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NIN ninein (GSK3B interacting protein)

Written2004-09José Luis Vizmanos
Departamento de Genética, Facultad de Ciencias, Universidad de Navarra, 31008 Pamplona, Navarra, Espana

(Note : for Links provided by Atlas : click)


Alias (NCBI)GSK3B-interacting protein
Glycogen synthase kinase 3 beta-interacting protein
Ninein centrosomal protein.
HGNC Previous nameninein (GSK3B interacting protein)
LocusID (NCBI) 51199
Atlas_Id 176
Location 14q22.1  [Link to chromosome band 14q22]
Location_base_pair Starts at 50725829 and ends at 50831121 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping NIN.png]
Local_order SAV1 (SAlvador homolog 1 Drosophila) is more centromeric.
C14orf29 (Chromosome 14 Open Reading Frame 29) is more telomeric.
  Genomic structure of NIN. Black boxes indicate exons.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
GTPBP4 (10p15.3)::NIN (14q22.1)MAP4K5 (14q21.3)::NIN (14q22.1)MAP4K5 (14q22.1)::NIN (14q22.1)
NIN (14q22.1)::ABHD12B (14q22.1)NIN (14q22.1)::DOK3 (5q35.3)NIN (14q22.1)::NIN (14q22.1)
NIN (14q22.1)::PDGFRB (5q32)NIN (14q22.1)::TAGLN (11q23.3)NIN (14q22.1)::TMX1 (14q22.1)
NIN (14q22.1)::TOGARAM1 (14q21.2)PDGFRB (5q32)::NIN (14q22.1)TAGLN (11q23.3)::NIN (14q22.1)


Description 31 exons spanning 111.3 Kb on 14q22.1. Transcription is from telomere to centromere.
Transcription 5 alternative transcripts:
  • Variant 2 encodes de longest isoform
  • Variant 1 contains a different 3' terminal region and the resulting protein has a distinct and shorter C-terminus.
  • Variant 3 contains also a different 3' terminal region and it encodes isoform 3 , with a shorter and distinct C-terminus than variant 2.
  • Variant 4 differs in the 5' and 3' UTRs, and has multiple differences in the coding region. The resulting isoform 4 contains an additional internal segment, when compared to isoform 2, has a longer and distinct N-terminus, and has a shorter and distinct C-terminus.
  • Variant 5 has multiple differences in the coding region and 3' UTR, the resulting isoform 5 contains an additional internal segment and has a distinct and shorter C-terminus. Isoform 5 has also been referred to as hNinein-Lm.

    4 alternative transcripts in EnsEMBL 1:

  • Q9HCK7 corresponding to RefSeq variant 4.
  • NIN corresponding to RefSeq variant 5.
  • NIN corresponding to RefSeq variant 4.
  • NM_182944 corresponding to RefSeq variant 1.
  • Protein

    Note Ninein (GSK3B interacting protein)
      Schematic representation of NIN. LZ: leuzine-zipper domain. Coiled-coil domains are indicated with asterisks.
    Description Homooligomer. Interacts with GSK3B (GSK3-beta) via its C-terminus domain, ait also interacts with C14ORF166 preventing its phosphorylation by GSK3-beta. NIN is a component of the core centrosome. Arranged in a tubular conformation with an open and a closed end within the centrosome. In the mother centrosome, it localizes at both ends of the centrosome tube, including the site of centrosome duplication, while in the daughter centrosome it is present only at the closed end. Requires PCM1 for centrosome localization. In interphase cells, it is localized in the centrosome. Decreases in metaphase and anaphase and reappears in telophase.
    Expression Ubiquitous. Highly expressed in heart and skeletal muscle.
    Localisation Centrosome.
    Function The centrosome is the major microtubulin-organizing center (MTOC) in most vertebrate cells. In a typical somatic cell, the centrosome is composed of a pair of centrioles surrounded by a mass of amorphous pericentriolar material (PCM) that may be involved in the complex of Y-tubulin, centrin, pericentrin and ninein. This protein play an important role as a microtubule minus-end capping, centriole position, anchoring factor and as a centrosome maturation factor. Localization of this protein to the centrosome requires three of its four leucine zippers in the central coiled-coil domain. In addition it has been suggested that ninein could play a role to ensure equal chromosome segregation prior to telophase/cytokinesis in the division cycle.
    Homology It presents homology in various species. It also belongs to ENSF00000001557 protein family.


