Full text data of ZNF259
ZNF259
(ZPR1)
[Confidence: low (only semi-automatic identification from reviews)]
Zinc finger protein ZPR1 (Zinc finger protein 259)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Zinc finger protein ZPR1 (Zinc finger protein 259)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75312
ID ZPR1_HUMAN Reviewed; 459 AA.
AC O75312; Q2TAA0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Zinc finger protein ZPR1;
DE AltName: Full=Zinc finger protein 259;
GN Name=ZNF259; Synonyms=ZPR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
RA Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
RT "Interaction of ZPR1 with translation elongation factor-1alpha in
RT proliferating cells.";
RL J. Cell Biol. 143:1471-1484(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Pancreas, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9763455; DOI=10.1091/mbc.9.10.2963;
RA Galcheva-Gargova Z., Gangwani L., Konstantinov K.N., Mikrut M.,
RA Theroux S.J., Enoch T., Davis R.J.;
RT "The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus
RT of proliferating cells.";
RL Mol. Biol. Cell 9:2963-2971(1998).
RN [5]
RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP
RT complex with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be a signaling molecule that communicates mitogenic
CC signals from the cytoplasm to the nucleus.
CC -!- SUBUNIT: Binds to the EGF and PDGF receptors. Binds to the
CC elongation factor 1-alpha EF1A (By similarity). Component of an
CC import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC Note=Translocates to the nucleolus after treatment with mitogens.
CC -!- SIMILARITY: Belongs to the ZPR1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF019767; AAC33514.1; -; mRNA.
DR EMBL; BT006642; AAP35288.1; -; mRNA.
DR EMBL; BC004256; AAH04256.1; -; mRNA.
DR EMBL; BC012162; AAH12162.1; -; mRNA.
DR EMBL; BC017349; AAH17349.1; -; mRNA.
DR EMBL; BC017380; AAH17380.1; -; mRNA.
DR EMBL; BC111028; AAI11029.1; -; mRNA.
DR RefSeq; NP_003895.1; NM_003904.3.
DR UniGene; Hs.7165; -.
DR ProteinModelPortal; O75312; -.
DR SMR; O75312; 47-440.
DR IntAct; O75312; 2.
DR MINT; MINT-1371628; -.
DR STRING; 9606.ENSP00000227322; -.
DR PhosphoSite; O75312; -.
DR PaxDb; O75312; -.
DR PRIDE; O75312; -.
DR DNASU; 8882; -.
DR Ensembl; ENST00000227322; ENSP00000227322; ENSG00000109917.
DR GeneID; 8882; -.
DR KEGG; hsa:8882; -.
DR UCSC; uc001ppp.3; human.
DR CTD; 8882; -.
DR GeneCards; GC11M116648; -.
DR HGNC; HGNC:13051; ZNF259.
DR HPA; CAB022596; -.
DR MIM; 603901; gene.
DR neXtProt; NX_O75312; -.
DR PharmGKB; PA37629; -.
DR eggNOG; COG1779; -.
DR HOGENOM; HOG000216492; -.
DR HOVERGEN; HBG002608; -.
DR InParanoid; O75312; -.
DR KO; K06874; -.
DR OMA; TVCDHCG; -.
DR PhylomeDB; O75312; -.
DR GeneWiki; ZNF259; -.
DR GenomeRNAi; 8882; -.
DR NextBio; 33353; -.
DR PRO; PR:O75312; -.
DR ArrayExpress; O75312; -.
DR Bgee; O75312; -.
DR CleanEx; HS_ZNF259; -.
DR Genevestigator; O75312; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR004457; Znf_ZPR1.
DR Pfam; PF03367; zf-ZPR1; 2.
DR SMART; SM00709; Zpr1; 2.
DR TIGRFAMs; TIGR00310; ZPR1_znf; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Metal-binding; Nucleus; Polymorphism;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1 459 Zinc finger protein ZPR1.
FT /FTId=PRO_0000119036.
FT ZN_FING 51 83 C4-type 1.
FT ZN_FING 259 291 C4-type 2.
