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Protein

Phosphoribosyl pyrophosphate synthase-associated protein 1

Gene

Prpsap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1915013. Prpsap1.

Subcellular locationi

GO - Cellular componenti

  1. ribose phosphate diphosphokinase complex Source: Ensembl
Complete GO annotation...

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.
ExpressionAtlasiQ9D0M1. baseline and differential.
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

        10         20         30         40         50
MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE
60 70 80 90 100
IKESVRGQDI FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP
110 120 130 140 150
YSKQSKMRKR GSIVCKLLAS MLAKAGLTHI ITMDLHQKEI QGFFSFPVDN
160 170 180 190 200
LRASPFLLQY IQEEIPNYRN AVIVAKSPDA AKRAQSYAER LRLGLAVIHG
210 220 230 240 250
EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP ITVVGDVGGR
260 270 280 290 300
IAIIVDDIID DVESFVAAAE ILKERGAYKI YVMATHGILS AEAPRLIEES
310 320 330 340 350
PIDEVVVTNT VPHELQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR

NITVDD
Length:356
Mass (Da):39,432
Last modified:June 1, 2001 - v1
Checksum:i0BCEA75BFE55401E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AK011290 mRNA. Translation: BAB27520.1.
BC029621 mRNA. Translation: AAH29621.1.
RefSeqiNP_080640.1. NM_026364.1.
UniGeneiMm.25125.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9D0M1.

Proteomic databases

MaxQBiQ9D0M1.
PaxDbiQ9D0M1.
PRIDEiQ9D0M1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi67763.
KEGGimmu:67763.

Organism-specific databases

CTDi5635.
MGIiMGI:1915013. Prpsap1.

Phylogenomic databases

eggNOGiCOG0462.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiQ9D0M1.

Miscellaneous databases

ChiTaRSiPrpsap1. mouse.
NextBioi325497.
PROiQ9D0M1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0M1.
ExpressionAtlasiQ9D0M1. baseline and differential.
GenevestigatoriQ9D0M1.

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.
ProtoNetiSearch...

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(2004) [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(2003) [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: March 4, 2015
This is version 95 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

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.