    Somatic t(5;14)(q33;q24) 5' NIN-PDGFRB 3' fusion in a chronic myeloprolifetrative disorder with eosinophilia

    Implicated in

    Entity , 5q33 myeloproliferative disease.
    Disease Chronic myeloproliferative disorder with eosinophilia and skin lesions ( "Atypical CML").
    Prognosis Good. Relative mild disease course over at least 13 years. Imatinib mesylate responsive disease.
    Cytogenetics t(5;14)(q33;q24)
    Hybrid/Mutated Gene 5' NIN-PDGFRB 3'
    Abnormal Protein NIN-PDGFRB
    Schematic representation of the fusion NIN-PDGFRB consecuence of the t(5;14)(q33;q24) in a chronic myeloprolifetrative disorder with eosinophilia. From up to down: PDGFRB, NIN and the putative chimeric NIN-PDGFRB structure. TM, transmembrane domain; TK, tyrosine kinase domain; LZ, leuzine-zipper domain. Coiled coil domains on NIN and NIN-PDGFRB are indicated with asterisks.


    Molecular characterisation of ninein, a new coiled-coil protein of the centrosome.
    Bouckson-Castaing V, Moudjou M, Ferguson DJ, Mucklow S, Belkaid Y, Milon G, Crocker PR
    Journal of cell science. 1996 ; 109 ( Pt 1) : 179-190.
    PMID 8834802
    Molecular characterization of human ninein protein: two distinct subdomains required for centrosomal targeting and regulating signals in cell cycle.
    Chen CH, Howng SL, Cheng TS, Chou MH, Huang CY, Hong YR
    Biochemical and biophysical research communications. 2003 ; 308 (4) : 975-983.
    PMID 12927815
    Assembly of centrosomal proteins and microtubule organization depends on PCM-1.
    Dammermann A, Merdes A
    The Journal of cell biology. 2002 ; 159 (2) : 255-266.
    PMID 12403812
    Re-evaluating centrosome function.
    Doxsey S
    Nature reviews. Molecular cell biology. 2001 ; 2 (9) : 688-698.
    PMID 11533726
    Pericentrin, a highly conserved centrosome protein involved in microtubule organization.
    Doxsey SJ, Stein P, Evans L, Calarco PD, Kirschner M
    Cell. 1994 ; 76 (4) : 639-650.
    PMID 8124707
    Genomic organization and molecular characterization of the human ninein gene.
    Hong YR, Chen CH, Chuo MH, Liou SY, Howng SL
    Biochemical and biophysical research communications. 2000 ; 279 (3) : 989-995.
    PMID 11162463
    A novel ninein-interaction protein, CGI-99, blocks ninein phosphorylation by GSK3beta and is highly expressed in brain tumors.
    Howng SL, Hsu HC, Cheng TS, Lee YL, Chang LK, Lu PJ, Hong YR
    FEBS letters. 2004 ; 566 (1-3) : 162-168.
    PMID 15147888
    Microtubule minus-end anchorage at centrosomal and non-centrosomal sites: the role of ninein.
    Mogensen MM, Malik A, Piel M, Bouckson-Castaing V, Bornens M
    Journal of cell science. 2000 ; 113 ( Pt 17) : 3013-3023.
    PMID 10934040
    A subset of centrosomal proteins are arranged in a tubular conformation that is reproduced during centrosome duplication.
    Ou Y, Rattner JB
    Cell motility and the cytoskeleton. 2000 ; 47 (1) : 13-24.
    PMID 11002307
    CEP110 and ninein are located in a specific domain of the centrosome associated with centrosome maturation.
    Ou YY, Mack GJ, Zhang M, Rattner JB
    Journal of cell science. 2002 ; 115 (Pt 9) : 1825-1835.
    PMID 11956314
    Human ninein is a centrosomal autoantigen recognized by CREST patient sera and plays a regulatory role in microtubule nucleation.
    Stillwell EE, Zhou J, Joshi HC
    Cell cycle (Georgetown, Tex.). 2004 ; 3 (7) : 923-930.
    PMID 15190203
    NIN, a gene encoding a CEP110-like centrosomal protein, is fused to PDGFRB in a patient with a t(5;14)(q33;q24) and an imatinib-responsive myeloproliferative disorder.
    Vizmanos JL, Novo FJ, Rom´n JP, Baxter EJ, Lahortiga I, Larr´yoz MJ, Odero MD, Giraldo P, Calasanz MJ, Cross NC
    Cancer research. 2004 ; 64 (8) : 2673-2676.
    PMID 15087377