FT VARIANT 264 264 A -> V (in dbSNP:rs35120633).
FT /FTId=VAR_052999.
SQ SEQUENCE 459 AA; 50925 MW; E3DB820F490F2835 CRC64;
MAASGAVEPG PPGAAVAPSP APAPPPAPDH LFRPISAEDE EQQPTEIESL CMNCYCNGMT
RLLLTKIPFF REIIVSSFSC EHCGWNNTEI QSAGRIQDQG VRYTLSVRAL EDMNREVVKT
DSAATRIPEL DFEIPAFSQK GALTTVEGLI TRAISGLEQD QPARRANKDA TAERIDEFIV
KLKELKQVAS PFTLIIDDPS GNSFVENPHA PQKDDALVIT HYNRTRQQEE MLGLQEEAPA
EKPEEEDLRN EVLQFSTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS
GGAVEPLGTR ITLHITDASD MTRDLLKSET CSVEIPELEF ELGMAVLGGK FTTLEGLLKD
IRELVTKNPF TLGDSSNPGQ TERLQEFSQK MDQIIEGNMK AHFIMDDPAG NSYLQNVYAP
EDDPEMKVER YKRTFDQNEE LGLNDMKTEG YEAGLAPQR
//
ID ZPR1_HUMAN Reviewed; 459 AA.
AC O75312; Q2TAA0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Zinc finger protein ZPR1;
DE AltName: Full=Zinc finger protein 259;
GN Name=ZNF259; Synonyms=ZPR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
RA Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
RT "Interaction of ZPR1 with translation elongation factor-1alpha in
RT proliferating cells.";
RL J. Cell Biol. 143:1471-1484(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Pancreas, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9763455; DOI=10.1091/mbc.9.10.2963;
RA Galcheva-Gargova Z., Gangwani L., Konstantinov K.N., Mikrut M.,
RA Theroux S.J., Enoch T., Davis R.J.;
RT "The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus
RT of proliferating cells.";
RL Mol. Biol. Cell 9:2963-2971(1998).
RN [5]
RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP
RT complex with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be a signaling molecule that communicates mitogenic
CC signals from the cytoplasm to the nucleus.
CC -!- SUBUNIT: Binds to the EGF and PDGF receptors. Binds to the
CC elongation factor 1-alpha EF1A (By similarity). Component of an
CC import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC Note=Translocates to the nucleolus after treatment with mitogens.
CC -!- SIMILARITY: Belongs to the ZPR1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF019767; AAC33514.1; -; mRNA.
DR EMBL; BT006642; AAP35288.1; -; mRNA.
DR EMBL; BC004256; AAH04256.1; -; mRNA.
DR EMBL; BC012162; AAH12162.1; -; mRNA.
DR EMBL; BC017349; AAH17349.1; -; mRNA.
DR EMBL; BC017380; AAH17380.1; -; mRNA.
DR EMBL; BC111028; AAI11029.1; -; mRNA.
DR RefSeq; NP_003895.1; NM_003904.3.
DR UniGene; Hs.7165; -.
DR ProteinModelPortal; O75312; -.
DR SMR; O75312; 47-440.
DR IntAct; O75312; 2.
DR MINT; MINT-1371628; -.
DR STRING; 9606.ENSP00000227322; -.
DR PhosphoSite; O75312; -.
DR PaxDb; O75312; -.
DR PRIDE; O75312; -.
DR DNASU; 8882; -.
DR Ensembl; ENST00000227322; ENSP00000227322; ENSG00000109917.
DR GeneID; 8882; -.
DR KEGG; hsa:8882; -.
DR UCSC; uc001ppp.3; human.
DR CTD; 8882; -.
DR GeneCards; GC11M116648; -.
DR HGNC; HGNC:13051; ZNF259.
DR HPA; CAB022596; -.
DR MIM; 603901; gene.
DR neXtProt; NX_O75312; -.
DR PharmGKB; PA37629; -.
DR eggNOG; COG1779; -.
DR HOGENOM; HOG000216492; -.
DR HOVERGEN; HBG002608; -.
DR InParanoid; O75312; -.
DR KO; K06874; -.
