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O75312 (ZPR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:ZNF259
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.6 Ref.8 Ref.10

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. 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 the EGFR kinase activity. May also bind to the PDGFR receptor. Ref.1 Ref.4 Ref.6 Ref.7

Subcellular location

Nucleus. Nucleusnucleolus. Nucleusgem. NucleusCajal body. Cytoplasmperinuclear region. Cytoplasm. Cell projectionaxon By similarity. Cell projectiongrowth cone By similarity. Note: Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons By similarity. 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. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. Ref.4 Ref.5 Ref.6 Ref.8 Ref.10

Tissue specificity

Expressed in fibroblast; weakly expressed in fibroblast of spinal muscular atrophy (SMA) patients. Ref.10

Sequence similarities

Belongs to the ZPR1 family.

Ontologies

Keywords
   Biological processDifferentiation
mRNA processing
mRNA splicing
   Cellular componentCell projection
Cytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCajal body organization

Inferred from mutant phenotype Ref.8. Source: UniProtKB

DNA endoreduplication

Inferred from sequence or structural similarity. Source: UniProtKB

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process involved in development

Inferred from sequence or structural similarity. Source: UniProtKB

axon development

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cell proliferation

Traceable author statement Ref.5. Source: ProtInc

cellular response to epidermal growth factor stimulus

Inferred from direct assay Ref.1. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of motor neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of RNA splicing

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein import into nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

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

Inferred from mutant phenotype Ref.8. Source: UniProtKB

pre-mRNA catabolic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of myelination

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement Ref.4. Source: ProtInc

spinal cord development

Inferred from sequence or structural similarity. Source: UniProtKB

trophectodermal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCajal body

Inferred from direct assay Ref.6Ref.8Ref.10. Source: UniProtKB

Gemini of coiled bodies

Inferred from direct assay Ref.6Ref.8Ref.10. Source: UniProtKB

SMN complex

Inferred from direct assay Ref.6. Source: UniProtKB

axon

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.6Ref.8Ref.1. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.1. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6Ref.1. Source: UniProtKB

perikaryon

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

translation initiation factor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Zinc finger protein ZPR1
PRO_0000119036

Regions

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

Natural variations

Natural variant2641A → V.
Corresponds to variant rs35120633 [ dbSNP | Ensembl ].
VAR_052999

Sequences

Sequence LengthMass (Da)Tools
O75312 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E3DB820F490F2835

FASTA45950,925
        10         20         30         40         50         60 
MAASGAVEPG PPGAAVAPSP APAPPPAPDH LFRPISAEDE EQQPTEIESL CMNCYCNGMT 

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

       130        140        150        160        170        180 
DSAATRIPEL DFEIPAFSQK GALTTVEGLI TRAISGLEQD QPARRANKDA TAERIDEFIV 

       190        200        210        220        230        240 
KLKELKQVAS PFTLIIDDPS GNSFVENPHA PQKDDALVIT HYNRTRQQEE MLGLQEEAPA 

       250        260        270        280        290        300 
EKPEEEDLRN EVLQFSTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS 

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

       370        380        390        400        410        420 
IRELVTKNPF TLGDSSNPGQ TERLQEFSQK MDQIIEGNMK AHFIMDDPAG NSYLQNVYAP 

       430        440        450 
EDDPEMKVER YKRTFDQNEE LGLNDMKTEG YEAGLAPQR 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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].
Tissue: Brain, Pancreas and Skin.
[4]"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: INTERACTION WITH EGFR, SUBCELLULAR LOCATION.
[5]"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.
[6]"Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN protein."
Gangwani L., Mikrut M., Theroux S., Sharma M., Davis R.J.
Nat. Cell Biol. 3:376-383(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMN1, SUBCELLULAR LOCATION.
[7]"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
[8]"Deficiency of the zinc finger protein ZPR1 causes defects in transcription and cell cycle progression."
Gangwani L.
J. Biol. Chem. 281:40330-40340(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF019767 mRNA. Translation: AAC33514.1.
BT006642 mRNA. Translation: AAP35288.1.
BC004256 mRNA. Translation: AAH04256.1.
BC012162 mRNA. Translation: AAH12162.1.
BC017349 mRNA. Translation: AAH17349.1.
BC017380 mRNA. Translation: AAH17380.1.
BC111028 mRNA. Translation: AAI11029.1.
CCDSCCDS8375.1.
RefSeqNP_003895.1. NM_003904.3.
UniGeneHs.7165.

3D structure databases

ProteinModelPortalO75312.
SMRO75312. Positions 47-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114401. 64 interactions.
IntActO75312. 2 interactions.
MINTMINT-1371628.
STRING9606.ENSP00000227322.

PTM databases

PhosphoSiteO75312.

Proteomic databases

MaxQBO75312.
PaxDbO75312.
PRIDEO75312.

Protocols and materials databases

DNASU8882.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227322; ENSP00000227322; ENSG00000109917.
GeneID8882.
KEGGhsa:8882.
UCSCuc001ppp.3. human.

Organism-specific databases

CTD8882.
GeneCardsGC11M116648.
HGNCHGNC:13051. ZPR1.
HPACAB022596.
MIM603901. gene.
neXtProtNX_O75312.
PharmGKBPA37629.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1779.
HOGENOMHOG000216492.
HOVERGENHBG002608.
InParanoidO75312.
KOK06874.
OMAFIMNDPA.
PhylomeDBO75312.
TreeFamTF313084.

Gene expression databases

ArrayExpressO75312.
BgeeO75312.
CleanExHS_ZNF259.
GenevestigatorO75312.

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

GeneWikiZNF259.
GenomeRNAi8882.
NextBio33353.
PROO75312.
SOURCESearch...

Entry information

Entry nameZPR1_HUMAN
AccessionPrimary (citable) accession number: O75312
Secondary accession number(s): Q2TAA0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM