Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O75312

- ZPR1_HUMAN

UniProt

O75312 - ZPR1_HUMAN

Protein

Zinc finger protein ZPR1

Gene

ZPR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 8333C4-type 1Add
    BLAST
    Zinc fingeri259 – 29133C4-type 2Add
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. translation initiation factor binding Source: UniProtKB
    3. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. apoptotic process involved in development Source: UniProtKB
    2. axon development Source: UniProtKB
    3. Cajal body organization Source: UniProtKB
    4. cell proliferation Source: ProtInc
    5. cellular response to epidermal growth factor stimulus Source: UniProtKB
    6. DNA endoreduplication Source: UniProtKB
    7. microtubule cytoskeleton organization Source: UniProtKB
    8. mRNA processing Source: UniProtKB-KW
    9. negative regulation of motor neuron apoptotic process Source: UniProtKB
    10. positive regulation of gene expression Source: UniProtKB
    11. positive regulation of growth Source: UniProtKB
    12. positive regulation of protein import into nucleus Source: UniProtKB
    13. positive regulation of RNA splicing Source: UniProtKB
    14. positive regulation of transcription involved in G1/S transition of mitotic cell cycle Source: UniProtKB
    15. pre-mRNA catabolic process Source: UniProtKB
    16. regulation of myelination Source: UniProtKB
    17. RNA splicing Source: UniProtKB-KW
    18. signal transduction Source: ProtInc
    19. spinal cord development Source: UniProtKB
    20. trophectodermal cell proliferation Source: UniProtKB

    Keywords - Biological processi

    Differentiation, mRNA processing, mRNA splicing

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc finger protein ZPR1
    Alternative name(s):
    Zinc finger protein 259
    Gene namesi
    Name:ZPR1
    Synonyms:ZNF259
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:13051. ZPR1.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. Cajal body Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. Gemini of coiled bodies Source: UniProtKB
    5. growth cone Source: UniProtKB
    6. neuronal cell body Source: UniProtKB
    7. nucleolus Source: UniProtKB
    8. nucleoplasm Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. perikaryon Source: UniProtKB
    11. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    12. SMN complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37629.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Zinc finger protein ZPR1PRO_0000119036Add
    BLAST

    Proteomic databases

    MaxQBiO75312.
    PaxDbiO75312.
    PRIDEiO75312.

    PTM databases

    PhosphoSiteiO75312.

    Expressioni

    Tissue specificityi

    Expressed in fibroblast; weakly expressed in fibroblast of spinal muscular atrophy (SMA) patients.1 Publication

    Gene expression databases

    ArrayExpressiO75312.
    BgeeiO75312.
    CleanExiHS_ZNF259.
    GenevestigatoriO75312.

    Organism-specific databases

    HPAiCAB022596.

    Interactioni

    Subunit structurei

    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.4 Publications

    Protein-protein interaction databases

    BioGridi114401. 64 interactions.
    IntActiO75312. 2 interactions.
    MINTiMINT-1371628.
    STRINGi9606.ENSP00000227322.

    Structurei

    3D structure databases

    ProteinModelPortaliO75312.
    SMRiO75312. Positions 47-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ZPR1 family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri51 – 8333C4-type 1Add
    BLAST
    Zinc fingeri259 – 29133C4-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1779.
    HOGENOMiHOG000216492.
    HOVERGENiHBG002608.
    InParanoidiO75312.
    KOiK06874.
    OMAiFIMNDPA.
    PhylomeDBiO75312.
    TreeFamiTF313084.

    Family and domain databases

    InterProiIPR004457. Znf_ZPR1.
    [Graphical view]
    PfamiPF03367. zf-ZPR1. 2 hits.
    [Graphical view]
    SMARTiSM00709. Zpr1. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR00310. ZPR1_znf. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    O75312-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGAVEPG PPGAAVAPSP APAPPPAPDH LFRPISAEDE EQQPTEIESL    50
    CMNCYCNGMT RLLLTKIPFF REIIVSSFSC EHCGWNNTEI QSAGRIQDQG 100
    VRYTLSVRAL EDMNREVVKT DSAATRIPEL DFEIPAFSQK GALTTVEGLI 150
    TRAISGLEQD QPARRANKDA TAERIDEFIV KLKELKQVAS PFTLIIDDPS 200
    GNSFVENPHA PQKDDALVIT HYNRTRQQEE MLGLQEEAPA EKPEEEDLRN 250
    EVLQFSTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS 300
    GGAVEPLGTR ITLHITDASD MTRDLLKSET CSVEIPELEF ELGMAVLGGK 350
    FTTLEGLLKD IRELVTKNPF TLGDSSNPGQ TERLQEFSQK MDQIIEGNMK 400
    AHFIMDDPAG NSYLQNVYAP EDDPEMKVER YKRTFDQNEE LGLNDMKTEG 450
    YEAGLAPQR 459
    Length:459
    Mass (Da):50,925
    Last modified:November 1, 1998 - v1
    Checksum:iE3DB820F490F2835
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti264 – 2641A → V.
    Corresponds to variant rs35120633 [ dbSNP | Ensembl ].
    VAR_052999

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS8375.1.
    RefSeqiNP_003895.1. NM_003904.3.
    UniGeneiHs.7165.

    Genome annotation databases

    EnsembliENST00000227322; ENSP00000227322; ENSG00000109917.
    GeneIDi8882.
    KEGGihsa:8882.
    UCSCiuc001ppp.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS8375.1.
    RefSeqi NP_003895.1. NM_003904.3.
    UniGenei Hs.7165.

    3D structure databases

    ProteinModelPortali O75312.
    SMRi O75312. Positions 47-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114401. 64 interactions.
    IntActi O75312. 2 interactions.
    MINTi MINT-1371628.
    STRINGi 9606.ENSP00000227322.

    PTM databases

    PhosphoSitei O75312.

    Proteomic databases

    MaxQBi O75312.
    PaxDbi O75312.
    PRIDEi O75312.

    Protocols and materials databases

    DNASUi 8882.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227322 ; ENSP00000227322 ; ENSG00000109917 .
    GeneIDi 8882.
    KEGGi hsa:8882.
    UCSCi uc001ppp.3. human.

    Organism-specific databases

    CTDi 8882.
    GeneCardsi GC11M116648.
    HGNCi HGNC:13051. ZPR1.
    HPAi CAB022596.
    MIMi 603901. gene.
    neXtProti NX_O75312.
    PharmGKBi PA37629.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1779.
    HOGENOMi HOG000216492.
    HOVERGENi HBG002608.
    InParanoidi O75312.
    KOi K06874.
    OMAi FIMNDPA.
    PhylomeDBi O75312.
    TreeFami TF313084.

    Miscellaneous databases

    GeneWikii ZNF259.
    GenomeRNAii 8882.
    NextBioi 33353.
    PROi O75312.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75312.
    Bgeei O75312.
    CleanExi HS_ZNF259.
    Genevestigatori O75312.

    Family and domain databases

    InterProi IPR004457. Znf_ZPR1.
    [Graphical view ]
    Pfami PF03367. zf-ZPR1. 2 hits.
    [Graphical view ]
    SMARTi SM00709. Zpr1. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR00310. ZPR1_znf. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiZPR1_HUMAN
    AccessioniPrimary (citable) accession number: O75312
    Secondary accession number(s): Q2TAA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3