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P41218

- MNDA_HUMAN

UniProt

P41218 - MNDA_HUMAN

Protein

Myeloid cell nuclear differentiation antigen

Gene

MNDA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    May act as a transcriptional activator/repressor in the myeloid lineage. Plays a role in the granulocyte/monocyte cell-specific response to interferon. Stimulates the DNA binding of the transcriptional repressor protein YY1.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. B cell receptor signaling pathway Source: UniProtKB
    2. cellular defense response Source: ProtInc
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. negative regulation of B cell proliferation Source: UniProtKB
    5. positive regulation of apoptotic process Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myeloid cell nuclear differentiation antigen
    Gene namesi
    Name:MNDA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7183. MNDA.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Uniformly distributed throughout the interphase cell nucleus. Associates with chromatin.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30895.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407Myeloid cell nuclear differentiation antigenPRO_0000153724Add
    BLAST

    Proteomic databases

    MaxQBiP41218.
    PaxDbiP41218.
    PeptideAtlasiP41218.
    PRIDEiP41218.

    PTM databases

    PhosphoSiteiP41218.

    Expressioni

    Tissue specificityi

    Expressed constitutively in cells of the myeloid lineage. Found in promyelocyte stage cells as well as in all other stage cells including peripheral blood monocytes and granulocytes. Also appear in myeloblast cells in some cases of acute myeloid Leukemia.1 Publication

    Inductioni

    Strongly induced by alpha interferon which selectively affects expression in late stage cells in the monocytic but not the granulocytic lineage. Induced in vitro by dimethylsulfoxide and 1,25 dihydroxyvitamin D3.1 Publication

    Gene expression databases

    ArrayExpressiP41218.
    BgeeiP41218.
    CleanExiHS_MNDA.
    GenevestigatoriP41218.

    Organism-specific databases

    HPAiHPA034532.

    Interactioni

    Subunit structurei

    Participates in a ternary complex with YY1 and the YY1 target DNA element. Binds nucleolin and nucleophosmin/NPM/B23.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    WHSC1L1Q9BZ952EBI-2829677,EBI-3390132

    Protein-protein interaction databases

    BioGridi110475. 3 interactions.
    IntActiP41218. 7 interactions.
    MINTiMINT-8373462.
    STRINGi9606.ENSP00000357123.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 118
    Turni12 – 165
    Helixi19 – 3315
    Helixi37 – 426
    Helixi45 – 5511
    Helixi60 – 689
    Helixi73 – 753
    Helixi76 – 8914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DBGNMR-A1-90[»]
    ProteinModelPortaliP41218.
    SMRiP41218. Positions 1-90, 205-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41218.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8888DAPINPROSITE-ProRule annotationAdd
    BLAST
    Domaini196 – 394199HIN-200PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi131 – 1377Nuclear localization signalSequence Analysis

    Domaini

    Its N-terminal half (200 amino acids) is sufficient for maximum enhancement of YY1 DNA binding and a portion of this sequence is responsible for binding YY1.

    Sequence similaritiesi

    Contains 1 DAPIN domain.PROSITE-ProRule annotation
    Contains 1 HIN-200 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG81691.
    HOGENOMiHOG000033871.
    HOVERGENiHBG006122.
    InParanoidiP41218.
    OMAiGKWHNIK.
    OrthoDBiEOG7ZD1V8.
    PhylomeDBiP41218.
    TreeFamiTF337385.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    InterProiIPR004020. DAPIN.
    IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF02760. HIN. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view]
    PROSITEiPS50824. DAPIN. 1 hit.
    PS50834. HIN_200. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P41218-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNEYKKILL LKGFELMDDY HFTSIKSLLA YDLGLTTKMQ EEYNRIKITD    50
    LMEKKFQGVA CLDKLIELAK DMPSLKNLVN NLRKEKSKVA KKIKTQEKAP 100
    VKKINQEEVG LAAPAPTARN KLTSEARGRI PVAQKRKTPN KEKTEAKRNK 150
    VSQEQSKPPG PSGASTSAAV DHPPLPQTSS STPSNTSFTP NQETQAQRQV 200
    DARRNVPQND PVTVVVLKAT APFKYESPEN GKSTMFHATV ASKTQYFHVK 250
    VFDINLKEKF VRKKVITISD YSECKGVMEI KEASSVSDFN QNFEVPNRII 300
    EIANKTPKIS QLYKQASGTM VYGLFMLQKK SVHKKNTIYE IQDNTGSMDV 350
    VGSGKWHNIK CEKGDKLRLF CLQLRTVDRK LKLVCGSHSF IKVIKAKKNK 400
    EGPMNVN 407
    Length:407
    Mass (Da):45,836
    Last modified:February 1, 1995 - v1
    Checksum:iF4943C38033C5A83
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti156 – 1561S → R.
    Corresponds to variant rs35417083 [ dbSNP | Ensembl ].
    VAR_034107
    Natural varianti286 – 2861V → L.
    Corresponds to variant rs1056771 [ dbSNP | Ensembl ].
    VAR_012055
    Natural varianti357 – 3571H → Y.
    Corresponds to variant rs2276403 [ dbSNP | Ensembl ].
    VAR_020483

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81750 mRNA. Translation: AAA69696.1.
    BC032319 mRNA. Translation: AAH32319.1.
    CCDSiCCDS1177.1.
    PIRiI55525.
    RefSeqiNP_002423.1. NM_002432.1.
    UniGeneiHs.153837.