DR OMA; TVCDHCG; -.
DR PhylomeDB; O75312; -.
DR GeneWiki; ZNF259; -.
DR GenomeRNAi; 8882; -.
DR NextBio; 33353; -.
DR PRO; PR:O75312; -.
DR ArrayExpress; O75312; -.
DR Bgee; O75312; -.
DR CleanEx; HS_ZNF259; -.
DR Genevestigator; O75312; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR004457; Znf_ZPR1.
DR Pfam; PF03367; zf-ZPR1; 2.
DR SMART; SM00709; Zpr1; 2.
DR TIGRFAMs; TIGR00310; ZPR1_znf; 2.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Metal-binding; Nucleus; Polymorphism;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1 459 Zinc finger protein ZPR1.
FT /FTId=PRO_0000119036.
FT ZN_FING 51 83 C4-type 1.
FT ZN_FING 259 291 C4-type 2.
FT VARIANT 264 264 A -> V (in dbSNP:rs35120633).
FT /FTId=VAR_052999.
SQ SEQUENCE 459 AA; 50925 MW; E3DB820F490F2835 CRC64;
MAASGAVEPG PPGAAVAPSP APAPPPAPDH LFRPISAEDE EQQPTEIESL CMNCYCNGMT
RLLLTKIPFF REIIVSSFSC EHCGWNNTEI QSAGRIQDQG VRYTLSVRAL EDMNREVVKT
DSAATRIPEL DFEIPAFSQK GALTTVEGLI TRAISGLEQD QPARRANKDA TAERIDEFIV
KLKELKQVAS PFTLIIDDPS GNSFVENPHA PQKDDALVIT HYNRTRQQEE MLGLQEEAPA
EKPEEEDLRN EVLQFSTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS
GGAVEPLGTR ITLHITDASD MTRDLLKSET CSVEIPELEF ELGMAVLGGK FTTLEGLLKD
IRELVTKNPF TLGDSSNPGQ TERLQEFSQK MDQIIEGNMK AHFIMDDPAG NSYLQNVYAP
EDDPEMKVER YKRTFDQNEE LGLNDMKTEG YEAGLAPQR
//
MIM
603901
*RECORD*
*FIELD* NO
603901
*FIELD* TI
*603901 ZINC FINGER PROTEIN 259; ZNF259
;;ZPR1
*FIELD* TX
CLONING
The zinc finger protein ZNF259, also called ZPR1, was originally
read moreidentified in mouse as a protein that binds to the cytoplasmic tyrosine
kinase domain of the nonactivated EGFR (131550) (Galcheva-Gargova et
al., 1996). Galcheva-Gargova et al. (1996) demonstrated that this
interaction is mediated by the zinc fingers of Znf259. The Znf259
protein is present in the cytoplasm of quiescent cells and translocates
to the nucleus after treatment with mitogens, such as EGF (131530).
Northern blot analysis of mouse tissues indicated that Znf259 is widely
expressed.
By screening a HeLa cell cDNA library with a mouse Znf259 cDNA,
Galcheva-Gargova et al. (1998) cloned human ZNF259 cDNAs. They also
isolated homologs of Znf259 in S. cerevisiae and S. pombe. The deduced
ZNF259 proteins share conserved structural motifs, including 2 zinc
fingers. The authors demonstrated that human ZNF259 accumulates in the
nucleolus of proliferating cells and that this nucleolar localization
requires RNA but not DNA.
GENE FUNCTION
Galcheva-Gargova et al. (1998) found that disruption of the S. pombe
znf259 gene, along with complementation analyses using the yeast and
mouse Znf259 genes, indicated that znf259 is essential for viability in
S. pombe. Loss of S. pombe znf259 function caused a depletion of the
rRNA precursor and a reduction in protein translation. Galcheva-Gargova
et al. (1998) concluded that ZNF259 is required for normal nucleolar
function.