    This paper should be referenced as such :
    Vizmanos, JL
    NIN (ninein (GSK3B interacting protein))
    Atlas Genet Cytogenet Oncol Haematol. 2004;8(4):300-302.
    Free journal version : [ pdf ]   [ DOI ]

    Other Leukemias implicated (Data extracted from papers in the Atlas) [ 4 ]
      t(5;6)(q33;q23) CEP85L::PDGFRB
    t(5;14)(q33;q24) NIN::PDGFRB
    t(14;14)(q22;q22) NIN::TMX1
    t(14;14)(q22;q32) NIN::UNC79

    External links

    HGNC (Hugo)NIN   14906
    Atlas Explorer : (Salamanque)NIN
    Entrez_Gene (NCBI)NIN    ninein
    GeneCards (Weizmann)NIN
    Ensembl hg19 (Hinxton)ENSG00000100503 [Gene_View]
    Ensembl hg38 (Hinxton)ENSG00000100503 [Gene_View]  ENSG00000100503 [Sequence]  chr14:50725829-50831121 [Contig_View]  NIN [Vega]
    ICGC DataPortalENSG00000100503
    TCGA cBioPortalNIN
    AceView (NCBI)NIN
    Genatlas (Paris)NIN
    SOURCE (Princeton)NIN
    Genetics Home Reference (NIH)NIN
    Genomic and cartography
    GoldenPath hg38 (UCSC)NIN  -     chr14:50725829-50831121 -  14q22.1   [Description]    (hg38-Dec_2013)
    GoldenPath hg19 (UCSC)NIN  -     14q22.1   [Description]    (hg19-Feb_2009)
    GoldenPathNIN - 14q22.1 [CytoView hg19]  NIN - 14q22.1 [CytoView hg38]
    Genome Data Viewer NCBININ [Mapview hg19]  
    OMIM608684   614851   
    Gene and transcription
    Genbank (Entrez)AA742651 AB046785 AF186776 AF212162 AF223937
    RefSeq transcript (Entrez)NM_016350 NM_020921 NM_182944 NM_182945 NM_182946
    Consensus coding sequences : CCDS (NCBI)NIN
    Gene ExpressionNIN [ NCBI-GEO ]   NIN [ EBI - ARRAY_EXPRESS ]   NIN [ SEEK ]   NIN [ MEM ]
    Gene Expression Viewer (FireBrowse)NIN [ Firebrowse - Broad ]
    GenevisibleExpression of NIN in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
    BioGPS (Tissue expression)51199
    GTEX Portal (Tissue expression)NIN
    Human Protein AtlasENSG00000100503-NIN [pathology]   [cell]   [tissue]
    Protein : pattern, domain, 3D structure
    Domain families : Pfam (Sanger)
    Domain families : Pfam (NCBI)
    Conserved Domain (NCBI)NIN
    Human Protein Atlas [tissue]ENSG00000100503-NIN [tissue]
    Protein Interaction databases
    Ontologies - Pathways
    PubMed75 Pubmed reference(s) in Entrez
    GeneRIFsGene References Into Functions (Entrez)
    REVIEW articlesautomatic search in PubMed
    Last year publicationsautomatic search in PubMed

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    indexed on : Thu Jan 20 14:13:03 CET 2022

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