    Genome annotation databases

    EnsembliENST00000368141; ENSP00000357123; ENSG00000163563.
    GeneIDi4332.
    KEGGihsa:4332.
    UCSCiuc001fsz.1. human.

    Polymorphism databases

    DMDMi730038.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81750 mRNA. Translation: AAA69696.1 .
    BC032319 mRNA. Translation: AAH32319.1 .
    CCDSi CCDS1177.1.
    PIRi I55525.
    RefSeqi NP_002423.1. NM_002432.1.
    UniGenei Hs.153837.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DBG NMR - A 1-90 [» ]
    ProteinModelPortali P41218.
    SMRi P41218. Positions 1-90, 205-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110475. 3 interactions.
    IntActi P41218. 7 interactions.
    MINTi MINT-8373462.
    STRINGi 9606.ENSP00000357123.

    PTM databases

    PhosphoSitei P41218.

    Polymorphism databases

    DMDMi 730038.

    Proteomic databases

    MaxQBi P41218.
    PaxDbi P41218.
    PeptideAtlasi P41218.
    PRIDEi P41218.

    Protocols and materials databases

    DNASUi 4332.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368141 ; ENSP00000357123 ; ENSG00000163563 .
    GeneIDi 4332.
    KEGGi hsa:4332.
    UCSCi uc001fsz.1. human.

    Organism-specific databases

    CTDi 4332.
    GeneCardsi GC01P158801.
    HGNCi HGNC:7183. MNDA.
    HPAi HPA034532.
    MIMi 159553. gene.
    neXtProti NX_P41218.
    PharmGKBi PA30895.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81691.
    HOGENOMi HOG000033871.
    HOVERGENi HBG006122.
    InParanoidi P41218.
    OMAi GKWHNIK.
    OrthoDBi EOG7ZD1V8.
    PhylomeDBi P41218.
    TreeFami TF337385.

    Miscellaneous databases

    ChiTaRSi MNDA. human.
    EvolutionaryTracei P41218.
    GeneWikii MNDA.
    GenomeRNAii 4332.
    NextBioi 17047.
    PROi P41218.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41218.
    Bgeei P41218.
    CleanExi HS_MNDA.
    Genevestigatori P41218.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    InterProi IPR004020. DAPIN.
    IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF02760. HIN. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view ]
    PROSITEi PS50824. DAPIN. 1 hit.
    PS50834. HIN_200. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the human myeloid cell nuclear differentiation antigen: regulation by interferon alpha."
      Briggs J.A., Burrus G.R., Stickney B.D., Briggs R.C.
      J. Cell. Biochem. 49:82-92(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Pancreas.
    3. "Characterization of the human myeloid cell nuclear differentiation antigen: relationship to interferon-inducible proteins."
      Burrus G.R., Briggs J.A., Briggs R.C.
      J. Cell. Biochem. 48:190-202(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    4. "The human myeloid cell nuclear differentiation antigen gene is one of at least two related interferon-inducible genes located on chromosome 1q that are expressed specifically in hematopoietic cells."
      Briggs R.C., Briggs J.A., Ozer J., Sealy L., Dworkin L.L., Kingsmore S.F., Seldin M.F., Kaur G.P., Athwal R.S., Dessypris E.N.
      Blood 83:2153-2162(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "Interferon alpha selectively affects expression of the human myeloid cell nuclear differentiation antigen in late stage cells in the monocytic but not the granulocytic lineage."
      Briggs R., Dworkin L., Briggs J., Dessypris E., Stein J., Stein G., Lian J.
      J. Cell. Biochem. 54:198-206(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY OF ALPHA-INTERFERON INDUCTION.
    6. "The closely linked genes encoding the myeloid nuclear differentiation antigen (MNDA) and IFI16 exhibit contrasting haemopoietic expression."
      Dawson M.J., Trapani J.A., Briggs R.C., Nicholl J.K., Sutherland G.R., Baker E.
      Immunogenetics 41:40-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL LOCATION, TISSUE SPECIFIC INDUCTION.
    7. "Human hematopoietic cell specific nuclear protein MNDA interacts with the multifunctional transcription factor YY1 and stimulates YY1 DNA binding."
      Xie J., Briggs J.A., Briggs R.C.
      J. Cell. Biochem. 70:489-506(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION.
    8. "Solution structure of the pyrin (PAAD-DAPIN) domain in human myeloid cell nuclear differentiation antigen."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-90.

    Entry informationi

    Entry nameiMNDA_HUMAN
    AccessioniPrimary (citable) accession number: P41218
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 127 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3