In cellular studies, Gangwani et al. (2001) showed that the ZPR1 protein
interacted with the SMN protein (600354) and that these 2 proteins
colocalized in small subnuclear structures, including gems and Cajal
bodies. ZPR1 and SMN redistributed from the cytoplasm to the nucleus in
response to serum. Deletion analysis indicated that the C-terminal
regions of both proteins, corresponding to the B domain of ZPR1 and exon
7 of SMN, were required for interaction and colocalization to the
nucleus. Defects in either protein resulted in marked inhibition of in
vitro pre-mRNA splicing. SMN derived from fibroblasts of patients with
spinal muscular atrophy I (SMA1; 253300) showed that the interaction of
ZPR1 with SMN was disrupted. Gangwani et al. (2001) concluded that ZPR1
is required for the proper localization of SMN and suggested that ZPR1
contributes to some of the functions of SMN.
ANIMAL MODEL
Doran et al. (2006) found that Zpr1-null mice exhibited an early
embryonic lethal phenotype. Zpr1 +/- mice were viable but exhibited
occasional seizures, fatigue, and an abnormal gait compared to wildtype
mice. Reduction of gene dosage by heterozygous Zpr1 gene ablation
resulted in decreased expression of the Zpr1 protein in the brain and
spinal cord of mice during development. By 12 months of age, Zpr1 +/-
mice showed progressive loss of spinal cord motor neurons and
progressive peripheral nerve axonopathy. Doran et al. (2006) concluded
that Zpr1 deficiency causes motor neuron degeneration in mice and
suggested that ZPR1 deficiency may contribute to spinal muscular atrophy
in humans.
*FIELD* RF
1. Doran, B.; Gherbesi, N.; Hendricks, G.; Flavell, R. A.; Davis,
R. J.; Gangwani, L.: Deficiency of the zinc finger protein ZPR1 causes
neurodegeneration. Proc. Nat. Acad. Sci. 103: 7471-7475, 2006.
2. Galcheva-Gargova, Z.; Gangwani, L.; Konstantinov, K. N.; Mikrut,
M.; Theroux, S. J.; Enoch, T.; Davis, R. J.: The cytoplasmic zinc
finger protein ZPR1 accumulates in the nucleolus of proliferating
cells. Molec. Biol. Cell 9: 2963-2971, 1998.
3. Galcheva-Gargova, Z.; Konstantinov, K. N.; Wu, I.-H.; Klier, F.
G.; Barrett, T.; Davis, R. J.: Binding of zinc finger protein ZPR1
to the epidermal growth factor receptor. Science 272: 1797-1802,
1996.
4. Gangwani, L.; Mikrut, M.; Theroux, S.; Sharma, M.; Davis, R. J.
: Spinal muscular atrophy disrupts the interaction of ZPR1 with the
SMN protein. Nature Cell Biol. 3: 376-383, 2001.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/1/2006
Victor A. McKusick - updated: 12/9/2003
Cassandra L. Kniffin - updated: 2/4/2003
*FIELD* CD
Sheryl A. Jankowski: 6/11/1999
*FIELD* ED
carol: 05/15/2012
wwang: 6/26/2006
ckniffin: 6/1/2006
terry: 12/9/2003
carol: 2/14/2003
ckniffin: 2/4/2003
psherman: 6/15/1999
psherman: 6/14/1999
*RECORD*
*FIELD* NO
603901
*FIELD* TI
*603901 ZINC FINGER PROTEIN 259; ZNF259
;;ZPR1
*FIELD* TX
CLONING
The zinc finger protein ZNF259, also called ZPR1, was originally
read moreidentified in mouse as a protein that binds to the cytoplasmic tyrosine
kinase domain of the nonactivated EGFR (131550) (Galcheva-Gargova et
al., 1996). Galcheva-Gargova et al. (1996) demonstrated that this
interaction is mediated by the zinc fingers of Znf259. The Znf259
protein is present in the cytoplasm of quiescent cells and translocates
to the nucleus after treatment with mitogens, such as EGF (131530).
Northern blot analysis of mouse tissues indicated that Znf259 is widely
expressed.
