. nucleotide biosynthetic process Source: UniProtKB-KW

    Keywords - Biological processi

    Nucleotide biosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosyl pyrophosphate synthase-associated protein 1
    Short name:
    PRPP synthase-associated protein 1
    Alternative name(s):
    39 kDa phosphoribosypyrophosphate synthase-associated protein
    Short name:
    PAP39
    Gene namesi
    Name:Prpsap1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1915013. Prpsap1.

    Subcellular locationi

    GO - Cellular componenti

    1. ribose phosphate diphosphokinase complex Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356Phosphoribosyl pyrophosphate synthase-associated protein 1PRO_0000141080Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei215 – 2151PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9D0M1.
    PaxDbiQ9D0M1.
    PRIDEiQ9D0M1.

    PTM databases

    PhosphoSiteiQ9D0M1.

    Expressioni

    Gene expression databases

    BgeeiQ9D0M1.
    GenevestigatoriQ9D0M1.

    Interactioni

    Subunit structurei

    Binds to PRPS1 and PRPS2.By similarity

    Protein-protein interaction databases

    BioGridi212425. 1 interaction.
    DIPiDIP-59971N.
    MINTiMINT-1857384.
    STRINGi10090.ENSMUSP00000101999.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D0M1.
    SMRiQ9D0M1. Positions 7-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0462.
    HOGENOMiHOG000210451.
    HOVERGENiHBG001520.
    InParanoidiQ9D0M1.

    Family and domain databases

    Gene3Di3.40.50.2020. 2 hits.
    InterProiIPR029099. Pribosyltran_N.
    IPR029057. PRTase-like.
    IPR005946. Rib-P_diPkinase.
    [Graphical view]
    PfamiPF14572. Pribosyl_synth. 1 hit.
    PF13793. Pribosyltran_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 2 hits.
    TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9D0M1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE    50
    IKESVRGQDI FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP 100
    YSKQSKMRKR GSIVCKLLAS MLAKAGLTHI ITMDLHQKEI QGFFSFPVDN 150
    LRASPFLLQY IQEEIPNYRN AVIVAKSPDA AKRAQSYAER LRLGLAVIHG 200
    EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP ITVVGDVGGR 250
    IAIIVDDIID DVESFVAAAE ILKERGAYKI YVMATHGILS AEAPRLIEES 300
    PIDEVVVTNT VPHELQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR 350
    NITVDD 356
    Length:356
    Mass (Da):39,432
    Last modified:June 1, 2001 - v1
    Checksum:i0BCEA75BFE55401E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011290 mRNA. Translation: BAB27520.1.
    BC029621 mRNA. Translation: AAH29621.1.
    RefSeqiNP_080640.1. NM_026364.1.
    UniGeneiMm.25125.

    Genome annotation databases

    GeneIDi67763.
    KEGGimmu:67763.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011290 mRNA. Translation: BAB27520.1 .
    BC029621 mRNA. Translation: AAH29621.1 .
    RefSeqi NP_080640.1. NM_026364.1.
    UniGenei Mm.25125.

    3D structure databases

    ProteinModelPortali Q9D0M1.
    SMRi Q9D0M1. Positions 7-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212425. 1 interaction.
    DIPi DIP-59971N.
    MINTi MINT-1857384.
    STRINGi 10090.ENSMUSP00000101999.

    PTM databases

    PhosphoSitei Q9D0M1.

    Proteomic databases

    MaxQBi Q9D0M1.
    PaxDbi Q9D0M1.
    PRIDEi Q9D0M1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 67763.
    KEGGi mmu:67763.

    Organism-specific databases

    CTDi 5635.
    MGIi MGI:1915013. Prpsap1.

    Phylogenomic databases

    eggNOGi COG0462.
    HOGENOMi HOG000210451.
    HOVERGENi HBG001520.
    InParanoidi Q9D0M1.

    Miscellaneous databases

    NextBioi 325497.
    PROi Q9D0M1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D0M1.
    Genevestigatori Q9D0M1.

    Family and domain databases

    Gene3Di 3.40.50.2020. 2 hits.
    InterProi IPR029099. Pribosyltran_N.
    IPR029057. PRTase-like.
    IPR005946. Rib-P_diPkinase.
    [Graphical view ]
    Pfami PF14572. Pribosyl_synth. 1 hit.
    PF13793. Pribosyltran_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 2 hits.
    TIGRFAMsi TIGR01251. ribP_PPkin. 1 hit.
    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.
      Tissue: Embryo.
    2. "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].
      Tissue: Colon.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiKPRA_MOUSE
    AccessioniPrimary (citable) accession number: Q9D0M1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 91 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3