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Q62384 (ZPR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein ZPR1
Alternative name(s):
Zinc finger protein 259
Gene names
Name:Zpr1
Synonyms:Zfp259, Znf259
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H2O(2)-induced neuronal cell death. Ref.1 Ref.5 Ref.7 Ref.9

Subunit structure

Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Interacts (via C-terminal region) with SMN1 (via C-terminal region); the interaction occurs after treatment with serum By similarity. Interacts with elongation factor 1-alpha EEF1A1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner. Interacts (via zinc fingers) with EGFR (via C-terminal cytoplasmic kinase domain); the interaction is negatively regulated in response to epidermal growth factor (EGF) stimulation and EGFR kinase activity. May also bind to the PDGFR receptor. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm. Nucleusnucleolus. Cytoplasmperinuclear region By similarity. Nucleusgem. NucleusCajal body. Cell projectionaxon. Cell projectiongrowth cone. Note: Localized predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner By similarity. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons. Ref.1 Ref.2 Ref.4 Ref.5 Ref.9

Tissue specificity

Expressed in brain. Expressed in the spinal cord motor neurons (at protein level). Expressed in spleen, liver, muscle, kidney and testis. Expressed in the frontal cortex, cornus ammonis, dentate gyrus of the hippocampus and in Purkinje cells of the cerebellum. Ref.1 Ref.6 Ref.7

Induction

Up-regulated by high fat diet. Ref.6

Involvement in disease

May contribute to the severity of spinal muscular atrophy by increasing spinal motor neurons degeneration (Ref.7).

Disruption phenotype

Die during early embryonic development. Embryos show growth delay, failed to form normal trophectoderm and to expand the inner cell mass. Ref.5

Sequence similarities

Belongs to the ZPR1 family.

Ontologies

Keywords
   Biological processDifferentiation
mRNA processing
mRNA splicing
   Cellular componentCell projection
Cytoplasm
Nucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionDevelopmental protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCajal body organization

Inferred from mutant phenotype Ref.5. Source: UniProtKB

DNA endoreduplication

Inferred from mutant phenotype Ref.5. Source: UniProtKB

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process involved in development

Inferred from mutant phenotype Ref.5. Source: UniProtKB

axon development

Inferred from mutant phenotype Ref.5Ref.7Ref.9. Source: UniProtKB

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

inner cell mass cell proliferation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule cytoskeleton organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of motor neuron apoptotic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of RNA splicing

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of growth

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of protein import into nucleus

Inferred from mutant phenotype Ref.5Ref.9. Source: UniProtKB

positive regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

pre-mRNA catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of myelination

Inferred from mutant phenotype Ref.9. Source: UniProtKB

spinal cord development

Inferred from mutant phenotype Ref.9. Source: UniProtKB

trophectodermal cell proliferation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentCajal body

Inferred from direct assay Ref.5Ref.9. Source: UniProtKB

Gemini of coiled bodies

Inferred from direct assay Ref.5Ref.9. Source: UniProtKB

SMN complex

Inferred from sequence or structural similarity. Source: UniProtKB

axon

Inferred from direct assay Ref.9. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.1. Source: MGI

growth cone

Inferred from direct assay Ref.5. Source: UniProtKB

neuronal cell body

Inferred from direct assay Ref.5. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1. Source: MGI

perikaryon

Inferred from direct assay Ref.9. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from physical interaction Ref.2. Source: UniProtKB

translation initiation factor binding

Inferred from physical interaction Ref.2. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Zinc finger protein ZPR1
PRO_0000119037

Regions

Zinc finger51 – 8333C4-type 1
Zinc finger259 – 29133C4-type 2

Secondary structure

................................................................................... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62384 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 771D38C7B806044F

FASTA45950,715
        10         20         30         40         50         60 
MSASGAVQPG HPGAAVGPSP AAAASPATGP LFRPLSAEDE EQQPTEIESL CMNCYRNGTT 

        70         80         90        100        110        120 
RLLLTKIPFF REIIVSSFSC EHCGWNNTEI QSAGRIQDQG VRYTLTVRSQ EDMNREVVKT 

       130        140        150        160        170        180 
DSATTRIPEL DFEIPAFSQK GALTTVEGLI SRAISGLEQD QPTRRAVEGA IAERIDEFIG 

       190        200        210        220        230        240 
KLKDLKQMAS PFTLVIDDPS GNSFVENPHA PQKDNALVIT YYDRTPQQAE MLGLQAEAPE 

       250        260        270        280        290        300 
EKAEEEDLRN EVLQFNTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS 

