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Protein

Protein prune homolog

Gene

Prune

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, is able to induce cell motility and acts as a negative regulator of NME1 (By similarity).By similarity

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

Activated by magnesium ions and inhibited by manganese ions. Inhibited by dipyridamole, moderately sensitive to IBMX and inhibited by vinpocetine (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Manganese 1By similarity
Metal bindingi30 – 301Manganese 2By similarity
Metal bindingi106 – 1061Manganese 1By similarity
Metal bindingi106 – 1061Manganese 2By similarity
Metal bindingi179 – 1791Manganese 2By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein prune homolog (EC:3.6.1.1)
Alternative name(s):
PRUNEM1
Gene namesi
Name:Prune
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1925152. Prune.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Protein prune homologPRO_0000337988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei411 – 4111PhosphothreonineCombined sources
Modified residuei415 – 4151PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BIW1.
MaxQBiQ8BIW1.
PaxDbiQ8BIW1.
PRIDEiQ8BIW1.

PTM databases

iPTMnetiQ8BIW1.
PhosphoSiteiQ8BIW1.

Expressioni

Developmental stagei

In the developing embryo, a high level of expression is confined to the nervous system particularly in the dorsal root ganglia, cranial nerves, and neural retina. From E10.5, expressed at low levels in the basal plate along the entire neural tube, while at E12.5 the expression in the nervous system is definitively stronger, especially in the cranial and dorsal root ganglia and in the spinal nerves. In the hypothalamus, the expression is confined to the retro-chiasmatic area (RCH) and is also detectable in the remnant of the Rathke's pouch. In the developing eye, exclusively expressed in the prospective neural retina, equally distributed in both the deep and superficial layers. At E16.5, expression is still detectable in the outer neuroblast layer of the neural retina.1 Publication

Gene expression databases

BgeeiQ8BIW1.
GenevisibleiQ8BIW1. MM.

Interactioni

Subunit structurei

Homooligomer. Able to homodimerize via its C-terminal domain. Interacts with NME1. Interacts with GSK3; at focal adhesion complexes where paxillin and vinculin are colocalized.By similarity

Protein-protein interaction databases

BioGridi230866. 3 interactions.
IntActiQ8BIW1. 2 interactions.
STRINGi10090.ENSMUSP00000015855.

Structurei

3D structure databases

ProteinModelPortaliQ8BIW1.
SMRiQ8BIW1. Positions 18-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni394 – 42128Essential for homodimerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi106 – 1083DHH motifBy similarity

Sequence similaritiesi

Belongs to the PPase class C family. Prune subfamily.Curated

Phylogenomic databases

eggNOGiKOG4129. Eukaryota.
COG1227. LUCA.
GeneTreeiENSGT00450000040262.
HOGENOMiHOG000115724.
HOVERGENiHBG058142.
InParanoidiQ8BIW1.
KOiK01514.
OMAiALRTTIC.
OrthoDBiEOG7327PG.
PhylomeDBiQ8BIW1.
TreeFamiTF323914.

Family and domain databases

InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BIW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDYLQDCRA ALQDSRPLHV VLGNEACDLD SMVSALALAF YLTKTSEAED
60 70 80 90 100
IFIPVLNIKR SELPLRGDNV FFLQEVKIPE PALIFRDEID LLALHQAGQL
110 120 130 140 150
TLILVDHHIL PKSDAALEEA VAEVLDHRPI EQKYCPPCHV SVELVGSCAT
160 170 180 190 200
LVTERILQGA PETLDRQTAA LLHGTIILDC VNMDTNIGKA TPKDSKYVEE
210 220 230 240 250
LEALFPDLPK RKDIFDSLQK AKFDVSGLTT EQMLRKDQKT VYRQGTKVAI
260 270 280 290 300
SAIYMDLKAF LQRTDLFTDL SSFCHDHSYD ALVAMTIFFN TQNEPVRQLA
310 320 330 340 350
IFCPHEALRM TICGILERST SPPLKLTPIP STSPNLQAYH QGNTQVSRKK
360 370 380 390 400
LLPVLQEALS AYLDSAKMAS GQSEVAVGMS REQVDKDLDK ASNSLISGLS
410 420 430 440 450
QDEEDPPLPP TPMNSLVDEC PLDQGLPKFS AEAVFEKCSQ ISLSQSARAC

TSNK
Length:454
Mass (Da):50,239
Last modified:March 1, 2003 - v1
Checksum:i646FBF6B345028E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751E → A in AAC95291 (PubMed:10602478).Curated
Sequence conflicti397 – 3982SG → LW in AAC95291 (PubMed:10602478).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051908 mRNA. Translation: AAC95291.2.
AK081637 mRNA. Translation: BAC38278.1.
AK142160 mRNA. Translation: BAE24953.1.
BC057546 mRNA. Translation: AAH57546.1.
BC058635 mRNA. Translation: AAH58635.1.
CCDSiCCDS17610.1.
RefSeqiNP_775482.1. NM_173347.2.
UniGeneiMm.14155.
Mm.486494.

Genome annotation databases

EnsembliENSMUST00000015855; ENSMUSP00000015855; ENSMUSG00000015711.
GeneIDi229589.
KEGGimmu:229589.
UCSCiuc008qiz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051908 mRNA. Translation: AAC95291.2.
AK081637 mRNA. Translation: BAC38278.1.
AK142160 mRNA. Translation: BAE24953.1.
BC057546 mRNA. Translation: AAH57546.1.
BC058635 mRNA. Translation: AAH58635.1.
CCDSiCCDS17610.1.
RefSeqiNP_775482.1. NM_173347.2.
UniGeneiMm.14155.
Mm.486494.

3D structure databases

ProteinModelPortaliQ8BIW1.
SMRiQ8BIW1. Positions 18-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230866. 3 interactions.
IntActiQ8BIW1. 2 interactions.
STRINGi10090.ENSMUSP00000015855.

PTM databases

iPTMnetiQ8BIW1.
PhosphoSiteiQ8BIW1.

Proteomic databases

EPDiQ8BIW1.
MaxQBiQ8BIW1.
PaxDbiQ8BIW1.
PRIDEiQ8BIW1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015855; ENSMUSP00000015855; ENSMUSG00000015711.
GeneIDi229589.
KEGGimmu:229589.
UCSCiuc008qiz.1. mouse.

Organism-specific databases

CTDi58497.
MGIiMGI:1925152. Prune.

Phylogenomic databases

eggNOGiKOG4129. Eukaryota.
COG1227. LUCA.
GeneTreeiENSGT00450000040262.
HOGENOMiHOG000115724.
HOVERGENiHBG058142.
InParanoidiQ8BIW1.
KOiK01514.
OMAiALRTTIC.
OrthoDBiEOG7327PG.
PhylomeDBiQ8BIW1.
TreeFamiTF323914.

Miscellaneous databases

PROiQ8BIW1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BIW1.
GenevisibleiQ8BIW1. MM.

Family and domain databases

InterProiIPR001667. DDH_dom.
IPR004097. DHHA2.
[Graphical view]
PfamiPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
SMARTiSM01131. DHHA2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for interaction between human PRUNE and nm23-H1 NDPKinase."
    Reymond A., Volorio S., Merla G., Al-Maghtheh M., Zuffardi O., Bulfone A., Ballabio A., Zollo M.
    Oncogene 18:7244-7252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "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: Head and Heart.
  3. "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: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; THR-411 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Spleen and Testis.

Entry informationi

Entry nameiPRUNE_MOUSE
AccessioniPrimary (citable) accession number: Q8BIW1
Secondary accession number(s): Q80VU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 103 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

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 one 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.