By screening a HeLa cell cDNA library with a mouse Znf259 cDNA,
Galcheva-Gargova et al. (1998) cloned human ZNF259 cDNAs. They also
isolated homologs of Znf259 in S. cerevisiae and S. pombe. The deduced
ZNF259 proteins share conserved structural motifs, including 2 zinc
fingers. The authors demonstrated that human ZNF259 accumulates in the
nucleolus of proliferating cells and that this nucleolar localization
requires RNA but not DNA.
GENE FUNCTION
Galcheva-Gargova et al. (1998) found that disruption of the S. pombe
znf259 gene, along with complementation analyses using the yeast and
mouse Znf259 genes, indicated that znf259 is essential for viability in
S. pombe. Loss of S. pombe znf259 function caused a depletion of the
rRNA precursor and a reduction in protein translation. Galcheva-Gargova
et al. (1998) concluded that ZNF259 is required for normal nucleolar
function.
In cellular studies, Gangwani et al. (2001) showed that the ZPR1 protein
interacted with the SMN protein (600354) and that these 2 proteins
colocalized in small subnuclear structures, including gems and Cajal
bodies. ZPR1 and SMN redistributed from the cytoplasm to the nucleus in
response to serum. Deletion analysis indicated that the C-terminal
regions of both proteins, corresponding to the B domain of ZPR1 and exon
7 of SMN, were required for interaction and colocalization to the
nucleus. Defects in either protein resulted in marked inhibition of in
vitro pre-mRNA splicing. SMN derived from fibroblasts of patients with
spinal muscular atrophy I (SMA1; 253300) showed that the interaction of
ZPR1 with SMN was disrupted. Gangwani et al. (2001) concluded that ZPR1
is required for the proper localization of SMN and suggested that ZPR1
contributes to some of the functions of SMN.
ANIMAL MODEL
Doran et al. (2006) found that Zpr1-null mice exhibited an early
embryonic lethal phenotype. Zpr1 +/- mice were viable but exhibited
occasional seizures, fatigue, and an abnormal gait compared to wildtype
mice. Reduction of gene dosage by heterozygous Zpr1 gene ablation
resulted in decreased expression of the Zpr1 protein in the brain and
spinal cord of mice during development. By 12 months of age, Zpr1 +/-
mice showed progressive loss of spinal cord motor neurons and
progressive peripheral nerve axonopathy. Doran et al. (2006) concluded
that Zpr1 deficiency causes motor neuron degeneration in mice and
suggested that ZPR1 deficiency may contribute to spinal muscular atrophy
in humans.
*FIELD* RF
1. Doran, B.; Gherbesi, N.; Hendricks, G.; Flavell, R. A.; Davis,
R. J.; Gangwani, L.: Deficiency of the zinc finger protein ZPR1 causes
neurodegeneration. Proc. Nat. Acad. Sci. 103: 7471-7475, 2006.
2. Galcheva-Gargova, Z.; Gangwani, L.; Konstantinov, K. N.; Mikrut,
M.; Theroux, S. J.; Enoch, T.; Davis, R. J.: The cytoplasmic zinc
finger protein ZPR1 accumulates in the nucleolus of proliferating
cells. Molec. Biol. Cell 9: 2963-2971, 1998.
3. Galcheva-Gargova, Z.; Konstantinov, K. N.; Wu, I.-H.; Klier, F.
G.; Barrett, T.; Davis, R. J.: Binding of zinc finger protein ZPR1
to the epidermal growth factor receptor. Science 272: 1797-1802,
1996.
4. Gangwani, L.; Mikrut, M.; Theroux, S.; Sharma, M.; Davis, R. J.
: Spinal muscular atrophy disrupts the interaction of ZPR1 with the
SMN protein. Nature Cell Biol. 3: 376-383, 2001.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/1/2006
Victor A. McKusick - updated: 12/9/2003
Cassandra L. Kniffin - updated: 2/4/2003
*FIELD* CD
Sheryl A. Jankowski: 6/11/1999
*FIELD* ED
carol: 05/15/2012
wwang: 6/26/2006
ckniffin: 6/1/2006
terry: 12/9/2003
carol: 2/14/2003
ckniffin: 2/4/2003
psherman: 6/15/1999
psherman: 6/14/1999