       310        320        330        340        350        360 
GGAVEPLGTR ITLHITDPSD MTRDLLKSET CSVEIPELEF ELGMAVLGGK FTTLEGLLKD 

       370        380        390        400        410        420 
IRELVTKNPF TLGDSSNPDQ SEKLQEFSQK LGQIIEGKMK AHFIMNDPAG NSYLQNVYAP 

       430        440        450 
EDDPEMKVER YKRTFDQNEE LGLNDMKTEG YEAGLAPQR 

« Hide

References

« Hide 'large scale' references
[1]"Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor."
Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T., Davis R.J.
Science 272:1797-1802(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EGFR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells."
Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.
J. Cell Biol. 143:1471-1484(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EEF1A1 AND EGFR, SUBCELLULAR LOCATION.
[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: Czech II.
Tissue: Mammary gland.
[4]"The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus of proliferating cells."
Galcheva-Gargova Z., Gangwani L., Konstantinov K.N., Mikrut M., Theroux S.J., Enoch T., Davis R.J.
Mol. Biol. Cell 9:2963-2971(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"ZPR1 is essential for survival and is required for localization of the survival motor neurons (SMN) protein to Cajal bodies."
Gangwani L., Flavell R.A., Davis R.J.
Mol. Cell. Biol. 25:2744-2756(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
[6]"Expression of zinc finger protein ZPR1 mRNA in brain is up-regulated in mice fed a high-fat diet."
Nogusa Y., Yanaka N., Sumiyoshi N., Takeda K., Kato N.
Int. J. Mol. Med. 17:491-496(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY.
[7]"Deficiency of the zinc finger protein ZPR1 causes neurodegeneration."
Doran B., Gherbesi N., Hendricks G., Flavell R.A., Davis R.J., Gangwani L.
Proc. Natl. Acad. Sci. U.S.A. 103:7471-7475(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INVOLVEMENT IN NEURODEGENERATION, TISSUE SPECIFICITY.
[8]"Generation of a zinc finger protein ZPR1 mutant that constitutively interacted with translation elongation factor 1alpha."
Yanaka N., Kaseda Y., Tanaka A., Nogusa Y., Sumiyoshi N., Kato N.
Biosci. Biotechnol. Biochem. 73:2809-2811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EEF1A1.
[9]"The zinc finger protein ZPR1 is a potential modifier of spinal muscular atrophy."
Ahmad S., Wang Y., Shaik G.M., Burghes A.H., Gangwani L.
Hum. Mol. Genet. 21:2745-2758(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMN1, INVOLVEMENT IN NEURODEGENERATION, SUBCELLULAR LOCATION.
[10]"Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes."
Mishra A.K., Gangwani L., Davis R.J., Lambright D.G.
Proc. Natl. Acad. Sci. U.S.A. 104:13930-13935(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 47-440, INTERACTION WITH EF1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41287 mRNA. Translation: AAC52662.1.
BC021397 mRNA. Translation: AAH21397.1.
CCDSCCDS23144.1.
RefSeqNP_035882.1. NM_011752.2.
UniGeneMm.17519.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QKDX-ray2.00A47-440[»]
ProteinModelPortalQ62384.
SMRQ62384. Positions 47-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204651. 1 interaction.
DIPDIP-46465N.

PTM databases

PhosphoSiteQ62384.

Proteomic databases

MaxQBQ62384.
PaxDbQ62384.
PRIDEQ62384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000156440; ENSMUSP00000117725; ENSMUSG00000032078.
GeneID22687.
KEGGmmu:22687.
UCSCuc009phh.1. mouse.

Organism-specific databases

CTD8882.
MGIMGI:1330262. Zpr1.

Phylogenomic databases

eggNOGCOG1779.
GeneTreeENSGT00390000005306.
HOVERGENHBG002608.
InParanoidQ62384.
KOK06874.
OMAFIMNDPA.
OrthoDBEOG7GQXVP.
TreeFamTF313084.

Gene expression databases

ArrayExpressQ62384.
BgeeQ62384.
CleanExMM_ZFP259.
GenevestigatorQ62384.

Family and domain databases

InterProIPR004457. Znf_ZPR1.
[Graphical view]
PfamPF03367. zf-ZPR1. 2 hits.
[Graphical view]
SMARTSM00709. Zpr1. 2 hits.
[Graphical view]
TIGRFAMsTIGR00310. ZPR1_znf. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ62384.
NextBio303121.
PROQ62384.
SOURCESearch...

Entry information

Entry nameZPR1_MOUSE
AccessionPrimary (citable) accession number: Q62384
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot